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 991 records · Page 55Linked to original sources
PubMed1985

[Prostatic acid phosphatase measured by immunoenzyme assay].

Prostatic acid phosphatase was determined with Merck-Kanto's test kit on the cases of prostatic cancer experienced at our University Hospital from August in 1983 to February in 1985. Untreated cases were 4 stage A cases, 1 stage B case, 3 stage C cases, 3 stage D1 cases and 12 stage D2 cases. Nine cases were determined before and after hormonal treatment. From 67 controlled cases and 19 recurrent cases, 144 and 56 samples were selected, respectively. This method showed good reproducibility and even the serum stored at -80 degrees C after separation could be used for determination by addition of tartrate just before the measurement. The occurrence of abnormal values in untreated prostatic cancer cases, was 0% for stage A, 1 case for stage B, 33% for stage C and D1 and 75% for stage D2. Hormonal treatment decreased the high values of 5 cases and 1 case returned to normal. Compared to the recurrent cases, controlled cases showed a significantly larger ratio of negative, and it suggests that the test is useful for follow-up. Prostatic hypertrophy showed the increase of the value in 6% of the cases. Both prostatitis and urinary tract stone cases remained in the normal range.

Acid Phosphatase↗
PubMed1982

A comparative study of the use of monoclonal antibodies using three different immunohistochemical methods: an evaluation of monoclonal and polyclonal antibodies against human prostatic acid phosphatase.

The use of immunohistochemical methods has been advocated for the detection and localization of prostatic acid phosphatase in paraffin sections of human prostate. This article explores the possible advantages of utilizing monoclonal antibodies in this method. Monoclonal antibodies, specific for human prostatic acid phosphatase, were integrated into three different immunohistochemical procedures. In the first method, a three-layer peroxidase-antiperoxidase (PAP) system was employed; the monoclonal antibody was followed by rabbit bridge antibody directed against mouse immunoglobulin and mouse PAP complex. The second method was a three-layer system utilizing biotin-labeled horse anti-mouse antibody as "bridge" antiserum between the primary monoclonal antibody and an avidin-biotin-horseradish peroxidase complex. The third method was a four-layer system; the monoclonal antibody was followed by rabbit anti-mouse serum, swine anti-rabbit immunoglobulin as the bridge antibody and rabbit PAP complex. It was found that some, but not all, monoclonal antibodies can be used for the detection of prostatic acid phosphatase in paraffin sections. The four-layer PAP method was found to be the most sensitive method of the three systems tested; however, the avidin-biotin method required the least amount of time. No significant difference in the quality of staining was observed between monoclonal antibodies and carefully absorbed conventional antiserum.

Acid Phosphatase↗
PubMed1985

Isoenzyme studies in human leukemia-lymphoma cells lines--II. Acid phosphatase.

This report describes the qualitative acid phosphatase (acP) isoenzyme profiles detected in permanent human hematopoietic cell lines. The acP activity was separated into its isoenzymes by isoelectric focusing on horizontal thin-layer polyacrylamide gels. The pattern of acP isoenzyme was investigated in a total of 86 cell lines. These cell lines were classified into five groups on the basis of their phenotypes characterized in the multiple marker analysis: 74 leukemia-lymphoma cell lines (26 T-, 34 B-, 6 myelomonocytic, 8 Non-T, Non-B cell lines) and 12 so-called 'normal' Epstein-Barr virus transformed B-lymphoblastoid cell lines. Their immunological features had been analysed in detail by use of a large panel of poly- and monoclonal antibodies which led to a further subclassification into stages of differentiation. A progressive increase in number and staining intensity of the isoenzymes which paralleled the expression of surface markers at different stages of differentiation along their developmental pathway was seen in the T- and B-leukemia-lymphoma cell lines. Some cell lines whose isoenzyme profiles did not correspond to the stage of differentiation as evidenced by surface antigen analysis might represent good examples of deranged gene expression in otherwise normally programmed malignant cells, i.e. in our study a mismatch between the isoenzymatic and immunological phenotypes. The tartrate-resistant isoenzyme was detected in 9 out of 74 leukemia-lymphoma cell lines (4 T-, 2 B-, 1 myelomonocytic, 2 Non-T, Non-B cell lines) and in 10 out of 12 normal B-lymphoblastoid cell lines; the only one studied hairy cell leukemia cell line did not express this isoenzyme. The relative specificity of the tartrate-resistant acP is discussed in detail. No leukemia-lymphoma specific isoenzyme or an additional isoenzyme which was not seen in normal hematopoietic cells could be observed. Nor did we find an isoenzyme or isoenzyme pattern characteristic for a certain cell lineage. This underlines the necessity of a combined analysis using markers from different disciplines in the 'multiple marker analysis' in order to accurately characterize normal and malignant blood cells. Furthermore, our results support the concept of maturation arrest at particular stages of differentiation together with the theory of normal gene expression in leukemic cells equivalent to that in their normal counterparts.

Acid Phosphatase↗
PubMed1986

Demonstration of various acid hydrolases and preliminary characterization of acid phosphatase in Naegleria fowleri.

Extracts of the pathogenic ameba Naegleria fowleri, prepared by freeze-thawing and sonication, were analyzed for their content of various hydrolytic enzymes that have acid pH optima. The organism is rich in acid phosphatase activity as well as a variety of glycosidases which include beta-glucosidase, beta-galactosidase, beta-fucosidase, alpha-mannosidase, hexosaminidase, arylsulfatase A, and beta-glucuronidase. The crude extract contained only negligible levels of sphingomyelinase, neuraminidase, or arylsulfatase B. All of the hydrolases exhibited higher activity at pH 5.5 than at 7.0, indicating that they are truly "acid" hydrolases. In general, after centrifugation (100,000 g, 1 h), except for arylsulfatase B, more than half of the activity of each of the various hydrolases was recovered in the supernatant fraction. The acid phosphatase in the high-speed supernatant was purified 45-fold (32% yield) by chromatography on QAE-Sephadex and Sephadex G-200 and shown to have the following properties: pH optima, 5.5; Km (4-methylumbelliferyl phosphate), 0.60 mM; molecular weight (estimated by gel filtration chromatography), 92,000; inhibited by heteropolymolybdate complexes but not by L(+) sodium tartrate (0.5 mM) or sodium fluoride (0.5 mM). In addition, unlike the tartrate-resistant acid phosphatase of Leishmania donovani, the major acid phosphatase of N. fowleri is less than 5% as effective in inhibiting superoxide anion production by f-Met-Leu-Phe-stimulated human neutrophils. The finding of high levels of a number of acid hydrolases in Naegleria fowleri raises several questions that merit further study: Do the hydrolases perform a housekeeping function in this single cell eukaryote or do they play some role in the pathogenic process that ensues when the organism infects a suitable host?

Acid Phosphatase↗
PubMed1985

The type 5, acid phosphatase from spleen of humans with hairy cell leukemia. Purification, properties, immunological characterization, and comparison with porcine uteroferrin.

The spleens of patients with hairy cell leukemia contain high levels of a tartrate-insensitive, cationic, acid phosphatase (the human Type 5 isozyme). This phosphatase has been purified by a procedure which involves only two chromatographic steps: CM-cellulose chromatography and immunoaffinity chromatography on sheep antibodies generated against porcine uteroferrin. Uteroferrin is an abundant iron-containing acid phosphatase that can be recovered readily from porcine uterine secretions. Like uteroferrin, the purified human Type 5 phosphatase is a glycoprotein of molecular weight about 34,000. It contains two atoms of iron/molecule. The human phosphatase and uteroferrin also resemble each other closely in electrophoretic mobility, substrate specificity, and response to a variety of activators and inhibitors. Mouse monoclonal antibodies have been raised to uteroferrin and to the human Type 5 phosphatase. Three monoclonal antibodies which bind with high affinities to distinct sites on the uteroferrin molecule also recognize the human spleen enzyme, but bind to it with much lower affinity. These antibodies also recognize cationic acid phosphatases purified from bovine and rat spleens. A monoclonal antibody raised against the human enzyme, but selected for binding to uteroferrin, appears to recognize a relatively conserved site on all four phosphatases. We conclude that the human Type 5 isozyme belongs to a growing class of structurally related, iron-containing acid phosphatases which includes the iron-transport protein, uteroferrin.

Acid Phosphatase↗
PubMed2006

Development and characterization of novel monoclonal antibodies against tartrate-resistant acid phosphatase 5.

Serum band 5 tartrate-resistant acid phosphatase (TRACP 5; EC 3.1.3.2) is a glycoprotein that exists as two very similar isoforms, TRACP 5a and TRACP 5b. The similarity of these two isoforms has made it difficult to establish monoclonal antibodies specific for either isoform. We report here the development of a monoclonal antibody with high specificity for TRACP 5b. We prepared TRACP 5b antigens from four sources: TRACP 5b purified from human bone, recombinant TRACP 5 from Escherichia coli, recombinant TRACP 5 from insect cells, and a synthetic TRACP 5b peptide. Thirty-seven mice were each immunized with 1 of the 4 different TRACP antigens to generate 473 antibody-producing clones. Three of these clones, Trk27, Trk49, and Trk62, reacted with TRACP 5b. These three clones were all established from mice exposed to native bone TRACP 5b antigen. In fact, none of the other antigens were able to generate anti-TRACP 5b monoclonal antibodies in mice. Furthermore, Trk62 interacted more strongly with TRACP 5b than with TRACP 5a. These results suggested that although recombinant proteins can be effective antigens, the native TRACP 5 protein might be more effective at generating monoclonal antibodies of greater specificity due to its more faithful representation of the native three-dimensional structure of the protein.

Acid Phosphatase↗
PubMed2002

Heterologous expression and characterization of recombinant purple acid phosphatase from red kidney bean.

Purple acid phosphatases (PAPs) are dinuclear metallohydrolases of widespread occurrence. In a first step to understand structure-function relationship of PAP from red kidney bean (kbPAP), we cloned its cDNA and functionally expressed the enzyme in insect cells. kbPAP cDNA encodes a protein of 459 amino acids with 99% identity to the published primary structure (T. Klabunde et al., Eur. J. Biochem. 226 (1994) 369-375). N-terminally the cDNA encodes 27 amino acids with characteristics for a signal directing the nascent protein to the endoplasmic reticulum. A baculovirus vector was constructed containing cDNAs of kbPAP and green fluorescent protein, the latter to serve as transfection and infection marker. Heterologous expression in High Five insect cells afforded a dimeric, disulfide-linked phosphatase of 110 kDa, identical to the mass of native kbPAP. Purification in three steps yielded 1.5 mg recombinant protein per liter of culture medium with a specific activity of 266 units/mg, slightly exceeding that of native kbPAP. The recombinant protein was functionally indistinguishable from native kbPAP, despite differences in glycosylation and sensitivity to redox reagents.

Acid Phosphatase↗
PubMed1984

[Localization of alkaline and acid phosphatases in the testes and epididymis of calves during postnatal development].

A histochemical investigation was carried out after Gomori's method on the activity and localization of the alkaline and acid phosphatase in the testis and epididymis of 28 calves of the Black-and-white breed as dependent on their age--from the first day following birth to the age of 12 months, divided into 14 test groups. It was found that both enzymes had analogous localization in the testis as well as in the various portions of the epididymis, however, the activity of the alkaline phosphatase was higher as compared to that of the acid phosphatase. While in the interstitium of the testis and epididymis on the 1st, 15th, and 30th day following birth the alkaline phosphatase had low activity the acid phosphatase on the same dates was found in the epididymis only.

Acid Phosphatase↗
PubMed1985

Age-related changes of activity of acid phosphatase in PHA-stimulated lymphocytes.

Peripheral blood lymphocytes of 70-year-old individuals as well as spleen cells of 18-month-old Balb/c mice were characterized by diminished activity of acid phosphatase in relation to the activity of that enzyme in cells from young subjects. Simultaneously performed histochemical tests revealed that aging process in both species examined was accompanied by a reduction of the number of cells, disclosing the activity of acid phosphatase. Age-related differences with regard to the level of acid phosphatase became more pronounced after stimulation of cells with PHA. The decrease of acid phosphatase activity during aging is discussed in relation to the function of lymphocytes.

Acid Phosphatase↗
PubMed1988

Bone scintigraphy, radiographic survey and prostatic acid phosphatase in patients with prostatic carcinoma. A comparison of sensitivity.

In 62 patients with histologically confirmed carcinoma of the prostate bone scintigraphy, radiographic survey and serum prostatic acid phosphatase determinations were carried out to evaluate the progression of the disease and to compare the relative sensitivity of the diagnostic tools. Thirty-five patients had scintigraphic evidence of skeletal metastases, whereas abnormal X-ray survey and elevated prostatic acid phosphatase levels were found in only 4 and 19 patients, respectively, all of whom had positive scintigraphic findings. Radiographic evidence of metastases was not found in any of the patients with normal scintigraphy, while elevated prostatic acid phosphatase was found in two patients. It is concluded that bone scintigraphy is far more sensitive than either radiographic survey or determination of prostatic acid phosphatases in the diagnosis of skeletal involvement in prostatic carcinoma, and should be the method of choice for this purpose.

Acid Phosphatase↗
PubMed1983

Acid phosphatase activity of human gingival fibroblasts measured using a simultaneous coupling semi-permeable membrane technique.

Acid phosphatase activity has been measured in cultured human gingival fibroblasts using a validated histochemical simultaneous coupling semi-permeable membrane technique. The histochemical reaction was linear over a three hour incubation period and had a pH optimum of 5.0. The activity was not increased by prior exposure to hypotonic acetate buffer and was inhibited by fluoride and molybdate but not by formaldehyde. These results indicate that the semi-permeable membrane technique described may be used for observing and measuring acid phosphatase activity in cultured fibroblasts. From results obtained using inhibitors, it appears that in these cells most of the acid phosphatase observed is lysosomal. The absence of any activation of activity following pre-incubation with hypotonic buffer indicates that the method is not suitable for monitoring lysosomal membrane function.

Acid Phosphatase↗
PubMed1977

Bone marrow acid phosphatase: another look.

Recent reports have indicated that bone marrow acid phosphatase is the most sensitive test in detecting bony metastases. The experience reported herein suggests that falsely positive results may be common, especially in patients with primary hematologic disorders. A plea is made that caution be given to the interpretation of this test so that some patients will not be denied appropriate therapy and the role of bone marrow acid phosphatase can be better defined by long-term followup in such patients.

Acid Phosphatase↗
PubMed1995

Characterization of the mouse tartrate-resistant acid phosphatase (TRAP) gene promoter.

Tartrate-resistant acid phosphatase (TRAP) is an iron-binding protein that is highly expressed in osteoclasts. To characterize the regulation of TRAP gene expression, progressive 5' and 3' deletions of a 1.8 kb fragment containing the 5'-flanking sequence were fused to a luciferase reporter gene. Two nonoverlapping regions of this 1.8 kb fragment had promoter activity. The upstream promoter (P1) was located within the region from -881 bp to -463 bp relative to the ATG, while the downstream promoter (P2) was located between -363 bp to -1 bp in a region we have previously shown to be an intron in transcripts originating from the upstream promoter. A putative repressor region for the P2 promoter at -1846 bp to -1240 bp and a putative enhancer region at -962 bp to -881 bp relative to the ATG were identified. PCR analysis of promoter-specific transcription of the TRAP gene in various murine tissues showed that both promoters were active in several tissues. Transferrin-bound iron increased P1 promoter activity 2.5-fold and hemin decreased P1 promoter activity, but neither had any effect on P2 activity. These data show that the transcriptional regulation of the TRAP gene is complex and that iron may play a key role in TRAP gene regulation.

Acid Phosphatase↗
PubMed2006

APHO1 from the yeast Arxula adeninivorans encodes an acid phosphatase of broad substrate specificity.

The extracellular acid phosphatase-encoding Arxula adeninivorans APHO1 gene was isolated using degenerated specific oligonucleotide primers in a PCR screening approach. The gene harbours an ORF of 1449 bp encoding a protein of 483 amino acids with a calculated molecular mass of 52.4 kDa. The sequence includes an N-terminal secretion sequence of 17 amino acids. The deduced amino acid sequence exhibits 54% identity to phytases from Aspergillus awamori, Asp. niger and Asp. ficuum and a more distant relationship to phytases of the yeasts Candida albicans and Debaryomyces hansenii (36-39% identity). The sequence contains the phosphohistidine signature and the conserved active site sequence of acid phosphatases. APHO1 expression is induced under conditions of phosphate limitation. Enzyme isolates from wild and recombinant strains with the APHO1 gene expressed under control of the strong A. adeninivorans-derived TEF1 promoter were characterized. For both proteins, a molecular mass of approx. 350 kDa, corresponding to a hexameric structure, a pH optimum of pH 4.8 and a temperature optimum of 60 degrees C were determined. The preferred substrates include p-nitrophenyl-phosphate, pyridoxal-5-phosphate, 3-indoxyl-phosphate, 1-naphthylphosphate, ADP, glucose-6-phosphate, sodium-pyrophosphate, and phytic acid. Thus the enzyme is a secretory acid phosphatase with phytase activity and not a phytase as suggested by strong homology to such enzymes.

Acid Phosphatase↗
PubMed2006

Structure and expression of two genes encoding secreted acid phosphatases under phosphate-deficient conditions in Pholiota nameko strain N2.

Twenty-three polypeptides secreted in response to a deficiency of inorganic phosphate (Pi) were previously found by two-dimensional polyacrylamide gel electrophoresis analysis in mycelia of Pholiota nameko strain N2. In this study, N-terminal sequencing revealed three of them to be identical to known acid phosphatases of P. nameko strain N114. Two cDNAs and the corresponding genomic DNAs of genes PNAP1 and PNAP2 which encode two of the three acid phosphatases were cloned. The deduced amino acid sequences of PNAP1 and PNAP2 showed high similarity to other fungal acid phosphatases and contained a putative catalytic active site of acid phosphatase. PNAP1 and PNAP2 are comprised of five and seven exons interrupted by four and six introns, respectively. Their promoter regions include two cis-acting elements found in Pi deficiency-inducible genes of Saccharomyces cerevisiae, together with several known functional elements such as a TATA box. Northern blot analysis showed that PNAP1 and PNAP2 are expressed in response to a deficiency of Pi.

Acid Phosphatase↗
PubMed1975

[Activity of acid phosphatase and succinate and dehydroorotate dehydrogenases during the interaction of allogeneic lymphocytes and target cells in tissue culture].

A study was made of the activity of acid phosphatase in interaction of lymphocytes and target cells; it was shown that in the lymphocytes its greatest increase occurred in the 1- and sometimes in the 3-hour cultures; sometimes the activity of the enzyme in the L-cells increased by the 3rd-6th hour. The initial activity of acid phosphatase was greater in the immune lymphocytes; later, on their addition to the L-cell culture, there was no significant difference in the changes in the activity of the enzyme in the immune and normal lymphocytes. In the L-cells the activity of acid phosphatase was lower on addition of normal lymphocytes in comparison with the immune ones. The activity of dehydrogenases in the lymphocytes increased by the 3rd hour of the incubation period and was greater in the immune lymphocytes than in the normal ones. The activity of the succininc- and dehydroorotic dehydrogenases altered practically at the same periods in the L-cells as in the lymphocytes. The intensification of the activity of the redox enzymes and of the acid phosphatase during the first hours of contact pointed to the rapid activation of the effector lymphocytes.

Acid Phosphatase↗
PubMed1989

Ultrastructural localization of tartrate-resistant, purple acid phosphatase in rat osteoclasts by histochemistry and immunocytochemistry.

The intracellular localization of the tartrate-resistant purple acid phosphatase in osteoclasts of developing rat bone has been determined immunocytochemically using an antiserum to the purified bone-derived purple acid phosphatase. The localization of the immunoreactivity was compared with the results of enzyme histochemistry using p-nitrophenylphosphate as substrate and 10 mM tartrate. Both methods revealed the presence of the enzyme in numerous vesicles of various sizes up to 2-3 microns in diameter and in granules. There was no immunoreactivity in the Golgi apparatus, and tartrate completely inhibited the histochemical activity of this organelle. No consistent extracellular activity could be detected, nor was any reaction product observed at the ruffled border. The localization of the tartrate-resistant purple acid phosphatase in osteoclasts is consistent with an intracellular function for this enzyme.

Acid Phosphatase↗
PubMed1990

Calcitonin gene-related peptide in primary afferent neurons of rat: co-existence with fluoride-resistant acid phosphatase and depletion by neonatal capsaicin.

Immunohistochemical and histochemical techniques were used to re-examine the extent to which neonatal capsaicin treatment depletes calcitonin gene-related peptide in the dorsal horn of the spinal cord, to determine the localization of calcitonin gene-related peptide in relation to that of fluoride-resistant acid phosphatase in lumbar dorsal root ganglia, and to compare the distribution of these primary afferent markers in the dorsal horn. A substantial depletion of calcitonin gene-related peptide was observed in the dorsal horn of adult rats treated neonatally with capsaicin suggesting that a large proportion of this peptide in the dorsal horn is contained within capsaicin-sensitive primary afferent fibers. In dorsal root ganglia 30% of all or 44% of small- and medium-sized calcitonin gene-related peptide-immunoreactive cells were positive for fluoride-resistant acid phosphatase. Conversely, 50% of cells positive for the phosphatase enzyme also displayed immunoreactivity for the peptide. In lamina II of the dorsal horn calcitonin gene-related peptide and fluoride-resistant acid phosphatase were found to have an overlapping distribution. The presence of fluoride-resistant acid phosphatase in a substantial proportion of neuropeptide-containing primary sensory neurons suggests a lack of segregation of sensory neuronal populations into peptide- and non-peptide-containing subgroups at least on the basis of non-peptide neurons defined as those containing fluoride-resistant acid phosphatase.

Acid Phosphatase↗