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PubMed2002

Protection of prostatic acid phosphatase activity in human serum samples by plasmin inhibitors.

BACKGROUND: The level of prostatic acid phosphatase in serum is an established marker for prostate carcinoma. METHODS: Inactivation of homogeneous prostatic acid phosphatase from human seminal fluid by purified plasmin and human serum was studied in the presence and absence of bovine pancreatic trypsin inhibitor, a plasmin inhibitor, or phenylmethylsulfonylfluoride, a serine protease inhibitor. RESULTS: Plasmin or serine protease inhibitors protect against prostatic acid phosphatase inactivation in serum samples. CONCLUSION: The immediate addition of serine protease inhibitors to serum samples taken for prostatic acid phosphatase determinations should provide more accurate results and permit extended storage of samples. The stabilization of the enzyme activity and immunological properties of prostatic acid phosphatase in blood samples by these protease inhibitors resurrects the clinical significance of prostatic acid phosphatase measurements in prostate cancer screenings.

Acid Phosphatase↗
PubMed1982

Prostatic acid phosphatase and sperm in the post-coital vagina.

Sperm and prostatic acid phosphatase identified in vaginal fluid after an alleged sexual assault constitute important physical evidence useful in courts of law during rape trials. The purpose of this study was to define a normal and abnormal range for acid phosphatase in the post-coital vagina for our emergency department and to compare the sensitivity of acid phosphatase versus sperm in determining recent coitus. Vaginal swabs obtained from 90 patients were analyzed for acid phosphatase activity by the Sigma p-nitrophenyl phosphate technique. Swabs were stored in a bovine albumin preservative broth. Pap smears for sperm identification were also performed. Acid phosphatase values greater than 50, especially those greater than 138 Sigma units/cc, correlated with intercourse within the preceding 24 hours (P .005). Values greater than 20 but less than 50 correlated with intercourse within 48 hours (P .005). The presence or absence of sperm was found to be less sensitive, and correlated poorly with the time since intercourse [of 12 cases less than or equal to 24 hours, 11 were acid phosphatase-positive (91.7%) while seven were sperm-positive (58.4%)].

Acid Phosphatase↗
PubMed1999

Tartrate-resistant purple acid phosphatase is synthesized as a latent proenzyme and activated by cysteine proteinases.

Purple acid phosphatases (PAPs) are binuclear acid metallohydrolases also referred to as tartrate-resistant acid phosphatases (TRAPs) or type 5 acid phosphatases. The cDNA sequences of TRAP/PAP enzymes from different species and organs indicate that these enzymes are translated as monomeric polypeptides of approx. 35 kDa, contrasting with the predominantly two-subunit structure observed in purified enzyme preparations. In the present study we have compared certain structural and enzyme-kinetic properties of recombinant rat PAP (monomeric) with those of the native rat bone TRAP/PAP enzyme (two-subunit), and examined effects on these parameters by cleaving the monomeric recombinant PAP with the serine proteinase trypsin or the cysteine proteinases papain or cathepsin B. Cleavage with trypsin resulted in a moderate activation of the recombinant enzyme and shifted the pH optimum to a slightly more basic value (5.0-5.5). Cleavage with papain resulted in complete activation and conferred similar properties to those of the bone PAP variant with regard to pH optimum (5.5-6.0) and sensitivity to reducing agents, as well as in the sizes of the subunits. Substrate specificity studies showed that the two-subunit bone PAP was considerably more active than the monomeric recombinant rat PAP towards a variety of serine-, threonine- and tyrosine-phosphorylated substrates. Of these substrates, bovine milk osteopontin seemed to be the most readily dephosphorylated substrate. In conclusion, the results suggest that the monomeric form of PAP represent a latent proenzyme with low enzymic activity towards both tyrosine- and serine/threonine-containing phosphorylated substrates. Besides being implicated in the catabolism of the extracellular matrix, members of the cysteine proteinase family might also exert a regulatory role in degradative processes involving the PAP enzymes by converting the newly synthesized PAPs to enzymically active and microenvironmentally regulated species.

Acid Phosphatase↗
PubMed1992

A reference preparation of human prostatic acid phosphatase: purification, characterization and field trials.

Acid phosphatase has been prepared in an apparently pure state by affinity chromatography from human prostatic tissue. When dissolved in an acidic albumin solution, lyophilized and stored at -20 degrees C for up to 2 years, no time-dependent loss of catalytic activity was detectable in the reconstituted material. Accelerated degradation tests also predicted complete stability. A preliminary distribution of the lyophilized preparation to 143 laboratories confirmed its robustness and demonstrated its potential usefulness as a calibrant to unify the results of different methods of measuring acid phosphatase activity.

Acid Phosphatase↗
PubMed1976

Histochemical studies on the effect of thyroid hormone on alkaline and acid phosphatase activities in liver of fish and amphibia.

The Lata fishes (Ophicephalus punctatus) showed increased alkaline and acid phosphatase activities in liver after immersion for 15-30 days in thyroxine-containing medium (0.025 mug/ml). A single injection of thyroxine (1-2 mug/g of body weight) caused increased acid phosphatase activity in liver of Lata fish in comparison to the controls on the 5th day after experiment but the alkaline phosphatase activity remained unchanged. Both alkaline and acid phosphatases showed increased activities in liver of Lata fishes treated with a single injection of 4 mug of thyroxine per g of body weight on the 5th day. Immersion of Lata fishes in thiourea solution (1 mg/ml) for 15 days did not show any alteration in alkaline or acid phosphatase activities but these enzyme activities decreased after 30 days' immersion in thiourea solution in comparison to the controls. A seasonal variation of alkaline and acid phosphatase activities was observed in liver of Lata fishes. More alkaline phosphatase activity was found in liver of summer fishes than in winter fishes. The winter fishes showed more acid phosphatase activity than the summer fishes. Three consecutive injections of thyroxine (0.1 mug/g of body weight) to toads (Bufo melanostictus) caused increased alkaline and acid phosphatase activities in liver on the 5th day of the experiment, in comparison to the controls.

Acid Phosphatase↗
PubMed1984

Raman and infrared studies of homogeneous forms of acid phosphatase from rat liver.

Raman spectra of acid phosphatase (orthophosphoric-monoester phosphohydrolase (acid optimum), EC 3.1.3.2) forms from rat liver in water solution, and infrared spectra of the same forms as thin films, have been investigated. The spectra show strong bands belonging to phosphodiester or phosphomonoester residues. These groups are modified during the postsynthetic modification of acid phosphatase and are probably connected with the process of bonding and splitting of mannose 6-phosphate and N-acetylglucosamine, in agreement with previous biochemical models for the intracellular transport of newly synthesized lysosomal hydrolases to lysosomes. Some other bands in the infrared spectra are assigned to vibrations of N-H groups which may belong to N-acetylglucosamine.

Acid Phosphatase↗
PubMed1994

An acid phosphatase from Aspergillus ficuum has homology to Penicillium chrysogenum PhoA.

Three secreted acid phosphatases had previously been characterized from Aspergillus ficuum grown under conditions of limited phosphate. One of these could not be readily separated from AFPhyB, a pH 2.5 optimum acid phosphatase with phytase activity. From extensive protein sequence analysis and subsequent cloning of the gene, we have shown that the AFPhyB protein fraction contains a fourth secreted acid phosphatase (AFPhoA) that has 64% homology to a phosphate-repressible acid phosphatase from Penicillium chrysogenum. Garnier plot analysis revealed that the putative phosphate catalytic domain of AFPhoA at His215Asp216 is similar to those of other acid phosphatases, but that AFPhoA lacks the phosphate-binding motif RHGXRXP of known histidine phosphatases.

Acid Phosphatase↗
PubMed1985

Intracellular maturation and secretion of acid phosphatase of Saccharomyces cerevisiae.

To elucidate intracellular maturation and secretion of acid phosphatase of Saccharomyces cerevisiae we prepared a monoclonal antibody that recognizes specifically the protein moiety of this cell surface glycoprotein. With this antibody membranes and soluble fractions of wild-type cells, grown in low-phosphate medium in the presence and absence of tunicamycin, were examined by the immunoblot technique. Similarly, secretory mutants, blocked at distinct steps in the secretory pathway at the restrictive temperature as well as a strain harboring several copies of the structural gene PHO5 for repressible acid phosphatase, were analyzed. The data suggest the following sequence of events in acid phosphatase maturation and secretion: three unglycosylated precursors with molecular masses of 60 kDa, 58 kDa and 56 kDa are synthesized into membranes of the endoplasmic reticulum, where these are core glycosylated in a membrane-bound form. They appear on sodium dodecyl sulfate gels as bands with molecular masses of 76 kDa and 80 kDa. Owing to a rate-limiting maturation step, occurring after core glycosylation, they can accumulate in a membrane-bound form. At the Golgi apparatus outer carbohydrate chains are attached to the core and the enzyme appears in a soluble form, indicating a release of acid phosphatase from the membrane between the endoplasmic reticulum and the Golgi. Pulse-chase experiments suggest that the time for acid phosphatase synthesis and its transport to the Golgi is about 5 min.

Acid Phosphatase↗
PubMed1982

Synthesis of repressible acid phosphatase in Saccharomyces cerevisiae under conditions of enzyme instability.

The synthesis of repressible acid phosphatase in Saccharomyces cerevisiae was examined under conditions of blocked derepression as described by Toh-e et al. (Mol. Gen. Genet. 162:139-149, 1978). Based on a genetic and biochemical analysis of the phenomenon these authors proposed a new regulatory model for acid phosphatase expression involving a simultaneous interaction of regulatory factors in the control of structural gene transcription. We demonstrate here that under growth conditions that fail to produce acid phosphatase the enzyme is readily inactivated. Furthermore, we demonstrate under these conditions the production of acid phosphatase mRNA which is active both in vitro and in vivo in the synthesis of enzyme. This eliminates any step prior to translation of acid phosphatase polypeptide as an explanation for the phenomenon. We interpret our results for the block in appearance of acid phosphatase as a result of both deaccelerated growth and cellular biosynthesis during derepression, accompanied by an enhanced instability of the enzyme.

Acid Phosphatase↗
PubMed1979

An objective look at acid phosphatase determinations: a comparison of biochemical and immunological methods.

Measurements of serum and bone marrow acid phosphatase were made by 3 enzymatic methods, alpha-naphthyl phosphate, beta-glycerol phosphate, and thymolphthalein monophosphate, and ocmpared to a double antibody radioimmunoassay. Serum and bone marrow acid phosphatase levels were studied in 46 controls with histologically proven benign prostatic hyperplasia and in 135 patients with various stages of prostatic carcinoma. In the control group the upper limit for bone marrow acid phosphatase was found to be significantly higher than the corresponding serum limit with respect to the enzymatic assays studied. The radioimmunoassay was the only method suitable for the analysis of the prostatic acid phosphatase content of bone marrow. A larger number of elevations were noted in patients with extracapsular and metastatic disease when prostatic acid phosphatase measurement was carried out by radioimmunoassay as compared to enzymatic methods. However, only 8% of the patients with intracapsular disease had elevations of prostatic acid phosphatase as measured by radioimmunoassay. Additional standardisation of immunological methods and clinical trials is required before comparison can be made of results from various centres using immunological methods for the measurement of prostatic acid phosphatase and a true assessment made of the usefulness of this procedure.

Acid Phosphatase↗
PubMed1987

Immunocytochemical localization of lysosomal acid phosphatase in normal and "I-cell" fibroblasts.

This study represents the first example of immunological localization of lysosomal acid phosphatase. The intracellular localization of lysosomal acid phosphatase was investigated with immunocytochemical methods at the light and electron microscopical level in cultured fibroblasts obtained from normal subjects and from a patient with I-cell disease. Double-labeling studies using fluorescence microscopy showed that acid phosphatase is present in the same organelles as other hydrolases. At the electron microscopic level in control fibroblasts acid phosphatase was found in the rough endoplasmic reticulum, lysosomes, at the plasma membrane, in vesicles just below the plasma membrane and in multivesicular bodies. This localization was comparable with that of other lysosomal enzymes tested (acid alpha-glucosidase, N-acetyl-beta-hexosaminidase, beta-galactosidase). Acid phosphatase labeling was mainly found in association with the lysosomal membrane and with membranous material present within the lysosome. In I-cell fibroblasts the label was present in the same subcellular organelles but always associated with membranous structures. We suggest that the association of acid phosphatase with membranes might explain the normal enzyme activity found in I-cell fibroblasts.

Acid Phosphatase↗
PubMed1977

Use of different chemical methods for acid phosphatase in cases of rape.

Generally acid phosphatase (ACP) assay is used for testing cases of alleged rape. Comparison of three different chemical methods for Acid Phosphatase (Andersch's method with p-nitrophenyl-phosphate substrate and tartrate inhibitor (A-Tart), Roy's method with thymolphthalein phosphate substrate (R-TMP), and Babson's method with alphanaphthyl phosphate substrate) indicated that Roy's method (R-TMP) should be the preferred one. This method had both acceptable sensitivity and confirmed specificity. Our data confirmed that the vaginal wash of normal healthy women has a very low level of ACP activity. Because of inconclusive data in the literature regarding this ACP level, a normal and equivocal range of ACP was suggested until more is known about causes and interferences. Possible sources of normal ACP activity in the wash fluids were also indicated.

Acid Phosphatase↗
PubMed2001

Serum acid phosphatase as a tumour marker in giant cell tumour of bone.

The serum acid phosphatase value was examined in nine patients with giant cell tumour of bone. Five showed a high level of acid phosphatase, which fell to within normal limits after surgery. Although the remaining four patients showed a normal acid phosphatase level before surgery, the postoperative acid phosphatase level was lower than the preoperative level in each case. Therefore, it is strongly suggested that serum acid phosphatase is a useful tumour marker in diagnosing giant cell tumour of bone as well as in evaluating the efficacy of treatment.

Acid Phosphatase↗
PubMed2000

Comparison of the efficacies of a novel aspergillus niger mycelium with separate and combined effectiveness of phytase, acid phosphatase, and pectinase in dephosphorylation of wheat-based feeds fed to growing broilers.

Efficacies of phytase, phosphorolytic enzymes (phytase + acid phosphatase), an enzymic "cocktail" (phytase + acid phosphatase + pectinase + citric acid), a novel Aspergillus niger (fungal) mycelium (FM), and FM enriched in phytase and antioxidants were investigated in growing broilers (Days 1 to 21) fed wheat-based diets. Broilers were fed the following seven diets at 0.69% Ca: 1) a negative control diet, 0.17% nonphytate P (NPP); 2) Diet 1 + 750 phytase units/kg diet; 3) Diet 1 + 750 phytase units + 3,156 units acid phosphatase/kg diet; 4) Diet 1 + 750 phytase units + 3,156 acid phosphatase units + 1,900 units of pectinase/g diet + 3% citric acid; 5) Diet 1 + 4% FM; 6) Diet 1 + 4% FM + 1,300 phytase units + 2% ascorbic acid and 1% of glucose oxidase; and 7) a positive control diet (Diet 1 + 0.24% NPP from dicalcium phosphate). The dietary treatments were fed to four pen replicates of eight birds each. Prior to feed formulation, mycelium and antioxidants dosages were optimized on Diet 1 by an in vitro technique and an experimental design module of a statistical software package. Phytase addition increased BW gain (BWG), feed intake, and P retention. Subsequent addition of acid phosphatase resulted in further increases in BWG, feed intake, and toe ash and reduced digesta viscosity; however, neither P nor Ca retention were improved. Body weight gain and feed intakes superior to those found in chicks fed Diet 7 were observed in birds receiving the cocktail of enzymes (Diet 4) or FM. Chicken fed Diet 6 had the highest percentage of toe ash and retained 76 and 51% of P and Ca, respectively. Supplementation of wheat-based 0.17% NPP diets with FM increased bursa of Fabricius weights and reduced the intestinal surface covered by Peyer's patches.

6-Phytase↗
PubMed1978

[Interrelationship between metabolic and genetic regulation of alkaline and acid phosphatases in E. coli cells].

The effect of exogenous orthophosphate and mutations in regulatory genes of alkaline phosphatase on the level of nonspecific acid phosphatase was studied. The level of this enzyme as well as the level of alkaline phosphatase were shown to be regulated by exogenous orthophosphate being derepressed under phosphate starvation. The derepression of acid phosphatase is accompanied by more rapid secretion of enzyme from membranes to soluble fraction. Mutations in all the four regulatory genes decrease the level of enzyme in cells. Genes phoR and phoS, participating in regulation of alkaline phosphatase, are required for the derepression of acid phosphatase under the conditions of phosphate starvation.

Acid Phosphatase↗
PubMed1987

Adverse implications of acid phosphatase levels in the upper range of normal.

A retrospective review of 102 consecutive patients with surgically staged, clinically localized prostatic carcinoma was performed to determine the relationship between pre-treatment enzymatic acid phosphatase values and histopathological extent of the tumor. Of 96 patients with normal pretreatment acid phosphatase titers (thymolphthalein monophosphate substrate) 77 (80 per cent) had values in the lower and 19 (20 per cent) had values in the upper half of the normal range. Of the latter 19 patients 16 (84 per cent) had histological evidence of extraprostatic tumor extension. Similarly, 5 of 6 patients (83 per cent) with elevated pre-treatment acid phosphatase titers had extraprostatic extension and 1 had a persistent postoperative acid phosphatase elevation that normalized with megestrol acetate therapy. Thus, 22 of 25 patients (88 per cent) with acid phosphatase values in or above the upper half of the normal range had either histological or clinical evidence of extracapsular tumor extension. By contrast, 41 of the 77 patients (53 per cent) with acid phosphatase titers in the lower half of the normal range had extracapsular extension. The predictive value for extraprostatic tumor extension of an acid phosphatase level in the upper half of the normal range was 84 per cent. Furthermore, in the 96 patients with normal acid phosphatase titers the incidence of extraprostatic tumor extension was significantly greater (p less than 0.01, chi-square) in those with values in the upper rather than the lower half of the normal range. Acid phosphatase titers in the upper half of the normal range were proportionately more common among patients with high grade and high clinical stage tumors. However, among patients with low grade and low stage tumors an acid phosphatase value in the upper half of the normal range was an independent variable that correlated with the presence of extracapsular tumor extension. These results confirm previously reported adverse prognostic implications of enzymatic acid phosphatase titers in or above the upper half of the normal range.

Acid Phosphatase↗
PubMed1988

Purification and physicochemical characterization of a human placental acid phosphatase possessing phosphotyrosyl protein phosphatase activity.

A 17-kilodalton (kDa) human placental acid phosphatase was purified 21,400-fold to homogeneity. The enzyme has an isoelectric point of pH 7.2 and a specific activity of 106 mumol min-1 mg-1 using p-nitrophenyl phosphate as a substrate at pH 5 and 37 degrees C. This placental acid phosphatase showed activity toward phosphotyrosine and toward phosphotyrosyl proteins. The pH optima of the enzyme with phosphotyrosine and with phosphotyrosyl band 3 (from human red cells) were between pH 5 and 6 and pH 5 and 7, respectively. The Km for phosphotyrosine was 1.6 mM at pH 5 and 37 degrees C. Phosphotyrosine phosphatase activity was not inhibited by tartrate or fluoride, but vanadate, molybdate, and zinc ions acted as strong inhibitors. Enzyme activity was also inhibited by DNA, but RNA was not inhibitory. It is a hydrophobic nonglycoprotein containing approximately 20% hydrophobic amino acids. The average hydrophobicity was calculated to be 903 cal/mol. The absorption coefficient at 280 nm, E1% 1cm, was determined to be 5.7. The optical ellipticity of the enzyme at 222 nm was -5200 deg cm2 dmol-1, which would correspond to a low helical content. Free sulfhydryl and histidine residues were necessary for the enzyme activity. The enzyme contained four reactive sulfhydryl groups. Chemical modification of the sulfhydryls with iodoacetate resulted in unfolding of the protein molecule as detected by fluorescence emission spectroscopy. Antisera against both the native and the denatured protein were able to immunoprecipitate the native enzyme. However, upon denaturation, the acid phosphatase lost about 70% of the antigenic determinants. Both antisera cross-reacted with a single 17-kDa polypeptide on immunoblotting.

Acid Phosphatase↗
PubMed1987

Cytochemical localization of alkaline and acid phosphatase in human vanishing bone disease.

This report is the first cytochemical investigation of vanishing bone disease "Gorham's Disease" (Gorham and Stout 1955). The ultrastructural localization of non-specific alkaline phosphatase and of specific and non-specific acid phosphatase activity was studied in slices of tissue removed from a patient with this rare disorder. Sodium beta-glycerophosphate and phosphorylcholine chloride were used as substrates. Alkaline phosphatase was present around the plasma membranes of osteoblasts and associated with extracellular matrix vesicles in new woven bone. This is consistent with the proposed role for this enzyme (Robison 1923) and for matrix vesicles (Bonucci 1967) in the mineralization of bone (Bernard and Marvaso 1981). Concentrations of specific secretory acid phosphatase reaction product in the cytoplasm of degenerating osteoblasts may contribute to the imbalance between bone formation and resorption. Osteoclasts, while few in number, showed non-specific and specific acid phosphatase activity. The Golgi apparatus and heterophagic lysosomes of mononuclear phagocytes were rich in non-specific acid phosphatase. This was also present in the Golgi lamellae and lysosomes of endothelial cells. Acid phosphatase cytochemistry suggests that mononuclear phagocytes, multinuclear osteoclasts and the vascular endothelium are involved in bone resorption in this disease.

Acid Phosphatase↗