Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:3.1.3.1 (alkaline phosphatase)
47,916 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

P1 protamines isolated from ejaculated human, stallion, bull, boar and ram spermatozoa and P2 protamines from human and stallion spermatozoa were subjected, after alkaline phosphatase treatment, to in vitro phosphorylation reactions using cAMP-dependent protein kinase (PKA) and protein kinase C (PKC). All P1 protamines were phosphorylated by PKA, whereas P2 protamines were phosphorylated only by PKC. In addition, human, stallion and boar, but not bull and ram, P1 protamines were phosphorylated by PKC. After phosphoamino acid analysis, the protamines showing positive signals for phosphoserine (P-Ser) were subjected to P-Ser conversion reaction and protein sequencing. Only stallion (St1) and human (HP1) P1 protamines contained P-Ser after PKA phosphorylation, located in the middle region of the molecule, i.e., at Ser29 in St1 and Ser28 in HP1. All other phosphorylated P1 protamines contained only P-Thr, which could not be further localized in the sequence with the present methods. After PKC phosphorylation, the internally located Ser residues in human (ser21) and stallion (Ser29) P1 protamines were phosphorylated and, in boar P1 protamine, only Thr43 was slightly phosphorylated. The N-terminally located Ser residues in P1 protamines, which are known to be phosphorylated in vivo, were not phosphorylated by either kinase, indicating that there must still be other types of protamine kinases in sperm cells responsible for their phosphorylation. Within P2 protamines, HP2 was equally well phosphorylated at all Ser residues in addition to some Thr phosphorylation, whereas, in St2, Ser32 was the main target for PKC phosphorylation in vitro. Collectively, PKC is a good candidate for in vivo phosphorylation of P2 protamines and PKA for phosphorylation of some hydroxyamino acid residues in P1 protamines.
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PMID:P2 protamines are phosphorylated in vitro by protein kinase C, whereas P1 protamines prefer cAMP-dependent protein kinase. A comparative study of five mammalian species. 803 90

In this study we have used acridine orange staining, as described by Evenson (1990), to follow changes in DNA packaging as they occur in hamster spermatozoa which have left the testis and are undergoing maturation in the epididymis. Measurement of the green and red fluorescent intensities of hamster sperm nuclei by flow cytometry demonstrated a decrease in acridine orange binding to DNA as sperm made their way from proximal corpus epididymis to the vas deferens. Using sperm from the cauda epididymis of the mature hamster as the standard, a method was developed for estimating the % of cells in a given sample that have matured with regard to DNA packaging. Staining with bromobimane was used to determine the extent of sulfhydryl oxidation in the nuclei. It was seen that sulfhydryl oxidation occurred mainly in the cauda epididymis whereas another process in chromatin condensation occurred earlier, during sperm passage through the caput epididymis. This earlier process could be mimicked by incubating sperm nuclei with alkaline phosphatase, suggesting that it consists of removal of phosphate in protamine.
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PMID:Chromatin condensation in hamster sperm: a flow cytometric investigation. 812 36

Semen of Jamunapari goat bucks was frozen in three diluents egg yolk-tris, egg yolk/citrate/glucose, and skim milk/egg yolk. In fresh ejaculated semen over 90% of the spermatozoa had normal head and acrosome morphology. Quantification of goat sperm structure with Giemsa stain revealed significant (P < 0.01) damage to acrosome on freezing which varied between 38 to 43% in three diluents. Scanning electron microscopy defined and revealed greater damage during freezing with 50% sperm heads having normal acrosome structure in three diluents. The ultrastructural changes detected in frozen goat sperm was protrusion at the anterior cap, broken tail, swelling of acrosome, and loss of acrosomal contents. The leakage of five enzymes GOT, GPT, hyaluronoglucosaminidase, acid phosphatase, and alkaline phosphatase measured simultaneously revealed a positive correlation between enzyme release and acrosomal damage.
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PMID:Acrosome damage and enzyme leakage of goat spermatozoa during dilution, cooling and freezing. 818 56

The level of seminal leucocytes and the prevalence of leucocytospermia was determined in a group of fertile and infertile southern Chinese men in Hong Kong. Sixteen normal fertile semen donors and 49 men with male factor infertility were studied prospectively. None had antisperm antibodies and past or present evidence of genital tract infection. Seminal leucocytes and their subsets were analysed using monoclonal antibodies and an immunocytochemical alkaline phosphatase-anti-alkaline phosphatase conjugate technique. Seminal leucocytes were detectable in 94% and 86% of the fertile and infertile men respectively, with the predominant subset being granulocytes. Leucocytospermia (> 1 x 10(6) leucocytes/ml) was found in only one of the 49 (2%) infertile men without clinical evidence of genito-urinary infection. Inverse correlations were observed between (1) the percentage of spermatozoa with normal morphology and the number of T-helper/inducer cells, (2) the linearity of sperm movement and the number of T-lymphocytes. In conclusion, the level of seminal leucocytes and the prevalence of leucocytospermia is low in infertile Chinese subjects. The effect of seminal leucocytes on sperm function in these subjects needs further evaluation.
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PMID:Seminal leucocyte subpopulations and sperm function in fertile and infertile Chinese men. 835 33

Semenogelin I and II (Sgl, Sgll) are two separate gene products of chromosome 20 with extensive (80%) identity in primary structure. They are mainly responsible for immediate gel formation of freshly ejaculated semen. Degradation of Sgl and Sgll is due to the proteolytic action of prostate-specific antigen (PSA); it results within 5-15 minutes in liquefaction of semen and release of progressively motile spermatozoa. By means of cDNA cloning and Northern blots, Sgl and Sgll transcripts have previously been shown to be abundant in human seminal vesicles, but Sgll alone is suggested to be expressed at low levels in the epididymis. To characterize the expression and tissue distribution of Sgl and Sgll in greater detail, we produced monoclonal immunoglobulin Gs (lgGs for immunocytochemistry (lCC) and specific [35S]-, digoxigenin-, or alkaline phosphatase-labeled 30-mer antisense probes to Sgl and Sgll for in situ hybridization (lSH). Immunocytochemical staining for both Sgl and Sgll, and lSH detection of both Sgl and Sgll transcripts, were demonstrated in the cytoplasm of seminal vesicle epithelium. lSH showed Sgll alone to be expressed in the epithelium of the epididymal cauda. Neither lCC nor lSH yielded any evidence of Sgl or Sgll expression in caput or corpus epithelium or in any stromal cells of the epididymis. Consistent with our previous findings using polyclonal lgG, monoclonal anti-Sgll Sgll lgGs identified epitopes on the posterior head, midpiece, and tail of ejaculated spermatozoa. Spermatozoa in the epididymal cauda were also immunoreactive, but those in the caput or corpus region of the epididymis as well as those in the testis were negative. As shown by lCC, neither Sgl nor Sgll were expressed in the testis, the prostate, the female genital tract, or other normal human tissue specimens. Although the significance of Sg attachment to epididymal and ejaculated spermatozoa remains to be established, monoclonal anti-Sg lgG might prove useful in establishing the origin of seminal vesicle tissue components in prostate core biopsies or other biopsy specimens.
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PMID:Distribution and tissue expression of semenogelin I and II in man as demonstrated by in situ hybridization and immunocytochemistry. 883 37

Before fertilization, equine spermatozoa adhere to oviduct epithelial cells (OEC) of the mare. The biochemical basis for this adhesion has not been determined. Our objective was to produce an antiserum to block this interaction. Ejaculated spermatozoa were subjected to nitrogen cavitation and spermatozoal plasma membranes enriched by sucrose density gradient centrifugation; membrane enrichment was confirmed by comparative alkaline phosphatase analysis, electron microscopy, and one- and two-dimensional PAGE. Periacrosomal plasma membrane was used as an immunogen for the production of an antiserum, which recognized several components of spermatozoal plasma membrane on Western blots. Antigen-binding fragments (Fab) were isolated by papain digestion from a specific antiserum and from nonimmunized rabbit IgG (control). The periacrosomal regions of epididymal and ejaculated spermatozoa were immunolabeled with antiserum Fab but not control Fab. The immunoneutralizing activity of antiserum Fab was tested in fluorescent cell-binding assays by competitive inhibition of the binding of spermatozoa to OEC monolayers or explants. In both assays, binding of spermatozoa to OEC was reduced as the concentration of specific Fab increased. These results suggest that one or more protein or glycoprotein components of the rostral spermatozoal plasma membrane mediate adhesion between spermatozoa and oviduct epithelium in vitro.
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PMID:Antibody directed against plasma membrane components of equine spermatozoa inhibits adhesion of spermatozoa to oviduct epithelial cells in vitro. 904 18

Effect of cyclophosphamide administration (100 mg/kg body weight, ip, for 5 consecutive days) was studied on albino rat testis and epididymidis after 3 and 6 weeks of treatment. Cyclophosphamide decreased testis and cauda epididymidal weights, sperm count, motile and viable spermatozoa and increased percentage of abnormal spermatozoa. The biochemical changes observed in the testis include increase in acid and alkaline phosphatase activities and decrease in proteins and activity of lactate dehydrogenase. The levels of lipids and total cholesterol were not affected. In the epididymidis cyclophosphamide caused decrease in the tubular diameter and increase in its epithelial height. It is concluded that cyclophosphamide brings about structural and biochemical changes in the testis and epididymidis.
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PMID:Cyclophosphamide-induced structural and biochemical changes in testis and epididymidis of rats. 941 79

Spermatic enzymes (fructose, alkaline phosphatase, gammaglutamyl transferase, alpha-glucosidase, dipeptydil aminopeptidase IV) were measured in 200 patients with secretory-toxic infertility. It is shown that in some variants of infertility changes in the levels of spermatic enzymes are compensatory. These changes may also reflect qualitative characteristics of spermatozoa.
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PMID:[Changes in the enzyme level of the sperm of men with infertility]. 957 5

A complex of biochemical tests and standard techniques were used in males with relative sterility (RS) for ejaculate study allowing to detect pathology by qualitative and quantitative characteristics of the activity of spermatic plasma enzymes: alkaline phosphatase, acid phosphatase, gamma-glutamyl transferase, dipeptyl aminotransferase IV. A comprehensive evaluation of spermatic plasma enzymes of membrane-bound and intrastructural location made in 602 patients helped to establish severity and pathogenetic mechanisms of spermatozoon membrane damage in male RS. Hyperenzymospermia in patients with RS was of membrane origin and could be due to destabilization of the membrane and spermatozoon intrastructural elements. Staging of and an original approach to pathogenesis of impaired fertilizing ability of spermatozoa in males with RS are proposed.
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PMID:[Role of spermatic plasma enzyme in pathogenesis of relative male sterility]. 1118 8

In this study the short term (3 months) toxicological effects of varying levels of Catha edulis leaves were examined on the plasma concentration of liver enzymes and the histopathology of tissue sections of various organs including the liver, kidneys, spleen and testis. Both the biochemical and histopathological data demonstrated, initial signs of Catha edulis toxicity. Our results show a significant increase in plasma levels of alkaline phosphatase (ALP) and alanine aminotransferase (ALT) with all levels of Catha edulis leaves tested and throughout the treatment period. The increase of ALP was more prominent than that of ALT. The plasma levels of aspartate aminotransferase (AST) were only moderately increased at the higher dose (30%) in the later stages of treatment. In addition, a time-dependent gradual increase in indirect bilirubin with a concomitant decrease in direct bilirubin levels was observed with the 30% Catha edulis with no signs of haemolysis. The histopathology of tissue sections of the liver displayed evidence of congestion of the central liver veins as well as acute hepatocellular degenerative and regenerative activities in the tissue sections obtained from animals treated with both 20% and 30% Catha edulis. Similarly, histopathological examination of the tissue sections of the kidneys showed some lesions, and the degree of the lesion increased as the dose of Catha edulis leaves increased including: the presence of fat droplets particularly seen in the upper cortical tubules; acute cellular swelling; hyaline tubules; and acute tubular nephrosis. In contrast, Catha edulis treatment did not affect the spleen and increased the rate of spermatogenesis in male rabbits with the spermatozoa being quite evident, the Leydig cells were in good condition and were not affected by the doses given.
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PMID:Investigation into the toxicological effects of Catha edulis leaves: a short term study in animals. 1193 13


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