Molecular cloning and characterization of a novel gene, CORS26, encoding a putative secretory protein and its possible involvement in skeletal development

Abstract

We cloned a novel mouse cDNA, CORS26 (collagenous repeat-containing sequence of 26-kDa protein), encoding a secretory protein by suppression subtractive hybridization between transforming growth factor-beta1-treated and untreated C3H10T1/2 cells. The deduced amino acid sequence of CORS26 consists of 246 amino acids with a secretory signal peptide and contains a collagenous region (Gly-X-Y repeats) at the NH(2) terminus and a complement factor C1q globular domain at the COOH terminus. CORS26 is structurally similar to C1q and to adipocyte-specific protein Acrp30. Transfection analysis suggested that CORS26 is a secretory protein. Northern blot analysis revealed that CORS26 mRNA was present at high levels in rib growth plate cartilage and at moderate levels in kidney of adult mice. CORS26 mRNA was not detected in NIH3T3 cells, BALB/3T3 cells, C3H10T1/2 cells, or osteoblastic MC3T3-E1 cells by reverse transcription-polymerase chain reaction analysis. In situ hybridization of mouse embryos between 13 and 15 days postcoitus revealed relatively high levels of CORS26 mRNA in condensed prechondrocytic cells of cartilage primordia and developing cartilages. However, CORS26 mRNA were undetectable in mature chondrocytes. Furthermore, overexpression of CORS26 enhanced the growth of C3H10T1/2 cells in vitro. The present findings suggest that the CORS26 gene may play an important role in skeletal development.