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[Acid phosphatase activity in cultures of glial tumors].

With 18 glial brain tumours serving as a base material the activity of acid phosphatase was studied dynamically in the course of cultivation. The enzyme is demonstrable both in differentiated and actively proliferating cells, as well as in those showing signs of dystrophy. The enzyme was found to display chiefly a moderate activity in monomorphic tumour cells, its content being higher in atypical neoplastic cells. A significantly rising activity of the acid phosphatase was discovered in cells presenting dystrophic and necrobiotic alterations.

Acid Phosphatase↗
PubMed1987

Sequence homology in the metalloproteins; purple acid phosphatase from beef spleen and uteroferrin from porcine uterus.

The primary structures of purple acid phosphatase and uteroferrin, two iron-binding glycoproteins isolated from beef spleen and porcine uterine fluids, respectively, have been examined by a combination of tandem mass spectrometry and classical Edman sequencing methods. Reported here are amino acid sequence data covering more than 90% of the primary structures for these two proteins. The sequence data reveal an unexpectedly high degree of homology, greater than 90%, for these two proteins.

Acid Phosphatase↗
PubMed1999

Genetic rearrangements in the tyrB-uvrA region of the enterobacterial chromosome: a potential cause for different class B acid phosphatase regulation in Salmonella enterica and Escherichia coli.

Unlike in Escherichia coli, in Salmonella enterica production of class B acid phosphatase (AphA) was detectable also in cells growing in the presence of glucose. Characterization of the aphA locus from a S. enterica ser. typhi strain showed that the aphA determinant is very similar to the E. coli homolog, and that its chromosomal location between the highly conserved tyrB and uvrA genes is retained. However, the aphA flanking regions were found to be markedly different in the two species, either between tyrB and aphA or between aphA and uvrA. The differences in the aphA 5'-flanking region, which in S. enterica is considerably shorter than in E. coli (183 vs. 1121 bp) and includes potential promoter sequences not present in E. coli, could be responsible for the different regulation of class B acid phosphatase observed in the two species.

Acid Phosphatase↗
PubMed1992

Changes in the amount and distribution of neuronal alkaline and acid phosphatase after chronic exposure of cultures of cingulate cortex to antidepressant drugs.

Enzyme histochemistry was used to examine alkaline and acid phosphatases in cultures of embryonic rat cingulate cortex after 14 days exposure in vitro to two tricyclic antidepressants (amitriptyline and desipramine) and two non-tricyclic antidepressants (mianserin and citalopram). An increased amount of acid phosphatase reaction product was observed in lysosomes of neurons in cultures treated chronically with the non-tricyclic antidepressants, mianserin or citalopram. More strikingly, reaction product was also present in the inner lamellae of the Golgi apparatus after this treatment, but never in controls. These observations suggest that non-tricyclic antidepressants significantly increase the rate of degradative processes in cingulate neurons. In cultures, treated chronically with desipramine or amitriptyline, pre- and postsynaptic membranes contained heavy deposits of alkaline phosphatase reaction product, whereas in control cultures not exposed to these drugs the corresponding membranes were entirely devoid of reaction product. An increase in the amount of alkaline phosphatase reaction product was also observed on the plasma membranes of neuronal cell bodies. These observations suggest that chronic exposure to antidepressants may influence transmembrane transport in cingulate neurons.

Acid Phosphatase↗
PubMed2003

Plant purple acid phosphatases - genes, structures and biological function.

The properties of plant purple acid phosphatases (PAPs), metallophosphoesterases present in some bacteria, plants and animals are reviewed. All members of this group contain a characteristic set of seven amino-acid residues involved in metal ligation. Animal PAPs contain a binuclear metallic center composed of two irons, whereas in plant PAPs one iron ion is joined by zinc or manganese ion. Among plant PAPs two groups can be distinguished: small PAPs, monomeric proteins with molecular mass around 35 kDa, structurally close to mammalian PAPs, and large PAPs, homodimeric proteins with a single polypeptide of about 55 kDa. Large plant PAPs exhibit two types of structural organization. One type comprises enzymes with subunits bound by a disulfide bridge formed by cysteines located in the C-terminal region around position 350. In the second type no cysteines are located in this position and no disulfide bridges are formed between subunits. Differences in structural organisation are reflected in substrate preferences. Recent data reveal in plants the occurrence of metallophosphoesterases structurally different from small or large PAPs but with metal-ligating sequences characteristic for PAPs and expressing pronounced specificity towards phytate or diphosphate nucleosides and inorganic pyrophosphate.

Acid Phosphatase↗
PubMed1996

Congenital muscular dystrophy syndromes distinguished by alkaline and acid phosphatase, merosin, and dystrophin staining.

Congenital muscular dystrophy syndromes are characterized by congenital weakness, contractures, and dystrophic features on muscle biopsy. However, these syndromes are often difficult to diagnose precisely because their clinical and pathologic characteristics are not specific and resemble changes in other myopathies. We examined muscle biopsies from 20 children with a congenital muscular dystrophy syndrome. Disease controls with dystrophies or other myopathies (n=19) and normal individuals (n=15) were studied for comparison. In each biopsy we determined (1) numbers of muscle fibers with alkaline phosphatase (AlkP) staining, (2) numbers of acid phosphatase-(AcP) positive cells, (3) dystrophin levels by immunocytochemistry, and (4) the distribution of merosin and laminin-A staining. A ratio of AcP:AlkP staining was calculated for each biopsy. In nine patients with congenital muscular dystrophy (younger than 4 years of age) with normal dystrophin, the AcP:AlkP ratio was low (0.09 +/- 0.03). In contrast, in Duchenne muscular dystrophy, the AcP:AlkP ratio was 15 times higher (1.6 +/- 0.04, p=0.001). The three children with congetial muscular dystrophy syndromes and reduced dystrophin and one child with facioscapulohumeral dystrophy had AcP:AlkP ratios in the range of Duchenne muscular dystrophy patients (2.4 +/- 1.4). Low Ac:AlkP ratios were related to relative absence of AcP-positive cells. Merosin staining was absent in 5 of the 17 congenital muscular dystrophy biopsies tested. None of the 5 children with merosin-negative but all 12 with merosin-positive stains walked (p=0.0002). We conclude that a pattern of few AcP-positive cells in the setting of numerous AlkP staining muscle fibers has specificity for congenital muscular dystrophy syndromes and provides histopathologic support for the diagnosis. Reduced merosin in muscle predicts more severe weakness and long-term disability.

Acid Phosphatase↗
PubMed1991

Acid phosphatase-1(1), a tightly linked molecular marker for root-knot nematode resistance in tomato: from protein to gene, using PCR and degenerate primers containing deoxyinosine.

With a view to cloning the root-knot nematode resistance gene Mi in tomato by chromosome walking, we have developed a molecular probe for the tightly linked acid phosphatase-1 (Aps-1) locus. The acid phosphatase-1 allozyme (APS-1(1], encoded by the Aps-1(1) allele originating from Lycopersicon peruvianum, was purified to apparent homogeneity from tomato roots and suspension cells. Microsequencing of CNBr and tryptic peptides generated from APS-1(1) provided a partial amino acid sequence, which accounted for approximately 23% of the protein and revealed two stretches of homology with soybean proteins KSH3 and VSP27, comprising 22 matches within 26 amino acid residues. The partial amino acid sequence information enabled us to isolate a 2.4 kb genomic Aps-1(1) sequence by means of the polymerase chain reaction (PCR), primed by degenerate pools of oligodeoxyribonucleotides, synthesized on the basis of the amino acid sequences. Synthesis of the 2.4 kb PCR product was specific for genomic templates carrying the L. peruvianum Aps-1(1) allele. Crucial to the priming specificity and the synthesis of the 2.4 kb genomic sequence was the use of degenerate primer pools in which the number of different primer species was limited by incorporating deoxyinosine phosphate residues at three and four base ambiguities. In using cDNA as a template, a 490 bp sequence was obtained, indicating a high proportion of intron sequences in the 2.4 kb genomic Aps-1(1) sequence. The Aps-1(1) origin of the PCR product was confirmed by RFLP (restriction fragment length polymorphism) analysis, using both a chromosome 6 substitution line and a pair of nearly isogenic lines, differing for a small chromosomal region around the Aps-1/Mi loci.

Acid Phosphatase↗
PubMed1995

The Aspergillus niger (ficuum) aphA gene encodes a pH 6.0-optimum acid phosphatase.

We have used the Aspergillus niger (An) aphA gene as a probe and cloned the A. ficuum (Af) SRRC 265 gene encoding an extracellular pH 6.0-optimum acid phosphatase (APase6) from a genomic library. The identity of the Af aphA gene was confirmed and its nucleotide (nt) sequence verified by comparing its deduced amino acid (aa) sequence to that of purified Af APase6. A comparison of the nt sequences of the An and Af genes suggested that errors were made in the previously reported An aphA sequence. Several regions of the An aphA were resequenced and the mistakes corrected. With its nt sequence corrected, the An aphA is nearly identical to the cloned Af gene encoding APase6, and in 90.4% agreement in the coding regions. Both genes have three conserved introns and when translated, both nt sequences code for a polypeptide of 614 aa. There is now evidence that the two cloned genes are homologous and code for acid phosphatases that are 96% identical.

Acid Phosphatase↗
PubMed1986

Age-related changes in tissue levels of prostatic acid phosphatase and prostate specific antigen.

Immunoperoxidase localization of prostatic tissue antigens has become useful in identifying the prostate as the origin of metastatic disease. Much research has been aimed at investigating the presence of these antigens in the adult prostate gland in benign and neoplastic states. Few studies have been done to determine the presence of these markers before puberty. We studied the prostate gland of 42 children of varying ages to determine the presence of these antigens at all age ranges to puberty. Sequential sections of the prostate were cut for prostate specific antigen, prostatic acid phosphatase, and hematoxylin and eosin staining. The degree of immunoperoxidase stain was graded from 0 to 4. The results showed that staining levels of prostate specific antigen and prostatic acid phosphatase were high at birth, decreased by age 6 months, reappeared by age 10 years and increased to puberty. Thus, the levels of prostate specific antigen and prostatic acid phosphatase appear to follow the testosterone levels, suggesting a hormonal dependence.

Acid Phosphatase↗
PubMed1982

Clinical value of different methods for determination of acid phosphatase in prostatic cancer.

The availability of a radioimmunoassay (RIA) and an enzyme immunoassay (EIA) for the prostate specific acid phosphatase required a study to compare these techniques with the conventional colorimetric assay. Our study is based on examinations of 188 normal persons and 136 patients with carcinoma of the prostate. The advantage of the immunologic methods - RIA and EIA - lies in their stable immunologic activity and their high specificity. However, RIA and EIA are not screening methods for incidental carcinoma because of their low sensitivity for stage-A tumors. Their good sensitivity at lower ranges of concentration makes them suitable for checking the course of a prostatic carcinoma during therapy. The level of prostatic acid phosphatase may allow conclusions about intra-or extracapsular growth of the prostatic carcinoma.

Acid Phosphatase↗
PubMed1976

Acid phosphatase in rat neurohypophyseal dispersions and its fractions enriched for neurosecretosomes and pituicytes after water deprivation and lactation.

Neurohypophyseal dispersions and fractions enriched for neurosecretosomes and pituicytes were prepared from rats subjected to 6 days of water deprivation and 9-10 days of lactation as stimuli of the hypothalamo-neurohypophyseal system (HNS). After water deprivation the content of the fractions changed in such a way that the neurosecretosomes, and to a lesser extent also the pituicytes, accumulated at a lower density within the gradient used for separation. Stimulation by means of lactation did not show such changes when a comparison was made with dioestrus. Microchemical and histochemical tests for acid phosphatase showed that most of the activity in the controls was present in the neurosecretosomes. A rough calculation, which takes into account the different yields for the dispersion elements, showed a rather equal distribution for acid phosphatase activity between axonal and pituicytic compartments of the intact neurohypophysis. The known acid phosphatase activity response of the neural lobe after HNS stimulation, which was also detectable in the dispersion, resulted histochemically in an increased staining intensity for both neurosecretosomes and pituicytes, but with microassay it was distributed along a gradient similar to oxytocin. It was therefore concluded that this lysosomal enzyme response within the neurophypophysis is preferentially localized in the neurohypophysis is preferentially localized in the neurosecretory axons.

Acid Phosphatase↗
PubMed1997

Temperature dependent expression of an acid phosphatase by Bordetella bronchiseptica: role in intracellular survival.

Bordetella bronchiseptica has the ability to invade and survive intracellularly. This potential to survive for extended periods within eukaryotic cells might play an important role in the pathogenesis of the infections caused by this microorganism. The bacterial factors involved in this process, however, have not yet been determined. In this study we have identified an acid phosphatase produced by B. bronchiseptica, but not by other Bordetella spp. The expression of this enzyme was demonstrated to be strictly regulated by temperature (optimal expression at 30 degrees C) and seems to be partially repressed by the product of the bvg locus. The enzyme was localized in the cytoplasmic fraction, the optimal activity was observed at pH 5.5, and the apparent molecular mass obtained by zymogram was 40 kDa. To further investigate the pathogenic role of this enzyme, mutants lacking acid phosphatase activity were obtained from both bvg-positive and bvg-negative parental strains using minitransposons. The growth pattern of these recombinant clones in vitro was similar to the parent strains, however, the tested clones exhibited a significant reduction (P < or = 0.05) in their intracellular survival ability. This newly described acid phosphatase from B. bronchiseptica seems to play a role in intracellular survival, and therefore represents a novel pathogenicity factor.

Acid Phosphatase↗
PubMed1982

Changes in epidermal acid phosphatase levels in response to chemical irritation.

Topical sodium laurate produced little or no immediate change in the amount of rat epidermal acid phosphatase but the levels of thid enzyme progressively increased to reach a maximum at about 3 days. This coincided with acanthosis and thickening of the stratum granulosum, indicating epidermal repair. The increase depended o protein synthesis as it could be blocked by treatment with cycloheximide. This inhibitory effect was associated histologically with loss of the stratum granulosum, supporting the belief that the expression of acid phosphatase is closely linked with this layer during normal keratinization.

Acid Phosphatase↗
PubMed1999

The respiratory burst-inhibiting acid phosphatase AcpA is not essential for the intramacrophage growth or virulence of Francisella novicida.

Acid phosphatases capable of inhibiting the respiratory burst of neutrophils have been identified in certain intracellular pathogens. Here we evaluate the role of AcpA, a respiratory burst-inhibiting acid phosphatase of Francisella, in the virulence and intracellular growth of this organism. An F. novicida acpA null mutant was created and found to exhibit wild-type growth kinetics in both cell-line and inflammatory mouse macrophages. The acpA mutant also shows wild-type replication in the spleens of experimentally infected mice. These data suggest that AcpA is not essential for the intracellular growth or virulence of F. novicida.

Animals↗