Role Of Acid Phosphatase Research Articles

The role of acid phosphatase during sucking blood of Haemaphysalis longicornis

In this study, a novel acid phosphatase was isolated from Haemaphysalis longicornis which may affect the reproductive development of the tick. The gene was isolated from a cDNA library named HLACP and analyzed by bioinformatics. Then, the spatial and temporal expression patterns of the genes were analyzed by real-time PCR. In addition, combined with RNAi interference platform and protein modification omics, the changes of protein expression and modification level of H. longicornis before and after blood feeding were analyzed after interference with HLACP.

Role of acid phosphatase in the tolerance of the rhizobial symbiosis with legumes to phosphorus deficiency

Phosphorus (P) deficiency initiates a myriad of transcriptional, biochemical and physiological responses stimulating either the root’s extracellular abilities to acquire soil P in the rhizosphere or optimize its intracellular use efficiency and allocation through all plant organs. Enhancing activity of acid phosphatase (APase) to acquire and remobilize Pi from organic P compounds is one important strategy for improving plant P nutrition. The release of APase to the rhizosphere is a typical and almost universal P-starvation response in higher plants. However, relatively little is known about the functions of intracellular APase in legume nodules. The aim of this review was to track the enzyme activity along with the intra-nodular localization of APase, and its contribution in the rhizobial symbiosis tolerance to P-deficiency. Our findings have revealed that expression of APase and phytases genes and activities of the corresponding enzymes were positively correlated with increases both of the P use efficiency for N2 fixation and nodule O2 permeability in the rhizobial symbiosis with legumes. The induced enzyme activity and the marked transcripts localization of APase and phytase in nodule cortex would control nodule respiration and contribute to adaptation of nodulated legumes to low-P availability. Thus, the increase of APase and phytase activities in legume nodules supports a physiological role of these enzymes in the regulation of nitrogenase activity in connection with the nodule-P status, and opens up a new scenario for a better understanding of the regulation of N2 fixation in legumes.

Acid phosphatase 2 (ACP2) is required for membrane fusion during influenza virus entry

Influenza viruses exploit host factors to successfully replicate in infected cells. Using small interfering RNA (siRNA) technology, we identified six human genes required for influenza A virus (IAV) replication. Here we focused on the role of acid phosphatase 2 (ACP2), as its knockdown showed the greatest inhibition of IAV replication. In IAV-infected cells, depletion of ACP2 resulted in a significant reduction in the expression of viral proteins and mRNA, and led to the attenuation of virus multi-cycle growth. ACP2 knockdown also decreased replication of seasonal influenza A and B viruses and avian IAVs of the H7 subtype. Interestingly, ACP2 depletion had no effect on the replication of Ebola or hepatitis C virus. Because ACP2 is known to be a lysosomal acid phosphatase, we assessed the role of ACP2 in influenza virus entry. While neither binding of the viral particle to the cell surface nor endosomal acidification was affected in ACP2-depleted cells, fusion of the endosomal and viral membranes was impaired. As a result, downstream steps in viral entry were blocked, including nucleocapsid uncoating and nuclear import of viral ribonucleoproteins. Our results established ACP2 as a necessary host factor for regulating the fusion step of influenza virus entry.

Effects of treatment of the fat body trophocytes of Melipona quadrifasciata anthidioides nurse workers and virgin queens in culture by juvenile hormone III and ecdysterone (20‐HE)

The fat body (FB) consists of two types of cells: throphocytes and oenocytes. Throphocytes are related to intermediary metabolism storing lipids, carbohydrates, and proteins while oenocytes play role in the lipids and lipoproteins production. The vitellogenin is the precursor of egg yolk (vitelline) and is synthesized on FB. The aim of this work was to analyze the effects of hormones acting in bee reproduction, as juvenile hormone (JH) and ecdisteroids (20 HE) on FB cells, where vitellogenin is synthesized. For the study were chose nurse workers that in Melipona quadrifasciata anthidioides present activated ovaries and produce eggs, and virgin queens whose ovaries are not yet activated, presenting only previtellogenic follicles. FB trophocytes from these classes of bees were cultivated in media containing different amounts of JH and 20-HE. The effects on trophocytes cytoplasm reserves of lipids, proteins, and activity of acid phosphatase were compared by observing preparations from cultured FB, treated and control, by transmission electron microscopy (TEM). The results showed that the hormones effects are related to the bee's caste and functional ovary stage. The role of acid phosphatase on mobilization of the trophocyte reserves was also determined.

PHOSPHATE DEFICIENCY AFFECTS ACID PHOSPHATASE ACTIVITY AND GROWTH OF TWO WHEAT VARIETIES

The effects of phosphate deficiency on the plant growth and acid phosphatase activity in two wheat cultivars (Triticum aestivum L. cv. ‘Bryza’ and ‘Opatka’) were studied. Pi content decreased significantly in the shoots and roots of all plants grown for one to three weeks in the nutrient medium without phosphate (−P). Phosphate starvation affected growth of both wheat cultivars in a similar way: significantly decreased shoot and root mass, especially after three weeks growth on −P medium, even up to 8–11% of control. However the ratio of root/shoot fresh weight of −P plants increased (2–3 times more than control). The shoot height of −P wheat plants decreased to about 50–60% of the control after two to three weeks of culture; less affected by Pi deficiency was root elongation—no significant changes were observed for both wheat cultivars during one to three weeks of culture. Phosphate deficiency increased the activity of extracellular and intracellular acid phosphatases in comparison to phosphate-sufficient plants. The increase of intracellular acid phosphatase activity in leaves and roots was generally more significant in ‘Bryza’ cultivar as compared to ‘Opatka’, especially after two to three weeks of growth on −P medium. The increase of root surface acid phosphatase activity was the highest for Pi-deficient wheat cv. ‘Bryza’, after three weeks of culture in the −P medium. Generally, the increase of activity of acid phosphatases secreted by the roots of −P wheat plants was higher than those of intracellular acid phosphatases. These results indicate an important role of acid phosphatases in the acclimation of both wheat cultivars to early Pi deficiency.

Transcriptional profiling on chromosome 19p indicated frequent downregulation of ACP5 expression in hepatocellular carcinoma

Chromosomal rearrangements unraveled by spectral karyotyping (SKY) indicated frequent chromosome 19 translocations in hepatocellular carcinoma (HCC). In an effort to characterize the aberrant 19 rearrangements in HCC, we performed positional mapping by fluorescence in-situ hybridization (FISH) in 10 HCC cell lines. SKY analysis indicated structural rearrangements of chromosome 19 in 6 cell lines, 4 of which demonstrated recurring 19p translocations with different partner chromosomes. Using fluorescence-labeled BAC probes, physical mapping indicated a breakpoint cluster between 19p13.12 and 19p12. A corresponding transcriptional mapping by cDNA array on 19p suggested the differential expression of a single downregulated gene ACP5 (tartrate-resistant acid phosphatase type 5). Quantitative RT-PCR confirmed the reduced expression of ACP5 and indicated a strong correlation of its repressed expression only in cell lines that contain a 19p rearrangement (p = 0.004). We further examined the expression of ACP5 in a cohort of 82 primary tumors and 74 matching nonmalignant liver tissues. In the primary HCC examined, a reduction of ACP5 transcripts by 2 to as much as 1,000-fold was suggested in 67% of tumors (55/82 cases). When compared to adjacent nonmalignant tissues, 46% of tumors (34/74 cases) demonstrated a lower expression level (p = 0.015). On closer examination, a high significance of ACP5 repression was suggested in the cirrhotic HCC subgroup that was derived from chronic hepatitis B infected patients (55%; 30/54 cases; p = 0.001). Functional examination of ACP5 ectopic expression in HCC cells further demonstrated a significant growth inhibitory effect of ACP5 on tumor cell survival (p < 0.001). In our study, the novel finding of common ACP5 downregulation in HCC may provide basis for further investigations on the role of acid phosphatase in hepatocarcinogenesis.

Changes in acid and alkaline phosphatase activities during the spoilage of raw muscle from horse mackerel Trachurus japonicus and gurnard Lepidotriga microptera

Abstract The aim of this work was to provide information on the role of acid phosphatase (Acp) and alkaline phosphatase (Alp) activities as spoilage indicators of raw fish. Horse mackerel Trachurus japonicus , a red-flesh fish, and gurnard Lepidotriga microptera , a white-flesh bottom fish, were stored at 4 °C. The aerobic bacteria count (APC) of horse mackerel skin increased from 10 3 to 10 7 CFU/cm 2 in seven days, the Alp activity increased about from 10 to 150 nmol p -nitrophenol/min/g tissue with increase of volatile basic nitrogen (VBN), an index of fish spoilage. The APC of gurnard skin also reached 10 7 CFU/cm 2 after 8 days’ storage. The Alp activity was twice that of the Acp activity in the fresh gurnard and the activity decreased slightly during the initial 4 days and increased from four days’ storage.

The structure of the bursa copulatrix in virgin and mated snails, Helisoma duryi (Mollusca): role of acid phosphatase in reproduction

Abstract. The fine structure of the bursa copulatrix of the virgin snails has been compared with that of mated snails. One of the noticeable changes after mating is an increase in the number of the Golgi and the secretory vesicles. Since some of the vesicles react positively for acid phosphatase it is suggested that this enzyme activity increases following mating. The bursa lumen of the virgin snail contains gel‐like materials devoid of spermatozoa, however, following mating, the lumen is full of semen containing live spermatozoa and bacteria. The source of bacteria in the lumen is not known. Acid phosphatase activity is significantly higher in the luminal content of mated snails than in the virgin snails. The activity is higher in the lumen than in the epithelial cells, suggesting that the enzyme is secreted into the lumen where it is utilized for extracellular degradation of spermatozoa. Following mating, the spermatozoa are motile in the lumen of the bursa for ∼3–7 d, but become immobile and finally undergo extracellular digestion so that intact spermatozoa are not recognizable by day 10. The use of castrated snails in mating experiments suggest that individuals of Helisoma duryi reproduce by cross fertilization and that the bursa may act as the holding organ from where the spermatozoa are periodically transported to the carrefour over ∼7 d. At day 10 following mating, however, autosperms appear in the hermaphroditic duct awaiting the next mating.

Prevotella intermedia が産生する酸性ホスファターゼに関する研究

Prevotella intermedia (P. intermedia), an anaerobic gram-negative bacterium, has been implicated as a pathogen in adult periodontitis, in acute necrotizing ulcerative gingivitis and in pregnancy gingivitis. P. intermedia has been known to have a high acid phosphatase (ACP) activity, one of the potential virulence factors in periodontopathogenic bacteria. However, little is known about the structure and function of ACPs from oral bacteria. In this study, in order to examine the potential role of ACP, the ACP from P. intermedia ATCC 25611 was purified to homogeneity and characterized. The ACP from P. intermedia was solubilized by extraction with 1% Triton X-114, and the crude extract was purified by ion-exchange chromatography on DEAE Bio-Gel, CM Bio-Gel and cellulose phosphate, followed by hydrophobic chromatography on Phenyl-Sepharose. On sodium dodecyl sulfate-polyacrylamide gel electrophoresis, the purified enzyme revealed a single protein band with a molecular weight of Mr &ap;30 kDa. The molecular weight of the native enzyme from P. intermedia was estimated to be &ap;30 kDa using a gel filtration column with TSK gel G3000SW in the HPLC system. These findings suggest that the purified ACP is a monomer. The optimum pH for the enzyme was about 4.9 and the optimum temperature was 46℃. The enzyme activity was inhibited by sodium orthovanadate, sodium molybdate, sodium fluoride and Zn^<2+>, which are known as the inhibitors of protein tyrosine phosphatase (PTP) activity. On the other hand, it was not inhibited by okadaic acid, which is known to be a specific inhibitor of protein serine/threonine phosphatase (PP) activity. The enzyme had high activities against o-phospho-L-tyrosine and phosphotyrosine-containing peptides. The purified ACP was found to dephosphorylate the tyrosine-phosphorylated protein of a molecular weight &ap;170 kDa in an A431 cell lysate. The N-terminal amino acid sequence was determined for the purified ACP, and significant homology (64.3% identical amino acid residues) was found using the Swiss Prot Protein database between the purified ACP and the Pho C, the acid phosphatase of Morganella morganii. Thus, these findings suggest the possibility that the ACP from P. intermedia constitutes a novel class of ACPs, which has a PTP-like activity.

Actinobacillus actinomycetemcomitans が産生する酸性ホスファターゼのプロテインチロシン/セリンホスファターゼ様の性質に関する研究

Actinobacillus actinomycetemcomitans has been implicated as one of the causative organisms of localized juvenile periodontitis and adult periodontitis. A. actinomycetemcomitans has been known to have a high acid phosphatase (ACP) activity, which is previously known to be one of the virulence factors in periodontopathic bacteria. Little is known about ACP from oral bacteria. In order to examine the potential role of ACP, the ACP of A. actinomycetemcomitans was purified to homogeneity and characterized. The ACP in the cell-associated form of A. actinomycetemcomitans was released from the membranes with Triton X-114, then purified by ion-exchange chromatography on DEAE Bio-Gel and Gel filtration, followed by affinity chromatography on Hi-Trap Blue. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the purified enzyme revealed a single protein band with a molecular weight of Mr &ap; 40, 000. The molecular weight of the native enzyme was estimated to be 80, 000 by gel filtration with a Superdex-200 column. The pH optimum for the purified enzyme was about 5.4 and the temperature optimum was 37℃. The purified enzyme was inhibited by sodium orthovanadate, which is one of the inhibitors of protein tyrosine phosphatase (PTP) activity. However, it was not inhibited by okadaic acid, which is a specific inhibitor of protein serine/threonine phosphatase (PP) activity. The purified enzyme dephosphorylated o-phospho-L-tyrosine, phosphotyrosine-containing peptides and Raytide, which are used as substrates for PTP. Also, the purified enzyme dephosphorylated O-phospho-L-serine and phosphoserine-containing peptides and casein, which is good substrate for PP. On the other hand, phosphorylase kinase, which is used as a substrate for PP, was not dephosphorylated by the purified enzyme. It turned out that ACP of A. actinomycetemcomitans is classified in the PTP family, while it is not an SH-enzyme because it does not completely need the thiol reducing agent. The purified enzyme exhibited substantial activity against both Tyr and Ser-containing substrates. Thus, these findings suggest for the first time the existence of a novel tyrosine/serine protein phosphatase in oral bacteria and that ACP of A. actinomycetemcomitans has unique biochemical properties compared with any known PTPs.

The role of acid phosphatases in plant phosphorus metabolism

The role of acid phosphatases in plant phosphorus metabolism

The role of acid phosphatases in plant phosphorus metabolism

Hydrolysis of phosphate esters is a critical process in the energy metabolism and metabolic regulation of plant cells. This review summarizes the characteristics and putative roles of plant acid phosphatase (APase). Although immunologically closely related, plant APases display remarkable heterogeneity with regards to their kinetic and molecular properties, and subcellular location. The secreted APases of roots and cell cultures are relatively non‐specific enzymes that appear to be important in the hydrolysis and mobilization of Pi from extracellular phosphomonoesters for plant nutrition. Intracellular APases are undoubtedly involved in the routine utilization of Pi reserves or other Pi‐containing compounds. A special class of intracellular APase exists that demonstrate a clear‐cut (but generally nonabsolute) substrate selectivity. These APases are hypothesized to have distinct metabolic functions and include: phytase, phosphoglycolate phosphatase, 3‐phosphoglycerate phosphatase, phosphoenolpyruvate phosphatase, and phosphotyrosyl‐protein phosphatase. APase expression is regulated by a variety of developmental and environmental factors. Pi starvation induces de novo synthesis of extra‐ and intracellular APases in cell cultures as well as in whole plants. Recommendations are made to achieve uniformity in the analyses of the different APase isoforms normally encountered within and between different plant tissues.

Localization of acid phosphatase in rice calli

Acid phosphatase is an important hydrolytic enzyme and widely distributed in plants. The role of acid phosphatase in plant tissues has been suggested involving in mobilization of nutrient reserves, sugar transport, differentiation of plastid, cell autolysis and senescence. In culture, the differentiating calli show the changes in isozyme patterns and activities, and anatomical localization. In this study, subcellular localization of acid phosphatase in regenerating callis is emphasized.Sterized rice seeds(Oryza sativaTainong 67) were grown on modified MS medium containing 2 ppm 2,4-D. After 2 weeks, calli 2 to 3 mm in size were transfered on differentiation medium containing 1 ppm NAA and 2 ppm kinetin. Different stages of calli were collected and cut into thin slice with razor blade. Slices were fixed in 2.5% glutaraldehyde in 0.1M phosphate buffer(pH 7.0) for 2h and then washed, overnight . Specimens were incubated in Gomori solution containing 3mM p- nitrophenyl phosphate as substrate at 37°C for 90 min, postfixed with 1% OsO4for lh, dehydrated in ethanol series and embedded in Spurr's resin. Control experiments were done as follows: l), incubation medium without substrate; 2),incubation medium without lead nitrate; 3), incubation medium containing 0.01% NaF. Sections were doubly stained with uranyl acetate and lead citrate, and finally observed under Hitachi H-600 at 75 KV.

A possible role for acid phosphatase with thiamin-binding activity encoded by PHO3 in yeast.

Periplasmic soluble thiamin-binding protein in Saccharomyces cerevisiae (Iwashima, A. et al. (1979) Biochim. Biophys. Acta 577, 217-220) was demonstrated to be encoded by PHO3 gene that codes for thiamin repressible acid phosphatase (Schweingruber, M.E. et al. (1986) J. Biol. Chem. 261, 15877-15882) by genetic analysis. The pho3 mutant cells of S. cerevisiae in contrast to the parent cells have markedly reduced activity of the uptake of [14C]thiamin phosphates, suggesting that thiamin repressible acid phosphatase plays a role in the hydrolysis of thiamin phosphates in the periplasmic space prior to the uptake of their thiamin moieties by S. cerevisiae.

A possible role for acid phosphatase with thiamin-binding activity encoded byPHO3in yeast

Periplasmic soluble thiamin-binding protein in Saccharomyces cerevisiae (Iwashima, A. et al. (1979) Biochim. Biophys. Acta 577, 217-220) was demonstrated to be encoded by PHO3 gene that codes for thiamin repressible acid phosphatase (Schweingruber, M.E. et al. (1986) J. Biol. Chem. 261, 15877-15882) by genetic analysis. The pho3 mutant cells of S. cerevisiae in contrast to the parent cells have markedly reduced activity of the uptake of [14C]thiamin phosphates, suggesting that thiamin repressible acid phosphatase plays a role in the hydrolysis of thiamin phosphates in the periplasmic space prior to the uptake of their thiamin moieties by S. cerevisiae.

Importance of acid phosphatase in response criteria for prostate cancer

The role of acid phosphatase in the definition of response to treatment for prostate cancer is unclear. To better define its predictive value, especially regarding survival rate, we reviewed the clinical course of 76 men with Stage D2 prostate cancer who were treated with combination chemotherapy.

Role of lysosomes in coronary artery lesions of hypertensive rats.

Electron microscopically the role of acid phosphatase (acid P) positive lysosomes in the pathogenesis of intramyocardial coronary artery lesions of hypertensive rats with bilaterally constricted renal arteries was studied. At 3 postoperative weeks, acid P positive lysosomes were increased in endothelial cells of the coronary arteries, but at 5 weeks and thereafter, they were decreased in number. In the intima, intimal smooth muscle cells with acid P positive lysosomes appeared at 3 postoperative weeks, but their number remained small as late as 9 postoperative weeks. The internal elastic lamina was fragmented into amorphous masses from 3 postoperative weeks, at 5 weeks and thereafter the fragmentation and disruption became severer, and at 9 weeks the lamina disappeared because of marked disruption. At 3 postoperative weeks, acid P positive extracellular lysosomes were observed in the gaps of the fragmented internal elastic lamina. At 5 weeks and thereafter, extracellular lysosomes and attenuated processes of medial smooth muscle cells with lysosomes were seen extending through the gaps of the fragmented internal elastic lamina. Necrosis of these extending cell processes and lysosomes remaining after the necrosis were observed. The findings suggested that the fragmentation and lytic change of the internal elastic lamina observed in hypertensive rat intramyocardial coronary arteries might be induced by extracellular lysosomes discharged not only from endothelial cells and intimal smooth muscle cells but also from the extending processes of medial smooth muscle cells into the gaps of the internal elastic lamina.

Age-dependent decline of natural killer and antibody-dependent cell mediated cytotoxicity activity of human lymphocytes is connected with decrease of their acid phosphatase activity

Decline of cytotoxic potential of lymphocytes of aged persons in ADCC and NK cell mediated cytotoxic reaction was paralleled by a drop in the activity of acid phosphatase. Intensity of ADCC reaction and the level of acid phosphatase activity showed statistically significant correlation when these two parameters were measured in peripheral blood of the same persons. The role of acid phosphatase in cytotoxic function of lymphocytes is discussed.

Studies of Vegetative Plant Tissue Compatibility/Incompatibility: The Role of Acid Phosphatase in Lethal Cell Senescence in an Incompatible Heterograft

Previous work has indicated that the graft incompatihility between Sedrmi telephoides and Solanum pennellil involves cell necrosis that results In a thick layer of collapsed cells at the graft Interface. This necrotic layer insulates the stock from the scion, which results in abscission of the Sedum scion after 4-6 weeks due to desiccation and starvation. Thus, cell autolysis (which is restricted to Sedum) characterizes the Incompatibility response in this system (1). In order to elucidate the events that lead to cell autolysis, and thus better understand the cellular site and mode of action of cellular incompatibility, the appearance and fate of the hydrolytlc enzyme acid phosphatase (AP) was followed in both the compatible Sedum autograft and the incompatible Sedum/Solanum heterograft. Acid phosphatase was localized by a modified Gomori-type reaction; positive (i.e., including NaF inhibitor) and negative (lacking substrate) controls showed no enzymatic precipitate. Following an initial association with the endoplasmic reticulum (ER) and dictyosomes at 6-10 hours after grafting, AP activity in the compatible Sedum autograft is associated primarily with the plasmalemma (Fig. 1). By 18-24 hours after grafting, the AP activity is restricted to the tono-plast and vacuole (Fig. 2). This strict compartmentation and absence of enzyme from the cytosol is maintained throughout the development of the compatible graft. While AP activity in the incompatible Sedum/Solanum heterograft is Initially similar to the compatible Sedum autograft (i.e., initially found on the ER and dictyosomes), there is a marked difference in enzyme localization in the two graft partners as the incompatibility response develops. As in the compatible autograft, Solanum cells at the graft interface show an Increase in AP activity that Is restricted to the vacuole and tonoplast, with little or no enzyme activity in the cytosol (Fig. 3). In comparable Sedum cells, however, there is a dramatic Increase In AP activity in the cytosol (Fig. h); this cytosollc AP activity is associated with thin fibril-like structures (Fig. 5) measuring approximately 60 A in diameter. This high cytoplasmic AP activity In Sedum cells results in cell autolysis, death, and eventual cell collapse to form the characteristic necrotic layer separating the two graft partners.

Acid phosphatase activity and cell death in mouse thymus.

The distribution of acid phosphatase activity in the thymus of young (8 week) and old (42 week) mice is presented. In 8 week old mice acid phosphatase positive cells represent 1.27 +/- 0.13% of the total population whereas in 42 week old mice, showing involution of the thymus, acid phosphatase positive cells represent 2.40 +/- 0.17% of the total population. Loci of free acid phosphatase activity have been interpreted as sites of cell lysis and death. This has been confirmed at electron microscope level where free acid phosphatase has been demonstrated in the cytoplasm of lysing thymic lymphocytes. Vacuolar sites of acid phosphatase activity have been demonstrated in macrophages which appear to dispose of the lymphocytes. Extensive autophagic activity occurs in the epithelial reticular cells. The role of acid phosphatase in thymic lymphocyte deletion and in the tissue dynamics of the thymus is discussed.