The Journal of Biochemistry
Online ISSN : 1756-2651
Print ISSN : 0021-924X
Molecular Cloning and Partial Characterization of a Novel Collagen Chain, α1(XVI), Consisting of Repetitive Collagenous Domains and Cysteine-Containing Non-Collagenous Segments
Noriko YamaguchiShioko KimuraO. Wesley McBrideHisae HoriYoshihiko YamadaTetsuko KanamoriHiroaki YamakoshiYutaka Nagai
Author information
JOURNAL FREE ACCESS

1992 Volume 112 Issue 6 Pages 856-863

Details
Abstract

In an effort to identify new members of the collagen family, we screened a human placenta cDNA library with a collagenous probe. A novel 3.7 kb cDNA was identified encoding an open reading frame of 1, 186 amino acids and containing a termination codon. The predicted polypeptide consists of 9 repetitive collagenous (stretches of Gly-X-Y) and several noncollagenous segments. Two cysteinyl residues separated by two amino acid residues (Cys-X-X-Cys) are regularly located in the N-terminal region of each non-collagenous segment. The deduced amino acid sequence described above is distinct from those of known types of collagen. Therefore, this novel collagen chain is designated α1(XVI). Northern blot analysis revealed an α1(XVI) mRNA of 5.2 kb, indicating that the overlapping cDNA clones isolated in this study covered nearly three-fourths of the mRNA. As a tool for further study on the expression of type XVI collagen, we prepared an antibody against the nonadecapeptide CFLSLERPRAEEARGDNSE, derived from the putative translation product of the cDNA. In immunoblot analysis, the antibody recognized a 160 kDa protein, which was bacterial collagenase-sensitive. Immunohistochemical stainings of human placental tissues with anti-peptide antibody revealed a positive reaction with amnion, the membranous tissue lining the amniotic cavity. The gene of α1(XVI) chain, COL16A1, is mapped on the short arm of human chromosome 1 (1p13-p34).

Content from these authors
© The Japanese Biochemical Society
Previous article
feedback
Top