Isoenzymes of Human Prostate Acid Phosphatase

Chu, T. Ming; Wang, M.C.; Merrin, Claude; Valenzuela, Luis; Murphy, G.P.

doi:10.1159/000225284

Cited by 23 publications

(8 citation statements)

References 5 publications

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“…Several PAcP isozymes with different molecular weights or pIs have been reported [24,25,28,81–84]. Vihko [24] proposed that a minor species of purified PAcP protein from prostate tissue is the authentic cPAcP in prostate cells and it exhibits only partial cross-reactivity with Ab to sPAcP.…”

Section: Structure Of Human Prostatic Acid Phosphatasementioning

confidence: 99%

Human Prostatic Acid Phosphatase: Structure, Function and Regulation

Muniyan

Chaturvedi

Dwyer

et al. 2013

IJMS

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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 sensitivity of PCa cells. Knockdown of cPAcP expression allows androgen-sensitive PCa cells to develop the castration-resistant phenotype, where cells proliferate under an androgen-reduced condition. Thus, cPAcP has a significant influence on PCa cell growth. Interestingly, promoter analysis suggests that PAcP expression can be regulated by NF-κB, via a novel binding sequence in an androgen-independent manner. Further understanding of PAcP function and regulation of expression will have a significant impact on understanding PCa progression and therapy.

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Section: Structure Of Human Prostatic Acid Phosphatasementioning

confidence: 99%

Human Prostatic Acid Phosphatase: Structure, Function and Regulation

Muniyan

Chaturvedi

Dwyer

et al. 2013

IJMS

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“…Disc gel electrophoresis was performed using a 7.5 % polyacrylamide gel (Davis, 1964). Acid phosphatase activity was detected by staining the gels with 0.1 % a-naphthyl phosphate/0.1 % Fast Red TR salt in 0.1 M-ammonium acetate buffer, pH 5.2 (Chu et al, 1978). The protein band was detected by staining with 0.04% Coomassie Brilliant Blue G-250 in 10% methanol (Chu et al, 1978).…”

Section: Gel Electrophoresismentioning

confidence: 99%

“…Acid phosphatase activity was detected by staining the gels with 0.1 % a-naphthyl phosphate/0.1 % Fast Red TR salt in 0.1 M-ammonium acetate buffer, pH 5.2 (Chu et al, 1978). The protein band was detected by staining with 0.04% Coomassie Brilliant Blue G-250 in 10% methanol (Chu et al, 1978). SDS/PAGE was performed with a 5-20 % acrylamide gradient gel (Laemmli, 1970).…”

Section: Gel Electrophoresismentioning

confidence: 99%

“…Analytical gel isoelectric focusing was carried out with 7% polyacrylamide slab gels containing Ampholine (pH 4.0-6.0) at 120 V/4°C for 20 h by the procedure described by Chu et al (1978). pI values were determined on one gel and enzyme activity on another.…”

Section: Isoelectrofocusingmentioning

confidence: 99%

“…Data obtained from electrophoresis and ion-exchange chromatography have suggested the presence of more than one acid phosphatase isoenzyme in the prostate (Choe & Rose, 1982;McTigue & Van Etten, 1982;Lin et al, 1983;Yeh et al, 1987). The heterogeneity of PAP is probably caused by different degrees of glycosylation on the protein molecule, yet the existence of true isoenzymes consisting of different polypeptide chains with a similar molecular mass of 100 kDa is also a possibility (Ostrowski et al, 1970;Chu et al, 1977Chu et al, , 1978Mahan & Doctor, 1979).…”

Section: Introductionmentioning

confidence: 99%

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Homodimer and heterodimer subunits of human prostate acid phosphatase

Lee

Chu

et al. 1991

Biochemical Journal

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Human prostatic acid phosphatase (PAP) isoenzymes, designated PAP-A and PAP-B, were isolated from human seminal plasma by sequential affinity chromatography on concanavalin A and L(+)-tartrate, a classic inhibitor of PAP. Both the major PAP-A and the minor PAP-B isoenzymes exhibited a similar molecular mass (100 and 105 kDa respectively), multiple pI values (5.05-5.35 and 5.05-5.12), and substrate and inhibitor specificity. Immunological characterization revealed that PAP-B possesses distinct antigenic determinants, in addition to the common sites shared with PAP-A. SDS/PAGE indicated that both isoenzymes are composed of two subunits of 50 kDa each. At high salt concentration, PAP-B dissociated completely into single subunits of 50 kDa, whereas PAP-A remained intact at 100 kDa. PAP-B was resolved by reverse-phase h.p.l.c. into three components, designated alpha, beta and gamma, each of 50 kDa, at a molar ratio of approx. 2:1:1. PAP-A contained a single component of molecular mass 50 kDa. The single component of PAP-A and the alpha component of PAP-B possessed identical amino acid compositions and N-terminal sequences, which were different from those of the beta and gamma components. These results indicate that human PAP contains three isoforms, alpha 2, alpha beta and alpha gamma. PAP-A, the major isoenzyme, is a homodimer consisting of two identical subunits (alpha 2), and PAP-B, the minor isoenzyme, is a mixture of two heterodimers, consisting of non-identical subunits (alpha beta and alpha gamma).

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Activity and isoenzymes of acid phosphatase in human B-cell lymphomas of low-grade malignancy: A novel aid in the classification of malignant lymphoma

Schmidt

Radzun

Schwarze

et al. 1980

Cancer

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Activity and isoelectric focusing (IEF) pattern of lysosomal acid phosphatase (E.C.3.1.3.2.) were investigated in 55 cases of low-grade malignant B-cell lymphoma, classified as chronic B-lymphocytic leukemia (B-CLL), centroblastidcentrocytic follicular lymphoma (CB/CC), lymphoplasmacytic/lympho-plasmacytoid lymphoma (Immunocytoma, IC), and plasmacytoma (PC), applying the criteria of the Kiel classification. The results show (1) that the four lymphoma types present a characteristic range of enzyme activity in an increasing order: B-CLL, CB/CC, IC, and PC. B lymphocytes, germinal center cells, and plasmacytes are the main constituents of these lymphomas. This sequence might reflect one possible mode of B-cell transformation into plasmacytes traversing an amplification stage in germinal centers under normal conditions. (2) All cases showed the basic IEF pattern of normal B lymphocytes with 12 bands localized in three regions between pH 6.1 and 3.9. This finding supports the B-cell origin and the close phenotypical relationship among the investigated lymphomas. (3) The IEF patterns of B-CLL and CB/CC did not differ from that of normal B lymphocytes, whereas two additional isoenzymes were encountered in cases of IC and seven in PC; this suggests that the higher enzyme activity of IC and PC is at least partly due to the appearance of "new" isoenzymes. The results support the validity of the underlying classification and indicate the individuality, B-cell origin, and close relationship among the four lymphoma entities investigated.

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Isoenzymes of Human Prostate Acid Phosphatase

Cited by 23 publications

References 5 publications

Human Prostatic Acid Phosphatase: Structure, Function and Regulation

Human Prostatic Acid Phosphatase: Structure, Function and Regulation

Homodimer and heterodimer subunits of human prostate acid phosphatase

Activity and isoenzymes of acid phosphatase in human B-cell lymphomas of low-grade malignancy: A novel aid in the classification of malignant lymphoma

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