| First Author | Docheva D | Year | 2005 |
| Journal | Mol Cell Biol | Volume | 25 |
| Issue | 2 | Pages | 699-705 |
| PubMed ID | 15632070 | Mgi Jnum | J:96005 |
| Mgi Id | MGI:3528544 | Doi | 10.1128/MCB.25.2.699-705.2005 |
| Citation | Docheva D, et al. (2005) Tenomodulin is necessary for tenocyte proliferation and tendon maturation. Mol Cell Biol 25(2):699-705 |
| abstractText | Tenomodulin (Tnmd) is a member of a new family of type II transmembrane glycoproteins. It is predominantly expressed in tendons, ligaments, and eyes, whereas the only other family member, chondromodulin I (ChM-I), is highly expressed in cartilage and at lower levels in the eye and thymus. The C-terminal extracellular domains of both proteins were shown to modulate endothelial-cell proliferation and tube formation in vitro and in vivo. We analyzed Tnmd function in vivo and provide evidence that Tnmd is processed in vivo and that the proteolytically cleaved C-terminal domain can be found in tendon extracts. Loss of Tnmd expression in gene targeted mice abated tenocyte proliferation and led to a reduced tenocyte density. The deposited amounts of extracellular matrix proteins, including collagen types I, II, III, and VI and decorin, lumican, aggrecan, and matrilin-2, were not affected, but the calibers of collagen fibrils varied significantly and exhibited increased maximal diameters. Tnmd-deficient mice did not have changes in tendon vessel density, and mice lacking both Tnmd and ChM-I had normal retinal vascularization and neovascularization after oxygen-induced retinopathy. These results suggest that Tnmd is a regulator of tenocyte proliferation and is involved in collagen fibril maturation but do not confirm an in vivo involvement of Tnmd in angiogenesis. |
