Journal of Biological Chemistry
Volume 270, Issue 5, 3 February 1995, Pages 2372-2378
Journal home page for Journal of Biological Chemistry

Nucleic Acids, Protein Synthesis, and Molecular Genetics
Differential Expression of an Acidic Domain in the Amino-terminal Propeptide of Mouse Pro-
2(XI) Collagen by Complex Alternative Splicing (∗)

https://doi.org/10.1074/jbc.270.5.2372Get rights and content
Under a Creative Commons license
open access

We isolated and sequenced genomic and cDNA clones encoding the complete amino-terminal portion and the 5′-untranslated region of mouse pro-α2(XI) collagen mRNA. Fourteen exons encoded the amino-terminal propeptide, which was divided into three consecutive domains (a long globular domain, an amino-terminal triple helical domain, and a telopeptide domain). The long globular domain was further divided into an upstream basic subdomain and a downstream highly acidic subdomain, as is the case for the amino-terminal propeptides of pro-α1(V) and pro-α1(XI) collagens. We also demonstrated that the primary transcript undergoes complex alternative splicing. Three consecutive exons (exons 6, 7, and 8) encoding most of the acidic subdomain showed alternative splicing which dramatically affected the structure of the amino-terminal propeptide of pro-α2(XI) collagen. Using the reverse transcription-polymerase chain reaction, we analyzed the expression of these exons in various tissues and in developing limb buds of mice. The pro-α2(XI) transcripts were abundant in cartilage, but most of them lacked the 3-exon sequences encoding the acidic domain. Most of other tissues also contained mRNAs that corresponded to longer splice variants, including exons 6-8. The differential expression of specific domains of pro-α2(XI) collagen may be important in modulating interactions between various components of the extracellular matrix and/or may influence heterotypic collagen assembly.

Cited by (0)

This work was supported in part by Scientific Research Grant 06454428 from the Ministry of Education, Science and Culture of Japan. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore by hereby marked “advertisement” in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBank™/EMBL Data Bank with accession number(s) D38412.