| First Author | Yamana K | Year | 2001 |
| Journal | Biochem Biophys Res Commun | Volume | 280 |
| Issue | 4 | Pages | 1101-6 |
| PubMed ID | 11162640 | Mgi Jnum | J:67301 |
| Mgi Id | MGI:1930358 | Doi | 10.1006/bbrc.2000.4245 |
| Citation | Yamana K, et al. (2001) Molecular cloning and characterization of CHM1L, a novel membrane molecule similar to chondromodulin-I. Biochem Biophys Res Commun 280(4):1101-6 |
| abstractText | Chondromodulin-I (ChM-I) is a cartilage-specific glycoprotein that stimulates the growth of chondrocytes and inhibits the tube formation of endothelial cells. In the present study, we identified a novel ChM-I like molecule, designated ChM1L. Cloning of full length cDNAs of human, mouse, and rat ChM1L revealed that ChM1L encodes 317 amino acids novel type II transmembrane protein. ChM1L protein was expressed on the cell surface as N-glycosylated and non-N-glycosylated protein with molecular mass of 45 and 40 kDa, respectively. In adult mouse tissues, ChM1L mRNA was highly expressed in eye, skeletal muscle, and whole rib. The temporal pattern of ChM1L mRNA was examined using whole embryo at day 10 to 19 of gestation. After day 11, ChM1L mRNA was detected and its level was progressively elevated in association with development of mouse embryo. These data suggest that ChM1L is a novel membrane molecule which is similar to ChM-I that plays a regulatory role in eye, skeletal muscle, and development of embryo. Copyright 2001 Academic Press. |
