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PubMed1990

Choline derivatives increase two different acid phosphatases in Rhizobium meliloti and Pseudomonas aeruginosa.

In Pseudomonas aeruginosa and Rhizobium meliloti several choline derivatives, utilized as the sole carbon and nitrogen source, increase acid phosphatase activity. The enzyme activity of both bacteria could be released into the surrounding medium by EDTA-lysozyme treatment. The R. meliloti acid phosphatase activity of crude periplasmic extracts measured with p-nitrophenylphosphate was not inhibited by the presence of 5 mM choline, betaine, trimethylammonium or phosphorylcholine. The activity could not be detected using phosphorylethanolamine or phosphorylcholine as substrates. Among several phosphoesters tested only pyridoxal-5-phosphate was hydrolyzed at a considerable rate. In 7.5% polyacrylamide slab gel electrophoresis (non-denaturing conditions) of crude extracts obtained from bacteria grown in the presence of serine, glutamate, aspartate or dimethylglycine a phosphatase activity with identical mobility could be detected with alpha-naphthylphosphate or pyridoxal-5-phosphate were used as substrates. In conclusion, although the choline metabolites are capable of increasing acid phosphatase activities in R. meliloti and in P. aeruginosa, there are two different enzymes involved, apparently in different metabolisms.

Acid Phosphatase↗
PubMed1997

The KIPHO5 gene encoding a repressible acid phosphatase in the yeast Kluyveromyces lactis: cloning, sequencing and transcriptional analysis of the gene, and purification and properties of the enzyme.

A secreted phosphate-repressible acid phosphatase from Kluyveromyces lactis has been purified and the N-terminal region and an internal peptide have been sequenced. Using synthetic oligodeoxyribonucleotides based on the sequenced regions, the genomic sequence, KIPHO5, encoding the protein has been isolated. The deduced protein, named KIPho5p, consists of 469 amino acids and has a molecular mass of 52520 Da (in agreement with the data obtained after treatment of the protein with endoglycosidase H). The purified enzyme shows size heterogeneity, with an apparent molecular mass in the range 90-200 kDa due to the carbohydrate content (10 putative glycosylation sites were identified in the sequence). A 16 amino acid sequence at the N-terminus is similar to previously identified signal peptides in other fungal secretory proteins. The putative signal peptide is removed during secretion since it is absent in the mature secreted acid phosphatase. The gene can be induced 400-600-fold by phosphate starvation. Consensus signals corresponding to those described for Saccharomyces cerevisiae PHO4- and PHO2-binding sites are found in the 5' region. Northern blot analysis of total cellular RNA indicates that the KIPHO5 gene codes for a 1.8 kb transcript and that its expression is regulated at the transcriptional level. Chromosomal hybridization indicated that the gene is located on chromosome II. The KIPHO5 gene of K. lactis is able to functionally complement a pho5 mutation of Sacch. cerevisiae. Southern blot experiments, using the KIPHO5 gene as probe, show that some K. lactis reference strains lack repressible acid phosphatase, revealing a different gene organization for this kind of multigene family of proteins as compared to Sacch. cerevisiae.

Acid Phosphatase↗
PubMed1990

Quantitative changes in acid phosphatase, alkaline phosphatase and 5'-nucleotidase activity in rat liver after experimentally induced cholestasis.

Acid phosphatase, alkaline phosphatase and 5'-nucleotidase activities were analyzed cytophotometrically in cryostat sections of rat liver up to 8 weeks after ligation and transsection of the common bile duct. Ligation resulted in cholestasis and induced alterations in both localization and activity of the enzyme investigated. The cellular distribution but not the activity of acid phosphatase changed in liver parenchyma. In control liver, the final reaction product was localized as discrete granules in the bile canalicular region of hepatocytes. The final reaction product was precipitated more diffusely within the cytoplasm after induction of cholestasis, most probably due to increased fragility of lysosomal membranes. In control liver, alkaline phosphatase activity was low and localized in the bile canalicular plasma membranes only. The total parenchymal activity increased threefold after the induction of cholestasis and is considered to be a compensatory mechanism in order to enhance the excretion of bile salts from hepatocytes. 5'-Nucleotidase was present at the bile canalicular and sinusoidal surfaces of plasma membranes of hepatocytes in control liver; total activity in pericentral areas was significantly higher than in periportal areas. Induction of cholestasis resulted in higher total activity and redistribution of the activity over all three surfaces of the plasma membranes, whereas heterogeneity over the different zones of the acinus disappeared. The appearance of the enzyme at lateral plasma membranes is suggested to be related to the formation of new sites for bile salt transport out of the hepatocytes. With respect to all three enzymes studied, alterations of liver parenchymal cells due to a disturbed bile transport were already established during the first week of cholestasis.

5'-Nucleotidase↗
PubMed1981

Seminal plasma fructose, zinc, magnesium and acid phosphatase in cases of male infertility.

Determinations of fructose, zinc, magnesium and acid phosphatase were performed in seminal plasma from male partners in 225 barren couples. No specific changes in the concentrations of these substances could be observed in men showing either visible or palpatory abnormalities of the external genitals, the prostate or of the seminal vesicles, extreme changes in the number, morphology or motility of the sperms, increased sperm antibody titre or abnormal serum levels of testosterone or gonadotrophins. However, when the prostatic fluid contained numerous leukocytes, the concentrations of zinc, magnesium and acid phosphatase were significantly lower than in men having a cytologically normal prostatic fluid. Determinations of these substances may thus be of aid in the diagnosis of chronic prostatovesiculitis.

Acid Phosphatase↗
PubMed1983

Acid phosphatases in the mouse testis: activity changes during development.

The histology and acid phosphatase activities of the developing testes in the mouse, from 4 days of age until maturity, were analyzed. The specific enzyme activity with p-nitrophenyl phosphate as substrate increased after 3 weeks of age and then reached a plateau. Cobalt and zinc markedly increased the specific activity after the third week. After fractionation the testicular homogenate revealed four acid phosphatases. Enzyme I maintained a high activity during the first 3 weeks but steadily declined thereafter. Enzyme II, present in all age groups, showed a moderate increase after the fourth week. Enzymes III and IV were low and declined further during the first 3 weeks with a subsequent increase. This occurred concomitantly with the appearance of spermatids and mature sperm cells. Changes in enzyme activities seem to reflect the alterations in cellular composition of the testis during the developmental process. Enzymes III and IV were probably associated with spermatids and sperm cells.

Acid Phosphatase↗
PubMed1981

Immunofluorescence for prostatic acid phosphatase: clinical applications.

An indirect immunofluorescence technique to detect cells producing prostatic acid phosphatase was used to evaluate 12 biopsies of soft tissue masses of possible metastatic prostatic carcinoma. In 10 patients varying degrees of immunofluorescence were observed, confirming the origin of the primary tumor. Specimens from 34 patients with prostatic carcinoma were obtained either by radical prostatectomy or transurethral resection of the prostate. A comparison of histological grade (Gleason), semiquantitative immunofluorescence for prostatic acid phosphatase and hormonal responsiveness was done. There was a suggestion of higher hormonal responsiveness in the group with a low Gleason score and a high percentage of positive immunofluorescence that presently cannot be evaluated completely since some patients still are under therapy. This method may be used in the future in conjunction with other techniques, such as androgen receptors, to define a population of patients most likely to respond to hormonal manipulation.

Acid Phosphatase↗
PubMed1995

Differential androgen regulation of rat prostatic acid phosphatase transcripts.

Steady-state levels of the mRNAs encoding rat prostatic acid phosphatase (rPAP) were measured from the ventral prostate of rats after castration and testosterone replacement. The longest and the most abundant mRNA molecule (4.9 kb) of the rPAP gene was quite resistant to the hormonal status of the prostate, whereas its medium-sized transcript (2.3 kb) and the shortest one (1.5 kb) were up-regulated by androgens. For comparison, we also analyzed the prostatic mRNA levels of rat lysosomal acid phosphatase (rLAP), whose gene expression is not considered to be hormonally dependent. Only modest variation was observed in the rLAP transcript after androgen withdrawal and replacement. Corresponding protein level investigations are analogous with our regulation studies, particularly in the case of 1.5-kb rPAP mRNA.

Acid Phosphatase↗
PubMed1982

Enzyme histochemical studies on acid phosphatase in the cerebellum of young Gunn rats.

Cerebella from 20-day-old homozygous (jj) and heterozygous (j+) Gunn rats were tested histochemically for the presence of acid phosphatase. The j+ rat cerebellum as well as the jj rat cerebellum with wet weights over 120 mg showed a strong acid phosphatase activity in the pia mater and in endothelial cells. A strong acid phosphatase activity was also recognized in small cells with a diameter of about 8 micrometers and large cells with a diameter of about 25 micrometers in the hypoplastic cerebellum of jj rats. The small cells were present in the lingula, centralis, culmen, declive, tuber, pyramis, and dorsal part of the uvula of the jj rat cerebellum with wet weight below 120 mg. The large cells were observed only in severely damaged lobes. Neither small cells nor large cells were found in the nodulus even in a cerebellum with a high degree of hypoplasia. Slightly damaged cerebella with wet weight of 100 to 150 mg showed hypoplasia mainly in the anterior lobe including the lingula, centralis, and culmen as well as in the declive and tuber, where no small cells were detected.

Acid Phosphatase↗
PubMed1982

Age-associated changes in acid phosphatase characteristics in rat ventral prostate and other organs.

Certain characteristics of acid phosphatase in the adult male rat are under androgenic control. In further investigations of this control, (1) the polyacrylamide gel electrophoretic pattern of enzyme activity, (2) enzyme specific activity, and (3) the extent of inhibition of enzyme activity by 1-tartrate were examined for prostate, seminal vesicles, kidney, liver and testes from immature, maturing, young, and old mature adult rats. On gel electrophoresis, lysosomal acid phosphatase activity was found for all tissues from all groups of animals. Secretory enzyme was found for the prostate gland, but only after maturation (it appeared between days 28 and 35). At the same time the percent inhibition of activity by tartrate decreases. For the other tissues, the percent inhibition by tartrate increases for the liver and seminal vesicles but not for the kidney and testes. These changes may reflect alterations in lysosomal enzyme characteristics and can be related to known changes in androgen production throughout the life span of the rat.

Acid Phosphatase↗
PubMed1986

Purification and characterization of the extracellular acid phosphatase of Leishmania donovani.

A tartrate sensitive acid phosphatase activity was purified from culture supernatants of Leishmania donovani promastigotes grown in a macromolecule-free defined medium. Purification was accomplished by ultrafiltration, lentil lectin affinity chromatography, and sucrose density gradient ultracentrifugation. This enzyme was determined to be an acid glycoprotein containing 0.37 mg hexose per mg protein. A molecular weight of 134 000 by sucrose density gradient centrifugation was observed, although on molecular sieve chromatography the enzyme eluted with an apparent molecular weight of greater than 700 000. The specific activity of the purified enzyme was greater than 200 mumol min-1(mg protein)-1 when assayed with 4-methylumbelliferylphosphate as the substrate. In addition to various hexose phosphates, the enzyme hydrolyzed phosphorylated amino acids, in particular phosphotyrosine. The purified enzyme was heterodisperse with respect to both protein and activity staining patterns upon polyacrylamide gel electrophoresis.

Acid Phosphatase↗
PubMed1964

CYTOCHEMICAL OBSERVATIONS ON THE RELATIONSHIP BETWEEN LYSOSOMES AND PHAGOSOMES IN KIDNEY AND LIVER BY COMBINED STAINING FOR ACID PHOSPHATASE AND INTRAVENOUSLY INJECTED HORSERADISH PEROXIDASE.

After incubation of formalin-fixed, frozen sections of kidney and liver from peroxidase-treated rats in an azo dye medium for acid phosphatase, and after subsequent incubation of the same sections with benzidine, phagosomes were stained blue and lysosomes were stained red in the same cells. It was observed that newly formed phagosomes were separate from preexisting lysosomes in the tubule cells of the kidney and in the Kupffer cells of the liver at early periods after treatment with peroxidase. At later periods, the color reactions for acid phosphatase and peroxidase occurred in the same granules. The reaction of peroxidase decreased gradually and disappeared from the phago-lysosomes after 2 to 3 days, whereas the reaction for acid phosphatase persisted. In the liver, most of the injected protein was concentrated in large phagosomes located at the periphery of the cells lining the sinusoids. The peribiliary lysosomes showed a relatively weak reaction for peroxidase in the proximity of the portal veins. After pathological changes of permeability, phagosomes and lysosomes lost their normal location and fused, in the interior of many liver cells, to form large vacuoles or spheres. The effects of a reduced load of peroxidase and the effects of the pretreatment with another protein (egg white) on the phago-lysosomes of the kidney were tested. The relationship of the fusion of phagosomes with lysosomes to the size of normal and pathological phago-lysosomes was discussed.

Acid Phosphatase↗
PubMed1989

Starfish sperm-oocyte jelly binding triggers functional changes in cortical granules. A study using acid phosphatase and ruthenium red ultrastructural histochemistry.

Starfish oocytes were examined before fertilization, immediately after insemination, and during the cortical reaction by means of acid phosphatase and ruthenium red ultrastructural histochemistry. Oocyte cortical granules are composed of a lamellar body and a surrounding matrix which is subdivided into dense and light portions. In unfertilized oocytes cortical granules are not stained by ruthenium red but show a weak acid phosphatase activity in the light portion of the granule matrix. Immediately after the adhesion of the spermatozoon to the oocyte jelly coat, the light matrix portion of cortical granules appears stained by ruthenium red and shows a strong acid phosphatase activity. During the cortical reaction, cortical granules are released into the perivitelline space and the lamellar body, surrounded by the stained matrix, fuses with the fertilization envelope. Our data suggest that membrane permeability changes and enzyme activation occur in the egg when the spermatozoon binds to the oocyte jelly coat.

Acid Phosphatase↗
PubMed1972

Alkaline and acid phosphatase in murine leukemia.

Alterations for acid and alkaline phosphatase levels and their pattern of splenic and lymph node activity in normal and virus-induced lymphoblastic leukemia were studied. Enzyme levels were examined by using both cytochemical and biochemical procedures. The GC leukemia virus, a ribonucleic acid murine virus antigenically related to the Rauscher-Moloney viruses, was used to stimulate acid and alkaline phosphatase by producing lymphomaceous disease in Ha/ICR mice. With the Burstone and Gomori cytochemical procedures, both enzymes were found in higher than normal levels in lymphomaceous spleen and lymph nodes. Confirmation of the cytochemical studies was obtained by enzyme assay of cell-free homogenates in each case with the exception of spleen acid phosphatase. The discrepancy between the cytochemical tests which showed significant elevation of spleen acid phosphatase and the enzyme assays which failed to reveal such elevation could be due to a labile acid phosphatase isozyme which is lost on cellular disruption during homogenate preparation. A significant spleen alkaline phosphatase specific activity elevation above normal was found with a 50% incidence only when leukemic spleen wet weight increased nearly threefold its normal value. This result suggests that alkaline phosphatase elevation is a secondary event occuring after the onset of disease and is not a fundamental metabolic alteration concerned with the onset of murine lymphoblastic leukemia.

Acid Phosphatase↗
PubMed2000

Purification and characterization of an acid phosphatase from the commercial mushroom Agaricus bisporus.

Acid phosphatase [AP; EC 3.1.3.2], a key enzyme involved in the synthesis of mannitol in Agaricus bisporus, was purified to homogeneity and characterized. The native enzyme appeared to be a high molecular weight type glycoprotein. It has a molecular weight of 145 kDa and consists of four identical 39-kDa subunits. The isoelectric point of the enzyme was found at 4.7. Maximum activity occurred at 65 degrees C. The optimum pH range was between 3.5 and 5.5, with maximum activity at pH 4.75. The enzyme was unaffected by EDTA, and inhibited by tartrate and inorganic phosphate. The enzyme exhibits a Km for p-nitrophenylphosphate and fructose-6-phosphate of 370 microM and 3.1 mM, respectively. A broad substrate specificity was observed with significant activities for fructose-6-phosphate, glucose-6-phosphate, mannitol-1-phosphate, AMP and beta-glycerol phosphate. Only phosphomonoesters were dephosphorylated. Antibodies raised against the purified enzyme could precipitate AP activity from a cell-free extract in an anticatalytic immunoprecipitation test.

Acid Phosphatase↗
PubMed1976

Histochemical studies of the development of alkaline and acid phosphatase activities in the ovary and oviduct of the fowl (Gallus domesticus).

Alkaline and acid phosphatase activities were studied in the ovary and oviducts of pullets from the age of 2-32 weeks. Adult fowls were similarly studied. Alkaline phosphatase activity was present only in the glandular grooves and crypts of the immature oviducts. Alkaline phosphatase activity appeared at the pits of epithelial evaginations as glandular formation commenced. The young, non-secreting glands also showed the enzyme activity. But in the mature oviduct, alkaline phosphatase activity was confined to only the uterovaginal glands or sperm host glands and the epithelium of the vagina. In the ovary, alkaline phosphatase activity in the theca interna increased as the diameter of the follicles increased. Acid phosphatase activity was not present in the ovary, but in the oviduct, the enzyme activity was present in the uterine (shell gland) glands and in the uterovaginal epithelium and glands (sperm host glands). Alkaline phosphatase activity in the ovarian follicles and in the immature oviduct is thought to be related to histodifferentiation of these structures.

Acid Phosphatase↗
PubMed1974

Steroid effect on the release of the lysosomal enzyme acid phosphatase in shock.

The effect of corticosteroids on cellular resistance in shock was studied by serial measurement of the serum concentration of the lysosomal enzyme acid phosphatase in untreated and steroid dogs subjected to hemorrhagic, endotoxin and cardiogenic shock. In each shock category, elevation in serum acid phosphatase was significantly less in steroid treated dogs as compared to untreated animals at corresponding time intervals. This difference was most apparent in endotoxin shock, next in hemorrhagic shock and least in cardiogenic shock. Steroid treatment also reduced the serum lactate increment in hemorrhagic and cardiogenic shock and delayed or reduced the onset and severity of the occurring acidosis, an apparent reflection of the ability of steroids to promote increased tissue perfusion. In addition, steroid treatment increased or prolonged survival in all three shock groups. By showing that glucocorticoids affect a reduction in the release of the lysosomal enzyme acid phosphatase during shock, the study offers direct evidence that steroids enhance cellular resistance to shock stress in the dog. Whether this salutary effect is due solely to the ability of steroids to stabilize cellular membranes or is in part secondary to promoting improved tissue hemodynamics could not be established. The interpretation and clinical application of these results must take into account the possibility of a species specific response.

Acid Phosphatase↗
PubMed1998

Soybean seed acid phosphatases: unusual optimum temperature and thermal stability studies.

In contrast to other acid phosphatases, four cytoplasmic isoforms (AP1, AP2, AP3A, and AP3B) purified from mature soybean seeds presented high activities at temperatures above 80 degrees C, when p-nitrophenylphosphate (p-NPP) was utilized as substrate. However, with tyrosine phosphate and inorganic pyrophosphate as substrates, maximum activities were observed at temperature of 60 degrees C during 10 min reaction. In the absence of substrate, enzymes lost only 20% activity after 60 min at 60 degrees C; the isoforms AP3A and AP3B retained 30% of activity at 70 degrees C after 60 min and all the isoforms were inactivated at 80 degrees C, after 5 min. Thermal inactivation studies indicated that the soybean enzymes showed different temperature dependences in relation to most plant acid phosphatases. A best protective effect was observed when the isoforms were preincubated, at 70 degrees C, with phosphate (10 mM) and p-nitrophenol (10 mM) which indicates that the enzyme inactivation was prevented only in the presence of both reaction products.

Acid Phosphatase↗