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Results for “ACID PHOSPHATASE”

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At least 199 records · Page 11Linked to original sources
PubMed1989

Inhibition of neutrophil and natural killer cell function by human seminal fluid acid phosphatase.

The major acid phosphatase of human seminal fluid was purified to homogeneity by chromatography on Sephadex G-150, and DEAE-Sephadex, and by isoelectric focusing (pI, 4.3). This purified preparation of seminal fluid acid phosphatase blocked superoxide anion production by neutrophils stimulated with fMet-Leu-Phe (fMLP) by 50%. The phosphatase also hydrolysed myo-inositol 1,4,5-trisphosphate (IP3) in vitro, an intracellular second messenger which releases Ca2+ from intracellular pools, at nearly one-third the rate at which the nonphysiologic substrate 4-methylumbelliferylphosphate (MUP) was cleaved. In contrast, two phosphoinositide lipids, namely phosphatidylinositol 4,5-bisphosphate and phosphatidylinositol 4-monophosphate, were poor phosphatase substrates. Following fMLP stimulation of [3H]inositol-labeled neutrophils, the quantity of IP3 produced by phosphatase-treated cells was reduced by 69%. These results indicate that the human seminal fluid acid phosphatase may compromise the neutrophil's microbicidal response to the organism by hydrolyzing a second messenger (IP3) which is directly involved in the regulation of intracellular Ca2+ concentrations. The seminal fluid phosphatase also inhibited by 85% the ability of murine natural killer (NK) cells to inactivate target cells.

Acid Phosphatase↗
PubMed1981

The use of serum isoenzymes of alkaline and acid phosphatase as possible quantitative markers of tumor load in prostate cancer.

The tumor burden of 98 patients with metastatic prostatic cancer was compared longitudinally with the activities of bone (BAP) and liver isoenzymes (LAP) of alkaline phosphatase, total acid phosphatase (AcP), and prostate-specific acid phosphatase (PAP). A quantitative association between these enzyme markers and the tumor mass was suggested by comparing the enzymes with 1) both the treatment response and the estimation of metastasis by radionuclide bone scanning; 2) metastasis based upon radiographic evidence. In addition, an apparent extensive pretreatment bone tumor load was predictive for an elevated BAP activity, which was also a suggestive poor prognosis as previously reported. An elevation of PAP, in contrast to AcP, may precede the clinical disease progression in some patients. Data presented in this report have indicated that the levels of these enzymes compared well with the extent of tumor involvement and therefore may be considered suitable as adjuvant and even quantitative biochemical markers of bone and liver metastasis.

Acid Phosphatase↗
PubMed1994

The amino acid sequence of the red kidney bean Fe(III)-Zn(II) purple acid phosphatase. Determination of the amino acid sequence by a combination of matrix-assisted laser desorption/ionization mass spectrometry and automated Edman sequencing.

Purple acid phosphatase of the common bean Phaseolus vulgaris is a homodimeric 110-kDa glycoprotein with a Fe(III)-Zn(II) center in the active site of each monomer. After exchange of Zn(II) for Fe(II), the enzyme spectroscopically and kinetically resembles the mammalian purple acid phosphatases with Fe(III)-Fe(II) centers in monomeric 35-kDa proteins. The kidney bean enzyme consists of 432 amino acids/monomer with five N-glycosylated asparagine residues. The complete amino acid sequence was determined by a combination of matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS) and classical sequencing methods. Our strategy involved mass determination and sequence analysis of all cyanogen-bromide-generated fragments by automated Edman degradation. Limited cleavages with cyanogen bromide were performed to obtain fragments containing still uncleaved Met-Xaa linkages. MALDI mass spectra of these products allowed the characterization of each fragment and the determination of the order of the cyanogen bromide fragments in the intact protein without producing overlapping peptides. For one large 30-kDa methionine-free fragment, the alignment of the Edman-degraded tryptic peptides was obtained by MALDI-MS analysis and enzymic microscale peptide laddering of overlapping Glu-C-generated fragments. The employed strategy shows that the classical method, in combination with modern mass spectrometry, is an attractive approach for primary structure determination in addition to the DNA sequencing method.

Acid Phosphatase↗
PubMed1982

The interrelationships between acid phosphatase, aminopeptidase, diamine oxidase, citric acid, beta-glucuronidase, pH and zinc in human prostatic fluid.

Biochemical analysis of 328 human prostatic fluid samples were performed. The urea concentration of 69 samples was similar to that of serum and not indicative of significant contamination with urine. The pH of normal fluids was acidic (mean pH = 6.7). The interrelationships between zinc, citrate, acid phosphatase aminopeptidase, beta-glucuronidase, diamine oxidase and pH were investigated by factor analysis. Two significant factors were extracted, the first accounted for 89% of their common variance and the second for 11%. Zinc, citrate, acid phosphatase and aminopeptidase were positively and pH was negatively related to factor one. Beta-glucuronidase was positively related to factor two and diamine oxidase was largely independent of both factors. It was concluded that variables related to factor one share a common secretory control and mechanism, that some other mechanism operates in the case of beta-glucuronidase and that diamine oxidase may not be a true secretory product of the prostate.

Acid Phosphatase↗
PubMed1990

Is the subunit of prostatic phosphatase active? Reversible denaturation of prostatic acid phosphatase.

Prostatic acid phosphatase [E.C. 3.1.3.2.] is a dimeric protein consisting of two identical subunits. This enzyme was denatured in 6 M urea solution at pH 2.5, and kinetical analysis of reactivation by dilution was performed. At low protein concentrations a second-order kinetics for reactivation of phosphatase, with rate constant 8.3 m M-1sec-1, was observed. At higher protein concentrations the reactivation obeyed first-order kinetics. These results seem to exclude the possibility that subunits of the prostatic phosphatase are catalytically active and suggest that the association of two monomers is necessary for full activity.

Acid Phosphatase↗
PubMed1996

Identification and cDNA cloning of 35-kDa phosphatidic acid phosphatase (type 2) bound to plasma membranes. Polymerase chain reaction amplification of mouse H2O2-inducible hic53 clone yielded the cDNA encoding phosphatidic acid phosphatase.

We previously described the purification of an 83-kDa phosphatidic acid phosphatase (PAP) from the porcine thymus membranes (Kanoh, H., Imai, S.-i., Yamada, K. and Sakane, F.(1992) J. Biol. Chem. 267, 25309-25314). However, we found that a minor 35-kDa protein could account for the PAP activity when the purified enzyme preparation was further analyzed. We thus determined the N-terminal sequence of the 35-kDa candidate protein and prepared antipeptide antibody against the determined sequence, MFDKTRLPYVALDVL. The antibody almost completely precipitated the purified enzyme activity. Furthermore, the antibody precipitated from the radioiodinated enzyme preparation a single 35-kDa protein, which was converted to a 29-kDa form when treated with N-glycanase. We also found that the immunoprecipitable PAP activity was exclusively associated with the plasma membranes of porcine thymocytes. These results indicated that the 35-kDa glycosylated protein represents the plasma membrane-bound (type 2) PAP. We surprisingly noted that the N-terminal sequence of the porcine PAP was almost completely conserved in the internal sequence encoded by a mouse partial cDNA clone, hic53, reported as a H2O2-inducible gene (Egawa, K., Yoshiwara, M., Shibanuma, M., and Nose, K.(1995) FEBS Lett. 372, 74-77). We thus amplified from the mouse kidney RNA the hic53 clone by polymerase chain reaction, and obtained a cDNA encoding a novel protein of 283 amino acid residues with a calculated Mr of 31,894. Methionine reported as an internal residue was found to serve as an initiator, and the C-terminal 64 residues were lacking in hic53. The protein contains several putative membrane-spanning domains and two N-glycosylation sites. When transfected into 293 cells, the cDNA gave more than 10-fold increase of the membrane-bound PAP activity, which could be precipitated by the antipeptide antibody. In [35S]methionine-labeled cells, the translational product was confirmed to be a 35-kDa protein, which became 30 kDa in cells treated with tunicamycin, an inhibitor of N-glycosylation. We thus succeeded first in identifying the porcine type 2 PAP and subsequently in determining the primary structure of a mouse homolog of the PAP.

Amino Acid Sequence↗
PubMed2001

Alkaline phosphatase and tartrate-resistant acid phosphatase in osteoblasts of normal and pathologic bone.

A review of histochemical and immunohistochemical studies on alkaline phosphatase (AP) and tartrate-resistant acid phosphatase (TRAP) in osteoblasts leads to the following conclusions: 1) AP is a typical (non-specific) marker of osteoblasts, and TRAP is a typical (non-specific) marker of osteoclasts; 2) both enzymes may be used to identify the precursors of these cells and are found in young osteocytes; 3) both are released into the extracellular space; 4) both are expressed by metaphyseal osteoblast-like cells whose ultrastructural characteristics are similar to those of post-osteoclastic cells of the basic multicellular unit (BMU) and are also exhibited by osteoblasts and macrophages; 5) the increased numbers of these cells in hypocalcemic animals suggests that the local calcium ion concentration may trigger the transition of the reversal into the formation phase of the BMU.

Acid Phosphatase↗
PubMed2004

Changes in receptor activator of nuclear factor-kappaB, and its ligand, osteoprotegerin, bone-type alkaline phosphatase, and tartrate-resistant acid phosphatase in ovariectomized rats.

We investigated time-course changes in the expression of receptor activator of nuclear factor-kappaB (RANK), its ligand (RANKL), osteoprotegerin (OPG), bone-type alkaline phosphatase (BAP), and tartrate-resistant acid phosphatase (TRAP) in ovariectomized (OVX) rats. Samples of sera and coccyges were used for analysis of the enzyme activities and expression levels of proteins and mRNAs, and an immunohistochemical analysis was also performed. Serum BAP activity increased to 158.6% of the pre-operation value at 1 week after OVX, and then decreased to 38.7% at 8 weeks after OVX. On the other hand, the serum TRAP activity increased to 130.9% of the pre-operation level at 1 week after OVX, and was maintained at a high level, compared with the pre-operation level. The patterns of BAP and TRAP activity in the coccyges specimens were similar to those seen in the sera. The expression profiles of TRAP, RANK, and RANKL proteins in the coccyx specimens were similar to the pattern of serum TRAP activity, while the profiles of the BAP and OPG proteins were similar to the pattern of serum BAP activity in OVX rats. The changes in the mRNA expression levels of the osteogenic proteins were similar to those for protein expression. These biochemical changes in OVX rats were confirmed by immunohistochemical studies. Our results suggest that not only osteoclastogenesis accelerated but also osteoblastogenesis transiently increased during the early phase of osteoporosis.

Acid Phosphatase↗