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Ca 2+ binding properties of type X collagen
Author(s) -
Kirsch Thorsten,
von der Mark Klaus
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)81363-d
Subject(s) - calcification , collagen, type i, alpha 1 , cartilage , type i collagen , type ii collagen , chemistry , calcium , fetus , dissociation constant , biophysics , microbiology and biotechnology , endocrinology , anatomy , biochemistry , medicine , extracellular matrix , biology , pregnancy , genetics , receptor , organic chemistry
Type X collagen is a developmentally regulated collagen that is only synthesized by chondrocytes of the hypertrophic and calcifying zone in fetal cartilage. There is evidence in the literature that type X collagen may be involved in cartilage calcification. Here we show that type X collagen synthesis precedes calcium deposition in nodules of fetal human chondrocytes forming in cell culture and present evidence that type X collagen binds calcium in a specific and dose dependent manner. In an assay using bovine type X collagen coupled to beads and 45 Ca 2+ we determined a total of about 15 binding sites per α1(X) chain with a dissociation constant of 32 μM.