Mild impairment of motor nerve repair in mice lacking PTP-BL tyrosine phosphatase activity

作者：Derick G. Wansink, Wilma Peters, Iris Schaafsma, Roger P.M. Sutmuller, Frank Oerlemans, Gosse J. Adema, Bé Wieringa, Catharina E.E.M. Van der Zee, Wiljan Hendriks · 发表于：Physiological Genomics · 年份：2004 · DOI：10.1152/physiolgenomics.00079.2004 · 被引用次数：40 · 研究领域：Protein Tyrosine Phosphatases、Galectins and Cancer Biology、PI3K/AKT/mTOR signaling in cancer

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.