| Literature DB >> 15226483 |
Derick G Wansink1, Wilma Peters, Iris Schaafsma, Roger P M Sutmuller, Frank Oerlemans, Gosse J Adema, Bé Wieringa, Catharina E E M van der Zee, Wiljan Hendriks.
Abstract
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.Entities:
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Year: 2004 PMID: 15226483 DOI: 10.1152/physiolgenomics.00079.2004
Source DB: PubMed Journal: Physiol Genomics ISSN: 1094-8341 Impact factor: 3.107