| First Author | Wansink DG | Year | 2004 |
| Journal | Physiol Genomics | Volume | 19 |
| Issue | 1 | Pages | 50-60 |
| PubMed ID | 15226483 | Mgi Jnum | J:92590 |
| Mgi Id | MGI:3054107 | Doi | 10.1152/physiolgenomics.00079.2004 |
| Citation | Wansink DG, et al. (2004) Mild impairment of motor nerve repair in mice lacking PTP-BL tyrosine phosphatase activity. Physiol Genomics 19(1):50-60 |
| abstractText | Mouse PTP-BL is a large, nontransmembrane protein tyrosine phosphatase of unclear physiological function that consists of a KIND domain, a FERM domain, five PDZ domains, and a COOH-terminal catalytic PTP domain. PTP-BL and its human ortholog PTP-BAS have been proposed to play a role in the regulation of microfilament dynamics, cytokinesis, apoptosis, and neurite outgrowth. To investigate the biological function of PTP-BL enzyme activity, we have generated mice that lack the PTP-BL PTP moiety. These PTP-BL(DeltaP/DeltaP) mice are viable and fertile and do not present overt morphological alterations. Although PTP-BL is expressed in most hematopoietic cell lineages, no alterations of thymocyte development in PTP-BL(DeltaP/DeltaP) mice could be detected. Sciatic nerve lesioning revealed that sensory nerve recovery is unaltered in these mice. In contrast, a very mild but significant impairment of motor nerve repair was observed. Our findings exclude an essential role for PTP-BL as a phosphotyrosine phosphatase and rather are in line with a role as scaffolding or anchoring molecule. |
