Isolation and sequence of a novel human chondrocyte protein related to mammalian members of the chitinase protein family

被引:171
作者
Hu, B [1 ]
Trinh, K [1 ]
Figueira, WF [1 ]
Price, PA [1 ]
机构
[1] UNIV CALIF SAN DIEGO,DEPT BIOL,LA JOLLA,CA 92093
关键词
D O I
10.1074/jbc.271.32.19415
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
We describe the isolation of a novel protein from the conditioned medium of human articular cartilage chondrocytes in primary culture, This 39-kDa protein has the N-terminal sequence YKL, which we have termed YKL-39, The 1434-nucleotide sequence of the YKL-39 cDNA predicts a 385-residue initial translation product and a 364-residue mature YKL-39, The amino acid sequence of YKL-39 is most closely related to YKL-40, followed by macrophage chitotriosidase, oviductal glycoprotein, and macrophage YM-1, All five proteins share significant sequence identity with bacterial chitinases and have the probable structure of an (alpha beta)(8) barrel, YKL-39 lacks the active site glutamate, which is essential for the activity of chitinases, and as expected has no chitinase activity, The highest level of YKL-39 mRNA expression is seen in chondrocytes, followed by synoviocytes, lung, and heart, YKL-39 accounts for 4% of the protein in chondrocyte-conditioned medium, prostromelysin accounts for 17%, and YKL-40 accounts for 33%, In contrast to YKL-40, YRL-39 is not a glycoprotein and does not bind to heparin.
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页码:19415 / 19420
页数:6
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