4.14.2010

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4.14.2010

  1. 1. 4.14.2010<br /><ul><li>Mistakes from Last lecture
  2. 2. Parapoptosis
  3. 3. Apaf-1 independent as well as cytochrome c
  4. 4. Does not activate caspase 9 via apaf-1
  5. 5. It activates an alternative caspase
  6. 6. ECM
  7. 7. Muscle
  8. 8. Nervous
  9. 9. Connective
  10. 10. types
  11. 11. Bone
  12. 12. Cells secrete ECM
  13. 13. Osteocytes
  14. 14. Mature cells of this cell type
  15. 15. Osteoblast – secretes ECM of molecules
  16. 16. Cartilage
  17. 17. Chrondrocytes
  18. 18. Mature cells of this cell type
  19. 19. Chrondroblasts
  20. 20. Secrete ECM of Cartilage
  21. 21. Loose connective tissue (under epithelium)
  22. 22. Blood
  23. 23. Lymphoid tissue
  24. 24. More ECM than cells
  25. 25. Epithelial Tissue more ECM than cells
  26. 26. Independent of connective tissue
  27. 27. Made of epithelial cells
  28. 28. Attach to basil lamina
  29. 29. Fibroblasts
  30. 30. Loose connective tissue
  31. 31. Skin
  32. 32. Epithelial cells
  33. 33. Linked by tight junctions to integrins
  34. 34. Underneath is loose connective tissue that proveide tensile strength
  35. 35. ECM of Loose connective Tissue
  36. 36. Proteoglycans
  37. 37. Made up of a core protein linked to many negatively charged polysaccharides that have a particular structure
  38. 38. This structure characterizes them as GAGS – glycosoaminoglycans
  39. 39. Negative charges attracts water
  40. 40. Now the ECM has a fluid-like component to it.
  41. 41. Presence of proteoglycans will determine how fluid the ECM is (bones don’t have much)
  42. 42. Fibrillar
  43. 43. Types
  44. 44. Collagen
  45. 45. Fibronectin
  46. 46. Elastin
  47. 47. Provides
  48. 48. Strength
  49. 49. Attachment sites for cell receptors
  50. 50. Collagen
  51. 51. Characterized by alpha subunit
  52. 52. Can combine in different ways to produce the different collagens
  53. 53. Synthesis of Collagen
  54. 54. Occurs in the ER lumen
  55. 55. Contain
  56. 56. Prolin
  57. 57. Heavily hydroxylated – form H bonds as single alpha chains come to form a triple helix between hydroxylated prolin
  58. 58. Hydroxylated lysine are also involved
  59. 59. Scurvy
  60. 60. Decrease in hydroxylated proline levels
  61. 61. Lack of vitamin c
  62. 62. Helps hydroxlate prolin
  63. 63. Glycine
  64. 64. Smallest amino acid
  65. 65. Every 3rd amino acid in a collagen chain is a glycine
  66. 66. Allows close interaction of chains to favor the formation of hydrogen bonds
  67. 67. Forms a fibril, about 270, are aligned so they overlap in a region ~ 67nm wide
  68. 68. Once fibrils assemble into a fiber, they are striated in form because of how the collagen molecule is offset. This allows tensile strength. This is a phenotype of the collagen and why it has a strong tensile strength
  69. 69. Type-1 Collagen
  70. 70. Tendons
  71. 71. Cornea of eye
  72. 72. ~95% of collagen in body
  73. 73. Type-1 fiber
  74. 74. Interaction between type 1 and type 4 allows a molecule that is rigid and flexible.
  75. 75. Mutations in Type-1
  76. 76. Usually heavily localized in bons
  77. 77. Osteogenesis imperfecta
  78. 78. Genetic, makes bones brittle.
  79. 79. Mutaions in Type-II
  80. 80. Chondrodisplasiaa
  81. 81. This collagen is heavily found in cartilage
  82. 82. Mutations in Type-III Collagen
  83. 83. Ehler-Danlos syndrome
  84. 84. Attachment of blood vessels and joints
  85. 85. Skin is fragile
  86. 86. Joints are hypermobile, blistering, skin rupturing.
  87. 87. Type-II Fibril Structure
  88. 88. Tye-II fibril
  89. 89. Associates with type-IX with flexible kinks
  90. 90. As It assembles, primarily in cartilage, n terminus stick out, so the space generated organizes collagen so it crisscrosses, and inbetween are proteoglycans, creates gel liked structure of cartilage
  91. 91. Proline
  92. 92. Disease
  93. 93. Rheumatoid Arthritis
  94. 94. Immune system attacks collagen
  95. 95. Normally collagen is not immunogenic
  96. 96. Fibronectin
  97. 97. Secreted by fibroblasts
  98. 98. Important roles out in the connective tissue to help organize connective tissue
  99. 99. Made of two large polypeptides
  100. 100. At COOH terminus, linked by di sulfide bonds to hold the polypeptides together
  101. 101. Binding sites on fibronetin
  102. 102. Blood clotting
  103. 103. Fibrin binding domain
  104. 104. Heparin
  105. 105. Arginine, glycine, asartate – form RGD sequence
  106. 106. Used for integrin receptors
  107. 107. Collagen Binding Domain
  108. 108. Heparin and fibrin
  109. 109. Integrins nteractct with fibronectin in connective tissue
  110. 110. Proteoglycans and Glycosaminoglycans
  111. 111. Chrondroitin Sulfate
  112. 112. Keratin Sulfate
  113. 113. Hyalurnoate
  114. 114. Don’t memorize the combinations of sugars, just know that there are different combinations of sugars to make different compounds.
  115. 115. Aggrecan
  116. 116. Core protein is heavily concentrated with hyalurnate
  117. 117. Proteoglycans stick of hyal molecule
  118. 118. Hyal organizes the prot glycs
  119. 119. Found in cartilage
  120. 120. Integrins
  121. 121. Alpha and beta chain
  122. 122. Can vary
  123. 123. Which can yield a specific function for that integrin
  124. 124. A7b1 – muscular distrophy

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