Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “ACID PHOSPHATASE”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 1,693 records · Page 94Linked to original sources
PubMed1993

Contents of fructose, citric acid, acid phosphatase, proteins and electrolytes in secretions of the accessory sex glands of the male golden hamster.

Secretions were collected from the ampullary gland, dorsolateral prostate, ventral prostate, coagulating glands and seminal vesicles of male golden hamsters aged 15-20 weeks. The concentrations of total protein, citric acid, fructose, acid phosphatase, chloride, sodium, potassium, calcium, magnesium and zinc were determined. The ampullary gland secreted predominantly citric acid, sodium and acid phosphatase. Zinc was secreted only by the prostatic complex, with the largest quantity coming from the coagulating gland. The highest concentrations of potassium, calcium and magnesium were found in secretions of the ventral prostate. The coagulating gland and dorsolateral prostate were the principal contributors to total protein. The hamster appears to be more related to the mouse than to the rat in terms of the secretory functions of its accessory sex glands.

Acid Phosphatase↗
PubMed1990

[Acid phosphatase and non-specific esterase activities in peripheral blood lymphocytes of coke plant workers].

In 32 workers of coking plants cytoenzymatic reaction was examined in lymphocytes peripheral blood to determine the presence of acid phosphatase and unspecific esterase expressed in total score values. Statistically significant decrease of unspecific esterase activity and lower mean values of acid phosphatase activity were found as compared to the results obtained in the control group. It seems that periodical determinations of cytoenzymatic activity of unspecific esterase in lymphocytes of peripheral blood may be useful in assessment of biological effects of occupational exposure in coking plants workers.

Acid Phosphatase↗
PubMed1986

Distinct specificities of repressible acid phosphatase from yeast toward phosphoseryl and phosphotyrosyl phosphopeptides.

By using [32P]-labeled phosphoaminoacids it has been shown that, at mu molar range concentrations, Tyr-32P but neither Ser-32P nor Thr-32P can be significantly dephosphorylated by highly purified repressible acid phosphatase from Saccharomyces cerevisiae. The phosphopeptide Arg-Arg-Ala-Ser(32P)-Val-Ala however, reproducing the phosphorylation site of pyruvate kinase and previously phosphorylated by cAMP-dependent protein kinase, can be very readily dephosphorylated with favourable kinetic constants (Km 0.28 microM, Vmax = 62 units/micrograms) while its derivatives Ala-Ser(32P)-Val-Ala, Arg-Arg-Ala-Thr(32P)-Val-Ala, Arg-Arg-Pro-Ser(32P)-Pro-Ala as well as other peptides and protein substrates phosphorylated by either protein kinase-C or casein kinase-2 are either unaffected or very slowly dephosphorylated by the phosphatase. Conversely Tyr-32P containing angiotensin, poly (Glu, Tyr) 4:1 and the phosphopeptide Asp-Ala-Glu-Tyr(32P)-Ala-Ala-Arg-Arg-Arg-Gly are all dephosphorylated with kinetic constants comparable to those of free phosphotyrosine (Km 0.2-1 microM; Vmax = 4-10 units/micrograms). It is proposed that, while acid phosphatase exhibits a broad specificity toward phosphotyrosine and phosphotyrosyl polypeptides, it is highly selective toward phosphoseryl sites fulfilling definite structural requirements which are reminiscent of those determining phosphorylation by cAMP-dependent protein kinase.

Acid Phosphatase↗
PubMed1982

Serum prostatic acid phosphatase determination in prostatic diseases: a critical comparison of an enzymatic and a radioimmunologic assay.

A prospective study comparing a new radioimmunologic and a classical enzymatic assay for prostatic acid phosphatase was done to evaluate their respective roles in patients with prostatic diseases. We studied 50 patients with cancer of the prostate, 101 with benign prostatic hypertrophy and 17 with prostatitis as well as patients with nonprostatic malignancy, and various hematological and bone diseases. The results showed a low incidence of elevated values in patients with early cancer of the prostate and a high incidence of false positive values with the radioimmunoassay in patients with benign prostatic diseases, especially prostatitis. These data suggest that tests for serum prostatic acid phosphatase levels remain disappointing in the assessment of prostatic disease regardless of the technique used.

Acid Phosphatase↗
PubMedDate not supplied

[Multiple molecular forms of acid phosphatase of certain tissues at different stages of pig embryonal development].

Disc electrophoresis in polyacrylamide gel was used to perform a comparative study of the quantitative and qualitative composition of multiply molecular forms of acid phosphatase (ES 3.1.3.2) in blood serum, extracts of liver tissues and femoral muscles of pig embryos. 7-12 fractions, possessing the acid phosphatase activity are detected in the investigated tissues as during embryo development. The quantitative and qualitative redistribution and high specificity of multiplied molecular forms of the enzyme are shown for each tissue under study at various stages of embryogenesis which may be used as biochemical indicators in estimating the degree of tissue differentiation under normal and anomalous development of pig embryos.

Acid Phosphatase↗
PubMed1976

An X-ray microanalytical azo dye technique for the localization of acid phosphatase activity.

A new method is described for the histochemical localization of acid phosphatase. Naphthol AS BI, enzymatically released from naphthyl AS BI phosphoric acid, is coupled with diazotized 2,5-dibromoaniline to produce a fine insoluble red azo dye. The histochemical and cytochemical localization of this final reaction product in rat liver is described. In the electron microscope, sites of the azo dye can be detected by X-ray microanalysis of ultrathin cryosections of reactive tissue.

Acid Phosphatase↗
PubMed1987

Analysis of alpha-factor secretion signals by fusing with acid phosphatase of yeast.

In yeast, Saccharomyces cerevisiae, the PHO5 gene encodes the repressible acid phosphatase (APase) whose activity can be easily monitored by either the staining of colonies or by colorimetric assay. Therefore, gene fusions to PHO5 provide a convenient system for structural and functional analysis of yeast genes. We have constructed fusions of the PHO5 gene with a MF alpha 1 gene of yeast to delineate the secretion signal(s) in the alpha-factor leader peptide. Gene fusion between MF alpha 1 and PHO5 codes for a hybrid protein in which the alpha-factor leader peptide of 89 amino acids (aa) directed the export of APase, a periplasmic protein, into the medium. Since the hybrid gene is transcribed from the alpha-factor promoter, expression of the APase activity from these hybrid genes showed cell type-specific regulation. Further analyses of another MF alpha 1-PHO5 fusion showed that only the first 22 aa of the 89-aa alpha-factor leader peptide contained sufficient information for the secretion of APase into the medium. This shows that, in addition to the analysis of gene regulation, PHO5 fusions can be used to study signals involved in the proper localization of proteins.

Acid Phosphatase↗
PubMedDate not supplied

Prostatic acid phosphatase: clinical utility in detection, assessment, and monitoring carcinoma of the prostate.

Prostatic carcinoma is a significant cause of male cancer death. The majority of cases present as incurable disease. The measurement of acid phosphatase has served to confirm clinically suspected disease and staging. The immunochemical methods have increased clinical sensitivity and specificity in detecting curable occult or confined disease, but not significantly so as to warrant mass screening. Prostatic acid phosphatase remains a test for confirming clinical staging of prostatic carcinoma and a response factor to therapy at present.

Acid Phosphatase↗
PubMed1999

The acid phosphatase-1 gene region in the Drosophila species of the subobscura cluster.

The acid phosphatase-1 (Acph-1) gene region was sequenced in three species of Drosophila: D. subobscura, D. madeirensis and D. guanche. These three closely related species, which are included in the obscura group, form the subobscura cluster. The different functional regions of the gene were identified by similarity with the sequence of D. melanogaster. The structure of Acph-1 is conserved in the four species. Average divergence at synonymous and nonsynonymous sites between D. melanogaster and the species of the subobscura cluster is Ks = 1.1354 and Ka = 0.1743, respectively. The rather high Ka value confirms that ACPH-1 is a rapidly evolving enzyme in Drosophila, as previously suggested by immunological studies. Amino acid replacements are not randomly distributed along the gene. In fact, an excess of replacements is detected in exon I, indicating that the signal peptide encoded by this exon evolves even faster than the rest of the protein. Divergence at the Acph-1 gene region is further evidence that D. madeirensis and D. subobscura are more closely related than D. guanche is to any of them. In addition, both silent divergence in noncoding regions and synonymous divergence in the coding region indicate that the split of the D. guanche lineage is about twice as old as the split of the lineages leading to D. madeirensis and D. subobscura. These phylogenetic relationships are, however, not supported by divergence at nonsynonymous sites since the lowest Ka estimate is between D. guanche and D. subobscura.

Acid Phosphatase↗
PubMedDate not supplied

Prostatic acid phosphatase immunoperoxidase staining of cytologically positive effusions associated with adenocarcinomas of the prostate and neoplasms of undetermined origin.

An immunoperoxidase staining technique was employed in an effort to demonstrate prostatic acid phosphatase in sections of the effusion cell blocks in a retrospective investigation of the incidence of malignant prostatic cells in body cavity effusions in 33 patients with histologically confirmed prostatic cancer. An attempt was also made to identify the prostate as a possible anatomic site of origin in 26 patients with an unknown primary but with cytologically positive fluids. Neoplastic cells were identified in the effusion specimens in 21.2% of the patients with confirmed prostatic cancer; the sources, however, were either primary or metastatic carcinomas of nonprostatic origin. None of the cytologic specimens in this study demonstrated a positive prostate-specific acid phosphatase staining reaction, as did the prostatic metastases to the lungs used as controls.

Acid Phosphatase↗
PubMed2001

Characterizations of recombinant human tartrate-resistant acid phosphatase from osteosarcoma: comparison study between recombinant and placental proteins.

We cloned the human tartrate-resistant acid phosphatase (TRAP) gene from human osteosarcoma cells (Saos-2), and produced recombinant human TRAP (rhTRAP) using a baculovirus vector expression system. RhTRAP from Sf9 culture medium was purified by cation exchange chromatography, gel filtration and affinity chromatography. The molecular mass and amino acid composition of the rhTRAP were consistent with the deduced amino acid composition from the TRAP gene. The N-terminal amino acid sequence of rhTRAP was identical to that of TRAP purified from osteoclastoma and hairy cell leukemia spleen. The monoclonal antibodies generated against rhTRAP also reacted to human placental TRAP (pTRAP). The optimum pH of rhTRAP and pTRAP were pH 5.0-5.5 and pH 6.0-6.5, respectively. The enzymatic activities of rhTRAP and pTRAP were activated by reducing agents such as 2-mercaptoethanol, dithiothreitol and ascorbic acid. The activities of rhTRAP and pTRAP were enhanced by Fe2+ ions, but were inhibited by Fe3+ ions. The present results indicate that rhTRAP has similar properties to the native human TRAP, and suggest that the enhancement of TRAP activity by reducing agents might be expressed via the reduction of Fe ions at the metal center.

Acid Phosphatase↗
PubMed1991

Active principle of swine prostate extract: I. Isolation of active principle activating prostatic acid phosphatase and its effect on testosterone uptake of the prostate in castrated rats.

There have been several reports concerning the therapeutic effect of an extract from animal prostates on benign prostatic hypertrophy. Previously, we reported that the swine prostate extract (PE) had the activity to enhance human prostatic acid phosphatase (PAPase) activity in vitro, and to increase the muscular tonicity of the urinary bladder by directly acting upon vesical muscles, suggesting that PE have an activity to elevate the intravesical voiding pressure in vivo. In the present study, it was attempted to isolate such an active principle of PE as activates human prostatic acid phosphatase (PAPase). The finally purified PE (PPE) was assessed as to some physico-chemical and pharmacological properties. 1) PPE was found to be a peptide with a molecular weight of about 8,800, composed largely of neutral amino acids (approximately 70%) and few of aromatic amino acids. 2) PPE activated PAPase in a dose-dependent fashion, resulting in an increase of the enzyme activity approximately twice in a dose of 2 X 10(-5) g/ml of PPE. Furthermore, PPE recovered PAPase activity dose-dependently from the 50% inhibition by 2 X 10(-3) M L-tartaric acid. 3) In castrated rats, the 3H-testosterone uptake of the prostate was significantly suppressed by the oral administration of PPE. PPE might be one of active principles of PE for the therapeutic effect on prostatic hypertrophy.

Acid Phosphatase↗
PubMed2001

Decreased expression of cellular prostatic acid phosphatase increases tumorigenicity of human prostate cancer cells.

PURPOSE: Understanding cell proliferation regulation in hormone refractory prostate cancer may provide answers for novel solutions. Protein tyrosine phosphatases have been thought to have key roles in regulating cell proliferation and be involved in oncogenesis, although to our knowledge their functional roles in human prostate cancer remain unknown. Human prostatic acid phosphatase (PAcP), a major phosphatase in prostate epithelium, has been shown to function as a neutral protein tyrosine phosphatase in these cells. We evaluated the biological significance of cellular prostatic acid phosphatase expression in human prostate cancer cells. MATERIALS AND METHODS: Immunohistochemical testing of human prostate cancer archival specimens was done to evaluate the expression of cellular PAcP. Immunoprecipitation and immunoblotting were performed to determine cellular PAcP and SH2 domain-bearing tyrosine phosphatase-1 levels as well as tyrosine phosphorylation of c-ErbB-2/neu in different human prostate cancer cells. The biological behavior of LNCaP derivative sublines was characterized in vitro and in vivo by soft agar analysis and xenograft animal inoculation. RESULTS: Immunohistochemical staining of human prostate clearly showed that cellular levels of PAcP significantly decreases in prostate cancer cells (p <0.001). The results of biochemical characterization revealed that the cellular level of PAcP but not SHP-1, another differentiation associated protein tyrosine phosphatase, consistently correlated negatively with the growth of several human prostate cancer cell lines. Reintroducing cellular PAcP activity in prostate cancer cells by PAcP complementary DNA transfection resulted in decreased tyrosine phosphorylation of c-ErbB-2/neu, decreased proliferation rates in culture as well as decreased anchorage independent growth in soft agar. The xenograft animal model demonstrated that a higher tumor growth rate as well as larger size is associated with a lower level of cellular PAcP. CONCLUSIONS: Cellular PAcP can down-regulate prostate cancer cell growth, at least partially by dephosphorylating c-ErbB-2/neu. Therefore, decreased cellular PAcP expression in cancer cells may be involved in prostate cancer progression.

Acid Phosphatase↗
PubMed1992

Isolation and analysis of the Penicillium chrysogenum phoA gene encoding a secreted phosphate-repressible acid phosphatase.

We have isolated the genomic sequence encoding a secreted phosphate-repressible acid phosphatase (PHOA) from Penicillium chrysogenum using synthetic oligodeoxyribonucleotide probes. Nucleotide sequence data revealed that this gene consists of two exons of 192 and 1047 bp separated by an intron of 52 bp in length. A sequence encoding a putative signal peptide, resembling known signal sequences of fungi, was identified at the 5'-end of the coding sequence. Northern blot analysis of total cellular RNA indicated that the phoA gene codes for a 1.6-kb transcript. The expression of this gene is regulated at the transcriptional level and is markedly affected by the inorganic phosphate concentration of the growth medium.

Acid Phosphatase↗
PubMedDate not supplied

Ozone sensitivity in aging WI-38 cells based on acid phosphatase content.

Young [16-19 population doubling level (PDL)] and senescing (50-53 PDL) WI-38 cell populations were exposed to 1 ppm ozone for 2 hr and the resultant extracellular and intracellular acid phosphatase concentration was measured. Dose-response curves were also determined for surviving populations of young and old cells after a 1 hr ozone exposure ranging in concentration from 0 to 1.00 ppm. Senescing cells released 8 times more acid phosphatase per million cells than the young cells. Both old and young cells showed a clear dose-response to the 1 hr ozone gradient exposure. However, the older cells demonstrated a consistent 17% average lower survival rate than the young cells. The higher acid hydrolase level in older WI-38 cells is probably related to the lower survival rate observed in the older cells in vitro.

Acid Phosphatase↗
PubMed2004

Activity of hydrolytic enzymes in fungi isolated from diabetic pregnant women: is there any relationship between fungal alkaline and acid phosphatase activity and glycemic control?

Ability to respond to environmental changes and secretion of hydrolases are considered to be important for Candida virulence. In this study we determined and compared the activities of 19 different hydrolases of the fungal strains isolated from diabetic and non-diabetic pregnant women. We also looked for the presence of a relationship between hydrolase activities and glycemic control, and, furthermore, evaluated the influence of gestational age on the activity of hydrolases. Mycological examinations were performed for 119 diabetic pregnant women: 47 with diabetes mellitus type I (DM), 72 with gestational diabetes (GDM), and for 132 healthy women (CON). Samples were collected from the vagina, rectum and oral cavity and cultured on Sabouraud media. The fungal hydrolase activities were evaluated using the API ZYM test (bioMerieux). For the 19 different fungal hydrolases tested, 13 activities were present in the isolated fungal strains. The activity of alkaline phosphatase (ALP) in vaginal strains (p=0.028) and acid phosphatase (ACP) in strains from the vagina (p=0.006) and rectum (p=0.049) was significantly lower in DM than in GDM and CON women. In conclusion, we describe for the first time that fungi isolated from pregnant diabetic women have lower activity of both phosphatases compared to fungi isolated from healthy women. Furthermore, similar differences of mean ALP and ACP activities were observed in the course of pregnancy in strains from the vagina and rectum of DM and CON women. However, strains from DM had lower activity at each stage of pregnancy. The highest activity of ALP and ACP was detected at the beginning, then declined, and had the lowest values between the 24(th) and 33(rd) week of gestation. After that period the activity of both phosphatases increased.

Acid Phosphatase↗
PubMed1976

Isoenzymes of acid phosphatase and non-specific esterases in cultures of neoplastic and normal tobacco tissues.

Axenic cultures of normal, habituated and crown gall teratoma were grown under varying conditions to examine the effects of environment on the expression of neoplastic character. Acid phosphatase patterns on polyacrylamide gels did not vary greatly among tissues although there were differences in acid phosphatase activity between various strains of Agrobacterium tumefaciens, the bacteria which cause crown gall. Certain esterase isoenzymes were found only in tissues grown on specific media, while others were tissue-specific but independent of the nature of the medium. Comparisons of liquid and solid grown cultures revealed that culture conditions also influence esterase expression. Both sunflower and tobacco crown gall tissue contained an esterase not found in habituated or normal tissues, and similar in electrophoretic mobility to an esterase found in extracts of the bacteria that had induced the tumors. The basic difference between the three tissue types studied is the manner in which they respond to a given environment.

Acid Phosphatase↗