CSB327H1 Lecture Notes - Lecture 10: Decorin, Disulfide, Bone Density
16 Nov 2012
School
Department
Course
Professor
Document Summary
Structure: cs/ds binding domain (n-terminal, disulfide loop with c-c disulfide bridge. Inhibitory effect on collagen fibrillogenesis: 10 leucine-rich repeats (lrr) High-affinity collagen binding site: disulfide loop with c-c disulfide bridge (c-terminal) Role in collagen fibril formation: a single collagen triple helix at the c-terminus fits in the arch-shaped structure of decorin, the lrrs are high affinity collagen binding sites, decorin-wt. Collagen fibrils are uniform in size and regularly spaced: decorin-null. Collagen fibrils are different sizes and unevenly spaced. Similar to eds: decorin controls the rate of collagen fibrillogenesis by h-bonding. Core protein regulates the size of the collagen fibrils. Cs-gags regulates the spacing of collagen fibrils. Role in tgf- signaling: tgf- signaling (fibrosis excessive ecm deposition) Characterized by increased ecm components (fn, collagens, sparc, opn, etc. : decorin binds and inhibits tgf- signaling. No decorin treatment: fibrosis in kidney leads to renal failure. Role in atherogenesis: ds form is present in arteries, skin and lungs, cs form is present in cartilage.
