Structure of human prostatic acid phosphatase gene
نویسندگان
چکیده
منابع مشابه
Human Prostatic Acid Phosphatase: Structure, Function and Regulation
Human prostatic acid phosphatase (PAcP) is a 100 kDa glycoprotein composed of two subunits. Recent advances demonstrate that cellular PAcP (cPAcP) functions as a protein tyrosine phosphatase by dephosphorylating ErbB-2/Neu/HER-2 at the phosphotyrosine residues in prostate cancer (PCa) cells, which results in reduced tumorigenicity. Further, the interaction of cPAcP and ErbB-2 regulates androgen...
متن کاملBiochemical properties of human prostatic acid phosphatase.
The electrophoretic pattern (in polyacrylamide gel) for acid phosphatases in the prostate gland was compared with that for other tissues. lsoenzyme 2 predominates in the prostate. The isoenzyme was isolated from the prostate and its biochemical properties were compared with those of acid phosphatases isolated from spleen. lsoenzyme 2 has a molecular weight of about 100,000. Its optimum pH is be...
متن کاملEmerging Roles of Human Prostatic Acid Phosphatase
Prostate cancer is one of the most prevalent non-skin related cancers. It is the second leading cause of cancer deaths among males in most Western countries. If prostate cancer is diagnosed in its early stages, there is a higher probability that it will be completely cured. Prostatic acid phosphatase (PAP) is a non-specific phosphomonoesterase synthesized in prostate epithelial cells and its le...
متن کاملProstatic acid phosphatase expression in human tissues.
Prostate cancer is the most common cancer and the second leading cause of cancer deaths among males in most Western countries. Autologous cellular immunotherapy for the treatment of cancer seeks to induce tumor-specific immunity in the patient and is consequently dependent on a suitable target antigen and effective presentation of that antigen to the patient's immune system. Prostatic acid phos...
متن کاملHuman prostatic acid phosphatase has phosphotyrosyl protein phosphatase activity.
The major secreted isoenzyme of human prostatic acid phosphatase (PAcP) (EC 3.1.3.2), which catalyses p-nitrophenyl phosphate (PNPP) hydrolysis at acid pH values, was found to have phosphotyrosyl protein phosphatase activity since it dephosphorylated three different phosphotyrosine-containing protein substrates. Several lines of evidence are presented to show that the phosphotyrosyl phosphatase...
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ژورنال
عنوان ژورنال: Biochemical and Biophysical Research Communications
سال: 1992
ISSN: 0006-291X
DOI: 10.1016/s0006-291x(05)80048-8