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:3.6.1.3 (ATPase)
65,361 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Lampropholis guichenoti is an oviparous lizard that lays eggs with a calcareous outer shell. We used immunofluorescence microscopy to describe the occurrence and distribution of Ca2+ ATPase pumps in the uterus of L. guichenoti at different stages of the reproductive and egg-shelling cycles. Ca2+ ATPase pumps were not demonstrated by immunofluorescent techniques in any uterine tissue until egg-shelling had commenced and at least partly calcified eggs were in the uterus. During egg-shelling, Ca2+ ATPase pumps occur on the apical and baso-lateral surfaces of uterine epithelial cells, and those of associated shell glands in the stroma of the uterus. We conclude that Ca2+ ATPase pumps provide a major mechanism for deposition of the calcareous eggshell of L. guichenoti and that the pumps are up-regulated when required in the reproductive cycle. Furthermore, it is likely that specific calcium glands in the stroma of the uterus are involved in the rapid transport required for egg-shelling, but the differential contribution of luminal and glandular epithelial cells is not known.
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PMID:Calcium ATPase expression in the oviducts of the skink, Lampropholis guichenoti. 1746 27

Present investigation was planned to evaluate the therapeutic effectiveness of chelating agents against vanadium intoxication on blood and reproductive organs of rats. Male and female albino rats were injected vanadyl sulphate (7.5 mg/kg, po, for 21 days, 5 days in a week). Chelating agents tiron (T) alone and in combination with lipoic acid (LA), vitamin E (vit E) and selenium (Se) were given for 2 days/week. With the administration of vanadyl sulphate to rats fructose level in seminal vesicles was significantly (P< or =0.05) declined. The activities of alkaline phosphatase and adenosine triphosphatase were also decreased, whereas glycogen content and acid phosphatase activity increased in testis, seminal vesicles, ovaries and uterus after toxicant exposure. Significant changes in serum transaminases, serum alkaline phosphatase and lactate dehydrogenase were recouped by chelation therapy. Lipid peroxidation, reduced glutathione level and triglycerides levels altered significantly after exposure to vanadium in rats. The ultrastructural damage in spermatogenic stages in treated animals showed recovery pattern after therapy. Co-treatment with antioxidants restored these activities. The most effective combination was tiron + selenium followed by tiron + vitamin E, and tiron + lipoic acid.
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PMID:Chelation therapy and vanadium: effect on reproductive organs in rats. 1758 85

The paper is devoted to comparative analysis of the influence of a new class of macrocyclic compounds - calixarens on enzymatic activity of two ATP-hydrolase systems localized in the plasmatic membrane of contractile (myocytes of the uterus) and mobile (spermatozoids) cells--Na+, K+ -ATPase and basal Mg2+ -ATPase. The experiments performed on plasmatic membrane suspensions of myometrium and spermatozoids treated with detergent the authors studied the influence of calixarens C-97, C-99, C-107 (identified by the codes), functionalized with fragments of alpha-hydroxyphosphonic, alpha-aminophosphonic and methylenbisphosphonic acids accordingly, on enzymatic activity. The results have shown that C-97 and C-107 calixarenphosphonic acids in 100 microM concentration (97-99%) inhibit Na+, K+ -ATPase activity in both cases almost completely. C-99 (100 microM) calixaren appeared to be less effective with regard of its influence on the enzymatic systems under study: in the case of plasmatic membranes of myometrium suspension the activity of Na+, K+ -ATPase was decreased by 84-88%, and in the case of spermatozoids suspension--just by 15-20% of the control. All the studied calixarens (for both objects) in the maximal concentration (100 microM) practically did not influence the activity of basal Mg2+ -ATP-ase. The calixarens inhibited the enzymatic activity of Na+, K+ -ATPase more effectively than ouabain: in the first case the value of apparent inhibition constant I(0,5) was 25-100 nM, and in the second case--20-100 microM. The inhibition influence of calixarens on Na+, K+ -ATPase activity is characterized by the phenomenon of negative cooperativity (Hill's coefficient nH <1); the influence of ouabain in the case of plasmatic membranes of myometrium suspension is also characterized by negative cooperativity (nH < 1), and in case of spermatozoids suspension--by positive cooperativity (nH >1). The above results show that the studied calixarens are effective inhibitors of Na+, K+ -ATPase plasmatic membrane of contractive and mobile cells (C-97, C-99, C-107 calixarens in case of myocytes of uterus, and C-97, C-107 calixarens in case of spermatozoids).
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PMID:[Comparative study of calixarene effect on Na+, K+ -ATPase activity in plasma membrane of contractile and mobile cells]. 1798 11

Investigation the influence of calyx[4]arenes C-90, C-91, C-97 and C-99 (codes are indicated) on the enzymatic activity of four functionally different Mg2+ -dependent ATPases from smooth muscle of the uterus: actomyosin ATPase, transporting Ca2+, Mg2+ -ATPase, ouabain-sensible Na+, K+ -ATPase and basal Mg2+ -ATPase. It was shown that calixarenes C-90 and C-91 in concentration 100 microM act multidirectionally on the functionally different Mg2+ -dependent ATP-hydrolase enzymatic systems. These compounds activate effectively the actomyosin ATPase (Ka = 52 +/- 11 microM [Ukrainian character: see text] 8 +/- 2 microM, accordingly), at the same time calixarene C-90 inhibited effectively activity of transporting Ca2+, Mg2+ -ATPase of plasmatic membranes (I(0,5) = 34.6 +/- 6.4 microM), but influence on membrane-bound Na+, K+ -ATPase and basal Mg2+ -ATPase. Calixarene C-91 reduce effectively basal Mg2+ -ATPase activity, insignificantly activating Na+, K+ -ATPase but has no influence on transporting Ca2+, Mg2+ -ATPase activity of plasmatic membranes. Calixarenes C-97 and C-99 (100 microM), which have similar structure, have monodirectional influence on activity of three functionally different Mg2+-dependent ATPases of the myometrium: actomyosin ATPase and two ATPases, that related to the ATP-hydrolases of P-type--Ca2+, Mg2+ -ATPase and Na+, K+ -ATPase of plasmatic membranes. Basal Mg2+ -ATPase is resistant to the action of these two connections. Results of comparative experiments that were obtained by catalytic titration of calixarenes C-97 and C-99 by actomyosin ATPase (I(0,5) = 88 +/- 9 and 86 +/- 8 microM accordingly) and Na+, K+ -ATPase from plasmatic membranes (I(0,5) = 33 +/- 4 and 98 +/- 8 nM accordingly) indicate to the considerably more sensitiveness of Na+, K+ -ATP-ase to these calixarenes than ATPase of contractile proteins. Thus, it is shown that calixarenes have influence on activity of a number of important enzymes, involved in functioning of the smooth muscle of the uterus and related to energy-supplies of the process of the muscle contracting and support of intracellular ionic homeostasis. The obtained results can be useful in further researches, directed at the use of calixarenes as pharmaceutical substance, able to normalize the contractile function of the uterus at some pregnancy pathologies in women's.
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PMID:[Comparative study of calixarene effect on Mg2+ -dependent ATP-hydrolase enzymatic systems from smooth muscle cells of the uterus]. 1798 14

Calcium ATPase (Ca2+-ATPase) is a key enzyme that participates in the translocation of calcium in the uterus of oviparous amniotes during eggshell formation. We used Western blot and indirect immunofluorescence microscopy to determine expression and localisation of uterine Ca2+-ATPase during the reproductive cycle of king quail and zebra finch. The pattern of Ca2+-ATPase expression and localisation during the reproductive cycle was similar for both species. Immunoblots of uterine extracts from quail and finch indicated that Ca2+-ATPase expression is reduced in non-reproductive compared to reproductive females. Similarly, in non-reproductive females, weak apical immunofluorescent staining of Ca2+-ATPase is localised to epithelial cells in a small number of uterine tubular glands. A large increase in apical immunofluorescent staining of tubular gland epithelia occurs in both vitellogenic and reproductive females. The presence of Ca2+-ATPase on the apical surface of tubular gland epithelial cells suggests that the enzyme is involved in the translocation of calcium out of the tubular gland epithelia and into the concentrated fluid of the uterine lumen. Presence of Ca2+-ATPase in vitellogenic females indicates that the enzyme is expressed prior to the time of ovulation and eggshell calcification.
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PMID:Expression and localization of Ca2+-ATPase in the uterus during the reproductive cycle of king quail (Coturnix chinensis) and zebra finch (Poephila guttata). 1798 11

Egg laying and shell calcification impose severe extra demands on ionic calcium (Ca2+) homeostasis; especially in birds characterized by their long clutches (series of eggs laid sequentially before a "pause day"). These demands induce vitamin D metabolism and expression. The metabolism of vitamin D is also altered indirectly, by other processes associated with increased demands for calcium, such as growth, bone formation and egg production. A series of intestinal, renal or bone proteins are consequently expressed in the target organs via mechanisms involving a vitamin D receptor. Some of these proteins (carbonic anhydrase, calbindin and calcium-ATPase) are also found in the uterus (eggshell gland) or are believed to be involved in calcium transport in the intestine or kidney (calcium channels). The present review deals with vitamin D metabolism and the expression of the above-mentioned proteins in birds, with special attention to the strongly calcifying laying bird.
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PMID:Calcium homeostasis and vitamin D metabolism and expression in strongly calcifying laying birds. 1868 98

Research of pH-dependence of inhibitory action of eosin Y (2',4',5',7'-tetrabromofluorescin) on ATPase of contractile proteins of smooth muscles of the uterus has shown that the increase of concentration of this inhibitor (from 0.1 to 10 microM) influenced the profile of pH-dependence of ATPase activity of actomyosin: in the presence of 0.1 microM eosin Y the change of optimal value of pH has been observed in more sour side in relation to the control; at the increase of concentration of eosin Y (from 0.5 to 10 microM) the strongly pronounced optimum of pH is absents in general. The ability of eosin Y to inhibit the ATPase activity of contractile complex is dependent on pH of incubation environment. The change of pH from 6.0 to 7.2 results in a 9-fold decrease of magnitude of apparent constant of inhibition Ki (from 6.5 +/- 0.8 microM to 0.74 +/- 0.07 microM). The obtained results indicate that the diminishing of concentration of H+ in an incubation environment favors the increase of affinity ATPase of actomyosin for eosin Y and prove the important role of ionization processes in the system "enzyme-substrate-inhibitor" for realization of inhibitory action of eosin Y.
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PMID:[pH-dependence of inhibitory action of eosin Y on ATPase activity of smooth muscle actomyosin complex of the uterus]. 1871 11

This study was designed to investigate the effects of oestrogen on sarcoplasmic reticulum (SR) Ca(2+)-ATPase activity and gene expression in ovariectomised rats under the condition of chronic intermittent hypoxia (CIH). Thirty-two female Sprague-Dawley rats were randomly divided into four groups: the normal control group (NC), the CIH group (CIH), the CIH-ovariectomised group (CIH+OVX), and the group of CIH-ovariectomised rats receiving estradiol replacement (CIH+OVX+E(2)). Rats in the latter three groups were exposed to CIH for 5 weeks. The animals were killed before genioglossus (GG) was rapidly excised, and their body and uterus mass were determined. Estradiol level was detected by radioimmunoassay. SR Ca(2+)-ATPase (SERCA) activity was observed by detecting inorganic phosphorus ion, and the SERCA mRNA level was measured using real-time quantitative polymerase chain reaction (real-time PCR). It was found that, compared with the NC group, the SERCA activity and mRNA level were remarkably reduced (p<.01) in the CIH group. And compared with the CIH group, the SERCA activity and mRNA level were also significantly reduced (p<.01) in the CIH+OVX group. Meanwhile, the SERCA activity and mRNA level significantly increased (p<.01) in the CIH+OVX+E(2) group compared with the CIH+OVX group, but lower than those in the NC group (p<.01). The results showed that CIH could reduce the SERCA activity and mRNA expression, and oestrogen-deficiency could exacerbate this effect; whilst estradiol replacement can partially reverse the effect of CIH in ovariectomised rats.
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PMID:Effects of oestrogen on sarcoplasmic reticulum Ca2+-ATPase activity and gene expression in genioglossus in chronic intermittent hypoxia rat. 1923 Aug 61

The uterine sacroplasmic reticulum (SR) takes up and stores calcium [Ca], using an ATPase (SERCA) and the Ca-buffering proteins, calsequestrin and calreticulin. This stored Ca can be released via IP(3)-gated Ca channels. Decreases in luminal Ca concentration [Ca] have been directly measured following agonist stimulation. During spontaneous contractions however, there appears to be no involvement of the SR, as Ca entry and efflux across the plasma membrane account for these phasic contractions. After over-viewing current knowledge concerning SR structure and function, we highlight three areas of research which suggest new ways of looking at the role of the SR in the uterus, although they may be controversial or speculative at the moment. Firstly, we review the evidence for the function, if any, of Ca-induced SR Ca release channels, the ryanodine receptor (RyR) and the lack of Ca sparks (the elemental release events from RyRs), in the uterus. Secondly, we ask does regulation of SERCA by the accessory protein, phospholamban, occur in the uterus and what is the effect of knocking out phospholamban on uterine activity? Thirdly, we address the question of when and how store-operated Ca entry occurs in the myometrium. By analogy with other, usually less excitable tissues, is there a mechanism that links store Ca depletion to plasma membrane Ca entry in smooth muscle cells within intact uterus and is it physiologically relevant and regulated? Are the recently described proteins ORAI and STIM-1 involved in uterine store-operated Ca entry? We end the review by integrating these new insights with previous data to present a new working model of the SR in the uterus.
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PMID:A review of recent insights into the role of the sarcoplasmic reticulum and Ca entry in uterine smooth muscle. 1928 73

In this article, we report the characterization of a novel DNA damage-regulated gene, named DNA damage-regulated overexpressed in cancer 45 (DOC45). Our results indicate that DNA damage-inducing agents, including doxorubicin (adriamycin), etoposide, and ionizing and UV radiation, strongly downregulate DOC45 expression, whereas endoplasmic reticulum stress-inducing agents do not. Our results also indicate that DOC45 is overexpressed in several human malignancies, including cancers of the colon, rectum, ovary, lung, stomach, and uterus. DOC45 harbors conserved nucleotide triphosphate-binding motifs and is capable of ATP hydrolysis, findings that highlight its function as a novel ATPase. Although predominantly cytoplasmic, DOC45 exhibits a characteristic nucleocytoplasmic distribution and, on inhibition of nuclear export, predominantly accumulates in the nucleoli. These results suggest that DOC45 may shuttle between nucleus and cytoplasm to carry out its function. Our results also indicate that DOC45 expression is enhanced during oncogenic Ras-mediated transformation and that its expression is linked to phosphoinositide 3-kinase signaling pathway. Furthermore, short hairpin RNA-mediated knockdown of DOC45 in human colon cancer cells inhibits their proliferation and enhances cellular sensitivity to doxorubicin-induced cell death, suggesting that DOC45 plays an important role in cell proliferation and survival. Collectively, our results indicate that DOC45 is a novel ATPase that is linked to cellular stress response and tumorigenesis, and may also serve as a valuable tumor marker.
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PMID:DOC45, a novel DNA damage-regulated nucleocytoplasmic ATPase that is overexpressed in multiple human malignancies. 2005 27


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