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)

Only in SW fish, Prolactin (PRL) treatment increased natremia and especially chloremia. In gill, the decreases of Mg++ ATPase and SCN-sensitive, HCO3-ATPase observed in control fish after transfert from SW to FW, were more marqued in FW 8 days PRL treated fish. Renal enzyme activities were not affected by PRL treatment. If PRL treatment acts effectively on branchial ionic extrusion mechanisms, the connection between HCO3-ATPase anc Cl--transport remains to be elucidated. These results can be explained with reference to existence of two chloride-cell types.
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PMID:[Effects of prolactin on chloremia and HCO3 dependant ATPase activities in kidney and gill of grey mullet, chelon Labrosus, during fresh water adaptation (author's transl)]. 3 24

The effect of Prolactin and LH on the activity of spermatozoal ATPase was studied. Both the hormones activated the enzyme activity suggesting that these hormones, as they are present in the seminal fluid may influence the energy metabolism of spermatozoa. The spermine, a polyamine present in large concentration in the semen, had significantly enhanced the ATPase activity of the spermatozoa in a dose related manner.
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PMID:Effect of LH, prolactin and spermine on ATPase activity of human spermatozoa. 15 8

1. Explants of mammary tissue from pseudopregnant rabbits were cultured at 37 degrees C in air for 24-48h in Medium 199 buffered with 20mm-Hepes [4-(2-hydroxyethyl)-1-piperazine-ethanesulphonic acid]. The medium contained insulin and corticosterone, or insulin, corticosterone and sheep prolactin in the presence or absence of ouabain, an inhibitor of Na(+)/K(+)-dependent adenosine triphosphatase. The responses of explants were assessed histologically, by measuring the tissue concentration of K(+), and by rates of synthesis of RNA, protein and fatty acids. The effect of ouabain on Na(+) and K(+) concentrations in slices of lactating rabbit mammary-gland tissue incubated for 1h at 37 degrees C in Krebs bicarbonate buffer was also studied. 2. Prolactin increased the concentration of K(+) in mammary explants, an effect prevented by ouabain. In slices of lactating tissue, there was a linear relationship between the log dose of ouabain (from 0.1 to 10mum) and increased Na(+) and decreased K(+) concentrations in the tissue. 3. Ouabain at concentrations up to 1mum did not affect the rate of synthesis of RNA, protein or fatty acids by explants cultured with insulin and corticosterone. By contrast, the stimulatory effect of prolactin on protein synthesis was diminished and the induction of medium-chain fatty acid synthesis by prolactin was almost abolished. RNA synthesis was unaffected. Histological examination showed no tissue damage by 1mum-ouabain. 4. Explants cultured in the presence of 2mum-ouabain for 24h retained their ability to respond to prolactin when the ouabain was removed from the culture medium. Between 24 and 48h they showed responses to prolactin of a magnitude similar to those of explants never exposed to ouabain. 5. These results show that a fully functional Na(+)/K(+)-dependent adenosine triphosphatase system is necessary for prolactin to promote secretory activity in rabbit mammary gland.
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PMID:Inhibition by low concentrations of ouabain of prolactin-induced lactogenesis in rabbit mammary-gland explants. 56 78

Small cultures of human amniotic cells were preincubated for 24 h. Human prolactin was then added to the medium. After a further short period of incubation the tubes were chilled, the medium removed and the cells rinsed with saline. The tubes then received cold Tris-sucrose and were frozen, to disrupt the cells. After thawing, adenosine triphosphatase (ATPase) and p-nitrophenyl phosphatase (PNPase) were measured. Buffer was added containing either ATP or PNP and the tubes were incubated for 30 min. Inorganic phosphate released from ATP and p-nitrophenol was measured spectrophotometrically. Prolactin stimulated both enzyme activities. The ATPase log dose-response curve was linear between approximately 12.5 and 200 mIU/l. It was inhibited by ouabain. Isobutyl-1-methylxanthine inhibited the ATPase but not the alkaline phosphatase activity. One of these human amniotic cell enzymes may provide the basis for a sensitive bioassay for human prolactin.
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PMID:Enzyme activation of human prolactin: a potential basis for a bioassay. 247 90

In freshwater-acclimated American eels (Anguilla rostrata LeSueur), ovine prolactin and grafts of the part of the pituitary gland containing the prolactin cells induced hypercalcemia. The hypercalcemia was associated with increased uptake of calcium from the water (resulting from increased influx and decreased efflux) and with enhanced high-affinity Ca2+-adenosinetriphosphatase (ATPase) activity in the gills, the putative biochemical correlate of the branchial Ca2+ pump. Kinetic analyses of ATPase-mediated Ca2+ transport in plasma membrane vesicles of branchial epithelium provided evidence that prolactin enhanced the maximum velocity of the Ca2+ pump. Prolactin treatments raised plasma cortisol levels slightly but significantly in eels. However, cortisol per se was not hypercalcemic in eels and did not stimulate the branchial Ca2+ pump. We conclude that the hypercalcemic potency of prolactin in fish relates to its stimulatory action on active Ca2+ transport in the gills.
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PMID:Calcitropic actions of prolactin in freshwater North American eel (Anguilla rostrata LeSueur). 252 94

Prolactin has been known to affect the water and electrolyte balance. Because increased lens hydration has been shown to be a common phenomenon in most, if not all types of cataracts, we have been interested in investigating a possible role of prolactin in sugar cataract induction and progression. For this study, we have used morphological and biochemical approaches. The prolactin delivery method involved intraperitoneal implantation of one or more pellets in Sprague-Dawley female rats. Following implantation of the desired number of prolactin or control (nonprolactin) pellets, animals were either fed galactose and lab chow, or lab chow diet. Gross morphological observations of whole lenses, slit-lamp examination of lenses and light microscopic analysis of lens sections showed that in the galactose-fed prolactin group, galactose associated alteration progressed faster and total opacification (mature cataract development) was achieved earlier than in the nonprolactin group. The levels of galactose and dulcitol were higher in the lenses of galactose-fed prolactin treated rats as compared to lenses from nonprolactin (control) rats. No significant difference in lens Na+-K+ ATPase activity between the prolactin and nonprolactin group was observed. Our results indicate that prolactin accelerates galactose-induced cataractogenesis in rats.
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PMID:Effect of prolactin on galactose cataractogenesis. 303 35

The acute effect of intraperitoneally administered prolactin (0.2, 0.4, and 0.6 mg/kg body weight) on passive calcium transport in duodenum, proximal jejunum, and ileum of sexually mature female Wistar rats was investigated by using an in vivo perfusion technique. Test solution containing (in mM) NaCl, 100; KCl, 4.7; MgSO4, 1.2; CaCl2, 20; D-glucose, 11; sodium ferrocyanide (Na4Fe(CN)6), an index of net water transport, 20; and 0.7 microCi 45CaCl2 (1 Ci = 37 GBq) was perfused through the 10-cm intestinal loop for 60 min. Results showed that 0.4 mg prolactin/kg body weight significantly increased duodenal net Ca absorption (net Ca) from 23.81 +/- 1.84 to 30.56 +/- 1.57 mmol/g dry weight (p < 0.05) by stimulating the lumen to plasma calcium flux (CaL-P). The jejunum responded to 0.2, 0.4, and 0.6 mg prolactin/kg body weight by reversing from net Ca absorption of 18.60 +/- 1.70 mmol/g dry weight to net secretion of -3.30 +/- 1.56, -10.39 +/- 2.21, and -11.79 +/- 2.04 mmol/g dry weight (p < 0.01), respectively, as a result of a dose-dependent increase in plasma to lumen calcium flux (CaP-L). Calcium fluxes in the ileum on the other hand did not respond to prolactin. There was a close correlation between net water flux and net calcium flux in all three intestinal segments under basal condition regardless of the luminal sodium concentration. However, this correlation was lost after prolactin administration, which while having no effect on net water flux, altered the duodenal and jejunal calcium fluxes. By varying the luminal concentration of sodium, it was found that the stimulatory effect of 0.4 mg prolactin/kg body weight on the duodenal CaL-P was reduced when compared with control, i.e., 17.84 +/- 0.91 vs. 26.64 +/- 1.05 mmol/g dry weight at a sodium concentration of 180 mM, and 14.48 +/- 0.99 vs. 20.12 +/- 1.34 mmol/g dry weight at a sodium concentration of 140 mM. At a sodium concentration of 80 mM, the prolactin effect was absent. Since duodenal Na(+)-K+ ATPase activity was increased by prolactin from 3.77 +/- 0.16 to 4.95 +/- 0.30 mumol Pi.mg-1 protein.h-1 (p < 0.05), sodium dependency of the prolactin-enhanced lumen to plasma calcium flux may be related to both sodium-induced water flow and calcium-sodium exchange across the basolateral membrane. Thus, it was postulated that under basal condition, net calcium transport in the small intestine occurred with the sodium-induced water transport along the paracellular pathway. However, after prolactin administration, this association was lost. Prolactin-enhanced lumen to plasma calcium flux in the duodenum was sodium dependent and involved the Na(+)-K+ ATPase activity. In the proximal jejunum, prolactin stimulated plasma to lumen calcium flux, but the mechanism was not known.
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PMID:Acute effects of prolactin on passive calcium absorption in the small intestine by in vivo perfusion technique. 963 55

Prolactin enhances progesterone-dependent transcription of the rabbit uteroglobin gene. RUSH transcription factors are implicated in the signal transduction pathway. The RUSH acronym identifies key features of these nuclear phosphoproteins, that is, RING-finger motif, binds the uteroglobin promoter, structurally related to the SWI/SNF family of transcription factors, and helicase-like. Cloned by recognition site screening, RUSH proteins bind to an 85-bp region (-170/-85) of the uteroglobin promoter that was subsequently identified as a novel prolactin-responsive region by promoter deletion analysis. Gel shift and linker-scanning assays further reduced the RUSH target site to -160/-110. A hexameric core of MCWTDK was identified as the RUSH-specific DNA-binding site (-126/-121) by CASTing. This site overlaps authentic HNF3 beta and OCT-1 binding sites. A unique Type IV P-type ATPase that is embedded in the inner nuclear membrane binds the RING domain of RUSH. The conformationally flexible loop portion of this RING-finger binding protein (RFBP) extends into the nucleoplasm to contact euchromatin. The physical association of RFBP with transcriptionally active chromatin supports the speculation that RFBP targets RUSH transcription factors to the active uteroglobin promoter.
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PMID:Uteroglobin gene transcription: what's the RUSH? 1119 55

Prolactin (PRL) is an important hormone for freshwater adaptation in many teleost species. In some euryhaline fishes, growth hormone (GH) and cortisol are involved in seawater adaptation by stimulating ion extrusion. When channel catfish (Ictalurus punctatus) were transferred from fresh water to dilute seawater (300-400 mOsm), their plasma osmolality was always higher than the environmental salinity. In correlation with the increase in plasma osmolality, significant increases in plasma cortisol were observed. However, no effect of ovine GH or cortisol was seen in plasma osmolality or gill Na, K-ATPase activity when the hormones were given during the course of acclimation to dilute seawater. When catfish in fresh water were hypophysectomized, plasma osmolality was significantly decreased by 24 h, reaching a minimum level after 2 days. When they were transferred to dilute seawater, the plasma osmolality of the sham-operated fish was consistently higher than that of environmental water, whereas the osmolality of the hypophysectomized fish was equivalent to the environmental salinity. Ovine PRL restored the plasma osmolality of the hypophysectomized fish in fresh water to the level of sham-operated fish. Cortisol was also effective, but the effect was less pronounced than the effect of PRL. Injection of PRL in combination with cortisol resulted in a marked additive increase in plasma osmolality to a level even above that of the sham-operated fish. Ovine GH was without effect. These treatments in hypophysectomized fish transferred to dilute seawater produced essentially the same results as those in fish in fresh water. Plasma osmolality was also increased after PRL treatment of the intact fish in fresh water. There was a synergistic effect between PRL and cortisol in hypophysectomized fish in dilute seawater as well as in intact fish in fresh water. PRL did not stimulate cortisol secretion either in hypophysectomized fish or in intact fish. In the stenohaline catfish, both PRL and cortisol seem to be involved importantly in ion uptake from the environment not only in fresh water but also in brackish water.
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PMID:Hormonal control of osmoregulation in the channel catfish Ictalurus punctatus. 1135 39

A large array of circulating and local signaling agents modulate transport of ions across the gill epithelium of fishes by either affecting transport directly or by altering the size and distribution of transporting cells in the epithelium. In some cases, these transport effects are in addition to cardiovascular effects of the same agents, which may affect the perfusion pathways in the gill vasculature and, in turn, affect epithelial transport indirectly. Prolactin is generally considered to function in freshwater, because it is the only agent that allows survival of some hypophysectomized fish species in freshwater. It appears to function by either reducing branchial permeability, Na,K-activated ATPase activity, or reducing the density of chloride cells. Cortisol was initially considered to produce virtually opposite effects (e.g., stimulation of Na,K-activated ATPase and of chloride cell size and density), but more recent studies have found that this steroid stimulates ionic uptake in freshwater fishes, as well as the activity of H-ATPase, an enzyme thought to be central to ionic uptake. Thus, cortisol may function in both high and low salinities. Growth hormone and insulin-like growth factor appear to act synergistically to affect ion regulation in seawater fishes, stimulating both Na,K-activated ATPase and Na-K-2Cl co-transporter activity, and chloride cell size, independent of their effects on growth. Some of the effects of the GH-IGF axis may be via stimulation of the number of cortisol receptors. Thyroid hormones appear to affect seawater ion regulation indirectly, by stimulating the GH-IGF axis. Natriuretic peptides were initially thought to stimulate gill ionic extrusion, but recent studies have not corroborated this finding, so it appears that the major mode of action of these peptides may be reduction of salt loading by inhibition of oral ingestion and intestinal ionic uptake. Receptors for both arginine vasotocin and angiotensin have been described in the gill epithelium, but their respective roles and importance in fish ion regulation remains unknown. The gill epithelium may be affected by both circulating and local adrenergic agents, and a variety of studies have demonstrated that stimulation of alpha-adrenergic versus beta-adrenergic receptors produces inhibition or stimulation of active salt extrusion, respectively. Local effectors, such as prostaglandins, nitric oxide, and endothelin, may affect active salt extrusion as well as gill perfusion. Recent studies have suggested that the endothelin inhibition of salt extrusion is actually mediated by the release of both NO and prostaglandins. It is hoped that modern molecular techniques, combined with physiological measurements, will allow the dissection of the relative roles in ion transport across the fish gill epithelium of this surprisingly large array of putative signaling agents.
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PMID:Cell signaling and ion transport across the fish gill epithelium. 1211 5


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