| First Author | Nagata T | Year | 2014 |
| Journal | Biochem Biophys Res Commun | Volume | 443 |
| Issue | 2 | Pages | 351-6 |
| PubMed ID | 24246674 | Mgi Jnum | J:211491 |
| Mgi Id | MGI:5575581 | Doi | 10.1016/j.bbrc.2013.11.029 |
| Citation | Nagata T, et al. (2014) Hepatocyte growth factor regulated tyrosine kinase substrate in the peripheral development and function of B-cells. Biochem Biophys Res Commun 443(2):351-6 |
| abstractText | Hepatocyte growth factor (HGF)-regulated tyrosine kinase substrate (Hrs) is a vesicular sorting protein that functions as one of the endosomal-sorting proteins required for transport (ESCRT). Hrs, which binds to ubiquitinated proteins through its ubiquitin-interacting motif (UIM), contributes to the lysosomal transport and degradation of ubiquitinated membrane proteins. However, little is known about the relationship between B-cell functions and ESCRT proteins in vivo. Here we examined the immunological roles of Hrs in B-cell development and functions using B-cell-specific Hrs-deficient (Hrs(flox/flox);mb1(cre/)(+):Hrs-cKO) mice, which were generated using a cre-LoxP recombination system. Hrs deficiency in B-cells significantly reduced T-cell-dependent antibody production in vivo and impaired the proliferation of B-cells treated in vitro with an anti-IgM monoclonal antibody but not with LPS. Although early development of B-cells in the bone marrow was normal in Hrs-cKO mice, there was a significant decrease in the number of the peripheral transitional B-cells and marginal zone B-cells in the spleen of Hrs-cKO mice. These results indicate that Hrs plays important roles during peripheral development and physiological functions of B lymphocytes. |
