| First Author | Mohlke KL | Year | 1999 |
| Journal | Cell | Volume | 96 |
| Issue | 1 | Pages | 111-20 |
| PubMed ID | 9989502 | Mgi Jnum | J:52069 |
| Mgi Id | MGI:1327771 | Doi | 10.1016/s0092-8674(00)80964-2 |
| Citation | Mohlke KL, et al. (1999) Mvwf, a dominant modifier of murine von Willebrand factor, results from altered lineage-specific expression of a glycosyltransferase. Cell 96(1):111-20 |
| abstractText | We have identified altered lineage-specific expression of an N-acetylgalactosaminyltransferase gene, Galgt2, as the gain-of-function mechanism responsible for the action of the Mvwf locus, a major modifier of plasma von Willebrand factor (VWF) level in RIIIS/J mice. A switch of Galgt2 gene expression from intestinal epithelial cell-specific to a pattern restricted to the vascular endothelial cell bed leads to aberrant posttranslational modification and rapid clearance of WVF from plasma. Transgenic expression of Galgt2 directed to vascular endothelial cells reproduces the low VWF phenotype, confirming this switch in lineage-specific gene expression as the likely molecular mechanism for Mvwf. These findings identify alterations in glycosyltransferase function as a potential general mechanism for the genetic modification of plasma protein levels. |
