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Publication : Structural variation of type XII collagen at its carboxyl-terminal NC1 domain generated by tissue-specific alternative splicing.

First Author  Kania AM Year  1999
Journal  J Biol Chem Volume  274
Issue  31 Pages  22053-9
PubMed ID  10419532 Mgi Jnum  J:56517
Mgi Id  MGI:1341490 Doi  10.1074/jbc.274.31.22053
Citation  Kania AM, et al. (1999) Structural variation of type XII collagen at its carboxyl-terminal NC1 domain generated by tissue-specific alternative splicing. J Biol Chem 274(31):22053-9
abstractText  This paper reports the identification of two structural variations in the NC1 domain of rat and mouse type XII collagen. The long NC1 domain encoding 74 amino acids showed homology to chicken type XII and XIV collagens. The short NC1 domain was composed of 19 amino acids. Through genomic DNA analyses, two alternative exons were identified, each of which contained the variable NC1 sequence. With the amino-terminal NC3 splicing alternatives, we propose here a new descriptive nomenclature: types XIIA-1 and XIIB-1 which include a long NC1 sequence encoded by exon 1 (from the 3'-end), and types XIIA-2 and XIIB-2 which include a short NC1 sequence encoded by exon 2. Types XIIA-1 and XIIB-1, the predominant transcripts in 15-day old mouse embryos, showed decreased expression in 17-day old embryos when type XIIB-2 expression was sustained at constant levels. In adult mice, type XIIB-1 associates with ligament and tendon, whereas type XIIB-2 is expressed in various other tissues. The long NC1 domain contains an extended acidic region (pI = 3.4) followed by a terminal basic region (pI = 13.8). Because the short NC1 domain lacks these features, structural variations in the type XII collagen NC1 domain suggests different functional roles in a tissue-specific fashion.
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