The 35 kDa acid metallophosphatase of the frog Rana esculenta liver: studies on its cellular localization and protein phosphatase activity

• Autorzy: Szalewicz A. , Strzelczyk B. , Sopel M. , Kubicz A.
• Języki publikacji: EN

Abstrakty

EN

The cellular localization of the 35 kDa, low molecular mass acid metallophosphatase (LMW AcPase) from the frog (Rana esculenta) liver and its activity towards P-Ser and P-Tyr phosphorylated peptides were studied. This enzyme was localized to the cyto­plasm of hepatocytes but did not appear in other cells of liver tissue (endothelium, macrophages, blood cells). This LMW AcPase does not display activity towards 32P-phosphorylase a under conditions standard for the enzymes of PPP family. Proteins containing P-Ser: rabbit 32P-phosphorylase a and phosvitin are hydrolysed only at acidic pH and are poor substrates for this enzyme. The frog AcPase is not inhibited by okadaic acid and F- ions, the Ser/Thr protein phosphatase inhibitors. Moreover, the frog enzyme does not cross-react with specific antisera directed against N-terminal fragment of human PP2A and C-terminal conserved fragment of the eukaryotic PP2A catalytic subunits. These results exclude LMW AcPase from belong­ing to Ser/Thr protein phosphatases: PP1c or PP2Ac. In addition to P-Tyr, this en­zyme hydrolyses efficiently at acidic pH P-Tyr phosphorylated peptides (hirudin and gastrin fragments). Km value for the hirudin fragment (7.55 ± 1.59 10–6M) is 2–3 orders of magnitude lower in comparison with other substrates tested. The enzyme is inhibited competitively by typical inhibitors of protein tyrosine phosphatases (PTPases): sodium orthovanadate, molybdate and tungstate. These results may suggest that the LMW AcPase of frog liver can act as PTPase in vivo. A different cellular localization and different response to inhibition by tetrahedral oxyanions (molybdate, vanadate and tungstate) provide further evidence that LMW AcPase of frog liver is distinct from the mammalian tartrate-resistant acid phosphatases.

Słowa kluczowe

EN

protein phosphatase; activity; acid phosphatase; enzyme; bicinchoninic acid; frog; liver; tyrosine protein phosphatase; Rana esculenta; metallophosphatase

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 2003
• Tom: 50
• Numer: 2
• Opis fizyczny: p.555-566,fig.

Twórcy

autor

Szalewicz A.

• University of Wroclaw, Tamka 2, 50-137 Wroclaw, Poland

autor

Strzelczyk B.

autor

Sopel M.

autor

Kubicz A.

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