| First Author | Kappler J | Year | 2002 |
| Journal | Biochem Biophys Res Commun | Volume | 294 |
| Issue | 3 | Pages | 742-7 |
| PubMed ID | 12056833 | Mgi Jnum | J:77241 |
| Mgi Id | MGI:2181238 | Doi | 10.1016/S0006-291X(02)00520-X |
| Citation | Kappler J, et al. (2002) Tenascins are associated with lipid rafts isolated from mouse brain. Biochem Biophys Res Commun 294(3):742-7 |
| abstractText | Lipid rafts are microdomains of the plasma membrane which are enriched in glycosphingolipids and specific proteins. The reported interactions of several raft-associated proteins (such as, e.g., F3) with tenascin C and tenascin R prompted us to consider that these oligomeric multidomain glycoproteins of the extracellular matrix (ECM) could associate with rafts. Here, we show punctate immunocytochemical distributions of tenascin C (TN-C) and tenascin R (TN-R) at the membrane surface of neural cells resembling the pattern reported for raft-associated proteins. Moreover, cholesterol depletion with methyl-beta-cyclodextrin reduced the punctate surface staining of TN-C. Consistently, TN-C was associated with lipid rafts of neonatal mouse brain according to sucrose density gradient centrifugation experiments. Furthermore, TN-R was also found in rafts prepared from myelin of adult mice. Thus, brain-derived tenascins are able to associate with lipid rafts. |
