| First Author | Gara SK | Year | 2011 |
| Journal | Matrix Biol | Volume | 30 |
| Issue | 4 | Pages | 248-57 |
| PubMed ID | 21477648 | Mgi Jnum | J:173953 |
| Mgi Id | MGI:5050592 | Doi | 10.1016/j.matbio.2011.03.006 |
| Citation | Gara SK, et al. (2011) Differential and restricted expression of novel collagen VI chains in mouse. Matrix Biol 30(4):248-57 |
| abstractText | Recently, three novel collagen VI chains, alpha4, alpha5 and alpha6, were identified. These are thought to substitute for the collagen VI alpha3 chain, probably forming alpha1alpha2alpha4, alpha1alpha2alpha5 or alpha1alpha2alpha6 heterotrimers. The expression pattern of the novel chains is so far largely unknown. In the present study, we compared the tissue distribution of the novel collagen VI chains in mouse with that of the alpha3 chain by immunohistochemistry, immunoelectron microscopy and immunoblots. In contrast to the widely expressed alpha3 chain, the novel chains show a highly differential, restricted and often complementary expression. The alpha4 chain is strongly expressed in the intestinal smooth muscle, surrounding the follicles in ovary, and in testis. The alpha5 chain is present in perimysium and at the neuromuscular junctions in skeletal muscle, in skin, in the kidney glomerulus, in the interfollicular stroma in ovary and in the tunica albuginea of testis. The alpha6 chain is most abundant in the endomysium and perimysium of skeletal muscle and in myocard. Immunoelectron microscopy of skeletal muscle localized the alpha6 chain to the reticular lamina of muscle fibers. The highly differential and restricted expression points to the possibility of tissue-specific roles of the novel chains in collagen VI assembly and function. |
