Primary structure of the long and short splice variants of mouse collagen XII and their tissue-specific expression during embryonic development

Developmental Dynamics : an Official Publication of the American Association of Anatomists
K BöhmeB R Olsen

Abstract

Type XII collagen, a member of the FACIT group of extracellular matrix proteins, consists of molecules that are trimers of alpha 1(XII) chains. The three chains in each molecule form a cross-shaped structure with a central globule from which a triple-helical tail and three finger-like regions (containing von Willebrand factor A-like regions (containing von Willebrand factor A-like domains and fibronectin type III repeats) extend. cDNA cloning/sequencing of chicken alpha 1(XII) collagen and protein studies with mouse, bovine, and human material suggest that the alpha 1(XII) collagen gene gives rise to two molecular variants, differing in the length of the finger-like regions, by alternative splicing of the primary transcript. To provide a basis for studies of the function of the two variants in an organism that can be genetically manipulated, we have isolated and sequenced mouse cDNAs encoding both splice variants. The sequence provides the first complete nucleotide and amino acid sequence of mammalian type XII collagen. From these cDNAs we have generated digoxigenin-labeled RNA probes for in situ hybridization of developing mouse embryos to find out whether the splicing mechanism responsible for generation of the two forms is d...Continue Reading

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