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PubMed1993

Isolation and characterization of the genes encoding mouse and human type-5 acid phosphatase.

The gene (mT5AP) encoding murine type-5 acid phosphatase has been isolated and completely sequenced while the gene (hT5AP) encoding human T5AP has been partly sequenced. The murine gene spans 4 kb and contains five exons. Exon 1 is completely non-coding and exon 2 starts with the initiation codon in both mT5AP and hT5AP. The positions of the intron/exon boundaries are completely conserved between mT5AP and hT5AP, but are distinct from the gene encoding the related porcine protein, uteroferrin (Utf). There is strong homology at both the nucleotide (nt) and amino acid (aa) levels between the inferred mouse cDNA and the sequences of rat T5AP and hT5AP, and pig Utf. The mT5AP and hT5AP genes were found to have multiple transcription start points (tsp) by primer extension analysis, consistent with the absence of a consensus TATA box. The sequences for the 5'-flanking regions of mT5AP and hT5AP were determined to -1.6 and -1.0 kb, respectively, relative to the tsp. A 2-kb segment of the mT5AP 5' flanking region linked to a luciferase-encoding reporter gene (Luc) was sufficient to direct tissue-specific transcription in the mouse macrophage cell line, RAW264. Significant sequence similarity between the mT5AP and hT5AP promoters is restricted to the most proximal 200 bp, which also resembles the porcine Utf gene, and a 300-bp segment 700 bp upstream. A progesterone-response element is present only in the mouse promoter and the estrogen- and iron-response elements described previously in the pig gene are absent from both the mouse and human genes. These differences may result in distinctive regulation of T5AP and Utf expression.

Acid Phosphatase↗
PubMed2005

Adsorption, desorption and activities of acid phosphatase on various colloidal particles from an Ultisol.

Adsorption, desorption and activity of acid phosphatase on various soil colloidal particles and pure clay minerals were studied. Higher adsorption amounts and low percentage of desorption of acid phosphatase were found on fine soil clays (<0.2 microm). Electrostatic force and ligand exchange are the major driving forces that are involved in the adsorption of enzymes on soil clays. More enzyme molecules were adsorbed on soil clays in the presence of organic components. However, enzymes on organic clays were more easily released. One-third of the enzyme on goethite was adsorbed via ligand exchange process. Some other interactions, such as van der Waals force, hydrophobic force and hydrogen bonding may be more important in the adsorption of enzyme on kaolinite and the enzyme in this system cannot be easily removed. Coarse clays (0.2-2 microm) and inorganic soil clays had higher affinities for enzyme molecules than fine clays and organic clays, respectively. The activity of enzyme bound on soil clays was inhibited and the thermal stability was increased in the presence of organic matter. Data obtained in this study are helpful for a better understanding of the interactions of enzymes with inorganic and organic constituents in soil and associated environments.

Acid Phosphatase↗
PubMed1984

Ultrastructural localization of acid phosphatase activity in the jejunal absorptive cells of fasted rats.

Ultrastructural localization of acid phosphatase activity was investigated in the jejunal absorptive cells of 21 d fasted rats (about 500 g). The enzyme activity was localized on the membrane of microvilli, the lateral cell membrane, the Golgi complex, the lysosomes and the GERL of Novikoff (a part of the smooth surfaced endoplasmic reticulum located in close proximity to the Golgi saccules) of jejunal absorptive cells. Moreover, the lysosomes of various sizes and shapes with acid phosphatase activity was characteristically encountered in the infranuclear cytoplasm. The lysosomes appeared to be autolysosomes .

Acid Phosphatase↗
PubMed1980

Localization of alkaline and acid phosphatases in healthy human adrenal cortex. Light and electron microscopic study.

Localization of alkaline and acid phosphatase activity was investigated in healthy human adrenal cortex by light and electron microscopy. The activity of both was found in the inner part of the adrenal cortex--mainly in the reticular zone. The reaction products of alkaline phosphatase were observed along the plasma membrane and those of acid phosphatase were observed mainly in the lysosomes and secretory vacuoles. The heavier deposit of phosphatase reaction products in the reticular zone may be explained by the fact that the reticular zone is most active in the steroidogenesis of glucocorticoid and adrenal androgen.

Acid Phosphatase↗
PubMed1988

Partial purification and characterization of acid phosphatase from sporulated oocysts of Eimeria tenella.

Acid phosphatase of Eimeria tenella oocysts (Peak II) was purified 77-fold with a recovery of 26% using protamine sulfate precipitation, DEAE-cellulose chromatography and Sephadex G-200 gel filtration. This enzyme occurs in multiple forms as indicated by two peaks which can be separated by DEAE-cellulose chromatography and polyacrylamide gel electrophoresis. The partially purified enzyme has optimal activity at pH 4.5. With p-nitrophenyl phosphate the Km and Vmax values for (Peak II) were 25 mM and 1.57 mumol/min/mg protein, respectively. The enzyme (Peak II) is strongly inhibited by Hg++, Cu++, iodoacetamide, fluoride and molybdate. Tartrate and other divalent metal ions have no effect on enzyme activity. The partially purified Peak II phosphatase is not a glycoprotein as it is not absorbed on concanavalin-A Sepharose and its treatment with bacterial neuraminidase does not alter its elution profile through DEAE cellulose.

Acid Phosphatase↗
PubMed1994

Calcitonin releases acid phosphatase from rat ventral prostate explants.

Inclusion of salmon calcitonin in the culture medium of rat ventral prostate explants diminished l-tartarate-sensitive acid phosphatase activity in the tissues with a concomitant increment of the enzyme activity in the medium. The effect of the hormone was dose-dependent for a dose range of 10(-12)-10(-6) M. Acid phosphatase activity in prostate explants decreased from 38.6 +/- 3.5 to 20.5 +/- 2.8, whereas it increased from 0.60 +/- 0.15 to 2.80 +/- 0.40 nmol p-nitrophenol liberated/mg protein/30 min in the culture medium. Tissues exposed to 10(-6) M salmon calcitonin had higher acetylcholinesterase activity (8.8 +/- 0.7) than non-exposed ones (6.2 +/- 0.5 mumol substrate hydrolyzed/g tissue/min). These results suggest that locally produced calcitonin causes a release for prostatic acid phosphatase from prostate tissues possibly through its interaction with the cholinergic system.

Acetylcholinesterase↗
PubMed1993

Increasing values of serum acid phosphatase in a child with Mycoplasma pneumoniae-associated hemophagocytic histiocytic syndrome.

We describe a 3 1/2-year-old boy with disseminated histiocytic disease probably induced by Mycoplasma pneumoniae. In this patient, acid phosphatase was elevated in serum and was also detected histochemically in the infiltrating histiocytes. The serum acid phosphatase levels increased as his histiocytosis progressed, apparently mirroring the activity of the disease. This observation suggests that serum acid phosphatase levels should be evaluated further to determine whether they will be a useful indicator of disease in children with different histiocytosis syndromes.

Acid Phosphatase↗
PubMed1980

Far infrared spectra of acid phosphatase from rat liver. Spectra of the native and the heat- and acid-denatured isoenzymes.

The spectrum of acid phosphatase, as well as that of its isoenzymes, shows in the region 100-500 cm-1 a band at 362 cm-1 which appears to be due to second-order structure (alpha-helix). The character of these spectra is unchanged by deuteration of the protein. Heat- and acid-denaturation affected all the spectra studied pointing to the occurrence of conformational changes, but a close similarity between the spectra of the two isoenzymes was consistently observed.

Acid Phosphatase↗
PubMed1983

Evaluation of prostate specific acid phosphatase and prostate specific antigen in identification of prostatic cancer.

The peroxidase-anti-peroxidase technique was used to stain for prostate specific acid phosphatase and prostate specific antigen in 12 patients with primary tumors and in 12 patients with metastases in whom the nature of the tumor was in doubt after routine histopathological studies. Nine of the primary tumors were positive for both markers and an additional 2 tumors stained for prostate specific antigen only. Six metastatic lesions stained for both markers and a seventh for prostate specific antigen alone. Thus, 11 of 12 primary tumors and 7 of 12 metastases studied were proved to be of prostatic orgin. While the peroxidase staining was sometimes weak and uneven this method, using prostate specific antigen and prostate specific acid phosphatase, allowed for ready identification of metastases. The heterogeneity of the tumors in regard to these 2 prostate markers is demonstrated, and the value of staining for prostate specific acid phosphatase and prostate specific antigen is emphasized.

Acid Phosphatase↗
PubMed1980

Lysosomal acid phosphatase: activity and isoenzymes in separated normal human blood cells.

The present study was devised to investigate the activity and isoenzymes of lysosomal acid phosphatase in individual normal human blood cells, including the T- and B-population of lymphocytes, with the aim to contribute to the classification of haematopoietic neoplasias on the basis of cell specific isoenzyme patterns. Platelets, erythrocytes, granulocytes, monocytes and T-lymphocytes were isolated from blood by gradient centrifugation or immune adsorption. B-lymphocytes were obtained from human tonsils. After purity control and isolation of lysosomes the concentration of acid phosphatase was assayed using the conventional spectrophotometric method. Isoenzymes were separated by isoelectric focusing on polyacrylamide thin layer slabs. Monocytes revealed the highest activity with 14 mU/10(7) cells, about three times more than granulocytes. T-lymphocytes showed an activity of 2.85 mU/10(7) cells and B-lymphocytes of 1.83 mU/10(7) CELLS. The lowest activity was found in platelets with 0.08 mU/10(7) cells. Granulocytes showed 12 isoenzyme bands, whilst the number for monocyte, B-lymphocytes, T-lymphocytes and platelets were respectively 11, 12, 1 and 4 isoenzyme bands. Thus it became evident that the different blood cell populations can be distinguished on the basis of their acid phosphatase isoenzyme pattern.

Acid Phosphatase↗
PubMed1985

The ultrastructural localization of prostatic specific antigen and prostatic acid phosphatase in hyperplastic and neoplastic human prostates.

A low temperature embedding, protein A-gold technique was used to localize prostatic specific antigen and prostatic acid phosphatase at the ultrastructural level in hyperplastic and neoplastic human prostates. Prostatic specific antigen immunoreactivity was localized over the endoplasmic reticulum, cytoplasmic vesicles and vacuoles, and within the lumina of prostatic glands. In contrast, prostatic acid phosphatase immunoreactivity was localized to lysosomal granules. The pattern of labelling was similar in both hyperplastic glands and adenocarcinomas. This is the first localization of prostatic specific antigen at the ultrastructural level. The localization of prostatic acid phosphatase by an immunochemical technique confirms and expands previous histochemical observations.

Acid Phosphatase↗
PubMed1971

Acid phosphatase activity in mouse brain infected with Venezuelan equine encephalomyelitis virus.

The mode of development of Venezuelan equine encephalomyelitis virus and the activity of acid phosphatase in the central nervous system of newborn mice were investigated. Precursor particles appeared to be formed in masses of viroplasm, migrating to the membrane of the Golgi cisterns and vacuoles or to the plasma membrane and being transformed into mature viral particles by budding. Mature viral particles were also found in the lumen of the blood vessels and around the myelin sheath of axons. Increased number of Golgi complexes and depletion of polysomes were the main ultrastructural alterations of the nerve cells. Acid phosphatase activity was found to be increased in the Golgi cisterns, vacuoles, and lysosomes of nerve cells. The presence of acid phosphatase activity in the rough endoplasmic reticulum and perinuclear cisterns suggests increased production of the enzyme in the nerve cells infected with Venezuelan equine encephalomyelitis virus.

Acid Phosphatase↗
PubMed1982

[Acid phosphatase isoenzyme composition of the lysosomes of normal and tumor cells].

Heterogeneity of acid phosphatase in lysosomes of the rat's liver and the Zhaidel hepatoma was studied by the DEAE-cellulose chromatography. It is found that different substrates are hydrolyzed by different molecular forms of the enzyme. It is suggested that variability in the increase of the enzyme activities, measured with different substrates under alteration of lysosomes, may be due to the heterogeneity of molecular forms of acid phosphatase.

Acid Phosphatase↗
PubMed2000

Identification of mammalian-like purple acid phosphatases in a wide range of plants.

Purple acid phosphatases (PAPs) comprise a family of binuclear metal-containing hydrolases, members of which have been isolated from plants, mammals and fungi. Polypeptide chains differ in size (animal approximately 35kDa, plant approximately 55kDa) and exhibit low sequence homology between kingdoms but all residues involved in co-ordination of the metal ions are invariant. A search of genomic databases was undertaken using a sequence pattern which includes the conserved residues. Several novel potential PAP sequences were detected, including the first known examples from bacterial sources. Ten plant ESTs were also identified which, although possessing the conserved sequence pattern, were not homologous throughout their sequences to previously known plant PAPs. Based on these EST sequences, novel cDNAs from sweet potato, soybean, red kidney bean and Arabidopsis thaliana were cloned and sequenced. These sequences are more closely related to mammalian PAP than to previously characterized plant enzymes. Their predicted secondary structure is similar to that of the mammalian enzyme. A model of the sweet potato enzyme was generated based on the coordinates of pig PAP. These observations strongly suggest that the cloned cDNA sequences represent a second group of plant PAPs with properties more similar to the mammalian enzymes than to the high molecular weight plant enzymes.

Acid Phosphatase↗
PubMedDate not supplied

[Enzymes of the peripheral blood leukocytes from the vertebrate host in an experimental Leishmania infection. 1. Neutrophil acid phosphatase].

The results of cytochemical identification of acid phosphatase in the neutrophils of mice, guinea pigs and golden hamsters inoculated with leishmanial promastigotes of different species and virulence and also of people vaccinated against zoonotic cutaneous leishmaniasis are presented. The reversible increase of the enzyme activity in host's blood neutrophils and its dependence on parasite species and virulence are shown.

Acid Phosphatase↗
PubMed1993

Purification and characterization of zinc-dependent acid phosphatase from bovine brain.

Zn(2+)-Dependent acid phosphatase (Zn(2+)-APase) was purified to homogeneity from bovine brain. The apparent molecular weight of the enzyme was estimated to be about 62000 by gel filtration and 31000 by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate. The enzyme exhibited an isoelectric point of approximately 4.8. The enzyme required Zn2+ ions for catalytic activity, but other cations had little or no effect. The maximum enzyme activity was obtained in the presence of about 5 mM of Zn2+ at pH 5.5 in 50 mM 2-(N-morpholino)ethanesulfonic acid-NaOH buffer. The enzyme significantly catalyzed the hydrolysis of p-nitrophenyl phosphate, phenyl phosphate, and phosphotyrosine. The enzyme was also active for myo-inositol-2-monophosphate and adenosine 2'-monophosphate of the other common phosphate esters tested, though significantly less active than for p-nitrophenyl phosphate. The optimum activity pH of the enzyme was around 5.5 with p-nitrophenyl phosphate and myo-inositol-2-monophosphate. The enzyme was resistant to fluoride ions. Two types of Zn(2+)-APases, a high molecular weight (molecular weight, M(r)., about 110,000) and a low molecular weight (M(r), about 62,000) type, were found to exist in various tissues of rat. Brain, lung, spleen, stomach, heart, skeletal muscle, and erythrocytes contained only the lower molecular weight type. On the other hand, liver and kidney contained mainly the higher molecular weight type, and the small intestine contained significant quantities of the both types.

Acid Phosphatase↗
PubMed1979

[Lymphocyte acid phosphatase activity in lymphocytic leukemia studied in tissue culture with the use of diffusion chambers].

The reported investigations showed that lymphocytes in chronic lymphocytic leukaemia with low acid phosphatase activity had a rise of this enzyme level during culture in diffusion chamber. This rise is caused by increased number of lymphocytes with activity grades 1 degree and 2 degrees, and from the 6th day of culture also the number of lymphocytes with 3 degrees and 4 degrees activity score rose as well, while at the same time the proportion of cells without acid phosphatase activity fell. In the lymphocytes of healthy subjects a rise in acid phosphatase activity was observed as well under the same culture conditions.

Acid Phosphatase↗
PubMed1982

Comparative studies on particulate acid phosphatases in sea urchin eggs.

1. Particulate acid phosphatases were partially purified and characterized in the eggs of six species of sea urchins and one species of sand dollar, Hemicentrotus pulcherrimus, Anthocidaris crassispina, Pseudocentrotus depressus, Strongylocentrotus purpuratus, S. francicanus, S. droebachiensis and Dendraster excentricus. 2. The enzymes of 7 species were strongly inhibited by NaF, tartrate, p-chloromercuribenzoate and HgCl2. 3. Substrate specificity of the enzymes of all species was broad.

Acid Phosphatase↗