Intra- and extracellular enzymes of collagen biosynthesis as biological and chemical targets in the control of fibrosis.
The several steps in the pathway for the biosynthesis of fibrillar collagen are reviewed to illustrate potential sites for the chemotherapeutic control of fibrosis. Particular emphasis is placed upon the properties and inhibition of lysyl oxidase, the enzyme which initiates the covalent crosslinking of extracellular collagen molecules converting these to insoluble fibers, and upon the properties and inhibition of prolyl hydroxylase, the intracellular enzyme which hyroxylates proline residues within collagen.
Kagan
H M
HM
Department of Biochemistry, Boston University School of Medicine, Boston, MA 02174, USA. kagan@med-biochem.bu.edu
D000629:Aminopropionitrile / Q000494:pharmacology; D000818:Animals; D001596:Benzylamines / Q000494:pharmacology; D002478:Cells, Cultured; D003094:Collagen / Q000096:biosynthesis* / Q000235:genetics; D004791:Enzyme Inhibitors / Q000494:pharmacology*; D004952:Esters / Q000494:pharmacology; D005021:Ethylamines / Q000494:pharmacology; D005355:Fibrosis / Q000517:prevention & control; D006801:Humans; D007783:Lactones / Q000494:pharmacology; D011393:Procollagen-Proline Dioxygenase / Q000037:antagonists & inhibitors* / Q000378:metabolism; D008249:Protein-Lysine 6-Oxidase / Q000037:antagonists & inhibitors* / Q000378:metabolism
D001596:Benzylamines; D004791:Enzyme Inhibitors; D004952:Esters; D005021:Ethylamines; D007783:Lactones; C004504:2-bromoethylamine; D000629:Aminopropionitrile; D003094:Collagen; D011393:Procollagen-Proline Dioxygenase; D008249:Protein-Lysine 6-Oxidase