Cloning of mouse type XV collagen sequences and mapping of the corresponding gene to 4B1-3: Comparison of mouse and human α1(XV) collagen sequences indicates divergence in the number of small collagenous domains

Abstract

We report on full-length mouse type XV collagen cDNAs that encode a 1367-residue α1(XV) chain. The amino acid sequences of the mouse and previously characterized human α1(XV) chains exhibit an overall identity of 72%. The highest homology between these chains and to the structurally related type XVIII collagen is observed in their C-terminal noncollagenous domains. Although the mouse and human α1(XV) chains are highly homologous and similar in their overall domain structure, the mouse chain contains only seven collagenous domains, whereas the human chain contains nine. Northern analysis of several mouse tissues indicated strong hybridization in the case of heart and skeletal muscle RNAs and moderate signals with kidney, lung, and testis RNAs. Analysis of type XV collagen mRNA levels at different stages of mouse embryonic development indicated a marked increase in the level between 11 and 15 days of development, which coincides with pronounced development of the muscles, heart, and vascular system in the mouse embryo. The mouse gene for type XV collagen was mapped by fluorescence in situ hybridization to chromosome 4, band B1-3. This result indicates that the mouse type XV collagen gene and its human counterpart are located in the chromosomal segments with conserved syntenies.