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Query: UNIPROT:P20020 (adenosine triphosphatase)
 3,299 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The cytochemical localization and intensity of adenosine triphosphatase (ATPase) activity in the spermatozoa from fertile and infertile human ejaculate were observed by an electron microscope. Sperm from fertile and infertile human ejaculate were fixed in 1% glutaraldehyde and treated histochemically to demonstrate calcium- and magnesium-dependent ATPase (Ca++- and Mg++-dependent). Furthermore, as substrates, ADP, AMP, and beta-glycerophosphate were used. The localization of Ca++-activated ATPase was not different from that of Mg++-activated ATPase. In the fertile human ejaculated sperm, ATPase activity was found on the surface of the acrosome and mitochondria consisting of the mitochondrial sheath, around the outer coarse fibers and in the axial filament complex. Compared with the result with fertile specimens, in the infertile human ejaculated sperm, ATPase activity on the motile structures, the outer coarse fibers, and the axial filament complex were considerably weaker and occasionally not recognized. From this study, it may be considered that ATPase around the outer coarse fibers and in the axial filament complex of sperm may serve to mediate contraction of the axonemal elements during motility. (Author's Modified)
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PMID:[The cytochemical localization of ATPase activity in the spermatozoa from fertile and infertile human ejaculate by electron microscope (author's transl)]. 13 69

The surface epithelium of vagina, uterovaginal region and uterus as well as the uterine and uterovaginal glands of 18 mature female quails were studied with histochemical methods. As in other avian species also in the quail a storage of spermatozoa in the lightly coiled uterovaginal glands takes place. The functional specialization of these glands is underlined by their distinct enzyme pattern. A strong reactivity of enzymes from oxidative pathways and of adenosine triphosphatase between epithelium and glandular luminal content. Alkaline phosphatase in the glandular epithelium was observed only when an egg is transported through the uterovaginal region. As in other vertebrate sperm storing sites also in the uterovaginal region of the quail the presence of a strong steroid dehydrogenase activity is registered.
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PMID:[On the histotopochemistry of the uterovaginal region in the quail (Coturnix coturnix japonica) (author's transl)]. 13 47

The "morphology" of the enzymatic activities of thiamine pyrophosphatase (TPPase), acid phosphatases (ACPases), adenosine triphosphatase (ATPase) and steroid-3 beta-ol dehydrogenase (St-3 beta-ol DH) has been described using as a basis the classification of the seminiferous epithelium of the rat into 14 stages as proposed by Leblond and Clermont (1952a, b). It was demonstrated (Figs. 1, 2) that 1. the kinetics of the enzymatic pattern is correlated with the developmental stages during spermatocyto- and spermiogenesis, and that therefore the chemocytostructure, especially of the germ cells, shows characteristic changes. 2. the enzymatic pattern yields information on the chemohistostructure of the testis, and thus indicates interactions between the germ cells and the coordinated somatic cells. This is valid especially for the behaviour of the "marker enzymes" TPPase and ACPases. Initially the activity of both enzymes is distributed in the cytoplasm: TPPase appears in stage VII in the preleptotene spermatocytes, and ACPases appear in stage VII in the pachytene spermatocytes. In the following stages the activity of TPPase and ACPases increases and becomes more and more concentrated, i.e. from stage IX to XIV and thereafter from stage I to XIII in the case of TPPase, and from stage I to XIII in the case of ACPases. Finally the enzymatic activity of both TPPase and ACPases is arranged in spherical bodies near the nucleus of the spermatocytes. Thus the late pachytene and diplotene spermatocytes, as well as the spermatocytes in diakinesis, are characterized by deeply stained spherical dots covering the region of the Golgi apparatus. Both enzymes disappear during the maturation divisions--parts of the cytoplasm of the II-spermatocytes during interphase react weakly positive--, reappear in the Golgi region of the newly formed spermatids in stage I, remain there up to stage V in the case of ACPases, and up to stage VII in the case of TPPase. From stages VIII to XIV TPPase is weakly positive in the Golgi apparatus of the elongating spermatids, moving within the cytoplasm from the head region towards the tail. Finally they appear in the cytoplasm of the Sertoli cells: (1) ACPases appear in the borderline region between the Sertoli cells and the elongated spermatids in stages XII to XIV (2) TPPase first appears in the basal region of the Sertoli cells in stages XI to XIV, and becomes positive in the subsequent stages I to IV as "streamer like" bands from the basement membrane up to the heads of the elongated spermatids. Both enzymes disappear gradually during stages I to III and IV to V respectively. Stage dependence of ATPase can be observed in the apical region of the Sertoli cells around the heads and the middle pieces of the elongated spermatids. ATPase appears for the first time in stages IX to X, and becomes increasingly more and more concentrated and condensed up to the point when the newly formed spermatozoa are released in stage VIII...
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PMID:Kinetics of the enzymatic pattern in the testis. I. Stage dependence of enzymatic activity and its relation to cellular interactions in the testis of the Wistar rat. 15 89

Certain phosphatases have been localized by histochemical techniques in various tissues of a pigeon cestode, Raillietina (Raillietina) johri. Acid phosphatase (AcPase), alkaline phosphatase (AlPase) and adenosine triphosphatase (ATPase) were present in almost all structures: tegument; subtegumental muscles; subtegumental cells; excretory canal; testes; sperm ductules; vas deferens; cirrus sac; cirrus; ovary; receptaculum seminis; vagina; vitelline gland cells; oocytes; uterus; embryonated eggs. AlPase was absent in parenchyma, spermatocytes, spermatids and spermatozoa. AlPase activity was more intense in the tegument of mature gravid proglottides. AcPase and ATPase were visualized in various stages of spermatogenesis of the parasite. ATPase activity was also observed in chromosomes. 5'-nucleotidase (AMPase) activity was restricted to embryonated eggs only. Functional significance of these phosphatases is discussed.
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PMID:Histochemical studies on Raillietina (Raillietina) johri (Cestoda: Davaineidae). I. Nonspecific and specific phosphatases. 22 30

Outer-arm dynein purified from trout spermatozoa was disrupted by low-ionic-strength dialysis, and the resulting subunits were separated by sucrose density-gradient centrifugation. The intact 19 S dynein, containing the alpha- an beta-heavy chains, intermediate chains (ICs) 1-5 and light chains (LCs) 1-6, yielded several discrete particles: a 17.5 S adenosine triphosphatase (ATPase) composed of the alpha- and beta-chains ICs 3-5 and LC 1; a 9.5 S complex containing ICs 1 and 2 together with LCs 2, 3, 4, and 6; and a single light chain (LC 5), which sedimented at approximately 4 S. In some experiments, ICs 3-5 also separated from the heavy chain complex and were obtained as a distinct subunit. Further dissociation of the 17.5 S particle yielded a 13.1 S ATPase that contained the beta-heavy chain and ICs 3-5. The polypeptide compositions of the complexes provide new information on the intermolecular associations that occur within dynein. Substructural features of the trout dynein polypeptides also were examined. The heavy chains were subjected to vanadate-mediated photolysis at the V1 sites by irradiation at 365 nm in the presence of Mg2+, ATP, and vanadate. Fragment pairs of relative molecular mass (Mr) 245,000/185,000 and 245,000/170,000 were obtained from the alpha- and beta-heavy chains, respectively. Photolysis of these molecules at their V2 sites, by irradiation in the presence of vanadate and Mn2+, yielded fragments of Mr 160,000/270,000 and 165,000/250,000, respectively. These values confirm that the alpha- and beta-heavy chains have masses of 430,000 and 415,000 daltons, respectively. Immunological analysis using monoclonal antibodies revealed that one intermediate chain from trout dynein (IC 2) contains epitopes present in two different intermediate chains from Chlamydomonas dynein. This indicates that specific sequences within the dynein intermediate chains have been highly conserved throughout evolution.
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PMID:Outer-arm dynein from trout spermatozoa: substructural organization. 169 10

Digitonin-permeabilized guinea pig spermatozoa undergo acrosomal matrix dispersion in response to 2.0 mM CaCl2. In this report, the effects of pH and metal ions on matrix dispersion in permeabilized spermatozoa are examined. Calcium-induced dispersion of the acrosomal matrix was dependent on the calcium concentration; the response was not observed at concentrations of CaCl2 less than 50 microM. Magnesium could not substitute for calcium and, in fact, had a retarding effect on the calcium-induced response. Matrix dispersion was also found to be pH-dependent. The induction of matrix dispersion was inhibited at pH 5.6 and pH 9.5 relative to the responses observed at pH 6.3 and pH 7.8. Nigericin induced acrosomal matrix dispersion in the absence of added calcium, indicating a possible role of Na+/H+ exchange across the outer acrosomal membrane in initiating the matrix modification. Sodium was required for the action of nigericin; the ionophore was ineffective in medium in which choline chloride or sucrose was substituted for NaCl. In contrast, the calcium-induced dispersion of the acrosomal matrix occurred in the absence of sodium. Furthermore, low concentrations of calcium inhibited an adenosine triphosphatase activity associated with isolated acrosomal apical segments. These data are consistent with the hypothesis that calcium induces alkalinization of the acrosome, leading to matrix dispersion. However, permeabilized spermatozoa incubated at either pH 9.5 or in the presence of 50 mM NH4Cl at pH 7.5 failed to undergo spontaneous matrix dispersion, suggesting that elevated intraacrosomal pH alone was not sufficient to initiate the reaction. The proposed alternative hypothesis is that calcium initiates matrix dispersion by a mechanism in which elevated intraacrosomal pH may be a secondary response.
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PMID:Regulation of acrosomal matrix dispersion in digitonin-permeabilized guinea pig spermatozoa. 214 57

Unknown factors in the seminal plasma of normal semen that affect the motility of spermatozoa have a positive effect on adenosine triphosphatase (ATPase) enzyme activity. In an attempt to produce such an effect, spermine, spermidine and kallikrein were added to the incubation media in which spermatozoal ATPase enzyme activity was determined. These seminal substances increased the triple ATPase enzyme activity of spermatozoa from oligoasthenozoospermic men. We propose that the ATPase enzyme activity of spermatozoa may indicate sperm motility as a biochemical test.
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PMID:The effect of spermine, spermidine and kallikrein on the triple adenosine triphosphatase enzyme activity of spermatozoa in males with oligoasthenozoospermia. 252 16

Inheritance of the mitochondrial genome is known to be exclusively maternal. To determine whether the loss of paternal mitochondria could be due to a deficiency of RNA in the spermatozoal mitochondria, the expression of mitochondrial genes was studied in testicular cells at various stages of spermatogenesis and in epididymal spermatozoa. The presence of mitochondrial transcripts was examined by Northern blot analysis using probes for the following mitochondrially encoded genes: 12 S and 16 S ribosomal RNAs and a group of mRNAs including cytochrome oxidase subunits I and II (COI-COII), cytochrome b (cyt b), adenosine triphosphatase (ATPase) subunits 6 and 8, and subunit 1 of the respiratory chain NADH dehydrogenase (ND1). Comparison of total testicular RNA preparations from prepuberal (6, 8, 12, 16, 18, 20, 22, and 30 days old) and sexually mature (45 days old) mice revealed no major qualitative or quantitative differences in the levels of the mitochondrial transcripts described above. Similar results were observed from enriched preparations of type A and B spermatogonia and interstitial cells obtained from the testes of 8-day-old mice. Transcripts for COI-COII, ATPase 6, or ND1 were reduced in amount in the enriched preparations of pachytene spermatocytes, round spermatids, and residual bodies when compared to the amount in total testis or liver RNA. Transcripts of all the mitochondrial genes analyzed were present in RNA preparations isolated from sperm midpiece tails obtained after sonication of epididymal spermatozoa. These studies demonstrate that (a) during testicular development the levels of mitochondrial RNA in total testicular extracts show no major qualitative and quantitative differences; (b) the mitochondrial transcripts in enriched populations of type A and type B spermatogonia are not different from those obtained from total testes extracts; (c) mitochondrial transcript levels gradually decrease in enriched preparations of pachytene spermatocytes, round spermatids, and residual bodies; and (d) the mitochondrial rRNAs and mRNAs encoded by several mitochondrial genes can be isolated from sperm midpiece tails.
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PMID:Mitochondrial gene expression in male germ cells of the mouse. 277 68

The preparation of a purified fraction of ram sperm plasma membranes is described and validated in this paper. Lipid analyses were performed on both the membrane preparation and whole spermatozoa; the main differences were that plasma membranes showed a significantly higher cholesterol: phospholipid molar ratio and a higher sphingomyelin content than did whole spermatozoa, but a lower proportional content of phosphatidylethanolamine. Enzymic assays revealed the presence of two distinct adenosine triphosphatase (ATPases) in the membrane fraction, activated independently by calcium and sodium ions. Arrhenius plots of the calcium-stimulated ATPase activity demonstrated that a change in energy of activation occurred in the region of 23 degrees C; it is believed that this is evidence for the occurrence of a thermal phase transition in the lipid environment of the enzyme molecules.
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PMID:Determination of lipid composition and thermal phase transition temperature in an enriched plasma membrane fraction from ram spermatozoa. 315 98

Comparison of beat frequencies with rates of dephosphorylation of adenosine triphosphate by glycerinated sea urchin spermatozoa as functions of adenosine triphosphate concentration suggests that each molecule of the flagellar adenosine triphosphatase, dynein, dephosphorylates one adenosine triphosphate molecule during each beat cycle.
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PMID:Adenosine triphosphate usage by flagella. 422 45


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