CSB327H1 Lecture Notes - Lecture 3: Triple Helix, Oxidative Deamination, Collagenase
21 Oct 2013
School
Department
Course
Professor
Document Summary
Lecture 3 supramolecular assembly and cross-linking of t1c molecules, dematosparaxis. Side by side interactions bw collagen molecules is stabilized by aldol cross-linkages bw two lysine side chains. Lysyl oxidase is dysregulated in tissue fibrosis, especially in cancer: oxidation of lysine side chains can lead to spontaneous formation of hydroxylysyl pyridinoline and lysyl pyridinoline cross-links. Inherently stable with lifetimes of 6+ months: triple helices are resistant to most proteases hence turnover is accomplished by matrix remodelling metalloproteines (mmps) Collagenases type of mmp that can break down collagen fibres, most mmps cannot see cleavage sites well until collagenases cleave collagen fibres 1st. Dermatosparaxis disease: failure to remove n-terminal prodomain of t1c; dd=eds. Signature collagen of cartilage = t2c, and adamts-3, if adamts-2 is mutated, cartilage will not be effected: no cleavage of c-terminus = end of game, bc alpha chains wouldn"t know who to assemble /w.
