امروزه مشخص شده است كه پسوريازيس يك بيماري مرتبط با سيستم ايمني بدن است. در طي اين بيماري سيستم ايمني با ارسال سيگنالهاي معيوب موجب تسريع رشد سلولهاي پوست ميشود. در واقع در حالت عادي سلولهاي پوست بطور دائم از لايههاي زيرين به طرف سطح حركت كرده، در آنجا هستههاي خود را از دست داده و بصورت پوستههاي مرده از بدن دفع ميشوند. اين روند بطور معمول حدود 4 هفته به طول ميانجامد، اما در جريان پسوريازيس، چرخه حيات سلولهاي پوست بر اثر همان اشكالات سيستم ايمني، سرعت يافته به حدود 2 هفته تقلیل می یابد، در نتيجه چندين لايه سلول مرده در سطح پوست تجمع پيدا ميكنند كه همان پوستههاي پسوريازيس را تشكيل ميدهند
کازمتیک - اسیدهای آمینه و پروتئین ها و اهمیت آنهاMohammad Baghaei
پروتئین ها و پپتید ها بلوک های ساختمان زندگی هستند . آنها بیوپلیمر های حیاتی هستند که از اسید ها آمینه تشکیل شده اند ، بسته به توالی اسید ، در ساختار همه فرم های حیات کارهای مختلف و گسترده ای را انجام می دهند . پروتئین ها برای شرایط پوست و مو از اهمیت اولیه ای برخوردارند . در پوست ، پروتئین های رشته ای ، مثل کلاژن و الاستین ، نقش ضروری ای را بازی می کنند . همچنین کراتین ها در مو و ناخن ما پروتئین های با مولکول بالا هستند.
This study identifies molecular chaperones that regulate the endoplasmic reticulum (ER) quality control of the thiazide-sensitive NaCl cotransporter (NCC). NCC forms complexes with the core chaperones Hsp90, Hsp70, and Hsp40 in the cytoplasm. Disruption of Hsp90 function accelerates NCC degradation, indicating Hsp90 promotes NCC folding. The cochaperones CHIP and HOP differentially regulate NCC turnover, with CHIP promoting degradation and HOP favoring biogenesis. Adjusting the folding environment enhances wild type NCC maturation but not disease mutants, which interact more strongly with Hsp70/Hsp40 and are selected for ER
امروزه مشخص شده است كه پسوريازيس يك بيماري مرتبط با سيستم ايمني بدن است. در طي اين بيماري سيستم ايمني با ارسال سيگنالهاي معيوب موجب تسريع رشد سلولهاي پوست ميشود. در واقع در حالت عادي سلولهاي پوست بطور دائم از لايههاي زيرين به طرف سطح حركت كرده، در آنجا هستههاي خود را از دست داده و بصورت پوستههاي مرده از بدن دفع ميشوند. اين روند بطور معمول حدود 4 هفته به طول ميانجامد، اما در جريان پسوريازيس، چرخه حيات سلولهاي پوست بر اثر همان اشكالات سيستم ايمني، سرعت يافته به حدود 2 هفته تقلیل می یابد، در نتيجه چندين لايه سلول مرده در سطح پوست تجمع پيدا ميكنند كه همان پوستههاي پسوريازيس را تشكيل ميدهند
کازمتیک - اسیدهای آمینه و پروتئین ها و اهمیت آنهاMohammad Baghaei
پروتئین ها و پپتید ها بلوک های ساختمان زندگی هستند . آنها بیوپلیمر های حیاتی هستند که از اسید ها آمینه تشکیل شده اند ، بسته به توالی اسید ، در ساختار همه فرم های حیات کارهای مختلف و گسترده ای را انجام می دهند . پروتئین ها برای شرایط پوست و مو از اهمیت اولیه ای برخوردارند . در پوست ، پروتئین های رشته ای ، مثل کلاژن و الاستین ، نقش ضروری ای را بازی می کنند . همچنین کراتین ها در مو و ناخن ما پروتئین های با مولکول بالا هستند.
This study identifies molecular chaperones that regulate the endoplasmic reticulum (ER) quality control of the thiazide-sensitive NaCl cotransporter (NCC). NCC forms complexes with the core chaperones Hsp90, Hsp70, and Hsp40 in the cytoplasm. Disruption of Hsp90 function accelerates NCC degradation, indicating Hsp90 promotes NCC folding. The cochaperones CHIP and HOP differentially regulate NCC turnover, with CHIP promoting degradation and HOP favoring biogenesis. Adjusting the folding environment enhances wild type NCC maturation but not disease mutants, which interact more strongly with Hsp70/Hsp40 and are selected for ER
The document discusses highly sensitive people (HSPs), who make up 15-20% of the population. It describes HSPs as "Priestly Advisors" who are quiet observers, trust others' opinions, and resolve differences through empathy. In contrast, it describes most others as "Warrior Kings" who make quick assumptions and prioritize power and success. The document outlines physiological and personality traits of HSPs, difficulties they may face, and how to thrive by embracing their sensitivity. It invites readers to discover their gifts and find creative passion.
Molecular chaperones such as Hsp70 and chaperonins assist in the folding of other proteins in the cell. Hsp70 binds to unfolded regions of proteins and prevents aggregation, then Hsp40 triggers a change in Hsp70 that traps the protein. Chaperonins form a cavity in which folding can occur. These chaperones are important for protein folding but do not actively promote folding. When proteins misfold it can lead to human diseases such as diabetes and neurodegenerative disorders.
HSP 101: BEGINNING TO UNDERSTAND THE HIGHLY SENSITIVE PERSONJoanne Conger
The document discusses the traits and experiences of highly sensitive persons (HSPs). It explains that HSP is a birth trait where some individuals may experience emotions, sensations, and stimuli more deeply and intensely than others. It describes how HSPs may feel emotions like love, sadness or disappointment more strongly. They may also be more deeply affected by the arts, empathy, and need more time and reassurance to process their feelings. The document advocates that HSP is not a weakness but part of someone's core nature, and requests that others allow HSPs to experience and process emotions in their own way.
The document summarizes the mechanism of protein folding in 3 sentences:
Protein folding is the physical process by which a polypeptide folds into its characteristic three-dimensional structure, driven by hydrophobic amino acids forming a core shielded from water and polar residues interacting with surrounding water. Key factors that stabilize the folded state include intramolecular hydrogen bonds and hydrophobic interactions. Molecular chaperones assist in protein folding in the crowded intracellular environment to prevent misfolding and aggregation.
Proteins are made up of elements like carbon, hydrogen, oxygen, nitrogen, sulfur, and phosphorus. They are formed through condensation reactions between amino acids and can be broken down through hydrolysis. There are four levels of protein structure: primary, secondary, tertiary, and quaternary. The primary structure is the linear sequence of amino acids, secondary structure involves alpha helices and beta sheets, tertiary is the overall 3D shape, and quaternary involves combinations of tertiary structures. There are essential and non-essential amino acids, with essential ones not synthesized by the body.
The document discusses the levels of protein structure from primary to quaternary structure. It defines the primary structure as the amino acid sequence. Secondary structure forms from hydrogen bonding between amino acids and includes alpha helices and beta pleated sheets. Tertiary structure results from folding influenced by interactions between amino acid side chains. Quaternary structure occurs when multiple polypeptide chains interact to form a protein complex. Examples including hemoglobin and glyceraldehyde-3-phosphate dehydrogenase are provided to illustrate the different levels of structure.
Proteins are composed of amino acids and play many essential roles in the body. They have four levels of structure: primary, secondary, tertiary, and quaternary. The primary structure is the amino acid sequence, secondary involves hydrogen bonding into shapes like alpha helices and beta sheets, tertiary is the 3D folding of these structures, and quaternary involves the assembly of multiple protein subunits. Proteins serve as enzymes, hormones, antibodies, and structures. They undergo synthesis from amino acids and breakdown through catabolism. Disorders can occur if amino acid metabolism is disrupted.
The document discusses highly sensitive people (HSPs), who make up 15-20% of the population. It describes HSPs as "Priestly Advisors" who are quiet observers, trust others' opinions, and resolve differences through empathy. In contrast, it describes most others as "Warrior Kings" who make quick assumptions and prioritize power and success. The document outlines physiological and personality traits of HSPs, difficulties they may face, and how to thrive by embracing their sensitivity. It invites readers to discover their gifts and find creative passion.
Molecular chaperones such as Hsp70 and chaperonins assist in the folding of other proteins in the cell. Hsp70 binds to unfolded regions of proteins and prevents aggregation, then Hsp40 triggers a change in Hsp70 that traps the protein. Chaperonins form a cavity in which folding can occur. These chaperones are important for protein folding but do not actively promote folding. When proteins misfold it can lead to human diseases such as diabetes and neurodegenerative disorders.
HSP 101: BEGINNING TO UNDERSTAND THE HIGHLY SENSITIVE PERSONJoanne Conger
The document discusses the traits and experiences of highly sensitive persons (HSPs). It explains that HSP is a birth trait where some individuals may experience emotions, sensations, and stimuli more deeply and intensely than others. It describes how HSPs may feel emotions like love, sadness or disappointment more strongly. They may also be more deeply affected by the arts, empathy, and need more time and reassurance to process their feelings. The document advocates that HSP is not a weakness but part of someone's core nature, and requests that others allow HSPs to experience and process emotions in their own way.
The document summarizes the mechanism of protein folding in 3 sentences:
Protein folding is the physical process by which a polypeptide folds into its characteristic three-dimensional structure, driven by hydrophobic amino acids forming a core shielded from water and polar residues interacting with surrounding water. Key factors that stabilize the folded state include intramolecular hydrogen bonds and hydrophobic interactions. Molecular chaperones assist in protein folding in the crowded intracellular environment to prevent misfolding and aggregation.
Proteins are made up of elements like carbon, hydrogen, oxygen, nitrogen, sulfur, and phosphorus. They are formed through condensation reactions between amino acids and can be broken down through hydrolysis. There are four levels of protein structure: primary, secondary, tertiary, and quaternary. The primary structure is the linear sequence of amino acids, secondary structure involves alpha helices and beta sheets, tertiary is the overall 3D shape, and quaternary involves combinations of tertiary structures. There are essential and non-essential amino acids, with essential ones not synthesized by the body.
The document discusses the levels of protein structure from primary to quaternary structure. It defines the primary structure as the amino acid sequence. Secondary structure forms from hydrogen bonding between amino acids and includes alpha helices and beta pleated sheets. Tertiary structure results from folding influenced by interactions between amino acid side chains. Quaternary structure occurs when multiple polypeptide chains interact to form a protein complex. Examples including hemoglobin and glyceraldehyde-3-phosphate dehydrogenase are provided to illustrate the different levels of structure.
Proteins are composed of amino acids and play many essential roles in the body. They have four levels of structure: primary, secondary, tertiary, and quaternary. The primary structure is the amino acid sequence, secondary involves hydrogen bonding into shapes like alpha helices and beta sheets, tertiary is the 3D folding of these structures, and quaternary involves the assembly of multiple protein subunits. Proteins serve as enzymes, hormones, antibodies, and structures. They undergo synthesis from amino acids and breakdown through catabolism. Disorders can occur if amino acid metabolism is disrupted.