Biochem Biophys Res Commun. 2000 Jun 24;273(1):62-5.

Inhibition of alanyl-aminopeptidase suppresses the activation-dependent induction of glycogen synthase kinase-3beta (GSK-3beta) in human T cells.

Lendeckel U, Scholz B, Arndt M, Frank K, Spiess A, Chen H, Roques BP, Ansorge S.

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Institute of Experimental Internal Medicine, Center of Internal Medicine, Otto-von-Guericke University of Magdeburg, Germany. uw.lendeckel@medizin.uni-magdeburg.de

Abstract

Inhibition of alanyl-aminopeptidase (APN, CD13) gene expression or enzymatic activity compromises T cell proliferation and function. Molecular mechanisms mediating these effects are not known as yet. Recently, we found the expression of the proto-oncogen Wnt-5a to be strongly affected by APN-inhibition. Wnt-5a and other members of the Wnt family of secreted factors are implicated in cell growth and differentiation. Here, we analyzed by quantitative RT-PCR and immunoblotting the expression in mitogen-activated T cells of a major constituent of the Wnt-5a pathway, glycogen synthase kinase-3beta (GSK-3beta). T cell activation by phytohaemagglutinin or pokeweed mitogen results in a strong increase of GSK-3beta mRNA amounts. At the protein level, we observed an up-regulation of both GSK-3beta and phosphorylated GSK-3beta. This induction-dependent increase of GSK-3beta is markedly reduced in response to inhibitors of alanyl-aminopeptidase, actinonin, leuhistin, and RB3014. These findings may provide a rational for the growth inhibition resulting from a diminished expression or activity of alanyl aminopeptidase.

PMID:: 10873564; [PubMed - indexed for MEDLINE]

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