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PubMedDate not supplied

The use of leukocyte acid phosphatase in the diagnosis of malignant disease. Case report and review of literature.

Tartrate resistant acid phosphatase (TRAP) has been demonstrated during relapse in the cells in the cerebral spinal fluid (CSF) in a patient with the clinical features of acute T cell lymphocytic leukemia which suggests this isozyme may be a marker for malignant transformation of some types of lymphocytes. The presence of TRAP may be helpful in establishing the diagnosis of a lymphocytic malignancy since normal lymphocytes appear to have tartrate sensitive acid phosphatase. The presence of TRAP can no longer be considered specific for hairy cell leukemia, since children with acute lymphocytic leukemia are being found with this isozyme in their malignant blasts. The presence of TRAP does not appear to be specific for T or B cell lines of malignant lymphocytes since it has been described in cells with either type of cell markers. The presence of TRAP seems most useful in differentiating lymphocytic malignancies from monocytic and histiocytic malignancies and from benign lymphocytoses when the cells of the peripheral blood and marrow may have similar morphologic features with routine staining.

Acid Phosphatase↗
PubMed1981

[Studies into carcino-embryonic antigen (CEA) and enzyme activities of alkaline and acid phosphatase in patients with fibrocystic breast disease (author's transl)].

CEA as well as alkaline and acid phosphatase were measured in patients with fibrocystic breast disease. The values recorded from the punctured fluids were compared to those in peripheral blood. CEA concentrations in cyst fluid were elevated in patients with proliferative breast disease, whereas no correlations could be established between alkaline and acid phosphatase, on the one hand, and various histological forms of breast disease, on the other.

Acid Phosphatase↗
PubMed1981

Quantitative histochemical investigations of semipermeable membrane techniques for the assay of acid phosphatase in skeletal muscle. III. A modified simultaneous coupling technique.

Meijer's semipermeable membrane technique for acid phosphatase was modified by treating sections immediately after incubation with 70% ethanol for 30 min at room temperature instead of with formalin. The modification improved the validity of the technique considerably, by stabilising the specific final reaction product formed in presumed enzyme-containing sites. The modified technique thus seems promising for assaying the activity of acid phosphatase in sections of skeletal muscle.

Acid Phosphatase↗
PubMed1993

Regulation of prostatic acid phosphatase expression and secretion by androgen in LNCaP human prostate carcinoma cells.

The expression and the secretion of human prostatic acid phosphatase (PAcP), a differentiation antigen which is the major acid phosphatase in prostate epithelial cells, are thought to be regulated by an androgen. We investigated this regulatory mechanism at the post-transcriptional level in LNCaP human prostate carcinoma cells using a cDNA clone for the secretory form of PAcP. 5 alpha-Dihydrotestosterone (DHT, an active form of endogenous androgen) stimulated the secretion of PAcP from cells grown in a steroid-reduced medium and in a defined serum-free medium, respectively. The secreted PAcP activity was increased following a DHT dose in a dose-dependent fashion at concentrations of up to 1 microM. Further, the stimulation of PAcP secretion occurred following the period of exposure to DHT. During a 5-day treatment period, with 10 nM of DHT in the steroid-reduced medium, the secretion of PAcP was stimulated approximately 150% over that from control cells. Nevertheless, PAcP was secreted from cells grown in the absence of added DHT. First, the androgen dependency of PAcP expression was examined. The expression and the secretion of PAcP were observed in cells that were grown in a defined serum-free medium and grown in a steroid-reduced medium, in the absence of DHT. The increased secretion by DHT was further demonstrated to be in part due to an increase in PAcP mRNA level, as evidenced by Northern blot analysis. PAcP mRNA levels were elevated approximately 2-fold and corresponded to an increase of approximately 2.5-fold in the secreted level of newly synthesized 35S-PAcP. Then, the effect of DHT on the secretory process was investigated. Results of pulse-chase labeling experiments indicated that the secretory rate of PAcP was stimulated by about 50% on average by DHT. In conclusion, our data demonstrated that, in LNCaP cells, the expression and the secretion of PAcP regulated by androgen are apparently hormone-responsive processes. Further, DHT stimulation of PAcP secretion operates within at least two levels: increased PAcP mRNA and stimulation of the secretory pathway.

Acid Phosphatase↗
PubMed1963

AN ANALYSIS OF CELLULAR AND SUBCELLULAR SYSTEMS WHICH TRANSFORM THE SPECIES CHARACTER OF ACID PHOSPHATASE IN ACETABULARIA.

Several species-specific molecular forms of acid phosphatase are known to exist in the unicellular green alga Acetabularia. In graft combinations between cells of Acetabularia mediterranea (med) and Acicularia Schenckii (acic) the expression of the med phosphatase is dominant over acic phosphatase. There is good evidence that in such grafts the preexisting acic phosphatase is converted on the molecular level via an intermediate form to the med phosphatase. This conversion can be initiated by the transplantation of a med cell nucleus to an anucleate acic cell, but will also take place in grafts between anucleate med and anucleate acic cells, indicating that the direct participation of a cell nucleus is not required. An incomplete conversion of acic phosphatase, which terminates at the intermediate stage, is induced in acic cells by injection of a concentrated homogenate of med cytoplasm. A similar partial conversion occurs in vitro in a mixture of homogenates from med and acic cells. Subcellular particles, such as chloroplasts or mitochondria, can be removed from the homogenates by centrifugation without impairing the reactions leading to the intermediate phosphatase type. Experimental evidence suggests that the transformation of phosphatase types is enzymatically catalyzed and may involve the conjugation of small molecules with the phosphatase protein. It was shown, however, that sialic acid is not involved, since the incubation of med or acic homogenates with neuraminidase did not modify the electrophoretic mobility of either enzyme type. Another type of phosphatase, which occurs in Acetabularia erenulata (cren) and can be distinguished electrophoretically from the aforementioned types, is not subject to interaction. In various mono- and multi-nucleate graft combinations between cren cells on one hand, and med or acic cells on the other hand, the cren phosphatase is synthesized independently of the enzyme of the graft partner.

Acetabularia↗
PubMed2002

Shigella apyrase--a novel variant of bacterial acid phosphatases?

A virulence-associated ATP diphosphohydrolase activity in the periplasm of Shigella, identified as apyrase, was found to be markedly similar to bacterial non-specific acid phosphatases in primary structure. When the Shigella apyrase sequence was threaded in to the recently published 3D structure of the highly similar (73%) Escherichia blattae acid phosphatase it was found to have a highly overlapping 3D structure. Our analysis, which included assays for phosphatase, haloperoxidase and catalase activities, led us to hypothesize that Shigella apyrase might belong to a new class of pyrophosphatase originating as one more variant in the family of bacterial non-specific acid phosphatases. It revealed interesting structure-function relationships and probable roles relevant to pathogenesis.

Amino Acid Sequence↗
PubMed1985

Simultaneous flow cytometric deoxyribonucleic acid and acid phosphatase analysis of benign and malignant lesions of the prostate.

Flow cytometry can differentiate benign from malignant lesions of the prostate through deoxyribonucleic acid distribution analysis. A method has been developed that permits simultaneous cytometric determination of deoxyribonucleic acid and acid phosphatase activity in the cell cycle compartments of prostatic biopsy specimens. Histograms of prostatic carcinoma reveal higher acid phosphatase activity and greater deoxyribonucleic acid content in the S and S + G2/M populations than the histograms representing benign lesions. This compartmental difference may have prognostic usefulness.

Acid Phosphatase↗
PubMed1986

Elevated prostatic acid phosphatase: a prognostic factor for stage C adenocarcinoma of the prostate.

The clinical course of 25 patients with clinical stage C adenocarcinoma of the prostate who had pre-treatment elevations of the prostatic acid phosphatase (Roy test) was analyzed retrospectively. All patients were treated with definitive external beam radiation therapy at our hospital between 1974 and 1980. Of the 25 patients 17 (68 per cent) have had disease progression. The median time to treatment failure for this group was 27 months (range 10 to 101 months), and the over-all median survival for these patients has not been reached (range 16 to 120 months). Local control of disease was achieved in 84 per cent (21 of 25) of the patients. The control group consisted of 75 consecutive age-matched patients with normal pre-treatment prostatic acid phosphatase levels whose disease was identically staged and treated at our hospital from July 1977 to January 1979. The median time to disease progression in this group has not yet been reached. Of these 75 patients 24 (32 per cent) have had disease progression within a median time of 38 months. Therefore, an elevated pre-treatment prostatic acid phosphatase value is a harbinger of systemic disease and indicates that radiotherapy will be significantly (p equals 0.002) less effective as a definitive local therapeutic modality.

Acid Phosphatase↗
PubMed1990

Lysosomal tartrate sensitive acid phosphatase deficiency in cells which contain lysosomal "high uptake forms".

The catalytic and immunological properties of acid phosphatases (EC 3.1.3.2.) in different tissues were studied. It was demonstrated that high uptake forms of lysosomal enzymes like beta-galactosidase isolated from human platelets and bovine testis are mature enzymes, which have not lost their mannose-6phosphate marker. The results presented indicate that this phenomenon is related to a low activity or the complete absence of the lysosomal tartrate sensitive acid phosphatase activity in the tissues concerned.

Acid Phosphatase↗
PubMed1988

Relationship of prostatic acid phosphatase localization in human prostate by a monoclonal antibody with the Gleason grading system.

Prostatic acid phosphatase (PAP) was localized in human prostate with a monoclonal antibody prepared against PAP isoenzyme II to determine patterns of its expression in normal, hyperplastic (BPH), and cancerous glands. The monoclonal antibody reacted with both isoenzymes II and IV in immunoblot studies. Formalin-fixed, paraffin-embedded tissue was used from patients who had not been treated with hormones or chemotherapy. In normal glands and BPH, there was marked variation in the intensity of PAP staining in morphologically otherwise similar epithelial cells. There was similar heterogeneity of staining in the adenocarcinomas. Rough quantification of the intensity patterns in the clinical groups indicated a slight shift to more intense staining in BPH and well-differentiated carcinomas but a progressive decline in the PAP staining in the moderately and poorly differentiated tumors. This decrease in intracellular staining with decreasing differentiation is not inconsistent with the clinical observation that serum levels of acid phosphatase generally increase with higher grade and disseminated tumors, since the enzyme is simply more accessible to the circulatory system in those cases. The same decrease may explain the few disseminated tumors that are not associated with elevated serum levels.

Acid Phosphatase↗
PubMed1984

A high-molecular weight complex with acid phosphatase activity in human breast cancer.

The presence of a high-molecular weight complex with acid phosphatase activity in the cytosol of human mammary tumors is reported. This complex appeared in the cytosol after tissue homogenization in the presence of dithiotreitol, with or without Triton X-100 and at acidic or neutral pH. Upon gel electrophoresis, this fraction showed only one band of enzyme activity which did not enter the fine pore gel. Lubrol or n-butanol had no apparent effect on this complex, and 8 M urea or 2% sodium dodecyl sulfate did not disaggregate this large molecule. After purification by gel filtration, ammonium sulfate precipitation and ion-exchange chromatography an apparent molecular weight or 10(6) was measured. It hydrolyzed typical acid phosphatase substrates such as p-NPP and alpha-NP, but also ATP and PPi. Only 44% inhibition was observed with L-(+)tartrate and it was still 40% active after 1 hr incubation at 60 degrees C. Reduction in the presence of SDS yielded several polypeptide bands. It was also detected in some samples of normal mammary tissues, but not in normal human placenta or liver.

Acid Phosphatase↗
PubMed2004

A model of the acid sphingomyelinase phosphoesterase domain based on its remote structural homolog purple acid phosphatase.

Sequence profile and fold recognition methods identified mammalian purple acid phosphatase (PAP), a member of a dimetal-containing phosphoesterase (DMP) family, as a remote homolog of human acid sphingomyelinase (ASM). A model of the phosphoesterase domain of ASM was built based on its predicted secondary structure and the metal-coordinating residues of PAP. Due to the low sequence identity between ASM and PAP (approximately 15%), the highest degree of confidence in the model resides in the metal-binding motifs. The ASM model predicts residues Asp 206, Asp 278, Asn 318, His 425, and His 457 to be dimetal coordinating. A putative orientation for the phosphorylcholine head group of the ASM substrate, sphingomyelin (SM), was made based on the predicted catalysis of the phosphorus-oxygen bond in the active site of ASM and on a structural comparison of the PAP-phosphate complex to the C-reactive protein-phosphorylcholine complex. These complexes revealed similar spatial interactions between the metal-coordinating residues, the metals, and the phosphate groups, suggesting a putative orientation for the head group in ASM consistent with the mechanism considerations. A conserved sequence motif in ASM, NX3CX3N, was identified (Asn 381 to Asn 389) and is predicted to interact with the choline amine moiety in SM. The resulting ASM model suggests that the enzyme uses an SN2-type catalytic mechanism to hydrolyze SM, similar to other DMPs. His 319 in ASM is predicted to protonate the ceramide-leaving group in the catalysis of SM. The putative functional roles of several ASM Niemann-Pick missense mutations, located in the predicted phosphoesterase domain, are discussed in context to the model.

Acid Phosphatase↗
PubMed1985

Biosynthesis of prostatic acid phosphatase in a normal human cell-line.

The biosynthesis of the prostatic form of human acid phosphatase was studied in normal embryonic lung cells, WI-38, by metabolic labeling with tritiated leucine and [32P]phosphate, followed by specific immunoprecipitation, gel electrophoresis, and fluorography. Of the total tartrate-inhibitable acid phosphatase activity in WI-38 cells, 30% is due to the prostatic form. The primary translation product that leads eventually to the mature prostatic enzyme is a precursor polypeptide of 112 kDa. The precursor polypeptide is processed to mature polypeptides of 59, 55, and 49 kDa via an intermediate 91-kDa precursor. WI-38 cells also secrete a 113-kDa peptide into the medium. The precursor and mature polypeptides are glycosylated and phosphorylated. Upon treatment with endo-beta-hexosaminidase H, the apparent molecular weighs of the polypeptides are reduced by approximately 4 kDa and phosphate is lost.

Acid Phosphatase↗
PubMed1998

Disruption of a gene encoding phosphatidic acid phosphatase causes abnormal phenotypes in cell growth and abnormal cytokinesis in Saccharomyces cerevisiae.

Phosphatidic acid phosphatase (PAP) is an enzyme involved in lipid metabolism. Diacylglycerol (DG) and phosphatidic acid (PA) are a substrate and a product of PAP, respectively, and function as second messengers in several signal transduction pathways in animals. To investigate the function of PAP in Saccharomyces cerevisiae, we analyzed changes in cellular phenotypes of a mutant that has a disrupted PAP gene. Two putative genes for PAP (ScPAP1 and ScPAP2) are in the S. cerevisiae genome. We generated a ScPAP1-null mutant and observed its cellular phenotypic changes. The ScPAP1-null mutant cells aggregated in liquid culture, and microscopical analyses showed that these mutant cells have an abnormal cell shape and abnormal cytokinesis during cell division. The ScPAP1 is possibly involved in cell growth and cytokinesis in S. cerevisiae. Yeast phosphatidic acid phosphatase is possibly involved in cell growth and cytokinesis.

Amino Acid Sequence↗
PubMed2005

Expression patterns of purple acid phosphatase genes in Arabidopsis organs and functional analysis of AtPAP23 predominantly transcribed in flower.

Purple acid phosphatases (PAPs) are metallo-phosphoesterases. Their expression and function have not been systematically investigated in higher plants. In this work, we compared the transcript levels of 28 Arabidopsis PAP (AtPAP) genes in five Arabidopsis organs. The 28 members, although differed in their expression patterns in vegetative organs, were all transcribed in flower. Furthermore, the transcription of seven members (AtPAPs 6, 11, 14, 19, 23, 24 and 25) occurred predominantly in the flower. To begin dissecting the role of AtPAP genes in flower development, further expression and functional analyses were conducted using AtPAP23. Histochemical staining of transgenic plants expressing AtPAP23 promoter-beta-glucuronidase (GUS) gene construct revealed that AtPAP23 transcription was strong in flower apical meristems, but became restricted to petals and anther filaments in fully developed flower. A GST (glutathione S-transferase) fusion protein of AtPAP23 (GST:AtPAP23) was expressed in bacterial cells, and was found to contain significant amounts of Fe and Mn (whereas the control GST protein contained none). In biochemical tests, GST:AtPAP23 showed typical acid phosphatase activities. The fusion protein was also highly active on phosphoserine, but not phosphotyrosine. Despite its highly specific expression pattern and the demonstrated biochemical function of its protein product, the RNAi (RNA interference), T-DNA knock-out and overexpression lines of AtPAP23 were indistinguishable from wild type plants in the development of flower (or other organs). Interestingly, the Fe and Mn contents were found significantly increased in AtPAP23 overexpression lines, which may offer a new direction for further functional studies of AtPAPs in Arabidopsis.

Acid Phosphatase↗
PubMed1985

Ultrastructural localization of acid phosphatase in nonhuman primate vaginal epithelium.

The vagina of the rhesus monkey is lined by a stratified squamous epithelium. However, little is known regarding the cytochemical composition of its cell organelles and the substances found in the intercellular spaces. In this study we have examined the ultrastructural distribution of acid phosphatase in the vaginal epithelium. In basal and parabasal cells reaction product was found in some Golgi cisternae and vesicles and in a variety of cytoplasmic granules. Reaction product was also found in some, but not all, membrane-coating granules. In the upper layers of the epithelium, the membrane-coating granules extruded their contents and acid phosphatase was localized in the intercellular spaces. The possible roles of acid phosphatase in keratinization, desquamation, or modification of substances in the intercellular compartment are discussed.

Acid Phosphatase↗
PubMed1977

Comparison of human prostatic acid phosphatase by measurement of enzymatic activity and by radioimmunoassay.

We compared results of measurement of prostatic acid phosphatase activity in serum and various tissues by enzymatic assay and radioimmunoassay. By enzymatic assay, activity in serum is lost rapidly, even at room temperature. In contrast, there was no change in antigenic activity during 48 h by radioimmunoassay. The radioimmunoassay was more specific in 12 tissues and in serum than were several enzymatic assays that make use of inhibitors of the enzyme. The enzymatic assay resulted in 26.6% (24/90) false positives from non-prostatic cancer patients. In contrast, with radioimmunoassay there were only 5.5% (5/90) false positives. We conclude that immunological detection of prostatic acid phosphatase is the more reliable technique.

Acid Phosphatase↗
PubMed1990

Targeting of a lysosomal membrane protein: a tyrosine-containing endocytosis signal in the cytoplasmic tail of lysosomal acid phosphatase is necessary and sufficient for targeting to lysosomes.

Lysosomal acid phosphatase (LAP) is synthesized as a transmembrane protein with a short carboxy-terminal cytoplasmic tail of 19 amino acids, and processed to a soluble protein after transport to lysosomes. Deletion of the membrane spanning domain and the cytoplasmic tail converts LAP to a secretory protein, while deletion of the cytoplasmic tail as well as substitution of tyrosine 413 within the cytoplasmic tail against phenylalanine causes accumulation at the cell surface. A chimeric polypeptide, in which the cytoplasmic tail of LAP was fused to the ectoplasmic and transmembrane domain of hemagglutinin is rapidly internalized and tyrosine 413 of the LAP tail is essential for internalization of the fusion protein. A chimeric polypeptide, in which the membrane spanning domain and cytoplasmic tail of LAP are fused to the ectoplasmic domain of the Mr 46 kd mannose 6-phosphate receptor, is rapidly transported to lysosomes, whereas wild type receptor is not transported to lysosomes. We conclude that a tyrosine containing endocytosis signal in the cytoplasmic tail of LAP is necessary and sufficient for targeting to lysosomes.

Acid Phosphatase↗