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Physiol. Genomics (June 29, 2004). doi:10.1152/physiolgenomics.00079.2004
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Submitted on April 1, 2004
Accepted on June 24, 2004

Mild Impairment of Motor Nerve Repair in Mice Lacking PTP-BL Tyrosine Phosphatase Activity

Derick G Wansink1, Wilma Peters1, Iris Schaafsma1, Roger P. M Sutmuller2, Frank Oerlemans1, Gosse J Adema2, Be Wieringa1, Catharina E. E. M van der Zee1, and Wiljan Hendriks1*

1 Department of Cell Biology, Nijmegen Center for Molecular Life Sciences, University Medical Center Nijmegen, Nijmegen, The Netherlands
2 Department of Tumor Immunology, Nijmegen Center for Molecular Life Sciences, University Medical Center Nijmegen, Nijmegen, The Netherlands

* To whom correspondence should be addressed. E-mail: w.hendriks{at}ncmls.kun.nl.

Mouse PTP-BL is a large, non-transmembrane protein tyrosine phosphatase of unclear physiological function that consists of a KIND domain, a FERM domain, five PDZ domains and a C-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{Delta}P/{Delta}P 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{Delta}P/{Delta}P 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.




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