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Papers In Press, published online ahead of print August 26, 2003
J. Biol. Chem, 10.1074/jbc.M211169200
Submitted on October 31, 2002
Revised on August 11, 2003
Accepted on August 26, 2003

PMA-induced Ectodomain shedding and phosphorylation of human meprin beta

Dagmar Hahn, Anastassios Pischitzis, Sandra Roesmann, Marianne K. Hansen, Boris Leuenberger, Ursula Luginbuehl, and Erwin E. Sterchi

Institute of Biochemistry and Molecular Biology, University of Berne, Berne, BE 3012

Corresponding Author: erwin.sterchi{at}mci.unibe.ch

Shedding of proteins localized at the cell surface is an important regulatory step in the function of many of these proteins. Human Meprin (N-benzoyl-L-tyrosyl-p-aminobenzoic acid hydrolase, PPH, E.C. 3.4.24.18) a zinc-metalloendopeptidase of the astacin family is an oligomeric protein complex of a- and b-subunits and is expressed abundantly in the intestine and kidney as well as in leukocytes of the lamina propria and in cancer cells. In transfected cells intracellular proteolytic removal of the membrane anchor results in the secretion of the meprina-subunit. In rats and mice, the b-subunit exists in a membrane-anchored form. In contrast, human meprinb is constitutively converted into a secretable form. We now show that phorbol 12-myristate 13-acetate (PMA) stimulates an increased release of hmeprinb from transfected COS-1 cells, whereas hmeprina secretion is not influenced. This stimulatory effect is inhibited by the PKC inhibitor staurosporine, suggesting that activation of PKC mediates PMA-induced hmeprinb shedding. The use of different protease inhibitors shows that two different metalloprotease activities are responsible for the constitutive and the PMA stimulated hmeprinb shedding. We identified tumor necrosis factor a converting enzyme (TACE or ADAM17) as the protease that mediates the PMA induced release. We also demonstrate that hmeprinb is phosphorylated by PMA-treatment on Ser687 within a PKC consensus sequence in the cytosolic domain of the protein. This phosphorylation of hmeprinb is not, however, implicated in the enhanced secretion by PMA treatment.


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