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At least 433 records · Page 24Linked to original sources
PubMed1998

Cloning and analysis of the promoter activity of the human prostatic acid phosphatase gene.

Human prostatic acid phosphatase (PAP) has been proposed to be a prostate-epithelium differentiation antigen and its expression can be regulated by androgen. Nevertheless, the regulatory mechanism at the molecular level is not completely understood. In this communication, we demonstrated the tissue-specific expression of PAP in the normal prostate epithelium. Furthermore, results of nuclear run-on experiments indicated that androgen could regulate the transcriptional rate of the PAP gene. This mode of regulation was modulated by cell density. To investigate the transcriptional regulation, we cloned and characterized a 1.4- kilobase (kb) fragment of DNA that flanks the 5' region of the PAP gene from LNCaP human prostate carcinoma cells. The results demonstrated that this 1. 4-kb DNA fragment can drive a chloramphenicol acetyltransferase (CAT) gene expression in LNCaP cells. Also, the promoter activity was inversely correlated with the growth of those cells.

Acid Phosphatase↗
PubMed1993

Radioimmunodetection of prostate cancer by 111In-labeled monoclonal antibody against prostatic acid phosphatase.

Purified human prostate acid phosphatase (PAP) was used to generate a specific monoclonal antibody (FC 3001) for detection of PAP expressed by some prostatic carcinomas. DTPA derivatives of MoAb-F(ab')2-fragments were labeled with indium-111 chloride. This labeled antibody was tested in 15 prostate cancer patients who underwent staging pelvic lymphadenectomy; 9 of them received labeled antibody alone whereas 6 received simultaneous injections of labeled and unlabeled antibody with two dose levels (40 or 80 mg). Biodistribution data obtained by direct blood measurements and imaging procedures indicated that simultaneous injection of unlabeled antibody reduced both the blood elimination rate and the accumulation in the liver. Accumulation of the radionuclide in pelvic lymph node metastases was observed in some patients but in a couple of patients accumulation was noted also in normal lymph nodes. The method cannot in its present design replace staging pelvic lymphadenectomy and further studies are needed for elaboration of clinically useful radioimmunodetection methods.

Acid Phosphatase↗
PubMed1986

Phenotypic variation in the phosphotransferase activity of human red cell acid phosphatase (ACP1).

Red cell acid phosphatase (ACP1) catalyses the transfer of phosphate from phosphate ester substrates to suitable acceptor alcohols such as methanol and glycerol. The rate of substrate turnover in the presence of acceptors is increased by the increment of the phosphotransferase reaction, thus allowing this activity to be measured. There is specificity with regard to acceptors: (a) polyols (e.g., glycerol) are better acceptors than the corresponding n-alcohols, and (b) polyol configuration and chain length determine acceptor activity. Ribitol was the most efficient acceptor found. Each of the three common ACP1 alleles is represented electrophoretically by two isozyme bands; the phosphotransferase activity of the anodal isozyme was found to be more than twice that of the cathodal isozyme. The extent of phosphotransferase activity is also genotype dependent. In the presence of 2 M glycerol, the relative phosphotransferase efficiencies for the three homozygote types were: ACP1 B = 3.7, ACP1 A = 3.4, and ACP1 C = 2.5. This pattern of B greater than A greater than C is the same as found for the modulation of ACP1 by purines and folates.

Acid Phosphatase↗
PubMed1981

Activation of lysosomal acid phosphatase of eosinophil leukocytes.

Acid phosphatase (AP) within the specific granules of eosinophils is held in a latent, inactive form prior to degranulation. Eosinophils responded to membrane stimuli with activation of AP throughout the granules of the cell, prior to degranulation. Activation occurred within the time required for fixation of the cells by glutaraldehyde. Whereas resting normal eosinophils demonstrated AP activity in 7.8 +/- 1.2 per cent of the granules, cells stimulated with opsonized staphylococci demonstrated activity in 78.9 +/- 5.0 per cent of the granules, and the amount of lead phosphate reactant deposited per active granule was considerably more intense in the stimulated than in the unstimulated cells. A similar stimulation of AP activity in eosinophils occurred with exposure to the surface-active agent phorbol myristate acetate or the calcium ionophore A23187. Activation was not altered by 5 microgram. per ml. of cytochalasin B or 4 x 10(-6) M colchicine. These aspects of the response closely parallel the stimulation of oxidative metabolism of eosinophils; however, the two were separable. Eosinophils obtained from a patient with chronic granulomatous disease, although unable to activate the normal oxidative metabolic burst, demonstrated a normal activation of AP.

Acid Phosphatase↗
PubMed1997

Localization and biochemical characterization of acid phosphatase isoforms in the olfactory system of adult rats.

Localization of acid phosphatases was studied with the use of beta-glycerophosphate and p-nitrophenyl phosphate as substrates in the brain with special emphasis on the olfactory system of adult rat at light and electron microscopic level. With the use of beta-glycerophosphate, a selective substrate for the lysosomal acid phosphatase, lead-containing reaction product was found in primary and secondary lysosomes of neurons, glial cells and perivascular macrophages as well as in the cytoplasm of olfactory sensory axons. Incubation with p-nitrophenyl phosphate as substrate additionally revealed a cytoplasmic isoform of acid phosphatase, which could not be inhibited by tartrate or fluoride and was predominantly located in dendrites. Acid phosphatase isoforms were biochemically characterized in samples prepared separately from the olfactory mucosa, olfactory nerve layer, olfactory bulb and its dendrodendritic synaptosomes isolated by subcellular fractionation. In the olfactory mucosa and olfactory nerve layer the lysosomal type (high molecular weight form) was the most prominent acid phosphatase form, whereas the isoform located in dendrites corresponded to the tartrate-resistant extralysosomal, cytosolic type (low molecular weight form). The functional significance of different isoforms of acid phosphatase in the olfactory sensory axons and dendritic elements is discussed.

Acid Phosphatase↗
PubMed2002

Identification and characterization of regulatory elements of the human prostatic acid phosphatase promoter.

Human prostatic acid phosphatase (PAcP) is a prostate epithelium-specific differentiation antigen. The cellular form of PAcP functions as a neutral protein-tyrosine phosphatase, and is involved in regulating prostate cell growth. Although some information on the PAcP gene structure has been obtained, little is known regarding the cis- and trans-acting factors that regulate its expression. Due to the biological importance of PAcP, we investigated the regulation of its expression. A region upstream of the PAcP gene from -2899 to +87 base pairs was linked to the coding sequence of the chloramphenicol acetyltransferase (CAT) gene. Sequential deletions of the sequence between -2899 and -205 revealed that, in addition to the basic promoter, the region between -1258 and -779 represents a positive regulatory element. This -1258/-779 fragment could enhance the PAcP promoter activity in PC-3 and DU 145 human prostate cancer cells, but not in non-prostate cancer cells, including WI-38 lung diploid cells, A-431 epidermoid carcinoma cells, and HeLa cervix epitheloid carcinoma cells. Furthermore, this cis-element together with the promoter sequence could drive a high level of expression of green fluorescent protein (GFP) in PC-3 cells, but not in HeLa cells. The prostate-specific expression was further examined by injecting naked plasmid DNA into the prostate and the hamstring muscle of mice. The fluorescence pattern clearly showed that the level of GFP expression is consistently higher in prostate cells than in muscle cells of the intact animal. The data collectively indicate that region between -1258 and -779 is involved in governing the cell type-specific expression of the PAcP gene.

Acid Phosphatase↗
PubMed2004

Type 2 diabetes and the genetics of signal transduction: a study of interaction between adenosine deaminase and acid phosphatase locus 1 polymorphisms.

Acid phosphatase locus 1 (ACP1) is a highly polymorphic enzyme that has an important role in flavoenzyme activity and in the control of insulin receptor activity and band 3 protein phosphorylation status. Adenosine deaminase (ADA) is a polymorphic enzyme that catalyses the irreversible deamination of adenosine to inosine and has an important role in regulating adenosine concentration. Based on the hypothesis that ACP1 counteracts insulin signaling by dephosphorylating the insulin receptor and that adenosine has an anti-insulin action, we reasoned that low ACP1 activity (low dephosphorylating action on insulin receptor) when associated with high ADA activity (low adenosine concentration) would result in a cumulative effect towards an increased glucose tolerance. On the contrary, high ACP1 activity when associated with low ADA activity would result in a cumulative effect towards a decreased glucose tolerance. A total of 280 adult subjects with type 2 diabetes from the population of Penne (Italy) were studied. There was a nonsignificant trend toward an increase in the proportion of subjects with the complex type with high ACP1 activity and low ADA activity (ie, *B/*B; *A/*C; *B/*C; *C/*C//ADA*1/*2 and *2/*2) in type 2 diabetes relative to that observed in newborn infants from the same population. High ACP1 activity/low ADA activity joint genotype was positively associated with high glycemic levels and with high body mass index (BMI) values. Low ACP1 activity/high ADA activity joint genotype was also positively associated with dyslipidemia. These findings suggest that both ACP1 and ADA contribute to the clinical manifestations of type 2 diabetes and probably also have a marginal influence on susceptibility to the disease. Both additive and epistatic interactions between the 2 systems seem to be operative.

Acid Phosphatase↗
PubMed1980

Nitrogen regulation of acid phosphatase in Neurospora crassa.

Neurospora crassa possesses a repressible acid phosphatase with phosphodiesterase activity which appears to permit it to utilize ribonucleic acid as a phosphorus and as a nitrogen source. This acid phosphatase, which is specified by the pho-3 locus, is derepressed approximately eightfold during nitrogen limitation and to an even greater extent during phosphorus limitation, but is unaffected by sulfur limitation. Derepression of the enzyme did not occur when adenosine 5'-monophosphate was the sole phosphorus or nitrogen source. Synthesis of the acid phosphatase is not under the control of the nit-2 locus, which regulates the expression of a large number of other nitrogen catabolic enzymes. The structural gene of the acid phosphatase appears to be a member of both the phosphorus and nitrogen regulatory circuits.

Acid Phosphatase↗
PubMed1985

Cytochemical localisation of acid phosphatase in the phagocytising conjunctival epithelium of the guinea pig.

The ultrastructural localisation of acid phosphatase activity was investigated on the guinea pig conjunctival epithelium incubated in vivo with a suspension of latex spheres. Deposits of acid phosphatase reaction product were concentrated on the elements of GERL, the phagocytic vacuoles, and the cell membrane. Acid phosphatase activity in GERL was intense in basal and suprabasal cells and decreased towards the superficial cells. Phagosomes containing latex spheres and reaction product of acid phosphatase were observed mainly in the centrospheral region of the superficial and intermediate epithelial cells. Acid phosphatase activity in phagocytising cells was not increased as compared to that in non-phagocytising cells. The observations indicate that existing acid phosphatase in unstimulated conjunctival epithelial cells is released into heterophagosomes brought within the lysosomal compartment. The number of secondary phagosomes seems to be increased by intercellular transport of latex spheres to the acid phosphatase rich cells in the deep layers of the epithelium.

Acid Phosphatase↗
PubMed1975

[The presence and isolation of a highly zinc activated acid phosphatase in the rat brain (author's transl)].

The paper describes an acid phosphatase from rat brain extracts, which is highly activated by zinc acetate. The separation of the different acid phosphatases was performed by gel electrofocusing. After staining with 1-naphthyl phosphate and hexazonium pararosanilin or stabilized diazonium salts in the presence of zinc acetate and sodium tartrate is this zinc activable enzyme fraction nearly selectively demonstrable. With the method of gelfiltration on Sephadex G 100 two fractions of acid phosphatase splitting 4-nitrophenyl phosphate with a very different molecular weight were obtained. In the presence of zinc acetate a third peak of acid phosphatase appears, which is highly activated by zinc and is different from the two other phosphatases. The gel electrofocusing of the last peak showed that it is identical with the above described, though not yet pure. By the fact that it can hydrolyze both 1-naphthyl phosphate and 4-nitrophenyl phosphate at pH = 4.8 and that it is activated by zinc acetate but resistant to tartrate, we would call it zinc activable tartrat resistant acid phosphatase. It is possible to demonstrate this enzyme histochemically. The enzyme activity is especially high in the stromal cells of the plexus chorioideus. After further purification and characterization of this enzyme it could be possible to distinguish it from other zinc activable acid phosphatases in different tissues and body fluids.

Acetates↗
PubMed1980

Ultrastructural localization of acid phosphatase in human laryngeal carcinoma.

The subcellular distribution of acid phosphatase in malignant keratinocytes of invasive laryngeal carcinoma was studied by ultrastructureal cytochemistry. The reaction product was localized in Golgi, ER, and some cytoplasmic vesicles. Acid phosphatase activity was also observed in lysosomal structures in the cortical cytoplasm of basal carcinoma cells. Extracellular acid phohphatase activity also occurred at the tumor-stroma junction in membrane-bound vesicular structures. The localization of acid phosphatase in this report is discussed in relation to acid phosphatase activity in other tumors. The findings lend further support to the important role of hydrolytic enzyme release in respect to tumor invasion into surrounding tissues.

Acid Phosphatase↗
PubMed1991

Acid phosphatase-1 from nematode resistant tomato : isolation and characterization of its gene.

Aps-1 encodes acid phosphatase-1, one of the many acid phosphatases present in tomato (Lycopersicon esculentum Mill.). Aps-1 is closely linked to Mi, a gene conferring resistance against nematodes. Thus, a clone of Aps-1 would provide access to the region of the genome containing Mi. Acid phosphatase-1 was purified from tomato suspension culture cells. Fragmentary amino acid sequences were derived from the purified protein and from its proteolytic and chemical digestion products. One of these amino acid sequences was used to design an oligodeoxyribonucleotide probe expected to hybridize to acid phosphatase-1 cDNA. This probe identified, in a cDNA library, a clone encoding the carboxyl-terminal sequence of a protein that is very similar, but not identical, to acid phosphatase-1. Using this clone, we discovered a second cDNA clone that corresponds in its carboxyl terminal sequence to acid phosphatase-1 but, surprisingly, retains sequences of an Aps-1 intron. The second cDNA clone was used to detect both a cDNA clone and a genomic clone corresponding to Aps-1. The identity of these clones was confirmed by sequence analysis and by the correlation of a restriction fragment length polymorphism with two Aps-1 alleles in a segregating tomato population. The deduced amino acid sequence of the Aps-1 open reading frame predicts a hydrophobic animoterminal signal sequence and a mature protein with a molecular weight of 25,000. The amino acid sequence of this protein has a strong similarity in size and sequence to a vegetative storage protein of soybean.

Journal Article↗
PubMed1984

[Metabolism of phosphate-limited Streptomyces cultures. II. Purification and characterization of acid phosphatase from culture filtrates of turimycin-producing Streptomyces hygroscopicus].

Acid phosphatase was purified from culture filtrates of Streptomyces hygroscopicus strain JA 6599-R 27/158. Method used included as first step either ammonium sulfate precipitation or adsorption of acid phosphatase on Bentonit and the desorption of enzyme from Bentonit with alkaline buffers, adsorption to DEAE-cellulose, column chromatography on Sephadex G 50 and isoelectric focusing in Sephadex gel. The specific activity of the resulting enzyme was 51 muMol/min/mg at 25 degrees C and pH of 6.25 with p-nitrophenylphosphate as substrate. The pI detected by isoelectric focusing was at pH 7.25. The molecular weight determined by gel chromatography and by SDS electrophoresis was found to be 27 000. The pH-dependence of hydrolytic activity of acid phosphatase was substrate specific. The enzyme was found to hydrolyze essentially at pH 6.2 phosphoenolpyruvate, ATP, ADP, fructose-1,6-diphosphate and tyrosine-O-phosphate. The activity was inhibited by phosphate, molybdate, arsenate, vanadate, pyrophosphate and tetraborate. In the culture medium the acid phosphatase caused the release of phosphate from solid and soluted substrates. Therefore the involvement of acid phosphatase in the regulation of secondary metabolism was discussed.

Acid Phosphatase↗
PubMed1990

Evidence for an acid phosphatase in African swine fever virus.

An acid phosphatase activity has been detected in purified preparations of African swine fever virus. Purified viral cores obtained after Nonidet-P40 and 2-mercaptoethanol treatment of the virus retained the activity as assayed with nitrophenyl phosphate as substrate at pH 5. Enzyme cytochemistry by electron microscopy showed that the acid phosphatase activity is localized mainly inside the core of the virion. The molecular weight and the isoelectric point of the virus acid phosphatase activity confirmed that it was distinct from the host cellular enzyme.

Acid Phosphatase↗
PubMed1988

PHO5-LACZ hybrid proteins block translocation of native acid phosphatase in Saccharomyces cerevisiae.

A set of protein hybrids composed of variable portions of the amino-terminal residues of the yeast phosphate-repressible acid phosphatase (product of PHO5) and an active fragment of bacterial beta-galactosidase has been constructed. When these PHO5-LACZ hybrids are expressed in a yeast strain carrying an intact chromosomal PHO5 gene, they show a size-dependent interference with the secretion of native acid phosphatase. Hybrid proteins containing approximately 50 residues of acid phosphatase do not affect secretion of native acid phosphatase. Hybrids containing greater than 200 residues of acid phosphatase reduce the amount of secreted acid phosphatase more than by 50%. The interference with secretion is specific for acid phosphatase. The hybrids do not affect secretion of invertase, and do not confer a growth-deficient phenotype on yeast. Both the hybrid proteins and acid phosphatase accumulate in non-glycosylated, membrane-bound forms which are sensitive to proteolysis from the cytoplasmic side of the membrane. The hybrids and accumulated acid phosphatase co-migrate on Percoll density gradients with markers of the endoplasmic reticulum, but not with markers of the Golgi or secretory vesicles. These results suggest that PHO5-LACZ hybrid proteins specifically block secretion of native acid phosphatase by interfering with enzyme after targeting but before translocation across the endoplasmic reticulum.

Acid Phosphatase↗
PubMed1983

Morphine blocks the increase in acid phosphatase in the substantia gelatinosa during pain.

Acid phosphatase activity in the rat substantia gelatinosa has been shown to increase in response to a formalin-induced painful stimulus. In the rat the substantia gelatinosa is the location of the first synapse in the pain pathway. One site of morphine's analgesic effect is at this first synapse. The present study shows that morphine blocks the previously observed increase in acid phosphatase activity during a painful stimulus. Naloxone antagonizes the morphine effect. These results point to a possible functional role of acid phosphatase in the afferent transmission of pain signals.

Acid Phosphatase↗
PubMed1987

Quantitative histochemical study of acid phosphatase activity in rat liver using a semipermeable membrane technique.

Acid phosphatase activity has been demonstrated in rat liver with the semipermeable membrane technique using naphthol AS-BI phosphate as substrate and hexazotized pararosaniline (HPRA) as simultaneous coupling agent. With this method the final reaction product (FRP) appeared in rat liver as intensely colored red granules in liver parenchymal cells and in Küpffer cells. The absorbance spectrum of the FRP peaks between 510 and 550 nm. A nonspecific reaction product, as has been found in skeletal muscle, did not occur in rat liver. A substrate concentration of 5 mM and a HPRA concentration of 10 mM result in optimum localization and activity. We concluded from the results with different enzyme inhibitors that lysosomal acid phosphatase was demonstrated. The mean absorbance of the FRP increased linearly with incubation time (15-60 min). Furthermore, we found a linear increase of the FRP with increasing section thickness (4-10 micron). When the simultaneous coupling method was replaced by a post-coupling technique, the colored reaction product was diffusely located throughout the cytoplasm. In conclusion, the simultaneous coupling technique in combination with the semipermeable membrane method is a valuable tool for detecting and quantifying lysosomal acid phosphatase activity in rat liver. We demonstrated that acid phosphatase activity is 1.2 times higher periportally than pericentrally in rat liver, and that 24 hr fasting before the experiments did not change the acid phosphatase activity.

Acid Phosphatase↗
PubMed1984

Circadian rhythm of acid phosphatase activity in rat liver microsomes and dependence of NADH 5 alpha-reductase on phosphatase activity.

The specific activity of acid phosphatase in male and female rats follows a circadian rhythm. Preincubation of liver microsomes with testosterone led to an increase of phosphatase activity and a loss of circadian rhythm. NADH 5 alpha-reductase was inactivated by several animal and bacterial acid and alkaline phosphatases while the acid phosphatase from potatoes was ineffective. The extent of inhibition depends on the course of circadian rhythm of NADH 5 alpha-reductase activity. Preincubation of microsomes in the presence of testosterone inhibited the NADH 5 alpha-reduction of testosterone. No such inhibition was observed after preincubation of microsomes with progesterone.

3-Oxo-5-alpha-Steroid 4-Dehydrogenase↗