| First Author | Sumoza-Toledo A | Year | 2006 |
| Journal | Exp Cell Res | Volume | 312 |
| Issue | 17 | Pages | 3312-22 |
| PubMed ID | 16919270 | Mgi Jnum | J:114379 |
| Mgi Id | MGI:3688936 | Doi | 10.1016/j.yexcr.2006.07.002 |
| Citation | Sumoza-Toledo A, et al. (2006) Differential localization of unconventional myosin I and nonmuscle myosin II during B cell spreading. Exp Cell Res 312(17):3312-22 |
| abstractText | Cross-linking of CD44 in vitro promotes chemokinesis and actin-based dendrite formation in T and B cells. However, the mechanisms by which the adhesion molecule CD44 induces cytoskeleton activation in lymphocytes are still poorly understood. In this study, we have investigated whether myosin isoforms are involved in CD44-dependent dendrite formation in activated B cells. Pharmacological inhibition of myosin with 2,3-butanedione monoxime strongly affected spreading and dendrite formation, suggesting that these cellular motors may participate in these phenomena. Furthermore, immunofluorescence analysis showed differences in subcellular localization of class I and class II myosin during B cell spreading. In response to CD44 cross-linking, myosin-1c was polarized to lamellipodia, where F-actin was high. In contrast, the distribution of cytosplasmic nonmuscle class II myosin was not altered. Expressions of myosin-1c and II were also demonstrated in B cells by Western blot. Although the inhibition of PLCgamma, PI3K and MEK-1 activation affected the spreading and dendrite formation in activated B cells, only PLCgamma and MEK-1 inhibition correlated with absence of myosin-1c polarization. Additionally, myosin-1c polarization was observed upon cross-linking of other surface molecules, suggesting a common mechanism for B cell spreading. This work shows that class I and class II myosin are expressed in B cells, are differentially distributed, and may participate in the morphological changes of these cells. |
