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PubMed1977

Ultrastructural localization of acid phosphatase activity in root tips by the p-(acetoxymercuric) aniline diazotate reagent and a comparison with a Gomori procedure.

The localization of acid phosphatase was studied in root tip cells of pea and mung bean by use of a heavy metal azo-dye technique. Diazotized p-(acetoxymercuric) aniline in a post-coupling procedure, using naphthol AS-BI phosphate as substrate, yielded a fine particulate reaction product within vacuoles, intercellular spaces, multivesicular bodies and at various sites throughout the cytoplasm of pea root cells and differentiating mung bean protoxylem cells. An ultrastructural comparison with a modified Gomori lead-salt precipitation method revealed differences in the subcellular location of beta-glycerophosphatase and naphthol AS-BI phosphatase. The distribution of acid phosphatases within plant meristematic cells is discussed.

Acid Phosphatase↗
PubMed1976

Elevated serum acid phosphatase levels with rectal carcinoid tumor.

A case of rectal carcinoid tumor with liver metastases is reported in which a markedly elevated serum acid phosphatase level was found. Tissue assays of the patient's tumor, liver metastasis, and uninvolved liver were performed which demonstrated very high tumor levels of acid phosphatase. The patient also had elevated plasma serotonin levels and urinary 5-hydroxyindole acetic acid levels and did not exhibit the carcinoid syndrome. Autopsy showed no prostate cancer or metastatic bone lesions. Serum acid phosphatase elevation may occur with carcinoid lesions of the rectum.

Acid Phosphatase↗
PubMed1990

Demonstration of secondary lysosomes in bovine megakaryocytes and platelets using acid phosphatase cytochemistry with cerium as a trapping agent.

The ultrastructure of lysosomes from bovine megakaryocytes (MK) and platelets was characterized using acid phosphatase cytochemistry with beta-glycerophosphate as substrate and cerium as a trapping agent. The technique was easily reproducible; cerium-phosphate precipitates were uniform, readily visualized, and there was a virtual absence of nonspecific reaction product. Acid phosphatase was localized in the trans aspect of the Golgi complex and/or granules of less than 50 nm to 650 nm diameters in MK at all stages of maturation. Forty percent of the MK lysosomes contained inclusions of variable shapes, sizes and electron-density and were classified as secondary lysosomes. Twenty-four percent of the platelet sections contained acid phosphatase-positive granules. Fifty-four percent of these were secondary lysosomes. This is the initial report demonstrating secondary lysosomes in either resting MK or platelets using acid phosphatase cytochemistry. These findings suggest that MK and platelet lysosomes have an intracellular function in resting MK and platelets.

Acid Phosphatase↗
PubMed1976

Acid phosphatases of the rat epididymis. I. Fractionation and substrate specificity.

Three separate acid phosphatases were found in the rat epididymal homogenate after fractionation by DEAE- and CM-cellulose chromatography as well as by electrophoresis. They differed from each other also in substrate specificity. This can possibly be utilized as an aid in their differential quantitation. Some other species including man, dog, rabbit, guinea pig and mouse also had a multiple composition of epididymal acid phosphatases.

Acid Phosphatase↗
PubMed1981

Transient high serum prostate-specific acid phosphatase measured by radioimmunoassay in prostatic infarction.

Extremely high concentration, 172-hold the upper limit of reference range, of serum prostate-specific acid phosphatase was measured by radioimmunoassay in a patient subsequently shown to have prostatic infarction associated with prostatic hyperplasia. Following retropubic prostatectomy, the serum concentration of acid phosphatase returned to normal range. This finding shows that even grossly elevated levels of prostatic acid phosphatase enzyme protein in serum are not specific for prostatic carcinoma.

Acid Phosphatase↗
PubMed1982

An improved method for combined autoradiography and histochemistry: the simultaneous detection of 6-3H thymidine and acid phosphatase activity in cryostat sections of mouse thymus and duodenum.

A new method is described that enables the simultaneous detection of 6-3H thymidine incorporation and acid phosphatase activity in the same tissue section. Histochemically, naphthol AS B1 released by tissue based acid phosphatase activity from the substrate naphthyl AS B1 phosphoric acid is coupled with a range of diazonium salts to produce insoluble azo dyes. The azo dye tests result in a particulate localization of lysosomal acid phosphatase and also label diffuse sources associated with cell death. The tests selected permit the application of photographic emulsion without the necessity of an inert barrier layer to separate the emulsion from the histochemically treated cryosections. The localization of 6-3H thymidine incorporation and cell death in mouse thymus and duodenum is demonstrated and comparative counts estimating the distribution of 6-3H thymidine incorporation and hydrolase labelled cell death in the thymus are presented. Young mouse thymus (5 weeks) was found to contain 1.36 +/- 0.12% dying cells and 6.78 +/- 0.03% thymidine incorporating cells, whilst old mouse thymus (53 weeks) was found to contain 2.34 +/- 0.6% dying cells and 5.29 +/- 0.37% thymidine incorporating cells.

Acid Phosphatase↗
PubMed2006

An 18 kDa acid phosphatase from chicken heart possesses phosphotransferase activity.

A low molecular weight acid phosphatase was purified to homogeneity from chicken heart with a specific activity of 42 U/mg and a recovery of about 1%. Nearly 800 fold purification was achieved. The molecular weight was estimated to be 18 kDa by SDS-polyacrylamide gel electrophoresis. Para-nitrophenyl phosphate, phenyl phosphate and flavin mononucleotide were efficiently hydrolysed by the enzyme and found to be good substrates. Fluoride and tartrate had no inhibitory effect while phosphate, vanadate and molybdate strongly inhibited the enzyme. The acid phosphatase was stimulated in the presence of glycerol, ethylene glycol, methanol, ethanol and acetone, which reflected the phosphotransferase activity. When phosphate acceptors such as ethylene glycol concentrations were increased, the ratio of phosphate transfer to hydrolysis was also increased, demonstrating the presence of a transphosphorylation reaction where an acceptor can compete with water in the rate limiting step involving hydrolysis of a covalent phospho enzyme intermediate. Partition experiments carried out with two substrates, para-nitrophenyl phosphate and phenyl phosphate, revealed a constant product ratio of 1.7 for phosphotransfer to ethylene glycol versus hydrolysis, strongly supporting the existence of common covalent phospho enzyme intermediate. A constant ratio of K (cat)/K (m), 4.3 x 10(4), found at different ethylene glycol concentrations, also supported the idea that the rate limiting step was the hydrolysis of the phospho enzyme intermediate.

4-Nitrophenylphosphatase↗
PubMed1978

Measurement of prostatic acid phosphatase in various cell lines.

In the last few years, we have developed a radioimmunoassay for the measurement of human prostatic acid phosphatase. This method, which requires samples of the patient's serum, has been proved to be more accurate than the conventional enzymatic assay for the detection of early stages of carcinoma of the prostate. We used the enzymatic assay and radioimmunoassay for the quantitation of prostatic acid phosphatase in cultured prostatic cell lines. We were unable to show any difference in the concentration of prostatic acid phosphatase between prostatic and any other established cell lines.

Acid Phosphatase↗
PubMed1982

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

In the present investigation we have examined the presence, distribution and probable role of acid phosphatase in lenses of normal and galactose-fed rats. Acid phosphatase was localized in lenses using two separate cytochemical procedures (Gomori and Barka-Anderson methods) and examined at the ultrastructural level. Both procedures, in general, provided similar sites of acid phosphatase activity, although with the Barka-Anderson method finer and larger amounts of well-defined reaction product were observable at the site of reaction. The reaction product was observed in lenses of both rats fed on regular laboratory chow and galactose-fed rats. The intracellular location of the reaction of this enzyme was primarily in lysosomes and occasionally in the endoplasmic reticulum cisternae. At the extracellular sites, it was near the epithelial cell membranes which abut each other and cortical fibers. However, in the cortical fibers the extracellular localization was at various sites on the entire intercellular space between neighboring fibers. The possible role of hydrolases in the lens tissue is discussed.

Acid Phosphatase↗
PubMed1977

[Acid phosphatase localization in the mucous membrane of chicken large intestine (author's transl)].

In the wall of chicken large intestine, acid phosphatase was found only in the mucous membrane. It is present in lysosomes of the Golgi zone of enterocytes, in lysosomes of goblet cells, and in the specific granules of globule leucocytes. In the epithelium of the neck of caecum and of the colon the amount of acid phosphatase decreases towards the tip of the villi. Localization differences of enzyme are present in the villiless caecum bodies, where the surface epithelium and the epithelium of the intestinal glands neck lack the acid phosphatase activity. In the Lamina propria mucosae the enzyme is localized in fibrocytes occurring in abundance in the stroma of the caecum neck and colon and between the intestinal glands of the caecum body.

Acid Phosphatase↗
PubMed1981

The activity of alkaline and acid phosphatase and non-specific esterase in experimental bovine cysticercosis at different stages of development.

The activity of alkaline and acid phosphatase and non-specific esterase was detected both in the parasite and in the tissue reaction on days 21, 23, 42, 168 and 261 after experimental infection. A very high activity of all enzymes was found in 21- and 23-day-old C. bovis in the tegument of whole bladder. In 42, 168 and 261 days old cysticerci the activity of alkaline acid phosphatase was limited only to a part of bladder surrounding the opening of the spinal canal, whereas the activity of non-specific esterase was present in the whole bladder. The activity of non-specific esterase was localized in subtegumental cells of the bladder wall and in small bodies in the bladder and scolex. These bodies increased in number with the age of the cysticercus. In the tissue reaction, a high activity of alkaline phosphatase was detected only in the period of about 20 days after infection in the layer of activated fibroblasts. The activity of acid phosphatase was demonstrated in the tissue reaction in all time periods and was localized in the histiocytes, macrophages, necrotic exudate, necrotic foci and pigment cells at the periphery of tissue reaction. These cells exhibited also the activity of non-specific esterase.

Acid Phosphatase↗
PubMed1986

Acid phosphatase in the rat prostate: comparison with other organs.

Properties of acid phosphatase in the rat ventral prostate were compared with those in seven other organs in adult male rats by the electrophoretic mobility in acrylamide gels, susceptibility to reactions with inhibitors, and by their response to castration and subsequent testosterone replacement. The enzyme in the spleen exhibited the highest values of Km and Vmax. These values in the prostate, the liver, and the kidney showed an intermediate level, while the lowest level was found in the heart, the lung, the adrenals, and the seminal vesicle. Upon electrophoresis, a total of six isoenzyme bands were resolved. Two major zones of activity were noted. They were the slow-moving anodal bands (isoenzymes 1,2, and 3) and the fast-moving cathodal bands (isoenzymes 4,5, and 6). The spleen possessed the highest number of isoenzymes (bands 1,2,4,5 and 6) and the prostate had three (bands 1,2, and 3). The heart contained only one (band 2). Two isoenzymes (bands 1 and 2) were found in remaining organs. Results of the effects of inhibitors showed that NaF inhibited all six isoenzymes, while L(+)tartrate inhibited mainly those in the anodal zone. D(-)tartrate and formaldehyde showed no significant inhibition to any of the isoenzymes. PCMB (para-chloromercuribenzoic acid) was found to be a specific inhibitor for isoenzyme 3. Upon castration in the hosts, the enzyme activity in the prostate, the liver, and the seminal vesicle was significantly reduced. This reduction in enzyme activity involved all isoenzymes in these three organs, but isoenzyme 3 in the prostate disappeared completely after castration. The activities of these isoenzymes were restored by testosterone replacement. These results indicate that acid phosphatase in rat tissues has multiple forms; each has its own electrophoretic mobility in acrylamide gels, sensitivity to inhibitors, and response to hormonal manipulation. Isoenzyme 3 is specific to the prostate and is uniquely sensitive to PCMB inhibition and to androgen stimulation.

Acid Phosphatase↗
PubMed1999

The lysosomal enzymes acid phosphatase and cathepsin D in rats intoxicated with Senna occidentalis seeds.

Chronic administration of Senna occidentalis seeds induces an experimental toxic myopathy characterized by skeletal muscle fibers atrophy, decrease in histochemical activity of cytochrome oxidase, and increase of the acid phosphatase activity in muscle fibres at the light microscopic level. The mechanisms that lead to the increase of this lysosomal enzyme activity are not known and could be related to other biochemical disturbs than the mitochondrial function impairment. The main aim of the present study is to localize the acid phosphatase activity using a cytochemical method at transmission electron microscopy level and to quantify cathepsin D in muscle of rats chronically intoxicated with Senna occidentalis seeds by immunoblotting. Acid phosphatase was observed in lysosomes and over profiles of some organelles apparently not involved by lysosomal membrane. In addition immunoblotting demonstrated a decrease in the content of the precursor and of the mature form of cathepsin D in samples of muscles and liver of intoxicated animals. We concluded that there is a selective increase in acid phosphatase activity in muscle--and maybe in other tissues--of animals intoxicated with Senna occidentalis, that can be related to the skeletal muscle atrophy and the intense decrease in weight gain of these animals. Further studies should be performed to establish the mechanisms of selectivity in increase of lysosomal enzymes in different situations and pathological states.

Acid Phosphatase↗
PubMed1993

Three-dimensional structure of rat acid phosphatase in complex with L(+)-tartrate.

The crystal structure of recombinant rat prostatic acid phosphatase in complex with the inhibitor L(+)-tartrate was determined to 3-A resolution with protein crystallographic methods. The inhibitor binds at the carboxyl end of the parallel strands of the alpha/beta domain. One of the carboxyl groups of the tartrate molecule interacts with the conserved residues Arg-11, His-12, and Arg-15, which form part of the phosphate binding site. Furthermore, the C2 and C3 hydroxyl groups interact with His-257 and Arg-79. The second carboxyl group is close to Arg-79 but makes no direct hydrogen bonds to the protein. A sequence comparison between tartrate-sensitive and -resistant acid phosphatases suggests that these enzymes have different three-dimensional structures.

Acid Phosphatase↗
PubMed1984

Photometric and fluorometric continuous kinetic assay of acid phosphatases with new substrates possessing longwave absorption and emission maxima.

A direct and continuous kinetic method for the photometric and fluorometric determination of various acid phosphatases is described. It is based on new coumarin-derived phosphates, which after enzymatic hydrolysis undergo dissociation to form intensely colored and strongly fluorescent phenolate anions. The latter have absorption maxima ranging from 385 to 505 nm, and fluorescence maxima between 470 and 595 nm. The new substrates were compared with respect to their rate of enzymatic hydrolysis, optimum pH, and detection limits of acid phosphatase from potato and wheat germ. Detection limits of 0.001 unit/ml were found by photometry, and as low as 0.00006 unit/ml by fluorometry. The principal advantages of the new substrates over existing ones are longwave absorptions and emissions, large Stokes shifts, and the low pKa values of the corresponding phenols, thus allowing a direct and continuous assay of acid phosphatase even in weakly acidic solutions.

Acid Phosphatase↗
PubMed1975

Separation of cells exhibiting acid phosphatase activity from disaggregated hamster prostate cells in an isokinetic gradient of Ficoll in tissue culture medium.

Cells exhibiting histochemically demonstrable acid phosphatase were separated from suspensions of hamster prostate cells with velocity and isopyknic sedimentation. Unseparated suspensions of hamster prostate cells contained 57.2 plus or minus 11.3% cells with histochemically apparent acid phosphatase. After the cells were separated by velocity sedimentation in a previously described isokinetic gradient, the purest fractions from the gradient contained 97.2 plus or minus 0.8% cells with histochemically evident acid phosphatase. More than 99% of these separated cells excluded trypan blue. These cells were thought to be the acinar cells of the prostate. Isopyknic sedimentation was not as effective as velocity sedimentation for the purification of these cells.

Acid Phosphatase↗
PubMed1978

Cytogenetic localization of the acid phosphatase-1 gene in Drosophila melanogaster.

A translocation in which a segment of chromosome 3 is inserted into the Y chromosome was found to contain the acid phosphatase-1 gene (Acph-1). In flies hyperploid for that gene, acid phosphatase-1 levels are proportional to the dose of the gene. The locus is placed within the salivary chromosome subdivisions 99D and 99E on the basis of its inclusion in the translocated segment and on the previous placement of the claret locus. Several chromosomal rearrangements involving heterochromatic breakpoints and euchromatic breakpoints adjacent to 99D-99E were tested for possible postiion-effect variegation of acid phosphatase-1. No decrease in the synthesis of the electorphoretic subunit encoded by the relocated gene was observed within any of the rearrangements.

Acid Phosphatase↗
PubMed1980

Ultrastruct and tartrate-resistant acid phosphatase localization in a T-cell hairy-cell leukemia cell line.

Hairy-cell leukemia is characterized clinically in splenomegaly and pancytopenia and pathologically by the proliferation in hematopoietic tissue of cells containing the tartrate-resistant isozyme 5 of acid phosphatase. We have described a patient with a T-lymphocyte variant of this disease. A permanent cell line obtained from the spleen of this patient has the biological and enzymatic characteristics of the fresh leukemic cells. We have used this line to study the surface morphology, ultrastructure, and ultrastructural localization of acid phosphatase in defined T-lymphoid hairy cells. The surface of the cells of the permanent line was smooth but many hair-like projections appeared after exposure to phytohemagglutinin (PHA). There was little acid phosphatase reaction produce visualized when beta-glycerophosphate was used as a substrate. With sodium haphthol AS-BI phosphoric acid heavy deposits were seen in the perinuclear membrane, mitochondria, and rough endoplasmic reticulum. Exposure to PHA and pokeweed mitogen resulted in increased reaction product, suggesting increased enzyme synthesis. Tartrate-resistant acid phosphatase was localized in the same organelles.

Acid Phosphatase↗