| First Author | Mazaki Y | Year | 1998 |
| Journal | J Biol Chem | Volume | 273 |
| Issue | 35 | Pages | 22435-41 |
| PubMed ID | 9712867 | Mgi Jnum | J:49586 |
| Mgi Id | MGI:1277726 | Doi | 10.1074/jbc.273.35.22435 |
| Citation | Mazaki Y, et al. (1998) Paxillin isoforms in mouse. Lack of the gamma isoform and developmentally specific beta isoform expression. J Biol Chem 273(35):22435-41 |
| abstractText | Paxillin, a focal adhesion protein, exists as multiple isoforms in humans (alpha, beta, and gamma). To understand more about the physiological role of each isoform, we have employed the mouse system. We found that although the alpha and beta isoforms are present in the mouse, the gamma isoform is not. The alpha isoform protein was detected clearly in most adult tissues, whereas the beta isoform protein was almost undetectable except in spleen, testis, thymus, and lung. On the other hand, mRNAs of both isoforms were detectable in all tissues we examined. High levels of the beta isoform protein was detected in peritoneal exudate macrophage cells in adult mouse as well as in cultured fibroblasts, together with the alpha isoform. The alpha isoform was expressed at a constant level throughout the embryonic stages we examined, whereas the beta isoform protein was detected at the mid-stages of development and increased to levels almost equal to those of the alpha isoform during the late stages of embryogenesis. Therefore, unlike the alpha isoform, expression of the beta isoform protein is restricted in adult tissues. Moreover, we showed that alpha and beta isoforms were colocalized within the same focal adhesion plaques, and cytoplasmic pools of both isoforms exist in the perinuclear area, colocalized with the Golgi apparatus. |
