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4.14.2010 lecture 2

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  • 1. 4.14.2010 Lecture 2 - ECM<br />
    • Tissue Types
    • 2. There are four tissue types
    • 3. Muscle Tissue
    • 4. Smooth Muscle
    • 5. Cardiac Muscle
    • 6. Striated Muscle
    • 7. Nervous System Tissue
    • 8. Neuronal cells
    • 9. Non-neuronal cells
    • 10. Connective Tissue
    • 11. Bone
    • 12. Osteocytes
    • 13. Mature bone cells
    • 14. Precursor is the osteoblast
    • 15. Secretes ECM during development of that tissue
    • 16. Cartilage
    • 17. Condroblasts
    • 18. Secrete ECM
    • 19. Loose connective Tissue
    • 20. Fibroblasts
    • 21. Secrete ECM
    • 22. Blood
    • 23. Lymphoid Tissue
    • 24. Made by cells
    • 25. Undifferentiated form of the mature cells that are characteristic of that tissue type
    • 26. Epithelial Tissue
    • 27. Epithelia
    • 28. Epithelial Cells
    • 29. Skin
    • 30. Intestinal Lining
    • 31. Held to one another and to the basal lamina
    • 32. Held to one another by tight junctions and adherins junctions
    • 33. Linked to basal lamina by integrins
    • 34. Integrins interact directly with the ECM
    • 35. Needs of basal lamina
    • 36. Loose connective tissue
    • 37. This is where we see the most gel-like structure in this type of connective tissue
    • 38. Fibroblasst secrete LCT
    • 39. Collagen
    • 40. Elastin
    • 41. Proteoglycans (more gel-like)
    • 42. Glycoproteins (more gel-like)
    • 43. Use intermediate filaments that are connected to the junctions between the cells and with the cell interaction between the basal lamina to withstand stress
    • 44. Connective Tissue Macromolecules
    • 45. ECM is made of two types of macromolecules
    • 46. Proteoglycans
    • 47. Protein core, which can vary, surrounded by GAGs
    • 48. Glycosomino Glycans
    • 49. They are negatively charged repeating units of sugars, polysaccharides, that covalently link themselves to the protein core, and useful in forming ECM because – charge attracts H20, creating a buffering sort of tissue that can withstand tensile stress and create a hydrated environment so cells can move and nutrients and waste can diffuse through and the cells can function because of those mobile molecules. Also cell motility
    • 50. Can link in complex ways
    • 51. The more GAGs, the more water and the more flexible that connective tissue is
    • 52. Fibrillar
    • 53. Types
    • 54. Collagen
    • 55. Fibronectin
    • 56. Elastin
    • 57. Importance
    • 58. Strong Structures
    • 59. Strength to the ECM
    • 60. Organization to the ECM
    • 61. Cell-ECM interaction
    • 62. From organized structure of ECM, allowing ECM to withstand pressure
    • 63. Holds tissue together when there is change or mechanical stress on the tissue
    • 64. Collagen
    • 65. Rheumatoid arthritis
    • 66. Inflammatory response, autoimmune, that is though to be genetic
    • 67. Immune system attacks collagen in ECM
    • 68. Unknown
    • 69. Causes pain and disfiguring of the joints
    • 70. Made of alpha chains
    • 71. Can assemble in a variety of ways
    • 72. Results in the types of collagen made
    • 73. Types of Collagen
    • 74. Type I – Fibrillar type
    • 75. 90% of ECM of the body
    • 76. Types can be differentiated by the roman numerals. Types can be placed into functional group:
    • 77. Fibrillar Forming collagen
    • 78. Fibril Associated collagen
    • 79. Network forming collagen
    • 80. Transmembrane collagen
    • 81. Synthesis of Collagen - ER
    • 82. Formed by the synthesis of an alpha chain
    • 83. Amino acid structure varies
    • 84. All have high concentrations of proline and glycine amino acids
    • 85. Proline: becomes heavily hydroxylated as the chain forms
    • 86. Form H bonds with neighboring amino acids
    • 87. Helps hold alpha chains together
    • 88. Glycine
    • 89. Smallest amino acid
    • 90. Present every third amino acid so the chains can interact very closely and tightly
    • 91. Three alpha chains fold together to make a procollagen triple helix, still in the ER
    • 92. On either end of the procollagen, amino acids hang off of amino and COOH termini
    • 93. Eventually clipped, which allows continual assembly
    • 94. Cannot occur until procollagen is secreted into cytoplasm
    • 95. Procollagen peptidase cleaves of terminal amino acids to make a mature collagen molecule ready to form into the fibril and fiber forms
    • 96. Assembly
    • 97. Procollagen align with one another with overlapping regions
    • 98. Creates striated pattern in the fibrillar collagen and allows for strength of collagen fiber in mature state
    • 99. Collagen fiber is generated as fibril wind around one another (~270 of collagen molecules that make up the fibril before the fiber)
    • 100. Occurs in cytoplasm after terminal amino acids are cleaved
    • 101. Types of Collagen
    • 102. Type I
    • 103. Fibrillar and associated collagen molecule (type 6)
    • 104. Type 6 – collagen regions, in between is a globular domain, which allows flexibility
    • 105. Purpose of flexibility: strength of fiber and flexibility of collagen associated protein
    • 106. Makes a strong fiber less rigid and more flexible
    • 107. Proteoglycan associates with the fibrils and carries with it the GAGs and water molecules, creating a buffer and gel like substrate for the absorption of force
    • 108. Bone
    • 109. Type II
    • 110. Cartilage
    • 111. Associated with non-fibrilar collagen, type IX
    • 112. Type IX has globular repeating units that interact with the fibrilar collagen
    • 113. Has a kink so amino terminus protrudes into ECS
    • 114. Organizes collagen fibers in cartilage
    • 115. Instead of aligned, they criss-cross one another
    • 116. More space = more proteoglycans and water
    • 117. Provides more flexibility to collagen, unlike bone
    • 118. Diseases/Mutations in Collagen
    • 119. Hydroxylated states of proline
    • 120. Scurvy
    • 121. Caused by a deficiency in vitamin C
    • 122. Teeth fall out
    • 123. Joints hurt
    • 124. All types of collagen break down because the deficiency causes a decrease in the ability of the cell to hydroxylate proline
    • 125. Less interaction of collagen and the assembly in the cytoplasm doesn’t take place
    • 126. Teeth not connected
    • 127. Type I mutation
    • 128. Affects bone tissue
    • 129. Osteogenesis Imperfecta
    • 130. Brittle bones
    • 131. Unbreakable movie
    • 132. Type II mutations
    • 133. Cartilage
    • 134. Condro displagia
    • 135. Abnormal joint formation and structure and function due to mutation
    • 136. Abnormal cartilage formation
    • 137. Type III
    • 138. ECM
    • 139. Ailers Danlow Syndrome
    • 140. Fragile skin
    • 141. Disruption in basal lamina
    • 142. Affects blood vessel strength (weak BVs)
    • 143. Hypermobile joints because tendons are very loose
    • 144. Recurrent joint dislocation and swelling
    • 145. Ruptured blood vessels
    • 146. Blister easily
    • 147. Fibronectin
    • 148. Fibrillar macromolecule
    • 149. Secreted by fibroblasts in the connective tissue
    • 150. Made of two polypeptides linked together at COOH terminus by disulfide bonds
    • 151. When secreted, has multiple roles because it has different regions that do different things
    • 152. Fibrin and heparin binding domains
    • 153. Sites where fibronectin molecules is associate with blood clot processes
    • 154. Helps induce reaction to blood clot formation
    • 155. Cell surface receptor binding domain
    • 156. RGD sequence – three amino acids
    • 157. Arginine, glycine, aspartate
    • 158. Important for interacting with cells in ECM
    • 159. Links with integrin receptors specifically in the PM
    • 160. Bind to fibronectin in the ECM
    • 161. If cell is on top of ECM, integrin poke down into ECM and interact with firboncetin at that particular site
    • 162. Collagen binding domain
    • 163. Allows fibronectin to interact with collagen and help organize ECM
    • 164. Interacts on PM with integrin receptors and the FN out in the environment
    • 165. Integrins transduce signals to the inside of the cells and link to the actin cytoskeleton
    • 166. As integrin binds to actin, actin will grow, so integrins help develop the structure of the cell
    • 167. Cells use these cues to move through environment
    • 168. Allows organization of cytoskeleton
    • 169. Allows functioning properly in the tissue types

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