Acid Phosphatases of the Human Placenta, Characterization and Immunological Comparison with Prostatic Acid Phosphatase

Lim

Biology of Reproduction

et al. 2014

Prostatic acid phosphatase (ACPP) is a glycoprotein that is mainly synthesized and secreted by glandular epithelial cells (GE) of the prostate, and it is well known as a biomarker for prostate cancer. Although ACPP was used as prognostic/diagnostic indicator and studied to elucidate regulatory mechanism(s) during several decades in humans, its role is not clearly understood. Gene profiling data using a chicken DNA microarray revealed that ACPP increased significantly during remodeling and recrudescence of the oviduct in response to estrogen. Thus, in this study, we investigated the expression and hormonal regulation of ACPP gene in the reproductive tracts of chickens. ACPP was specifically detected in the luminal cells (LE) and GE of chicken oviduct, and diethylstilbestrol (a synthetic nonsteroidal estrogen) stimulated its expression during development of the oviduct. In addition, ACPP mRNA and protein were localized to LE and GE during the regeneration phase of the oviduct of laying hens during induced molting. Furthermore, ACPP mRNA and protein were abundant in GE of ovarian carcinoma, but not in normal ovaries. Moreover, strong expression of ACPP protein was detected in epithelial cells of cancerous ovaries from women. Collectively, results of the present study are the first to show that ACPP is a novel estrogen-stimulated gene in the oviductal epithelial cells of the chicken and that its expression increases significantly in epithelial cells of ovarian carcinoma, which indicates that it may be a candidate biomarker for diagnosis of epithelia-derived ovarian cancer in women.

Section: Discussionsupporting

confidence: 82%

Avian Prostatic Acid Phosphatase: Estrogen Regulation in the Oviduct and Epithelial Cell-Derived Ovarian Carcinomas1

Lim

Biology of Reproduction

et al. 2014

British Journal of Urology

“…This indicates that the specificity of the RIA used is not absolute. In fact, several observations indicate that antibodies raised against pure PAP cross-react with enzymes in leucocytes (Lam et al, 1979), female human urine (Wojciesyn et al, 1979) and human placenta (Skinningsrud, 1982). Because of the possibility of leakage from white blood cells, one would expect the difference between the results of BM-PAP (RIA) and S-PAP (RIA) to be dependent on the technique used for the bone marrow aspiration.…”

Section: Discussionmentioning

confidence: 99%

Prostatic Acid Phosphatase in Serum and Bone Marrow in Patients with Prostatic Carcinoma

Fosså

Skinningsrud

Kaalhus

et al. 1983

Sixty-two per cent of 61 patients with prostatic carcinoma showed elevated levels of serum acid phosphatase, analysed by radioimmunoassay (RIA). Enzymatically determined serum acid phosphatase was raised in only 38% of the same patients. Bone marrow acid phosphatase determined by RIA was raised in 41%. In untreated metastatic patients with prostatic carcinoma, radioimmunologically determined serum acid phosphatase was elevated in 12 of 13 patients, whereas bone marrow acid phosphatase (RIA) and enzymatically determined serum prostatic acid phosphatase were increased only in about half of the patients. In a control group the upper reference limit of bone marrow acid phosphatase determined by RIA was significantly raised above that obtained by serum analyses. This indicates that nonprostatic acid phosphatases (possibly from bone marrow cells) cross-react with prostatic acid phosphatase in an unpredictable way, even when using a specific radioimmunoassay. In patients with metastatic carcinoma of the prostate, the results of bone marrow acid phosphatase determinations, analysed by RIA, seem to lack diagnostic and/or prognostic information additional to that obtainable by serum acid phosphatase (RIA) analysis.

Demonstration of prostatic-type acid phosphatase in non-lysosomal granules in the crypt epithelium of the human duodenum

1987

Human prostatic-type of acid phosphatase has been demonstrated by biochemical methods to be expressed in a number of cells and tissues in addition to the prostate gland. However, the function of this activity is unknown, nor has the enzyme been convincingly localized at the cellular level in any non-prostatic tissues. Using biochemical and immunocytochemical methods, we demonstrate that human intestinal epithelium contains both a lysosomal and prostatic type of acid phosphatase. The prostatic-type enzyme is present only in the epithelium of the crypts and to a lesser extent in the transitional zone at the base of the villi, in contrast to the widely-distributed lysosomal type. The prostatic enzyme is contained in granules that do not react with anti-lysosomal acid phosphatase and are probably secretory in nature.