[Studies on prostatic phosphatase. II. Study on serum acid phosphatase].
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Acid Phosphatase↗
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Immunoreactive prostatic acid phosphatase in prostatic cancer: diagnosis and followup of patients.
We compared the measurements of serum acid phosphatase activity to those obtained by radioimmunoassay of prostatic acid phosphatase in the sera of 126 untreated prostatic cancer patients. The catalytic activity of prostatic acid phosphatase was elevated in 32 per cent of the patients and the serum concentration of prostatic acid phosphatase was elevated in 66 per cent. Of these 126 patients 16 had stage T0-2M0N0-x disease, and enzyme activity and prostatic acid phosphatase concentration were increased in 0 and 38 per cent, respectively, in this group. Of the 110 patients with proved extracapsular cancer the corresponding figures were 36 and 70 per cent, respectively. We followed 109 of these 126 patients for 1 or more years after orchiectomy. A salient finding was that return of elevated serum prostatic acid phosphatase concentration to the health-associated reference interval within 7 days following castration indicated no progression of the disease at 1 year irrespective of the initial staging. The same was not detected by the measurement of catalytic activity of serum acid phosphatase. Our findings substantiate data showing that the measurement of circulating prostatic acid phosphatase is achieved better by immunological techniques than by measurements of catalytic activity of the enzyme. A novel aspect is the usefulness of immunological prostatic acid phosphatase measurements in evaluation of the prognosis of patients with metastatic prostatic carcinoma following ablative endocrine treatment.
Acid Phosphatase↗
Determination of acid phosphatase activity in normal human lymphocytes.
Acid phosphatase levels in pure lymphocytes from normal individuals were determined cytochemically on intact cells and spectrophotometrically on cell extracts. Good correlation was demonstrated between the results obtained with both methods. Biochemical assay showed that a normal range of 7.2 +/- 0.9 and 7.1 +/- 1.0 mMoles per 10(6) lymphocytes was obtained without and with tartrate inhibition, respectively. A significant loss of acid phosphatase level in the extract was found on storage. Seventy-five, 49 and 45 percent of the acid phosphatase activity remained after 3.5, 24, and 48 hours refrigeration at 4 degrees C, with 51 percent and 32 percent after 24 and 48 hours refrigeration at -20 degrees C, respectively. The spectrophotometric assay is less variable than the cytochemical stain. The widely utilized cytochemical method, although less reproducible, allows for evaluation of intracellular distribution of the enzyme in addition to level of activity.
Acid Phosphatase↗
Pre-treatment and post-treatment evaluation of prostatic adenocarcinoma for prostatic specific acid phosphatase and prostatic specific antigen by immunohistochemistry.
Prostatic specific acid phosphatase and prostatic specific antigen have been used as specific markers of prostatic adenocarcinoma in immunohistochemical studies, particularly when seeking the primary site of a poorly differentiated metastasis. We herein evaluate the effect of therapy on the persistence of these markers in surgically obtained tissues. Prostatic biopsies from 30 patients with adenocarcinoma of the prostate gland before and after treatment with orchiectomy alone, diethylstilbestrol, external beam radiation or combined radiation and diethylstilbestrol were studied for prostatic specific acid phosphatase and prostatic specific antigen using the indirect immunoperoxidase technique. The interval between biopsies ranged from 3 to 72 months, with an average of 28 months. All pre-treatment biopsies stained positively for prostatic specific acid phosphatase and prostatic specific antigen. Staining for prostatic specific antigen and prostatic specific acid phosphatase was seen easily in 29 of 30 post-treatment biopsies, while in 1 case infiltrating anaplastic cells surrounded by stroma showed staining for these antigens in an extremely small percentage of cells, which were overlooked easily unless examined carefully. In view of this small number of positively staining cells this case was designated as equivocal. While some cases demonstrated less intense staining in post-treatment biopsies compared to pre-treatment, this finding was by no means constant. With these primary antisera a higher percentage of cytologically malignant cells stained positively for prostatic specific acid phosphatase than for prostatic specific antigen in adjacent tissue sections in some cases. Prostatic specific acid phosphatase and prostatic specific antigen appear to be sensitive and persistent markers of prostatic adenocarcinoma despite morphologic changes accompanying various therapies.
Acid Phosphatase↗
Giant cell tumor of bone: fine structural localization of acid phosphatase.
The fine structural localization of acid phosphatase in the different cells in a benign giant cell tumor of bone has been studied. Stromal cells type 1 and 2 (fibroblast-like and macrophage-like, respectively) showed the presence of lead phosphate precipitate following incubation in a Gomori-type lead salt medium only in conventional lysosomes. In the multinucleated giant cells, the final product was deposited over lysosome-like organelles, and also over Golgi cisternae, vesicles, and vacuoles. Furthermore, evidence for presence of acid phosphatase was obtained in smooth-surfaced tubular, sausage-, horse-shoe-, and ring-shaped structures and over digestive vacuoles of autophagic or heterophagic origin. Finally, in these cells, many of the tubular and vacuolar elements located subjacent to areas of the plasma membrane with microvillous specializations (abortive brush borders?) were shown to carry acid phosphatase.
Acid Phosphatase↗
Physicochemical and kinetic properties of acid phosphatase from Saccharomyces cerevisiae.
Acid phosphatase from yeast Saccharomyces cerevisiae was purified, and its physicochemical and kinetic properties were investigated. The sedimentation coefficient has been determined to be s0(20,w) = 13.6 S. The diffusion constant has been found to be 3.9 X 10(-7) cm2s-1, and the calculated partial specific volume was v = 0.663 cm3/g. From these data, a molecular weight of 252,000 was calculated. Electrophoresis on gel slabs, with a linear concentration gradient of polyacrylamide (4-30%), showed size heterogeneity of the native enzyme preparation and indicated an apparent molecular weight in the range of 170,000 to 360,000. In the presence of sodium dodecyl sulfate, the molecular weight was in the range of 82,000 to 165,000, indicating dimeric structure of the native enzyme, which was confirmed by cross-linking experiments. Isoelectric focusing demonstrated charge heterogeneity of enzyme preparation. From CD spectrum it was calculated that the enzyme contains about 29% of alpha-helical structure. Excitation at 278 nm gave an emission fluorescence spectrum with a maximum at 340 nm. Amino acid analysis revealed a high content of aspartic acid, serine, and threonine. Glycine is found as the NH2-terminal amino acid. Initial velocity dependence on substrate concentration, as well as on pH, and thermostability studies indicated the presence of at least two enzyme forms in the preparation.
Acid Phosphatase↗
Phosphatase and oxygen radical-generating activities of mammalian purple acid phosphatase are functionally independent.
Bone-resorbing osteoclasts and activated macrophages express large amounts of tartrate-resistant acid phosphatase (TRAP), an iron-containing enzyme with unknown biological function. We studied acid phosphatase (AcP) and reactive oxygen species (ROS)-generating activities of recombinant rat TRAP. pH optimum was 4.5 for AcP activity and 6.5 for ROS-generating activity. Replacement of His113 and His216 by site-directed mutagenesis severely inhibited AcP activity, but had no significant effects on ROS-generating activity. Substrate specificity was not affected by the mutations. These results suggest that AcP and ROS-generating activities of TRAP are functionally independent.
Acid Phosphatase↗
Clinical studies of prostatic cancer imaging with radiolabeled antibodies against prostatic acid phosphatase.
Conventional antibodies against prostatic acid phosphatase, labeled with iodine-131, have been administered to patients with prostatic carcinoma for the external scintigraphic imaging of tumors containing prostatic acid phosphatase (radioimmunodetection). The method has been found to be safe and reliable for imaging of primary tumors and non-bone metastases, even differentiating between lung tumors of prostatic and pulmonary origin.
Acid Phosphatase↗
[Spectroscopic analysis of the interaction of ethanol and acid phosphatase from wheat germ].
Conformational and activity changes of acid phosphatase from wheat germ in ethanol solutions of different concentrations were measured by fluorescence spectra and differential UV-absorption spectra. The effect of ethanol on kinetics of acid phosphatase was determined by using the double reciprocal plot. The results indicate the ethanol has a significant effect on the activity and conformation of acid phosphatase. The activity of acid phosphatase decreased linearly with increasing the concentration of ethanol. Differential UV-absorption spectra of the enzyme denatured in ethanol solutions showed two positive peaks at 213 and 234 nm, respectively. The peaks on the differential UV-absorption spectra suggested that the conformation of enzyme molecule changed from orderly structure to out-of-order crispation. The fluorescence emission peak intensity of the enzyme gradually strengthened with increasing ethanol concentration, which is in concordance with the conformational change of the microenvironments of tyrosine and tryptophan residues. The results indicate that the expression of the enzyme activity correlates with the stability and integrity of the enzyme conformation to a great degree. Ethanol is uncompetitive inhibitor of acid phosphatase.
Acid Phosphatase↗
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.
Acid Phosphatase↗
Acid phosphatase levels of irrigant solution during transurethral prostatectomy.
The acid phosphatase level of irrigant solution used during transurethral prostate resections was measured in 20 patients. The mean acid phosphatase of the irrigant solution was 45.3 IU/L (S.D. 50.7). The degree of elevation of irrigant acid phosphatase was related to the weight of tissue resected, the duration of the resection, and the total volume of irrigant used. A transient elevation of serum acid phosphatase occurred postoperatively which was associated with the level of urinary acid phosphatase elevation and the amount of absorbed irrigant solution based on changes in serum sodium.
Acid Phosphatase↗
Glucose repression and autolysis of Saccharomyces cerevisiae cells: alterations in the cytochemical localization of acid phosphatase.
Alterations in the localization of acid phosphatase in Saccharomyces cerevisiae during glucose repression and during autolysis have been studied. Cell morphology becomes distinctly changed after only 2 h in the presence of high glucose concentration while after 3 h of glucose repression the majority of the mitochondrial structures resemble promitochondria. Yeast cells repressed for 6 h contain almost completely degraded mitochondrial structures and numerous lipid droplets in the central vacuole and cytoplasm. Destruction of mitochondria is accompanied by the accumulation of acid phosphatase in these organelles and in the cytoplasm, whereas its activity in the central vacuole is lowered, most probably because of the leakage of the enzyme into the cytoplasm. No preferential breakdown of mitochondria is observed during autolysis. On the contrary, mitochondria are apparently the last to be degraded. Digestion of cytoplasmic regions and membranous elements occurs intravacuolarly after sequestration by protrusions of the central vacuole which are formed at the initial stages of autolysis. Acid phosphatase is not released from the central vacuole, suggesting indirectly that vacuole enzymes do not migrate into the cytoplasm during autolysis.
Acid Phosphatase↗
Isolation and some properties of acid phosphatase-1(1) from tomato leaves.
An isozyme of acid phosphatase-1, acid phosphatase-1(1), was purified from the leaves of tomato (Lycopersicon esculentum) to homogeneity and characterized. The purified enzyme was homogeneous on polyacrylamide gel electrophoresis with or without sodium dodecyl sulfate. The gel filtration analysis showed that the native molecule had a relative molecular mass of about 61 kilodaltons (kDa). The relative molecular mass of the subunit on gel electrophoresis with sodium dodecyl sulfate was about 32 kDa, indicating that the native form of the enzyme was a homodimer. It was suggested by periodic acid-Schiff staining on the gel that the enzyme was a glycoprotein. The Km for p-nitrophenylphosphate was 2.9 x 10(-3) M. The enzyme had a pH optimum of 4.5 in 0.15 M potassium acetate buffer with p-nitrophenylphosphate as a substrate. This enzyme was activated by divalent metal ions, such as Zn2+, Mg2+, and Mn2+. The N-terminal amino acids were sequenced after the purified enzyme was treated with pyroglutamylpeptidase. It was suggested that the N-terminal amino acid was pyroglutamate.
Acid Phosphatase↗
Immunochemical evaluation of the organ specificity of prostatic acid phosphatase.
In a survey of normal and cancerous human tissues we determined the distribution of immunoreactive prostatic acid phosphatase, using rabbit antiserum to acid phosphatase purified from prostatic fluid. In all normal tissues and blood cells studied except leukocytes we found less than 0.1% (expressed as micrograms per gram of wet weight of tissue) of the quantity of immunoreactive prostatic acid phosphatase detected in normal prostate tissue by radioimmunoassay. A small quantity of cross-reactive antigen (2.5 microgram/10(8) cells) was found in leukocytes. In all normal and cancerous nonprostate tissues surveyed by an immunohistochemical technique we detected no immunoreactive prostatic acid phosphatase, except in kidney tissue. Faint but reproducible staining was detected in the lumen of distal tubules and collecting ducts and within interstitial capillaries. Immunoreactive prostatic acid phosphatase was detected in the urine of pre- and post-pubertal males and females. We propose that this material is from serum (low concentrations of immunoreactive prostatic acid phosphatase are present in the serum of men and women) and that it is excreted into urine by the kidneys. Full proof of this must await future experimentation. The specificity of our antiserum for prostatic acid phosphatase was demonstrated by the fact that the Mr 100 000 and 20 000 liver acid phosphatase isoenzymes did not cross with our antiserum in either the radioimmunoassay or double-diffusion analysis. Similarly, preparations of isoenzymes 5A and 5B are human serum albumin did not cross react.
Acid Phosphatase↗
[Simultaneous detection of acid phosphatase, choline, spermine and amino acids in seminal stains by paper chromatography].
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Acid Phosphatase↗
Dimeric nature and amino acid compositions of homogeneous canine prostatic human liver and rat liver acid phosphatase isoenzymes. Specificity and pH-dependence of the canine enzyme.
Two isoenzymes of rat liver acid phosphatase (orthophosphoric-monoester phosphohydrolase (acid optimum) EC 3.1.3.2) have been purified to homogeneity, at least one of these for the first time. Both of the rat liver isoenzymes have identical specific activities towards p-nitrophenyl phosphate. Molecular weights of the native enzymes are 92 000 for rat liver isoenzyme I and 93 000 for isoenzyme II, while the subunit molecular weights are 51 000 and 52 000 respectively. Data on substrate specificity and pH dependence are presented for the homogeneous canine prostatic enzyme, which is also isolated as a dimeric enzyme of (native) molecular weight 89 000. Carbohydrate analysis data are presented for canine prostatic acid phosphatase and it is further noted that both isoenzymes of rat liver acid phosphatase are also glycoproteins. The amino acid compositions of the two rat liver isoenzymes are presented together with those of the similar dimeric acid phosphatase of human liver and of canine prostate. Comparison of these results with published data for the amino acid composition of human prostatic acid phosphatase shows substantial similarities. However, significant differences are seen in the amino acid composition of rat liver acid phosphatase isoenzyme I as compared to a previous literature report. Most notably, 17 histidine residues are found per mol of isoenzyme I and 18 for isoenzyme II.
Acid Phosphatase↗
Molecular cloning of the mouse lysosomal acid phosphatase.
The mouse cDNA for lysosomal acid phosphatase was cloned. The deduced amino-acid sequence shows 89 and 96% identity with that of the human and rat enzyme, respectively. Namely all residues known to be important for the structure, catalytic activity and transport of lysosomal acid phosphatase are conserved among the three species.
Acid Phosphatase↗
Crystallization and preliminary X-ray diffraction data for a purple acid phosphatase from sweet potato.
Purple acid phosphatase from sweet potato is a homodimer of 110 kDa. Two forms of the enzyme have been characterized. One contains an Fe-Zn centre similar to that previously reported for red kidney bean purple acid phosphatase. Another isoform, the subject of this work, is the first confirmed example of an Fe-Mn-containing enzyme. Crystals of this protein have been grown from PEG 6000. They have unit-cell parameters a = b = 118.4, c = 287.4 A and have the symmetry of space group P6(5)22, with one dimer per asymmetric unit. Diffraction data collected using a conventional X--ray source from a cryocooled crystal extend to 2.90 A resolution. The three-dimensional structure of the enzyme will provide insight into the coordination of this novel binuclear metal centre.
Acid Phosphatase↗