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PubMed1981

Studies of heterogeneity of angiotensin-converting enzyme and acid phosphatase in granulomatous lesions of skin.

Activities of angiotensin-converting enzyme and acid phosphatase were markedly elevated in the lesions of metal-induced hypersensitivity and foreign body types of granulomas. We biochemically studied these enzymes by means of gel filtration and electrophoresis and compared them with the same enzymes of normal dermis. Two forms of angiotensin-converting enzyme found in normal dermis were increased proportionally. Catalytic properties and heat stability of the enzyme in the lesions and normal dermis were the same. On the other hand, acid phosphatase in the lesions showed a different isozyme pattern from that seen in normal dermis. The enzyme from normal dermis had apparent molecular weight of 150000 and 90000, whereas an additional enzyme with a molecular weight of 230000 was detected in granulomatous lesions. Three isozymes were demonstrable in normal dermis but two additional isoenzymes appeared in granulomatous lesions: the isozyme patterns between the foreign body and hypersensitivity granulomas are different.

Acid Phosphatase↗
PubMed1978

D-Ephedrinephosphate, DEP: a new substrate with specificity for prostatic acid phosphatase (PAP).

This report describes the synthesis and physical (including spectral) properties of a new substrate, D-ephedrinephosphate, DEP1, which is histochemically highly specific for a secreted non-lysosomal prostatic acid phosphatase, PAP. This specificity is in contrast to other substrates which are nonspecific, i.e., which demonstrate acid phosphatases that originate from various cell types and are mainly lysosomal. When this substrate is used for light and electron microscopic histochemistry in a modified Gomori medium, PAP is demonstrated mainly in secretory granules and in the Golgi apparatus (and its related vacuoles) of prostatic epithelial cells of several species of mammals including man. This corroborates our previous suggestion that PAP is not a lysosomal enzyme as are many of the other acid phosphatases. This high degree of specificity of DEP for PAP supports the usefulness of this compound in the histochemical and biochemical characterization of PAP, and in the diagnosis of localized or disseminated prostatic disease.

Acid Phosphatase↗
PubMed1976

Phosphatidic acid phosphatase and phospholipdase A activities in plasma membranes from fusing muscle cells.

Plasma membrane from fusing embryonic muscle cells were assayed for phospholipase A activity to determine if this enzyme plays a role in cell fusion. The membranes were assayed under a variety of conditions with phosphatidylcholine as the substrate and no phospholipase A activity was found. The plasma membranes did contain a phosphatidic acid phosphatase which was optimally active in the presence of Triton X-100 and glycerol. The enzyme activity was constant from pH 5.2 to 7.0, and did not require divalent cations. Over 97% of the phosphatidic acid phosphatase activity was in the particulate fraction. The subcellular distribution of the phosphatidic acid phosphatase was the same as the distributions of the plasma membrane markers, (Na+ + k+)-ATPase and the acetylcholine receptor, which indicates that this phosphatase is located exclusively in the plasma membranes. There was no detectable difference in the phosphatidic acid phosphatase activities of plasma membranes from fusing and non-fusing cells.

Adenosine Triphosphatases↗
PubMed1986

Effects of physiological concentrations of parathyroid hormone on acid phosphatase activity in cultured rat bone cells.

The mechanism by which parathyroid hormone (PTH) induces osteoclastic bone resorption is still incompletely understood. Recent evidence suggests that the hormone exerts its effects indirectly, via the osteoblasts. Bone cells isolated from fetal rat calvaria by enzymatic digestion were used. Two heterogeneous cell populations were isolated by equilibrium density centrifugation on Percoll gradients and maintained by differential culture conditions. These two populations, which are morphologically distinguishable from one another by light and electron microscopy, have been characterized previously both biochemically and with regard to their hormonal (PTH and calcitonin) responses. We have called them type C cells (containing cells with some of the properties of osteoclasts) and type B cells (containing osteoblast-like cells, as well as fibroblasts, chondrocytes and other stromal cells). In the present study, we have further characterized the functional relationship between the two cell populations, with particular regard to the hormonal responses of type C cultures. Acid phosphatase, measured cytochemically in individual cells, was used as a marker for C cell responses. C cells had significantly higher levels of acid phosphatase activity than either B cells or spleen macrophages. Calcitonin (0-10 pg/ml) decreased C cell acid phosphatase activity but was without effect on B cells or spleen macrophages. Co-culture of C cells with B cells produced increased enzyme activity only in the former; this effect could be mimicked if fibroblasts replaced B cells and cell contact was essential for this response. PTH (0-10 pg/ml) raised enzyme activity further in C cells only when they were cultured with B cells. When C cells were cultured so that they shared medium, but were not in contact, with B cells, PTH (2 pg/ml) still increased enzyme activity in the former. Fibroblasts were ineffective in this system. Spleen macrophages were also unresponsive to PTH when substituted for C cells. Calcitonin (10 pg/ml) blocked the effects of PTH on C cells. These results indicate that macrophages are probably not a significant proportion of the C cell population, and that PTH may produce increased acid phosphatase activity in C cells via a humoral factor produced by cells present in B cell cultures.

Acid Phosphatase↗
PubMed1997

Lysosomal acid phosphatase activity and progesterone secretion by porcine corpora lutea at various periods of the luteal phase.

Four types of porcine corpora lutea were excised at four different stages of the luteal phase. One group of corpora lutea was homogenized and the concentration of progesterone was assayed. The second part was homogenized for measurement of acid phosphatase (ACPase) activity. The third part was sectioned at -20 degrees C in a cryostat and stained histochemically for acid phosphatase activity. The product of acid phosphatase reaction indicated fewer lysosomes in the luteal cells of early developing corpora lutea, increasing as luteal phase progressed. As the level of progesterone declined in the terminal phase of the cycle, there was a maximal increase in the number of lysosomes and ACPase activity. These events resulted in final regression of corpora lutea. The decrease of the lysosomal reaction in the late regressing corpora lutea is probably due to the extreme fragility of the lysosomes at that stage.

Acid Phosphatase↗
PubMed1991

Serum prostatic acid phosphatase activity and prostate specific antigen when the prostate gland is enlarged.

Serum prostatic acid phosphatase activity and prostate specific antigen levels were measured in the serum of 113 patients undergoing transurethral resection of an enlarged prostate gland, and the results compared with the histological diagnosis. Prostate-specific antigen was found to be the more sensitive indicator of malignancy, but prostatic acid phosphatase was more specific.

Acid Phosphatase↗
PubMed1980

Current experience with radioimmunoassay techniques for prostatic acid phosphatase.

Data are presented demonstrating that radioimmunoassay techniques for measurement of serum prostatic acid phosphatase are more sensitive than enzymatic methods in the detection of all stages of prostatic cancer. The possibility of using a solid phase RIA technique to screen for prostatic cancer is considered. Sixty-three hundred and twenty men over age 45 entering a clinical laboratory for any indication were evaluated using the RIA test for PAP. In this group 444 (7%) had elevated test values. Clinical recall and urologic review of the patients with elevated test results yielded 67 who were suspect for prostatic cancer, of whom 59 (88%) were confirmed by prostatic needle biopsy. These data suggest that the RIA for prostatic acid phosphatase as an isolated clinical procedure is not sufficiently specific to be used for screening due to the large number of false-positive results. However, the RIA-PAP test in combination with a follow-up urologic examination is quite specific and deserves further consideration as a screening method for prostatic malignancy.

Acid Phosphatase↗
PubMed1983

Acid phosphatase localization in prostatic carcinoma. A comparison of monoclonal antibody to heteroantisera.

A series of 39 prostatic carcinomas was characterized in terms of grade, stage, histologic pattern, and serum acid phosphatase values. These cases were studied immunohistochemically with two different heteroantisera, a goat and rabbit antiserum, and with a monoclonal antibody to prostatic acid phosphatase (PAP). Eighty-three percent of carcinomas had some degree of PAP positivity when stained by the goat anti-PAP. Seventy percent were positive with the rabbit antiserum, and 59% showed positivity with the monoclonal antibody. Microacinar patterns were consistently the most positive for PAP, followed by cribriform patterns. The least positivity was observed in the undifferentiated, single-file and sheet-like patterns. Likewise, there was more PAP positivity in the lower Gleason and Mostofi grades. When the serum PAP positivity (done by counterimmunoelectrophoresis [CIEP]) was compared with tissue positivity (using the same goat antiserum), 37% were positive in both serum and tissue; 48% were negative in serum, but positive in tissue; and in only 9% the tissue sample was negative when the serum was positive. Based on these data, conclusions are drawn about the significance of the serum acid phosphatase elevations and the role of monoclonal antibodies and heteroantisera in clinical-diagnostic and research work.

Acid Phosphatase↗
PubMed1977

Investigations of capillary network in the myocardium, skeletal muscles, and other organs by modified Gomori's method for determination of acid phosphatase activity.

A modification of Gomori's sulfide method for the determination of acid phosphatase activity is presented, which visualizes the walls of all capillaries in the myocardium, skeletal muscles, synovial membranes, and some other organs (liver, kidney). Blocks of investigated organs (edge lengths 2--3 mm) are cold-fixed in acetone for 2--3 days. Fixed frozen tissues are cut to sections 90--120 micrometer thick and incubated for 2--3 days in an incubation mixture (1% lead/II) acetate, 90 ml; acetate buffer solution pH 6.2, 10 ml; 2% sodium beta-glycerophosphate 1 ml. The sections are then processed with 0.5% sodium sulfide solution for 10--15 min and embedded into glycerine-gelatin gel. In preparations processed in this way, acid phosphatase is visualized on the walls of all capillaries and precapillaries, makig visible the capillary network. In addition to the capillaries, the transverse striation of myofibrils is visualized as well. The described method is useful for investigating not only the cytochemistry of the vascular wall, but also the blood supply to the myocardium, skeletal muscles, and other organs in both normal and pathological states.

Acid Phosphatase↗
PubMed1997

Involvement of apoptosis and lysosomal hydrolase activity in the oviducal regression during induced molting in chickens: a cytochemical study for end labeling of fragmented DNA and acid phosphatase.

Induced molting improves egg producing functions in hens. We investigated the mechanism of oviducal regression during induced molting. Involvement of apoptosis and autolysis in the oviducal regression process was analyzed by terminal deoxynucleotidyl transferase (T'dt)-mediated biotinylated deoxyuridine triphosphates (dUTP) nick end-labeling TUNEL) and an enzyme histochemistry for acid phosphatase. Nuclei positive for TUNEL were negligible and acid phosphatase staining was weak in the oviduct of laying hens. The frequency of TUNEL-positive nuclei was significantly increased in tubular gland cells of magnum, isthmus, and shell gland 2 d after cessation of egg laying and significantly decreased thereafter. The intensity of acid phosphatase staining was gradually increased during oviducal regression and extremely high on Day 7 after cessation of egg laying. These results suggest that during oviducal regression in induced molting hens, apoptosis is induced in the earlier stage of oviducal regression and autolysis occurs thereafter eventually, the glandular cells disappear.

Acid Phosphatase↗
PubMed1985

Acid phosphatase II. Cytochemical localization in lenses of normal and galactose-fed rats.

Previous cytochemical and biochemical studies have shown an increase in the activity of acid phosphatase and arylsulfatase during the induction of galactose cataracts in rat lenses. It was postulated that these enzymes may be involved in lens fiber degradation observed during cataractogenesis, however, the role of these enzymes in the repair process was not ruled out. The present investigation has evaluated the level of acid phosphatase activity in lenses in which the induction of opacity is inhibited with the aldose reductase inhibitor sorbinil and during the recovery of galactose induced opacity. Sprague-Dawley rats received 50% galactose diet, or galactose diet with sorbinil, or laboratory chow diet. Following 20 days on this diet all rats received lab chow plus 50 mg kg-1 sorbinil (recovery diet). The lenses were removed at desired intervals following the initiation of the above three diets and following the transfer of animals to the recovery diet. Cytochemical localization and biochemical quantitation of acid phosphatase activity were performed with methods previously reported. Most of the enzyme activity was localized within the epithelial cells and superficial cortical fibers. In the epithelial cell layer, the enzyme activity was primarily localized in lysosomes and at extracellular sites near the epithelial cell membrane which abut each other and cortical fibers. In cortical fibers the enzyme activity was observed at various extracellular sites between the cell membranes of neighboring fibers. The effect of sorbinil, if any, and the possible role of acid hydrolases in the repair process during cataract reversal is discussed.

Acid Phosphatase↗
PubMedDate not supplied

[Acid phosphatase activity in breast dysplasias and in carcinomas of the breast].

The histochemical reactions of acid phosphatase were studied in tissues deriving from normal breasts, from mammary dysplasia, and from breast carcinoma. Acid phosphatase was demonstrated in all cases with more intense activity in breast carcinoma where activity was particularly accentuated in the stroma. In benign tumours and fibroadenosis, phosphatase was prevalently localized in the periductal cells and within the ducts. Exceptions were the cases of fibroadenosis with acute or chronic collateral inflammation where phosphatase granules were located in the stroma also, even though they were always quantitatively inferior to the corresponding localization of cases of breast carcinomas.

Acid Phosphatase↗
PubMed1997

Fluorescent cytochemistry of acid phosphatase and demonstration of fluid-phase endocytosis using an azo dye method.

The aim of this work was the development of a fluorescent microscopy technique to visualize acid phosphatase activity in living and pre-fixed cells. We have shown that a coupling azo dye method, using naphthol AS-MX phosphate (NP) as substrate and fast red TR (FR) as a diazonium salt coupling agent, gives rise to a fluorescent azo dye reaction product which permits a highly sensitive demonstration of lysosomal acid phosphatase in both living and pre-fixed monolayer cell cultures. The granular staining is prevented by inhibition of acid phosphatase activity using fluoride and/or orthovanadate in both living and pre-fixed preparations. Lysosomal staining in living cells is also abolished by inhibition of fluid-phase endocytosis using low temperatures or inhibition of oxidative phosphorylation. It was shown that whilst NP entered living cells by passive diffusion, occurrence of FR in lysosomes resulted from fluid-phase endocytosis. Spectroscopic analysis of the emission and absorption features of FR, NP, naphthol AS-MX (N), and the N-FR azo dye reaction product in solution corroborated our microscopic results. The differing uptake mechanisms, and the occurrence of lysosomally localized azo dye, were also in keeping with the predictions of quantitative structure-activity relationship models of this system.

Acid Phosphatase↗
PubMed1980

Studies on vinblastine-induced autophagocytosis in mouse liver. II. Origin of membranes and acquisition of acid phosphatase.

The origin of the membranes of autophagic vacuoles (AV) and acquisition of acid phosphatase into AV's were studied in vinblastine-induced autophagocytosis (VBL, 50 mg/kg, i.p.) in mouse hepatocytes. Using unbuffered OsO4, very intense staining was observed in the outer cisternae of the Golgi apparatus and also frequently in the cavity between the double membranes obviously destined to form AV's as well as in the cavity between the double membranes of newly formed AV's. There may occur a transformation process in the membranes limiting an AV analogous to that observed at the Golgi cisternae. The transformation of the outer AV membrane occurs independently of fusion with lysosomes. Inosine diphosphatase activity was localized within the cisternae and on the membranes of the endoplasmic recticulum and occasionally within the innermost cisterna of the Golgi apparatus. The results together with the unbuffered OsO4-staining pattern suggest that the membranes of most AV's are derived from the transformed smooth surfaced cisternae of the endoplasmic reticulum which do not have inosine diphosphatase activity. Acid phosphatase activity was localized in lysosomes, occasionally within the innermost cisternae of the Golgi apparatus, between the double membranes of a few newly formed AV's and within most older single membranes of a few newly formed AV's and within most older single membrane-limited AV's. VBL did not prevent the fusion of lysosomes with AV's.

Acid Anhydride Hydrolases↗
PubMed1998

Phosphotyrosine-protein-phosphatase and diabetic disorders. Further studies on the relationship between low molecular weight acid phosphatase genotype and degree of glycemic control.

We have studied a new sample of 276 NIDDM patients from the population of Penne (Italy). Comparison of the new data with those of 214 diabetic pregnant women from the population of Rome reported in a previous paper has shown that the pattern of association between low molecular weight acid phosphatase genotype and degree of glycemic control is similar in the two classes of diabetic patients. Among nonobese subjects the proportion of ACP1*A (the allele showing the lowest enzymatic activity) is lower in diabetic patients with high glycemic levels (mean value greater than 8.9 mmol/l) than in diabetic patients with a low glycemic level (mean value less than 8.9 mmol/l). Among obese subjects no significant association is observed between glycemic levels and ACP1. Among nonobese subjects the concentration of f isoform of ACP1 is higher in patients showing a high glycemic level than in patients showing a low glycemic level. No significant difference is observed for s isoform.

Acid Phosphatase↗
PubMed2005

Purification and partial characterization of two acid phosphatase forms from pearl oyster (Pinctada fucata).

The present study describes the details about the acid phosphatase forms in the pearl oyster, Pinctada fucata. Two isoenzymes (AcPase I and II) of acid phosphatase were separated and purified from viscera of pearl oyster, P. fucata to homogeneity by chromatography on DEAE-Sepharose Fast Flow, Sephadex G-200 superfine and ConA Sepharose 4B, and partial biochemical properties of AcPase I and II were studied. AcPase I and AcPase II had molecular weights of 208.8 and 64.3 kDa, respectively. AcPase I was a single polypeptide chain, while AcPase II was a dimeric enzyme composed of two equivalent subunits. AcPase I and II showed optimal pHs at 4.6 and 3.2 with p-nitrophenylphosphate as substrate. The optimal catalytic reaction temperature was 47 degrees C for AcPase I and 57 degrees C for AcPase II. Both enzyme forms were stable when incubated at 50 degrees C for 40 min. Tartrate and fluoride were the most effective inhibitors of the enzymes. Fe(3+), Zn(2+), Cu(2+) and Pb(2+) inhibited the activity of AcPase I and II to differing extents. AcPase I and II were apparently nonspecific and hydrolyzed various phosphoric esters. The different properties of AcPase I and II suggested that the two enzymes may play different roles in the pearl oyster.

Acid Phosphatase↗
PubMed1979

Comparison of acid phosphatase isoenzymes of human seminal fluid, prostate, and leukocytes.

We used ion-exchange column chromatography and electrophoresis on polyacrylamide gel to compare the acid phosphatase isoenzymes of prostate and leukocytes. The major isoenzyme of the prostate is band 2A; only a trace of band 2B was observed. However, the major isoenzymes of leukocytes are band 4 and band 2B, and only a small amount of band 2A was observed. The three isoenzymes isolated from leukocytes or prostate gland react to the antiserum prepared against the aicd phosphatase isoenzyme of seminal fluid. Acid phosphatases of leukocytes other than the three isoenzymes mentioned above did not interact with the antiserum.

Acid Phosphatase↗
PubMed1993

The cloning and sequencing of the genes encoding phytase (phy) and pH 2.5-optimum acid phosphatase (aph) from Aspergillus niger var. awamori.

The genes encoding phytase (EC 3.1.3.8) and pH 2.5-optimum acid phosphatase (EC 3.1.3.2) have been cloned and sequenced from Aspergillus niger var. awamori. The translated nucleotide sequences yielded polypeptides of 467 and 479 amino acids (aa) for phytase and acid phosphatase, respectively. The genes were isolated using oligodeoxyribonucleotide probes based on the aa sequences of the purified proteins. Recombinant A. niger var. awamori strains carrying additional copies of the gene sequences demonstrated elevated enzyme activities.

6-Phytase↗