Macromolecules of Extracellular Matrix: Determination of Selective Structures and Their Functional Significance

被引:6
|
作者
Butler, William T. [1 ,2 ]
机构
[1] Univ Texas Hlth Sci Ctr, Dent Branch, Houston, TX USA
[2] Baylor Coll Dent, Dallas, TX 75246 USA
基金
美国国家卫生研究院;
关键词
D O I
10.1080/03008200802471864
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
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 DMPI-in bone extracts. These fragments are from the NH2-terminal (37 kDa) and COON-terminal (57 kDa) regions of DMPI. Our studies showed that, similar to DSPP, DMPI is proteolytically processed-by cleavages at X-Asp bonds.
引用
收藏
页码:383 / 390
页数:8
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