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Journal of Nippon Medical School =... 2022Serum tartrate-resistant acid phosphatase 5b is well known to be increased in giant cell tumors of bone. However, there are only a few studies that analyzed the...
BACKGROUND
Serum tartrate-resistant acid phosphatase 5b is well known to be increased in giant cell tumors of bone. However, there are only a few studies that analyzed the association with tartrate-resistant acid phosphatase 5b expression in those patients. Therefore, we analyzed the characteristics of patients with giant cell tumors of bone and high tartrate-resistant acid phosphatase 5b expression.
METHODS
This retrospective study included 26 patients with giant cell tumors of bone. The correlation between tartrate-resistant acid phosphatase 5b before initial treatment and tumor volume was evaluated. Patients were divided into two groups according to tartrate-resistant acid phosphatase 5b level. Statistical analysis was performed between the two groups.
RESULTS
Tartrate-resistant acid phosphatase 5b was elevated in 17/26 patients, and the mean value was 852 mU/dL. There was no correlation with tumor volume (r = 0.034, P = 0.86). The mean age of 34.5 years in the HT group was significantly younger than the mean age of 47.4 years in the LT group (P = 0.040). Pathologically, 19/26 cases showed at least one focal area with features of typical giant cell tumor of bone. Although 11/18 patients in the LT group exhibited relatively noticeable secondary changes, all patients in the HT group exhibited typical features (P = 0.0074).
CONCLUSIONS
Tartrate-resistant acid phosphatase 5b levels were not elevated in some giant cell tumors of bone. This study suggested that tartrate-resistant acid phosphatase 5b may be elevated in younger patients and in cases with fewer pathological secondary changes, regardless of tumor volume.
Topics: Humans; Adult; Middle Aged; Tartrate-Resistant Acid Phosphatase; Acid Phosphatase; Retrospective Studies; Giant Cell Tumor of Bone; Tumor Burden; Bone Neoplasms; Biomarkers
PubMed: 36725001
DOI: 10.1272/jnms.JNMS.2022_89-611 -
Leukemia Jan 1997
Review
Topics: Acid Phosphatase; Animals; Bone Resorption; Cloning, Molecular; Cytoplasm; Gene Expression Regulation, Enzymologic; Humans; Isoenzymes; Mice; Organelles; Promoter Regions, Genetic; Swine; Tartrate-Resistant Acid Phosphatase
PubMed: 9001411
DOI: 10.1038/sj.leu.2400532 -
Journal of Chemical Education Dec 1977
Topics: Acid Phosphatase; Biochemistry
PubMed: 591585
DOI: No ID Found -
Journal of Inorganic Biochemistry Jan 2023Biomimetics hold potential for varied applications in biotechnology and medicine but have also attracted particular interest as benchmarks for the functional study of... (Review)
Review
Biomimetics hold potential for varied applications in biotechnology and medicine but have also attracted particular interest as benchmarks for the functional study of their more complex biological counterparts, e.g. metalloenzymes. While many of the synthetic systems adequately mimic some structural and functional aspects of their biological counterparts the catalytic efficiencies displayed are mostly far inferior due to the smaller size and the associated lower complexity. Nonetheless they play an important role in bioinorganic chemistry. Numerous examples of biologically inspired and informed artificial catalysts have been reported, designed to mimic a plethora of chemical transformations, and relevant examples are highlighted in reviews and scientific reports. Herein, we discuss biomimetics of the metallohydrolase purple acid phosphatase (PAP), examples of which have been used to showcase synergistic research advances for both the biological and synthetic systems. In particular, we focus on the seminal contribution of our colleague Prof. Ademir Neves, and his group, pioneers in the design and optimization of suitable ligands that mimic the active site of PAP.
Topics: Acid Phosphatase; Biomimetics; Catalysis; Catalytic Domain
PubMed: 36371912
DOI: 10.1016/j.jinorgbio.2022.112061 -
PloS One 2021Wheat germ acid phosphatase (WGAP) is a commercial preparation of partially purified protein commonly used in laboratory settings for non-specific enzymatic...
Wheat germ acid phosphatase (WGAP) is a commercial preparation of partially purified protein commonly used in laboratory settings for non-specific enzymatic dephosphorylation. It is known that these preparations contain multiple phosphatase isozymes and are still relatively crude. This study therefore aimed to identify the protein components of a commercial preparation of wheat germ acid phosphatase using mass spectroscopy and comparative genomics. After one post-purchase purification step, the most prevalent fifteen proteins in the mixture included heat shock proteins, beta-amylases, glucoseribitol dehydrogenases, enolases, and an aminopeptidase. While not among the most abundant components, eight unique dephosphorylation enzymes were also present including three purple acid phosphatases. Furthermore, it is shown that some of these correspond to previously isolated isozymes; one of which has been also previously shown by transcriptome data to be overexpressed in wheat seeds. In summary, this study identified the major components of WGAP including phosphatases and hypothesizes the most active components towards a better understanding of this commonly used laboratory tool.
Topics: Acid Phosphatase; Chromatography, Affinity; Germ Cells; Isoenzymes; Kinetics; Substrate Specificity; Triticum
PubMed: 33750963
DOI: 10.1371/journal.pone.0248717 -
Annals of Emergency Medicine Jun 1983
Topics: Acid Phosphatase; Female; Humans; Male; Rape; Spermatozoa
PubMed: 6859643
DOI: 10.1016/s0196-0644(83)80495-8 -
International Journal of Molecular... Oct 2021Acid phosphatase and its regulation are important objects of biological and clinical research and play an important role in the development and treatment of prostate and...
BACKGROUND
Acid phosphatase and its regulation are important objects of biological and clinical research and play an important role in the development and treatment of prostate and bone diseases. The newly patented aminoalkanol (4-[2-hydroxy-3-(propan-2-ylamino)propyl]-1,7-dimethyl-8,9-diphenyl-4-azatricyclo[5.2.1.02,6]dec-8-ene-3,5,10-trione hydrochloride) (I) and (4-[3-(dimethylamino)-2-hydroxypropyl]-1,7-dimethyl-8,9-diphenyl-4-azatricyclo[5.2.1.02,6]dec-8-ene-3,5,10-trione hydrochloride) (II) derivatives have potential anticancer activity, and their influence on enzymatic activity can significantly impact the therapeutic effects of acid phosphatase against many diseases. Therefore, in this study, we investigated the action of compounds (I) and (II) on acid phosphatase.
METHODS
Capillary electrophoresis was used to evaluate the inhibition of acid phosphatase. Lineweaver-Burk plots were constructed to compare the Km of this enzyme in the presence of inhibitors (I) or (II) with the Km in solutions without these inhibitors.
RESULTS
Compound (I) showed a stronger competitive inhibition against acid phosphatase, whereas derivative (II) showed a weaker competitive type of inhibition. The detailed kinetic studies of these compounds showed that their type and strength of inhibition as well as affinity depend on the kind of substituent occurring in the main chemical molecule.
CONCLUSIONS
This study is of great importance because the disclosed inhibition of acid phosphatase by compounds (I) and (II) raises the question of whether these compounds could have any effect on the treatment possibilities of prostate diseases.
Topics: Acid Phosphatase; Amino Alcohols; Antineoplastic Agents; Drug Discovery; Enzyme Inhibitors; Humans; Kinetics; Male; Molecular Docking Simulation; Prostate
PubMed: 34769193
DOI: 10.3390/ijms222111761 -
Parasitology Research Jun 2007Acid phosphatases are putative virulence factors in different pathogenic microorganisms. Acid phosphatases can also inhibit the respiratory burst of human neutrophils....
Acid phosphatases are putative virulence factors in different pathogenic microorganisms. Acid phosphatases can also inhibit the respiratory burst of human neutrophils. In Cryptosporidium parvum, a protozoan parasitic, the study of enzymes is limited. In this paper, we report the presence of a membrane-bound acid phosphatase activity in C. parvum oocysts. The enzymatic activity was inhibited by protein tyrosine phosphatase inhibitors such as sodium orthovanadate, ammonium molybdate, and sodium tungstate and was not affected by protein serine/threonine phosphatase inhibitors such as okadaic acid and calyculin. Antibodies against the catalytic domain of human placental PTPase 1B cross-reacted with two molecules of 30 and 31 kDa present in membrane fraction of a Cryptosporidium oocyst homogenate. This is the first demonstration of acid phosphatase activity in Cryptosporidium.
Topics: Acid Phosphatase; Animals; Cryptosporidium parvum; Gene Expression Regulation
PubMed: 17252269
DOI: 10.1007/s00436-006-0457-8 -
Journal of Molecular Recognition : JMR Sep 2023Helicobacter pylori is the most common cause of gastric ulcers and is associated with gastric cancer. The enzyme HppA of class C nonspecific acid phosphohydrolases...
Helicobacter pylori is the most common cause of gastric ulcers and is associated with gastric cancer. The enzyme HppA of class C nonspecific acid phosphohydrolases (NSAPs) of H. pylori plays a crucial role in the electron transport chain. Herein, we report an in silico homology model of HppA consisting of a monomeric α + β model. A high throughput structure-based virtual screening approach yielded potential inhibitors against HppA with higher binding energies. Further analyses of molecular interaction maps and protein-ligand fingerprints, followed by molecular mechanics-generalized Born surface area (MM-GBSA) end point binding energy calculations of docked complexes, resulted in the detection of top binders/ligands. Our investigations identified potential substrate-competitive small molecule inhibitors of HppA, with admissible pharmacokinetic properties. These molecules may provide a starting point for developing novel therapeutic agents against H. pylori.
Topics: Acid Phosphatase; Helicobacter pylori; Molecular Dynamics Simulation; High-Throughput Screening Assays; Molecular Docking Simulation
PubMed: 37553866
DOI: 10.1002/jmr.3049 -
British Medical Journal Feb 1971
Topics: Acid Phosphatase
PubMed: 5541935
DOI: 10.1136/bmj.1.5745.406