Macromolecules of extracellular matrix: determination of selective structures and their functional significance.
In this brief review, I recount events and scientific endeavors in which I have been privileged to participate. The descriptive information includes discovery and characterization of hydroxylysine glycosides from collagen, isolation of dentin sialoprotein (DSP), investigations on dentin phosphoprotein (DPP), and the discovery of a single gene for both DSP and DPP that requires posttranslational proteolytic cleavage of the parent DSPP molecule to generate the two fragments. Finally, I address our unexpected finding of fragments of DMP1 in bone extracts. These fragments are from the NH2-terminal (37 kDa) and COOH-terminal (57 kDa) regions of DMP1. Our studies showed that, similar to DSPP, DMP1 is proteolytically processed by cleavages at X-Asp bonds.
Butler
William T
WT
Dental Branch, University of Texas Health Science Center, Houston, Texas, USA. wbutler@bcd.tamhsc.edu
D000818:Animals; D001842:Bone and Bones / Q000737:chemistry; D003804:Dentin / Q000737:chemistry; D016326:Extracellular Matrix Proteins / Q000737:chemistry / Q000266:history* / Q000378:metabolism; D049673:History, 20th Century; D049674:History, 21st Century; D006801:Humans; D006901:Hydroxylysine / Q000031:analogs & derivatives* / Q000737:chemistry / Q000266:history / Q000378:metabolism
D016326:Extracellular Matrix Proteins; C022819:hydroxylysine glycoside; D006901:Hydroxylysine