The cytoskeleton and extracellular matrix are essential components of eukaryotic cells. The cytoskeleton is made up of three main types of protein filaments - actin filaments, microtubules, and intermediate filaments. These filaments help establish cell shape, provide mechanical strength, and enable intracellular transport. Actin filaments are assembled from globular actin subunits and play roles in cell motility and structure. Microtubules are hollow polymers of tubulin that nucleate from microtubule organizing centers and help separate chromosomes during cell division. Accessory proteins tightly regulate the dynamics of both filament types. The extracellular matrix provides structural support outside the cell and influences cellular behavior.
The document discusses the key components of the cytoskeleton - microtubules, microfilaments, and intermediate filaments - and how they work together to maintain cell shape, allow movement of organelles and vesicles, transport materials within the cell, and enable cell movement through polymerization and interaction with motor proteins like myosin and kinesin. The cytoskeleton is a dynamic network that forms various structures through accessory proteins and allows rapid changes in cell morphology.
The extracellular matrix (ECM) provides physical scaffolding and biochemical signals outside cells that are essential for tissue development and homeostasis. The ECM is composed of glycoproteins like collagen and proteoglycans that form a network, as well as glycoproteins like fibronectin that attach cells to the network. Collagen provides tensile strength and there are various types of collagen with different structures and functions. The ECM allows communication between cells through connections like tight junctions, desmosomes, and gap junctions. It also binds growth factors and interacts with cell receptors to regulate gene expression. Disruptions to the ECM can cause diseases like scurvy or emphysema.
The document discusses the composition and functions of the extracellular matrix (ECM) and cell-cell junctions. The ECM provides structural support to cells and regulates cell behavior. It is composed of fibrous proteins like collagen, polysaccharides like glycosaminoglycans, and adhesion proteins like fibronectin and laminin. Cells interact with the ECM through integrin receptors. Cell-cell junctions allow communication between cells and include adherens junctions, desmosomes, tight junctions, and gap junctions. The ECM and cell-cell junctions are essential for tissue structure and function.
Cell junctions connect neighboring cells and classify into three main types - occluding, communicating, and anchoring junctions. Occluding junctions prevent molecules from passing between cells, like tight junctions. Communicating junctions allow transfer of substances between cells via channels, such as gap junctions. Anchoring junctions provide structural strength, exemplified by desmosomes attaching cells to each other or hemidesmosomes attaching cells to the extracellular matrix. Cell adhesion molecules like cadherins and selectins are transmembrane proteins that mediate cell-cell binding and participate in various cellular processes during development, wound healing, and immune responses.
Microtubules are an essential component of the cytoskeleton that help maintain cellular structure and enable various cellular movements and transport processes. They are composed of alpha and beta tubulin subunits that polymerize to form protofilaments which assemble into microtubules. Microtubules are dynamic structures that undergo growth and shrinkage. Recent research has provided new insights into how microtubules and motor proteins self-organize to form larger cellular structures like spindles during cell division. Additionally, a protein called DRG1 has been found to promote microtubule polymerization and bundling, helping to regulate spindle assembly and dynamics.
1. The cytoskeleton is a network of fibers that organizes cell structures and activities.
2. It is composed of three main types of fibers: microtubules, microfilaments, and intermediate filaments.
3. Microtubules are hollow tubes that help maintain cell shape and enable intracellular transport. Microfilaments are thin fibers involved in cell motility and structure. Intermediate filaments provide mechanical strength and anchor organelles.
The document discusses the key components of the cytoskeleton - microtubules, microfilaments, and intermediate filaments - and how they work together to maintain cell shape, allow movement of organelles and vesicles, transport materials within the cell, and enable cell movement through polymerization and interaction with motor proteins like myosin and kinesin. The cytoskeleton is a dynamic network that forms various structures through accessory proteins and allows rapid changes in cell morphology.
The extracellular matrix (ECM) provides physical scaffolding and biochemical signals outside cells that are essential for tissue development and homeostasis. The ECM is composed of glycoproteins like collagen and proteoglycans that form a network, as well as glycoproteins like fibronectin that attach cells to the network. Collagen provides tensile strength and there are various types of collagen with different structures and functions. The ECM allows communication between cells through connections like tight junctions, desmosomes, and gap junctions. It also binds growth factors and interacts with cell receptors to regulate gene expression. Disruptions to the ECM can cause diseases like scurvy or emphysema.
The document discusses the composition and functions of the extracellular matrix (ECM) and cell-cell junctions. The ECM provides structural support to cells and regulates cell behavior. It is composed of fibrous proteins like collagen, polysaccharides like glycosaminoglycans, and adhesion proteins like fibronectin and laminin. Cells interact with the ECM through integrin receptors. Cell-cell junctions allow communication between cells and include adherens junctions, desmosomes, tight junctions, and gap junctions. The ECM and cell-cell junctions are essential for tissue structure and function.
Cell junctions connect neighboring cells and classify into three main types - occluding, communicating, and anchoring junctions. Occluding junctions prevent molecules from passing between cells, like tight junctions. Communicating junctions allow transfer of substances between cells via channels, such as gap junctions. Anchoring junctions provide structural strength, exemplified by desmosomes attaching cells to each other or hemidesmosomes attaching cells to the extracellular matrix. Cell adhesion molecules like cadherins and selectins are transmembrane proteins that mediate cell-cell binding and participate in various cellular processes during development, wound healing, and immune responses.
Microtubules are an essential component of the cytoskeleton that help maintain cellular structure and enable various cellular movements and transport processes. They are composed of alpha and beta tubulin subunits that polymerize to form protofilaments which assemble into microtubules. Microtubules are dynamic structures that undergo growth and shrinkage. Recent research has provided new insights into how microtubules and motor proteins self-organize to form larger cellular structures like spindles during cell division. Additionally, a protein called DRG1 has been found to promote microtubule polymerization and bundling, helping to regulate spindle assembly and dynamics.
1. The cytoskeleton is a network of fibers that organizes cell structures and activities.
2. It is composed of three main types of fibers: microtubules, microfilaments, and intermediate filaments.
3. Microtubules are hollow tubes that help maintain cell shape and enable intracellular transport. Microfilaments are thin fibers involved in cell motility and structure. Intermediate filaments provide mechanical strength and anchor organelles.
Cytoskeleton - microtubules ,microfilaments and intermediate filamentsBIOTECH SIMPLIFIED
The cytoskeleton is made up of three main filament systems - microtubules, microfilaments, and intermediate filaments. Microtubules are the thickest and made of tubulin, forming hollow tubes that help transport cellular cargo and separate chromosomes during cell division. Microfilaments are the thinnest and made of actin, enabling cell movement and shape changes. Intermediate filaments are in between the other two in diameter and made of various proteins, maintaining cell shape. Collectively, the cytoskeleton gives cells their structure, allows movement, and aids transport within cells.
MITOCHONDRIA ,STRUCTURE ,Mt DNA ,PROTEIN TRANSPORT,ETC,OXIDATIVE PHOSPHORYLATIONLIFE SCIENCES
introduction, structure , functions,how proteins are transported into mitochondria,functions,electron transport chain,oxidative phosphorylation with animated videos
Cell adhesion molecules help cells stick to each other and their surroundings through proteins. There are several types of cell adhesion molecules including immunoglobulin super family CAMs, integrins, selectins, and cadherins. Cadherins like E-cadherin form adherens junctions between cells and link to actin through catenins. Changes in cell adhesion can lead to diseases such as cancer where reduced adhesion allows cancer cells to invade other tissues. Cell adhesion molecules are important for tissue development and function.
Details of cytoskeleton element-microtubule. The Microtubule associated protein-type and function, Treadmilling and dynamic instability, Structure of cilia and flagella
1. Membrane trafficking allows the transfer of cargo between organelles through transport vesicles that form and fuse with target membranes.
2. Transport vesicles are coated with protein complexes that help generate the vesicles and select cargo for transport. Vesicles move cargo between organelles like the ER, Golgi apparatus, and endosomes.
3. Rab GTPases and SNARE proteins ensure vesicles dock and fuse with the correct target membrane, delivering cargo to its destination compartment.
It is a network of protein filaments in the cytoplasm of a cell
It provides structural framework to the cell.it also helps in the cell movement and movement of cytoplasmic components during several processes such as phagocytosis,endocytosis and exocytosis.
It consists of main three components microfilaments,microtubules and intermediate filament
Lysosomes and peroxisomes are membrane-bound organelles that play important roles in cellular processes. Lysosomes contain digestive enzymes and function in intracellular digestion, breaking down materials through phagocytosis, autophagy, and programmed cell death. Peroxisomes contain enzymes involved in breaking down hydrogen peroxide and performing beta-oxidation of fatty acids. Both are formed by budding from the Golgi apparatus. Defects in the enzymes of lysosomes or peroxisomes can lead to metabolic storage disorders.
The document discusses the cytoskeleton of eukaryotic cells. It provides background on the history and components of the cytoskeleton. The cytoskeleton consists of three main types of fibers - microtubules, microfilaments, and intermediate filaments. Microtubules are hollow rods that help with cell structure and mobility. Microfilaments are made of actin and resist tension. Intermediate filaments are specialized for bearing tension and maintaining cell shape.
The extracellular matrix is a network of proteins and carbohydrates that binds cells together, supports and surrounds cells, and regulates their activities. It is composed of collagens, elastic fibers, proteoglycans, hyaluronan, and adhesive glycoproteins. These molecules provide mechanical support, regulate embryonic development, enable cellular migration, facilitate wound healing, and manage growth factors. Collagen is the most abundant protein and forms fibrils and sheets that are linked together by connecting collagens. Proteoglycans and hyaluronan form hydrated gels within the matrix. Adhesive glycoproteins such as laminins and fibronectins attach cells to the matrix and regulate their behavior. The basal lam
The document summarizes key components of the extracellular matrix (ECM). It describes three main classes of ECM molecules: structural proteins like collagen and elastin that provide structure, proteoglycans that embed the structural proteins, and adhesive glycoproteins like fibronectin and laminin that attach cells to the matrix. It provides details on the composition, structure and function of proteoglycans, collagen, elastic fibers, reticular fibers and adhesive glycoproteins. It also discusses how defects in ECM synthesis can lead to diseases and conditions like muscular dystrophy.
This presentation gives an overview of Lipid Rafts, how it was discovered, its importance and the future research in this area,Feel free to comment and ask any questions
Cell adhesion molecules (CAMs) help cells bind to other cells and to the extracellular matrix. There are five major families of CAMs: cadherins, Ig superfamily CAMs, selectins, integrins, and mucins. Cadherins are calcium-dependent adhesion molecules that form desmosomes and bind cells together through homophilic or heterophilic adhesion. Integrins exist as alpha and beta subunits and bind to extracellular matrix proteins via outside-in and inside-out signaling to connect cells and regulate processes like adhesion, migration, differentiation, and apoptosis. CAMs play important roles in development by mediating cell-cell interactions and signals that direct tissue formation and gene expression.
Cell adhesion molecules are proteins located on cell surfaces that allow cells to adhere to each other and maintain tissue structure. The most important type are cadherins, which are calcium-dependent transmembrane proteins that connect to other cadherins on adjacent cells and link to the actin cytoskeleton. Cadherins help organize cell layers and tissues during development by promoting adhesion between similar cell types and separation between dissimilar ones. Other classes of cell adhesion molecules include integrins, IgCAMs, and selectins, which provide both calcium-dependent and calcium-independent adhesion between cells and the extracellular matrix.
The document discusses the cytoskeleton, which is composed of microfilaments, intermediate filaments, and microtubules. Microfilaments are composed of actin and are involved in cell motility and structure. Intermediate filaments provide mechanical strength and support cellular structures. Microtubules are composed of tubulin and are involved in maintaining cell shape and intracellular transport. The cytoskeleton is a dynamic network that maintains cell structure and enables various cell functions and movements.
Cell adhesion molecules and matrix proteinsUSmile Ï Ṩṃïlệ
Cell adhesion molecules are proteins located on cell surfaces that are involved in binding between cells or between cells and the extracellular matrix. The three main types are cadherins, integrins, and selectins. Cadherins are calcium-dependent proteins that mediate cell-cell adhesion. Integrins are transmembrane receptors that bind to components of the extracellular matrix and mediate cell-matrix adhesion as well as cell signaling. Selectins mediate the initial capture and rolling of leukocytes along vascular surfaces. Cell adhesion molecules play important physiological roles in processes like leukocyte trafficking, blood coagulation, and morphogenesis. They also have applications as therapeutic targets in areas such as cancer, osteoporosis, and inflammatory diseases.
The document discusses the biological membrane and its chemical composition. It notes that the plasma membrane is the outer boundary of cells, consisting of a double layer of lipid molecules with embedded proteins. The major components of membranes are glycerophospholipids, sphingolipids, and cholesterol. Glycerophospholipids are amphipathic lipids that form the lipid bilayer structure. The fluid mosaic model describes membranes as a fluid structure with lipids and proteins able to move laterally. Membrane proteins can be integral or peripheral, and help with cell functions like transport and signaling. Membrane fluidity is influenced by temperature and lipid composition.
The cytoskeleton is a network of fibers that extends throughout the cytoplasm and provides structural support to the cell. It is composed of three main types of fibers - microtubules, microfilaments, and intermediate filaments. The cytoskeleton also functions in cell motility through motor proteins that interact with the fibers to transport vesicles and organelles within the cell. It plays an important role in cell division and shape change.
Actin and myosin are proteins that play important roles in muscle contraction. Actin exists as monomers called G-actin and polymers called F-actin that form microfilaments. Myosin has a head domain that binds to actin and uses ATP to generate force and move along actin filaments. During muscle contraction, myosin heads attach to actin, exert tension through a power stroke, causing actin filaments to slide and muscles to shorten. Precise interactions between actin and myosin are crucial for muscle function and movement.
The cytoskeleton is composed of three main components - actin filaments, microtubules, and intermediate filaments. Actin filaments are made up of actin monomers that polymerize to form double helical structures. They play important roles in cell shape, movement, division, and intracellular transport. Microtubules are composed of tubulin dimers that assemble into hollow rods. They are involved in determining cell shape, movement, and transport of organelles. Both actin and microtubules undergo dynamic instability, rapidly assembling and disassembling in response to cellular signals.
1) Actin microfilaments are composed of globular actin subunits that polymerize to form filaments approximately 8 nm in diameter.
2) Actin polymerization is regulated by actin-binding proteins that nucleate, depolymerize, sever, cross-link, or cap actin filaments.
3) In nonmuscle and muscle cells, actin microfilaments interact with myosin to generate forces responsible for cell motility, shape changes, and muscle contraction.
Cytoskeleton - microtubules ,microfilaments and intermediate filamentsBIOTECH SIMPLIFIED
The cytoskeleton is made up of three main filament systems - microtubules, microfilaments, and intermediate filaments. Microtubules are the thickest and made of tubulin, forming hollow tubes that help transport cellular cargo and separate chromosomes during cell division. Microfilaments are the thinnest and made of actin, enabling cell movement and shape changes. Intermediate filaments are in between the other two in diameter and made of various proteins, maintaining cell shape. Collectively, the cytoskeleton gives cells their structure, allows movement, and aids transport within cells.
MITOCHONDRIA ,STRUCTURE ,Mt DNA ,PROTEIN TRANSPORT,ETC,OXIDATIVE PHOSPHORYLATIONLIFE SCIENCES
introduction, structure , functions,how proteins are transported into mitochondria,functions,electron transport chain,oxidative phosphorylation with animated videos
Cell adhesion molecules help cells stick to each other and their surroundings through proteins. There are several types of cell adhesion molecules including immunoglobulin super family CAMs, integrins, selectins, and cadherins. Cadherins like E-cadherin form adherens junctions between cells and link to actin through catenins. Changes in cell adhesion can lead to diseases such as cancer where reduced adhesion allows cancer cells to invade other tissues. Cell adhesion molecules are important for tissue development and function.
Details of cytoskeleton element-microtubule. The Microtubule associated protein-type and function, Treadmilling and dynamic instability, Structure of cilia and flagella
1. Membrane trafficking allows the transfer of cargo between organelles through transport vesicles that form and fuse with target membranes.
2. Transport vesicles are coated with protein complexes that help generate the vesicles and select cargo for transport. Vesicles move cargo between organelles like the ER, Golgi apparatus, and endosomes.
3. Rab GTPases and SNARE proteins ensure vesicles dock and fuse with the correct target membrane, delivering cargo to its destination compartment.
It is a network of protein filaments in the cytoplasm of a cell
It provides structural framework to the cell.it also helps in the cell movement and movement of cytoplasmic components during several processes such as phagocytosis,endocytosis and exocytosis.
It consists of main three components microfilaments,microtubules and intermediate filament
Lysosomes and peroxisomes are membrane-bound organelles that play important roles in cellular processes. Lysosomes contain digestive enzymes and function in intracellular digestion, breaking down materials through phagocytosis, autophagy, and programmed cell death. Peroxisomes contain enzymes involved in breaking down hydrogen peroxide and performing beta-oxidation of fatty acids. Both are formed by budding from the Golgi apparatus. Defects in the enzymes of lysosomes or peroxisomes can lead to metabolic storage disorders.
The document discusses the cytoskeleton of eukaryotic cells. It provides background on the history and components of the cytoskeleton. The cytoskeleton consists of three main types of fibers - microtubules, microfilaments, and intermediate filaments. Microtubules are hollow rods that help with cell structure and mobility. Microfilaments are made of actin and resist tension. Intermediate filaments are specialized for bearing tension and maintaining cell shape.
The extracellular matrix is a network of proteins and carbohydrates that binds cells together, supports and surrounds cells, and regulates their activities. It is composed of collagens, elastic fibers, proteoglycans, hyaluronan, and adhesive glycoproteins. These molecules provide mechanical support, regulate embryonic development, enable cellular migration, facilitate wound healing, and manage growth factors. Collagen is the most abundant protein and forms fibrils and sheets that are linked together by connecting collagens. Proteoglycans and hyaluronan form hydrated gels within the matrix. Adhesive glycoproteins such as laminins and fibronectins attach cells to the matrix and regulate their behavior. The basal lam
The document summarizes key components of the extracellular matrix (ECM). It describes three main classes of ECM molecules: structural proteins like collagen and elastin that provide structure, proteoglycans that embed the structural proteins, and adhesive glycoproteins like fibronectin and laminin that attach cells to the matrix. It provides details on the composition, structure and function of proteoglycans, collagen, elastic fibers, reticular fibers and adhesive glycoproteins. It also discusses how defects in ECM synthesis can lead to diseases and conditions like muscular dystrophy.
This presentation gives an overview of Lipid Rafts, how it was discovered, its importance and the future research in this area,Feel free to comment and ask any questions
Cell adhesion molecules (CAMs) help cells bind to other cells and to the extracellular matrix. There are five major families of CAMs: cadherins, Ig superfamily CAMs, selectins, integrins, and mucins. Cadherins are calcium-dependent adhesion molecules that form desmosomes and bind cells together through homophilic or heterophilic adhesion. Integrins exist as alpha and beta subunits and bind to extracellular matrix proteins via outside-in and inside-out signaling to connect cells and regulate processes like adhesion, migration, differentiation, and apoptosis. CAMs play important roles in development by mediating cell-cell interactions and signals that direct tissue formation and gene expression.
Cell adhesion molecules are proteins located on cell surfaces that allow cells to adhere to each other and maintain tissue structure. The most important type are cadherins, which are calcium-dependent transmembrane proteins that connect to other cadherins on adjacent cells and link to the actin cytoskeleton. Cadherins help organize cell layers and tissues during development by promoting adhesion between similar cell types and separation between dissimilar ones. Other classes of cell adhesion molecules include integrins, IgCAMs, and selectins, which provide both calcium-dependent and calcium-independent adhesion between cells and the extracellular matrix.
The document discusses the cytoskeleton, which is composed of microfilaments, intermediate filaments, and microtubules. Microfilaments are composed of actin and are involved in cell motility and structure. Intermediate filaments provide mechanical strength and support cellular structures. Microtubules are composed of tubulin and are involved in maintaining cell shape and intracellular transport. The cytoskeleton is a dynamic network that maintains cell structure and enables various cell functions and movements.
Cell adhesion molecules and matrix proteinsUSmile Ï Ṩṃïlệ
Cell adhesion molecules are proteins located on cell surfaces that are involved in binding between cells or between cells and the extracellular matrix. The three main types are cadherins, integrins, and selectins. Cadherins are calcium-dependent proteins that mediate cell-cell adhesion. Integrins are transmembrane receptors that bind to components of the extracellular matrix and mediate cell-matrix adhesion as well as cell signaling. Selectins mediate the initial capture and rolling of leukocytes along vascular surfaces. Cell adhesion molecules play important physiological roles in processes like leukocyte trafficking, blood coagulation, and morphogenesis. They also have applications as therapeutic targets in areas such as cancer, osteoporosis, and inflammatory diseases.
The document discusses the biological membrane and its chemical composition. It notes that the plasma membrane is the outer boundary of cells, consisting of a double layer of lipid molecules with embedded proteins. The major components of membranes are glycerophospholipids, sphingolipids, and cholesterol. Glycerophospholipids are amphipathic lipids that form the lipid bilayer structure. The fluid mosaic model describes membranes as a fluid structure with lipids and proteins able to move laterally. Membrane proteins can be integral or peripheral, and help with cell functions like transport and signaling. Membrane fluidity is influenced by temperature and lipid composition.
The cytoskeleton is a network of fibers that extends throughout the cytoplasm and provides structural support to the cell. It is composed of three main types of fibers - microtubules, microfilaments, and intermediate filaments. The cytoskeleton also functions in cell motility through motor proteins that interact with the fibers to transport vesicles and organelles within the cell. It plays an important role in cell division and shape change.
Actin and myosin are proteins that play important roles in muscle contraction. Actin exists as monomers called G-actin and polymers called F-actin that form microfilaments. Myosin has a head domain that binds to actin and uses ATP to generate force and move along actin filaments. During muscle contraction, myosin heads attach to actin, exert tension through a power stroke, causing actin filaments to slide and muscles to shorten. Precise interactions between actin and myosin are crucial for muscle function and movement.
The cytoskeleton is composed of three main components - actin filaments, microtubules, and intermediate filaments. Actin filaments are made up of actin monomers that polymerize to form double helical structures. They play important roles in cell shape, movement, division, and intracellular transport. Microtubules are composed of tubulin dimers that assemble into hollow rods. They are involved in determining cell shape, movement, and transport of organelles. Both actin and microtubules undergo dynamic instability, rapidly assembling and disassembling in response to cellular signals.
1) Actin microfilaments are composed of globular actin subunits that polymerize to form filaments approximately 8 nm in diameter.
2) Actin polymerization is regulated by actin-binding proteins that nucleate, depolymerize, sever, cross-link, or cap actin filaments.
3) In nonmuscle and muscle cells, actin microfilaments interact with myosin to generate forces responsible for cell motility, shape changes, and muscle contraction.
The document summarizes key aspects of the cytoskeleton, focusing on actin filaments. It describes how actin filaments: 1) maintain cell shape and generate force for cell movements through polymerization and depolymerization; 2) integrate cells through attachments to cell adhesions; and 3) produce movements within cells and at the cell membrane through interactions with myosin motor proteins. Accessory proteins regulate actin dynamics by capping, bundling, severing, and crosslinking filaments.
The document summarizes key aspects of the cytoskeleton, focusing on actin filaments. It describes how actin filaments: 1) maintain cell shape and generate force for cell movements through polymerization and depolymerization; 2) integrate cells through attachments to cell adhesions; and 3) produce movements within cells and at the cell membrane through interactions with myosin motor proteins. Accessory proteins regulate actin dynamics by capping, bundling, severing, and crosslinking filaments.
Cell movement is accomplished through the cytoskeleton, which is composed of three main types of fibers: actin filaments, microtubules, and intermediate filaments. Actin filaments interact with motor proteins like myosin to generate movement and play roles in cell adhesion, crawling, and contraction. Microtubules and their motor proteins kinesin and dynein facilitate intracellular transport and movement of cilia and flagella. Intermediate filaments provide structural support to cells but are not involved in motility. The three fiber types work together with associated proteins to control cell shape, division, transport, and movement.
The cytoskeleton is a network of fibers that organizes cell structures and activities. It is composed of three main types of fibers: microtubules, microfilaments, and intermediate filaments. Microtubules are the thickest fibers and help maintain cell shape. They also interact with motor proteins to transport vesicles within cells. Intermediate filaments provide mechanical strength and resist shear stress.
1. The document discusses the structure and function of eukaryotic cells and their organelles. It describes the plasma membrane, mitochondria, nucleus, endoplasmic reticulum, Golgi apparatus, lysosomes, peroxisomes, and cytoskeleton.
2. Key organelles include the mitochondria, which produces ATP through oxidative phosphorylation, and the nucleus, which contains DNA and directs protein synthesis.
3. The cytoskeleton is composed of microfilaments, microtubules, and intermediate filaments which help maintain cell shape and enable cell movement.
1) Actin is a globular protein that polymerizes to form microfilaments, one of the three main types of cytoskeletal filaments. Microfilaments are involved in cell movement, internal transport, and muscle contraction.
2) Microfilaments are polarized and dynamically assemble and disassemble at their barbed and pointed ends. Actin binding proteins regulate this process and organize microfilaments into bundles and networks.
3) Myosin motor proteins interact with actin filaments to generate force and drive movement of cargo within cells and contraction of muscle fibers. The sliding filament model explains how actin and myosin interact in sarcomeres to cause muscle contraction.
This document describes the crystal structure of human fibrinogen determined through x-ray crystallography. It is a large, multi-domain glycoprotein composed of three polypeptide chains that circulates in the blood and plays a central role in coagulation. Crystallization was challenging due to the protein's intrinsic flexibility. Reproducible crystals were obtained using the chemical chaperone TMAO and proteolysis to remove flexible regions. The crystal structure revealed differences in domain twisting and bending compared to other species, providing insight into fibrinogen's flexibility in solution. It also showed novel carbohydrate clusters and weak domain interactions that are important for fibrin formation.
The document provides an overview of cytoskeletal proteins and their functions, as well as how bacterial pathogens interact with and manipulate the host cytoskeleton during infection. It discusses the major cytoskeletal components microfilaments and microtubules. It also reviews how bacteria can alter host actin and microtubule dynamics through various mechanisms to facilitate infection of both phagocytic and non-phagocytic cells. The complex pathways regulating cytoskeletal dynamics are targeted by pathogenic bacteria through different strategies to subvert the host cytoskeleton for their own benefit during the infection process.
The cytoskeleton is composed of three main elements - microfilaments, microtubules, and intermediate filaments. Microfilaments are composed of actin and are involved in cell motility. Microtubules are composed of tubulin and form rigid hollow cylinders that help maintain cell shape and transport organelles within cells. Motor proteins like kinesin and dynein interact with cytoskeletal elements to transport materials. The cytoskeleton provides structure, helps position organelles, transports materials, and generates the forces necessary for cell movement.
The document discusses actin filaments and their assembly into various cellular structures. It focuses on structures at the plasma membrane, including sheet-like protrusions like lamellipodia and finger-like protrusions like filopodia. There are three known classes of actin nucleation factors - Arp2/3 complex, formins, and spire - that initiate actin filament assembly. The Arp2/3 complex produces a branched network of filaments near the leading edge of lamellipodia that drives protrusion, while formins and spire produce unbranched filaments throughout the lamellipodia and lamella.
The document discusses the three main types of filaments that make up the cytoskeleton - microtubules, microfilaments, and intermediate filaments. Microtubules are involved in cell division and structure other organelles. Microfilaments called actin filaments function in cell division, shape, and motility. Intermediate filaments provide strength and stability to cells and tissues. The cytoskeleton allows cells to maintain their shape and rearrange their internal structure during growth, division, and environmental changes.
a summary about the intermediate filaments
REFERENCE//
MOLECULAR CELL BIOLOGY (5TH EDITION) –LODISH – BERK – MATISUDAIRA – KAISER – KRIEGER – SCOTT – ZIPURSKY – DARNELL
The cytoskeleton is composed of three main types of protein filaments that provide structure and enable movement within cells. Microtubules are made of tubulin proteins and help maintain cell shape. Microfilaments are actin fibers that allow cell surface movement and structure microvilli. Intermediate filaments provide strength and resist stresses. Together, these filaments organize cell structures, drive motility, and play essential roles in processes like cell division and muscle contraction.
1) Microtubules grow by the addition of tubulin dimers to the plus end, with polymerization favored at this end. The plus end carries a GTP cap that stabilizes the microtubule.
2) Microtubules undergo treadmilling as the GTP cap moves down the length of the microtubule until reaching the minus end, where GTP is hydrolyzed.
3) Dynamic instability occurs when a microtubule switches between growth and shrinkage, providing a source of tubulin for other microtubules. Growing microtubules are favored when GTP-tubulin concentrations are high.
1. The sliding filament theory of muscle contraction describes how myosin cross-bridges interact with actin filaments through ATP hydrolysis, generating force and causing filament sliding.
2. Calcium binding to troponin exposes actin binding sites, allowing myosin cross-bridge binding and force generation through its power stroke.
3. Repeated myosin cross-bridge cycling causes incremental filament sliding, shortening the sarcomere and generating muscle contraction. ATP is required to detach cross-bridges between cycles.
This document provides information about muscle physiology and the structure of muscle fibers at the microscopic level. It discusses the basic units of muscles including myofibrils, myofilaments, sarcomeres, and the proteins actin and myosin that make up the thin and thick filaments. It describes the striated banding pattern visible in muscle fibers due to the organized arrangement of these contractile proteins. It also covers concepts related to muscle membrane potential including ion gradients and the role of the sodium-potassium pump in establishing the resting potential.
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This document discusses intellectual property rights (IPR) and patents in India. It defines intellectual property and IPR, and outlines the types of intellectual property including patents, designs, trademarks, geographical indications, and copyright. It then discusses the history and development of patent laws in India, prerequisites for a patent, and differences between the Indian and US patent acts. The document also outlines the patent procedure in India and types of special patents including for textiles, electronics, software, food, pharmaceuticals, and microorganisms.
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1. Describe the organisation of respiratory center
2. Describe the nervous control of inspiration and respiratory rhythm
3. Describe the functions of the dorsal and respiratory groups of neurons
4. Describe the influences of the Pneumotaxic and Apneustic centers
5. Explain the role of Hering-Breur inflation reflex in regulation of inspiration
6. Explain the role of central chemoreceptors in regulation of respiration
7. Explain the role of peripheral chemoreceptors in regulation of respiration
8. Explain the regulation of respiration during exercise
9. Integrate the respiratory regulatory mechanisms
10. Describe the Cheyne-Stokes breathing
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1. Chapter 42, Guyton and Hall Textbook of Medical Physiology, 14th edition
2. Chapter 36, Ganong’s Review of Medical Physiology, 26th edition
3. Chapter 13, Human Physiology by Lauralee Sherwood, 9th edition
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The key to a good grip on asthma is proper knowledge and management strategies. Understanding the patient-specific symptoms and carving out an effective treatment likewise is the best way to keep asthma under control.
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Co-Chairs, Val J. Lowe, MD, and Cyrus A. Raji, MD, PhD, prepared useful Practice Aids pertaining to Alzheimer’s disease for this CME/AAPA activity titled “Alzheimer’s Disease Case Conference: Gearing Up for the Expanding Role of Neuroradiology in Diagnosis and Treatment.” For the full presentation, downloadable Practice Aids, and complete CME/AAPA information, and to apply for credit, please visit us at https://bit.ly/3PvVY25. CME/AAPA credit will be available until June 28, 2025.
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In addition to infrastructure and capacity constraints, CAR-Ts face a very different risk-benefit dynamic in autoimmune compared to oncology, highlighting the need for tolerable therapies with low adverse event risk. CAR-NK and Treg-based therapies are also being developed in certain autoimmune disorders and may demonstrate favorable safety profiles. Several novel non-cell therapies such as bispecific antibodies, nanobodies, and RNAi drugs, may also offer future alternative competitive solutions with variable value propositions.
Widespread adoption of cell therapies will not only require strong efficacy and safety data, but also adapted pricing and access strategies. At oncology-based price points, CAR-Ts are unlikely to achieve broad market access in autoimmune disorders, with eligible patient populations that are potentially orders of magnitude greater than the number of currently addressable cancer patients. Developers have made strides towards reducing cell therapy COGS while improving manufacturing efficiency, but payors will inevitably restrict access until more sustainable pricing is achieved.
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1. Cytoskeleton
&
Extracellular
Matrix
Pradeep Singh
M.Sc. Medical Biochemistry
HIMSR, JAMIA HAMDARD
Fig: A section of mouse intestine
stained for actin (red), the
extracellular matrix protein laminin
(green), and DNA (blue). Each blue
dot of DNA indicate the presence of a
cell.
3. Introduction
Eukaryotic cells contain protein
filaments that are collectively called as
cytoskeleton.
These protein filaments are involved in:
─ establishing cell shape
─ provide mechanical strength
─ help in locomotion of cell
─ chromosome separation
─ intracellular transport of organelles
4. The three major cytoskeleton
filaments are:
1. Actin filaments
2. Microtubules
3. Intermediate filaments
In addition, a large number of
accessory proteins, including the
motor proteins, are also required
for the properties associated with
each of these filaments.
6. 1. Actin
• Actin was first isolated in 1942, from muscle cells in which it constitutes
approximately 20% of the total cell protein.
• The three-dimensional structures of both individual actin molecules and
actin filaments were determined in 1990.
• Actin filaments (F-Actin) also known as microfilaments, made up of small
subunits called G-Actin.
• G-Actin are globular proteins consisting of 375 amino acids. G-Actin is
described as having a pointed end and a barbed end.
Pointed End: Minus end
Barbed End: Plus end
8. Assembly of Actin Filament (F-Actin)
• G-Actin monomers polymerize to form actin filaments (F-Actin) having a
diameter of about 8nm.
• F-Actin is a helical structure.
• Steps of formation of actin filament:
a) Nucleation
b) Elongation
9. • Nucleation: For the formation of a new actin filament, subunits must
assemble into a small aggregate or nucleus which then elongate rapidly
by addition of new G-Actin subunits. This process is called filament
nucleation.
• Actin filament nucleate most frequently at the plasma membrane and
nucleation is regulated by external signals.
• Nucleation is the rate limiting step in the formation of a cytoskeletal
polymer.
• Elongation: G-Actin are added to the both ends but addition of new
subunits is faster at plus end.
11. Concept of Critical Concentration
• The number of monomers that are added to the polymer per second will be
proportional to the concentration of the free subunit (KonC), but the subunits will
leave the polymer end at a constant rate (Koff) that does not depend on C.
• Polymerization: Polymerization is a reversible process which depends on the
critical concentration (KonC) of the monomers.
• At a concentration > KonC, filament grows at each end but growth is faster at
the barbed end.
• At a concentration < KonC, filament shrink at both ends.
12. Nucleotide Hydrolysis
• Each actin molecule carries a tightly bound ATP molecule that is
hydrolysed to a tightly bound ADP molecule soon after its assembly into
the polymer.
• Hydrolysis of the bound nucleotide reduces the binding affinity of the
subunit for neighbouring subunits and makes it more likely to dissociate
from each end of the filament. It is usually the T-form that adds to the
filament and D-form that leaves.
13.
14. Treadmilling
• At the steady state, subunits undergo a
net assembly of monomers at the plus
end and a net disassembly at the minus
end at an identical rate.
• The polymers maintains a constant
length, even though there is net flux of
subunits through the polymer, known as
treadmilling.
15. Chemical Inhibitors of Actin
• The functions of the actin filaments are inhibited by both polymer-
stabilizing and polymer-destabilizing chemicals.
• These chemicals are used as an important tools in the study of the
filaments.
Table: Chemical Inhibiters of Actin
Chemical Effect on filaments Mechanism Original source
Latrunculin Depolymerizes Binds actin subunits Sponges
Cytochalasins B Depolymerizes Caps filament plus ends Fungi
Phalloidin Stabilizes Binds along filaments Amanita mushroom
16. Filament Elongation Is Modified By Proteins That
Bind To The Free Subunits
• In most non-muscle vertebrate cells, approximately 50% of the actin
is in filament form and 50% in soluble form while the monomer
concentration is 50-200 μM, well above the critical concentration (0.1
μM) .
Question: why does so little of the actin polymerize into filaments?
The actin is not polymerized as it is bound to special proteins, such as
thymosin. Actin monomers bound to thymosin are locked where they
cannot associate with either the (+) end or (-) end of the actin filament.
18. Actin Binding Proteins
• A number of different types of actin binding proteins remodel or modify
existing filaments.
Cellular Role Representative Proteins
Monomer binding Thymosin, Profilin
Filament initiation and polymerization Arp2/3, formin
Filament stabilization Tropomyosin
End capping CapZ, tropomodulin
Filament severing Cofilin, gelsolin
Filament cross-linking α-actinin, fimbrin, filamin
Actin filament linkage to other
proteins
Spectrin
19. A. Monomer Binding Proteins
• Thymosin: Actin monomer bound to thymosin are in a locked state, where
they cannot associate with either the plus end or minus ends of actin
filaments and can neither hydrolyse nor exchange their bound nucleotide.
• Profilin: Profilin binds to the actin monomer (G-Actin) opposite to the ATP-
binding cleft, blocking the side of the monomer that would normally
associate with the filament minus end, while leaving exposed the site on
the monomer that binds to the plus end.
• Profilin competes with thymosin for binding to individual actin monomer.
Thus, by regulating the local activity of profilin, cells can control the length
of actin filaments.
20.
21. B. Filament Initiation And Polymerization
1. Arp2/3: Arp stands for ‘Actin Related Proteins’.
― The Arp2/3 complex comprises 7 protein sub units.
― Both Arp2 and Arp3 are about 45% identical to actin.
― Arp2/3 complex nucleates actin filament growth from minus end, allowing
rapid elongation at the plus end.
― The ARP complex can also attach to the side of another actin filament while
remaining bound to the minus end of the filament that it has nucleated
resulting in the formation of web like structure.
22. Differences on the sides and minus end prevent the ARPs from forming filament on
their own.
23.
24.
25. 2. Formins: Formins are dimeric proteins that nucleate the growth of straight,
unbranched filaments that can be cross linked by other proteins to form protein
bundles.
― Formin dimer remains associated with the rapidly growing plus end while still
allowing the addition of new subunits at that end.
― Formin dependent actin filament growth is strongly enhanced by the addition of
profiling linked actin monomers.
26.
27. C. Filament Stabilization Proteins
• Tropomyosin: Tropomyosin, an elongated protein that binds simultaneously to six
or seven adjacent actin subunit along each of the two grooves of the helical actin
filament.
― In addition to stabilizing and stiffening the filament, the binding of
tropomyosin can prevent the actin from interacting with other proteins.
― Tropomyosin plays an important in the control of muscle contraction.
28. D. End Capping Proteins
• Tropomodulin: Tropomodulin is an end capping protein that binds
tightly to the minus ends of the actin filaments that have have been
coated and stabilized by tropomyosin.
• CapZ: CapZ is named so because of its location in the muscle Z band.
CapZ binds to the actin filament at the plus end, stabilizing the actin
filament by greatly reducing the rates of filament growth and
depolymerisation.
29. E. Filament Severing Proteins
• Sever means “breaking’.
• These proteins breaks an actin filaments into many smaller
fragments.
• The fate of these fragments depends on the presence of other
accessory proteins.
• Under some conditions, newly formed ends acts as nucleus and
promotes filament elongation.
• Under other conditions, severing promotes the depolymerization of
old fragments.
30. 1. Gelsolin superfamily: These proteins are activated by high levels of cytosolic Ca2+ .
― Gelsolin interact with the side of the actin filament and contains two subdomains that
binds to two different sites: one that is exposed on the surface of the filament and
another that is hidden between the adjacent subunit.
― Gelsolin creates a small gap between neighbouring subunits and inserts itself into the
gap to break into the filament.
― Gelsolin remains attached to the actin filament and caps the new plus end.
Two superfamilies of severing proteins are:
1. Gelsolin
2. Cofilin
32. 2. Cofilin superfamily: Also called actin depolymerizing factor.
― Cofilin binds along the length of the actin filament, forcing the filamentto
twist a little more tightly.
― Mechanical stress generated weakens the contacts between the actin
subunits in the filament, generating filament ends that undergo rapid
disassembly.
― Cofilin binds to ADP-containing actin filaments rather than to ATP-containing
filaments.
― Since, ATP hydrolysis is usually slower than filament assembly, the newest
actin filament in the cell still contain mostlt ATP and are resistant to
depolymerisation by cofilin.
― Cofilin therefore tends to dismantle the older filaments in the cell.
34. F. Filament Cross Linking Proteins
1. α-Actinin: α-Actinin includes
myosin and links oppositely
charged actin filaments into
contactile bundles.
2. Fimbrin: Fimbrin excludes
myosin and links actin
filaments into non contractile
parallel bundles.
35. 3. Filamin: Filamin promote the formation of a loose and highly
viscous gel by clamping two actin filaments roughly at right angles.
36. G. Actin Filaments Linking to Other Proteins
• Spectrin: Spectrin was first identified in RBC.
― Spectrin is a long, flexible protein made out of four elongated polypeptide
chains (two α subunits and two β subunits), arranged so that two actin
binding sites are 200 nm apart.
― In RBC, spectrin is concentrated just beneath the plasma membrane.
Spectrin has separate binding sites to actin filaments and other peripheral
proteins of plasma membrane.
―Spectrin allows the RBC to get back to normal shape after squeezing through
the capillary blood vessels.
37. ACTIN BASED MOTOR PROTEINS
• The first motor protein to be identified in the skeletal muscles was
Myosin.
• Consist of two heavy chains and two copies of each of two light chain.
• Helps in the muscle contraction.
38. Functions of Actin Filaments
― By forming a band under the plasma membrane, actin filaments allow cells to
adopt different shapes and perform different functions
― Generate locomotion in cells such as white blood cells and amoeba.
Villi Contractile
bundles
Sheet-like &
Finger-like
protrusions
Contractile
ring
39. ― Link transmembrane proteins to cytoplasmic proteins
― Form contractile ring during cytokinesis in animal cells
― Cytoplasmic streaming
― Interact with myosin to provide force of muscular contraction
41. 2. Microtubules
• Microtubules are hollow cylindrical structure
which are polymers of the protein tubulin.
• The tubulin subunit is a heterodimer made up
of two globular proteins called α-tubulin and β-
tubulin.
• The wall is composed of 13 parallel
protofilaments, each composed of αβ-tubulin
heterodimers stacked from head to tail.
• The α- and β-subunits of the tubulin dimer can
bind one molecule of GTP. The GTP in the α-
tubulin subunit is never hydrolyzed while β-
subunit may be in either GTP or the GDP form.
43. Polymerization of tubulin to
form microfilament
• Microtubule growth is generally
nucleated from specific locations with
in the cell known as microtubule-
organizing centre (MTOC).
• Many animal cells have single MTOC
called as centrosome, located near
nucleus.
• MTOC are highly enriched in another
type of tubulin called γ-tubulin which
form γ-tubulin ring complex (γ-
TuRC).This γ-tubulin ring complex
helps in the nucleation of
microtubules.
44. Mechanism:
• Two accessory proteins bind directly
to the γ-tubulin along with several
other proteins that help to create a
spiral ring of γ-tubulin molecules,
which serves as a template that create
a microtubule with 13 protofilaments.
• The microtubule then grows by
addition of free subunits.
• After incorporation of a dimeric
subunit into a microtubule, the GTP on
the β-tubulin is hydrolysed to GDP
CENTROSOME
46. Treadmilling and Dynamic Instability
Treadmilling is addition
of subunit at one end
and their loss at the
other end.
Dynamic instability is
the oscillation between
growth and shrinkage.
Catastrophe: The
change from growth to
shrinkage.
Rescue: The change from
shrinkage to growth
47. Centrosome
• Centrosome in animal cells
located near the nucleus.
• It contain centrioles and a
variable number of small dense
bodies called as centriolar
satellites.
• It consist of an amorphous
matrix of proteins containing the
γ-tubulin ring complexes that
nucleate microtubule growth.
• They serve as basal bodies and
sites of anchor for epithelial cilia.
48. Centrioles and Cell Division
• Duplication of the centrosomes takes place during ‘S’ phase cell division. To
form two separate MTOCs at opposite poles of the mitotic spindle.
• Two centrosomes then separate and move to opposite sides of the nucleus,
forming the two poles of the mitotic spindle.
• As the cell enters mitosis, the dynamics of microtubules assembly and
disassembly also change dramatically.
• First, the rate of microtubule disassembly increases about tenfold, resulting
in overall depolymerisation and shrinkage of microtubules.
• At the same time, the number of microtubules emerging from the
centrosome increases by five-to-tenfold.
49.
50. • As mitosis proceeds, the two chromatids of each chromosome are
then pulled to opposite poles of the spindle. This chromosome
movement is mediated by motor proteins associated with the spindle
microtubules.
• In the final stage of mitosis, nuclear envelopes reform, the
chromosome decondense, and cytokinesis takes place.
• If mitotic cells are exposed to drugs like colchicine (binds to
monomeric tubulin and prevent polymerization), vinblastine and taxol
(disrupt microtubule dynamics), microtubule disappear and mitosis is
arrested because of inadequate formation of the mitotic spindle.
These drugs are useful in the treatment of certain cancers.
51. Microtubules Associated
Proteins (MAP)
• Microtubule polymerization
dynamics is very different in cells
than in solutions of pure tubulin
(in vitro).
• Proteins that binds to
microtubules are collectively
called as microtubule-associated
proteins.
• MAP can be divided into two
groups:
1. Microtubule stabilizing proteins
2. Microtubule destabilizing
proteins.
52. TABLE: Proteins That Modulate Microtubule (MT) Dynamics
Protein Location Function
Microtubule Stabilizing
Proteins
MAP1 Dendrites and axons; non-
neuronal cells
Assembles and stabilizes MTs
MAP2 Dendrites Assembles and cross-links MTs to one
another and to intermediate filaments.
MAP4 Most cell types Stabilizes MTs
Tau Dendrites and axons Assemble stabilizes and cross-links MTs
Microtubule
Destabilizing Proteins
Stathmin Most cell types Binds tubulin dimers
katanin Most cell types Microtubule Severing
53. Microtubule Stabilizing Proteins
• Microtubule stabilizing proteins
helps in the organization of
microtubule bundles.
• MAPs have at least one domain
that binds to the microtubule and
another that project outwards.
• The length of the projecting
domain determine how closely
MAP-coated microtubules pack
together.
54. Microtubule Destabilizing Proteins
• One molecule of the small stathmin binds to two tubulin
heterodimerers and prevents their addition to the ends
of the microtubules.
• Stathmin thus decreases the effective concentration of
tubulin subunits that are available for polymerization.
• Phosphorylation of stathmin inhibits its binding to
tubulin.
1. Stathmin: Also
known as tubulin-
sequestering
protein.
55. 2. Katanin: katanin is also known as microtubule-severing protein.
• Katanin is named after the Japanese word for “sword”.
• Katanins release microtubules from their attachment to MTOC and
contribute to rapid microtubule depolymerisation observed at the
poles of spindles during mitosis.
• Katanin is made up of two subunits:
1. Smaller Subunit - Hydrolyze ATP and perform severing.
2. Larger Subunit – Direct katanin to the centrosome.
56.
57. Microtubule Ends Binding Proteins
Proteins that bind to the ends of microtubules can control microtubule positioning
58. Motor Proteins Move Along Microtubules
• Two major classes of microtubule-
based motors are:
1. Kinesins – Move towards (+) end
2. Dyneins – Move towards (-) end
• They use the energy of ATP
hydrolysis to move along
microtubules.
• They mediate the sliding of
filaments relative to one another
and the transport of membrane-
enclosed organelles along filament
tracks.
59. A. Kinesin
• Kinsesin-1 has two kinesin motor head domains:
• Rear or Lagging head domain: tightly bound to
microtubule and ATP.
• Front or leading head domain: loosely bound to
microtubule with ADP in its binding site.
• Most of them have the motor domain at the N-terminus of
the heavy chain and walk toward the plus end of the
microtubule.
• The forward displacement of the rear motor head domain
is driven by the hydrolysis of ATP and binding of ATP in the
leading head domain.
• They use “hand-over-hand” motion to walk over the
microtubule.
60.
61. B. Dyneins
• Dyneins are a family of minus end directed
motor proteins.
• The motor domain is present at the C-terminus
of the heavy chain and walk toward the minus
end of the microtubule.
• They are composed of one, two or three heavy
chains and a large number of light chains.
• Dynein requires the presence of a large number
of accessory proteins to associate with the
membrane-enclosed oragnelles.
• They are highly specialized for the rapid and
efficient sliding movement of the microtubules
that derive the beating of cilia and flagella.
63. 3. Intermediate Filaments
• Third major type of cytoskeletal protein.
• Present particularly in the cytoplasm of cells which are subjected to
mechanical stress.
• Generally absent in animals that have rigid exoskeleton.
• Structurally similar but biochemically distinct from actin and myosin
filaments.
• Intermediate filaments are extremely difficult to break and can be
stretched to over 3 times their length.
64. Structure of Intermediate Filaments
• Monomer is consist of α-helical
domain containing 40 or more hepted
repeat motifs.
• First Stage: Two monomers coil
together to form the dimer.
• Second Stage: A pair of parallel
dimers associates in antiparallel
fashion to form a staggered tetramer.
Thus, they lack structural polarity.
• Third Stage: Lateral association of 8
tetramers.
• Fourth Stage: Addition of 8 tetramers
to growing filament.
65.
66. Characteristics
• Intermediate filaments are generally more stable than actin filaments
or microtubules.
• Intermediate filaments can be modified by phosphorylation which
can regulate their assembly and disassembly.
67. Table: Major Types of Intermediate Filament Proteins in Vertebrate Cells
Types of Intermediate Filament Component Polypeptides Location
Nuclear Lamins A,B and C Nuclear Lamina (Inner
lining of nuclear
envelope)
Vimentin-like Vimentin Many cells of
mesenchymal origin
Desmin Muscle
Peripherin Some neuron
Epithelial Type I keratins (acidic) Epithelial cells and
their derivatives.Type II keratins
(neutral/basic)
Axonal Neurofilament proteins
(NF-L, NF-M, and NF-H)
Neurons
68. 1. Nuclear Lamins: Nuclear lamins are fibrous proteins providing
structural function and transcriptional regulation in the cell nucleus.
• Found in many eukaryotes but missing from unicellular organisms.
• Forms a meshwork that lines the ineer membrane of the nuclear envelope.
• Provide anchorage sites for chromosomes and nuclear pores.
2. Both Vimentin and Keratin attach to nuclear envelop serving to
position and anchor nucleus within the cell.
3. Desmin connects individual actin-myosin assemblies of muscle cell
to each other as well as to the plasma membrane.
4. Neurofilaments are major intermediate filaments of motor neurons.
69. Cell Junctions
• Intermediate filaments also form cell junctions.
• There are generally two types of cell junction:
1. Cell-cell junction
2. Cell-matrix junction
• Cell-cell junction formed by intermediate filaments – Desmosomes
• Cell- Matrix Junction formed by intermediate filaments –
Hemidesmosomes.
70.
71. Diseases of Intermediate Filament
• Epidermis Bullosa Simplex: Mutations in the keratin gene form skin
blister resulting from cell lysis after minor trauma.
72. • Lou Gehrig’s Disease: Also known as Amyotrophic lateral sclerosis
which leads to progressive loss of motor neurons which lead to
muscle atrophy, paralysis and eventual death.
74. “Half of the secrets of the cell are outside the cell.”
Dr. Mina Bissell
Oct. 17, 2007
Erlanger Auditorium
75. Why do all multicellular animals have ECM?
• Act as structural support to maintain cell organization and integrity (epithelial
tubes; mucosal lining of gut; skeletal muscle fiber integrity)
• Compartmentalize tissues (Pancreas: islets vs. exocrine component; skin:
epidermis vs. dermis)
• Provide hardness to bone and teeth (collagen fibrils become mineralized)
• Present information to adjacent cells:
• Inherent signals (e.g., RGD motif in fibronectin)
• Bound signals (BMP7, TGFγ, FGF, SHH)
• Serve as a highway for cell migration during development (neural crest
migration), in normal tissue maintenance (intestinal mucosa), and in injury or
disease (wound healing; cancer)
76. Extracellular Matrix
• Two broad categories of tissue that are found in all animals are:
1. Epithelial Tissue
2. Connective tissue
• Tissues are not only made up of cells. They also contain a remarkably complex
and intricate network of macromolecules constituting the Extracellular Matrix.
• The matrix can become calcified to form the rock-hard structures of bone or
teeth or it can form transmembrane substance of cornea etc.
• In most connective tissue, the matrix molecules are secreted by cells called
fibroblast.
77. • The extracellular matrix is constructed from three major classes of
macromolecules:
1. Glycosaminoglycas (GAGs) – Highly charged polysaccharide
covalently linked to proteins to form proteoglycans
2. Fibrous Proteins – Collagen, Elastin
3. Glycoproteins
78. 1. Glycosaminoglycan (GAGs)
• Glycosaminoglycans are unbranched polysaccharide chains composed
of repeating disaccharide units.
• One of the two sugars in the repeating disaccharide is always an
amino sugar (N-acetylglucosamine or N-acteylgalactosamine) which in
most cases in sulfated.
• GAGs are highly negatively charged because of the presence of sulfate
and carboxyl groups on most of their sugars.
79. • Four main groups of GAGs are distinguished by their sugars, the type
of linkage between the sugars, and the number and location of sulfate
groups:
1. Hyaluronan: D-Glucuronate + N-Acetyl-D-Glucosamine
2. Chondroitin sulfate and Dermatan sulfate
• Chondroitin Sulfate: D-Glucuronate + N-Acetyl-D-Galactosamine-4-sulfate
• Dermatan Sulfate: L-Iduronate + N-Acetyl-D-Galactosamine-4-sulfate
3. Heparan sulfate: L-Iduronate-2-sulfate + N-Sulfo-D-Glucosamine-6-
sulfate
4. Keratan sulfate: D-Galactose + N-Acetyl-D-Glucosamine-6-sulfate
80. Proteoglycans
• Proteoglycans are composed of GAG chains covalently linked to
proteins as proteoglycans.
• Except for hyaluronan, all GAGs take part in the synthesis of
proteoglycans.
• Synthesis of Proteoglycans: Membrane bound ribosomes make the
polypeptide chain or core protein which is then threaded into the
lumen of the ER.
• The polysaacharide chains are mainly assembled on this core protein
in the Golgi apparatus before delivery to the exterior of the cell by
exocytosis.
81. • Examples of proteoglycans:
1. Aggrecan:
─ Major Component of cartilage
─ Contain over 100 GAG chains.
2. Decorin:
─ Secreted by fibroblasts, contain only 1-10 GAG chains
─ Decorin binds to collagen fibrils and regulate fibrils assembly and fibril
diameter.
• Function: The proteoglycan molecules in connective tissue
typically form a highly hydrated, gel-like “ground substance”
in which collagens and glycoproteins are embedded.
82. 2. Fibrous Proteins
1. Collagen:
─ Collagens are a family of fibrous proteins
─ Collagens are the most abundant proteins in
animals, where they constitute 25% of the
total protein mass.
• Structure:
─ Triple helix
─ Has 3.3 residue per turn
─ Every 3rd amino acid residue is a glycine
residue
─ Gly-X-Y (X is commonly proline or
hydroxyproline while Y can be any amino acid)
83. Biosynthesis of Collagen
1. Synthesis of a chain of pre-procollagen on free ribosomes. A signal
protein that directs them to RER.
2. Cleavage of signal protein forms free ribosomes.
3. Hydroxylation of lysine and proline
4. Glycosylation: Addition of galactose and glucose to some hydroxylysine
residues. (Enzyme – Galactosyl transferase and Glycosyl transferase)
m-RNA
Signal protein
84. 5. Assembly of three α-chains to form procollagen
6. Secretion of procollagen molecules by exocytosis into the extra
cellular space.
S
S
Registration
peptides
S
S
S
S
S
S
S
S
S
S
α-helices
Procollagen
85. 7. Cleavage of the additional peptides leads to formation of
tropocollagen.
8. Self-assembly or polymerization of tropocollagen molecules form
collagen fibrils
Procollagen
peptidase
Procollagen
peptidase
86. Types of Collagen
1. Fibril Forming Collagens:
• Type I,II and III are fibril forming collagens.
• They have rope like structures.
2. Network Forming Collagens:
• Type IV and VIII forms a three dimensional mesh, rather than distinct fibrils.
3. Fibril Associated Collagens
• Type IX and XII binds to the surface of the collagen fibrils, linking these fibrils
to one another and to other components in the ECM.
87. Disease Associated with Collagen
1. Ehlers-Danlos Syndrome
• It is an inheritable defect.
• Caused by:
A. Deficiency of collagen-processing
enzymes
a) Lysyl hydroxylase
b) N-Procollagen peptidase
B. Mutations in the amino acid sequences
of collagen types I, III or V.
88. 2. Scurvy
• Caused due to deficiency of Vitamin-C.
• Ascorbate is required for Propyl hydroxylase and Lysyl hydroxylase
activities.
• Acquired disease of fibrillary collagen
• Manifestations:
1. Bleeding gums
2. Subcutaneous haemorrhage
3. Poor wound healing
89. 3. Menke’s Syndrome
Characterized by kinky hair and
growth retardation
Due to dietary deficiency of copper
which is require by lysyl oxidase
which catalyzes a key step in the
formation of the covalent cross-links
that strengthen collagen fibers.
90. 2. Elastin
• Connective tissue protein with rubber -
like properties
• Found in lungs, walls of large blood
vessels and elastic ligaments
• Can be stretched to several times their
normal length, but recoil to their
original shape when relaxed.
91. • It is synthesized as a soluble monomer of 70 KDA called tropoelastin.
• Composed primarily of small non polar amino acids residues (e.g. G,
A, V)
• Also rich in proline and lysine like collagen but not glycosylated,
contains little hydroxyproline and hydroxylysine.
• Long inelastic collagen fibrils are interwoven with elastic fibers to limit
the extent of stretching and prevent the tissue from tearing.
92. Genetic Abnormalities of Elastin
William’s Syndrome
• Deletion of elastin gene (7q 11.23) results in defective development
of the connective tissues in various organs including the CVS.
• Supravalvular aortic stenosis is a feature of this disorder. This severly
impairs the blood flow to various organs.
Pulmonary Emphysema
• It is accompanied by fragmentation or decrease in elastin protein in
lungs leading to destruction and lung cavity formation.
93. COLLAGEN ELASTIN
Triple helix No triple helix; random coil
conformations permitting
stretching
(Gly-X-Y)n repeating structure No ( Gly-X-Y)n repeating
structure
Presence of hydroxylysine
Carbohydrate-containing
No or very little hydroxylysine
No carbohydrate
Intramolecular aldol
cross-links
Intramolecular desmosine
cross-links
Presence of extension
peptides during bio-synthesis
No extension peptides present
during biosynthesis
94. 3. Glycoproteins
• Glycoproteins are proteins that contain oligosaccharide chains
covalently attached to the polypeptide side-chains.
• Glycoproteins have multiple domains, each with specific binding sites
for other matrix macromolecules and for receptors on the surface of
cells.
• Major type of glycoproteins are:
A. Fibronectins
B. Fibrilin
C. Laminin
D. integrins
95. A. Fibronectin
• Fibronectin is a dimer composed of two
very large subunits joined by di-sulphide
bonds at their C-terminal ends.
• Each subunit contains a series of small
repeated domains separated by short
stretches of polypeptide chain.
• Each domain is usually encoded by a
separate exon.
• Both the Arg-Gly-Asp (RGD) and the
“synergy” sequences are important for
binding to integrins on cell surfaces.
96. Fibronectin Binds to Integrins
• Fibronectins can exist in both forms:
1. Soluble form – Circulating in the blood and other body fluids
2. Insoluble fibronectin fibrils – fibronectin dimer cross link to one another by
additional disulphide bonds.
• Fibronectin molecules assemble into fibrils only on the surface of cells
where cells possess appropriate fibronectin-binding proteins
particularly integrins.
• Tight binding of integrins with the fibronectin requires more than just
the RGD sequence.
97. • Integrins provide a linkage from the fibronectin outside of the cell to
the actin cytoskeleton inside it.
• Integrin molecules allow fibronectin and actin filaments to bind
directly to one another. Thus, intracellular cytoskeleton align with the
extracellular fibronectin to determine cell shape.
• Fibronectin molecules assemble where there is a mechanical need for
them not in inappropriate locations such as bloodstream.
• In many kinds of cancer, cells are unable to make fibronectins, loose
shape and detach from the extracellular matrix to become malignant.
98. • During cell movement (as during embryogenesis), pathways of
fibronectins guide cells to their destinations.
• Soluble plasma fibronectin promotes blood clotting by direct binding
of fibrin.
• Fibronectins guide immune cells to wounded areas and thus promote
wound healing.
99. B. Laminin
• Laminin is a very large protein comprised of three
proteins that form a cross.
• Laminin and Type IV collagen are major components
of the basal lamina.
• The basal lamina acts as a selective barrier to the
movement of cells, as well as a filter for molecules.
• In the kidney, thick basal lamina helps to prevent the
passage of macromolecules from the blood into the
urine.
• Basal lamina is also important in tissue regeneration
after injury.
• Progeria (early onset of aging), is possibly due to a
defective laminin.
100. C. Integrins
• Group of transmembrane
glycoproteins.
• Allow cells to attach to ECM
constituents (laminins and
fibronectins mainly).
• Most integrins are receptors for
extracellular matrix proteins that
helps in the cell signalling.
• Integrins on the surface of
leukocytes plays an important
role in inflammation.
101. Summary
• Cytoskeleton and Extracellular matrix works in coordinated manner to
regulate the normal functioning of the cell.