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The Devonian cemented brachiopod Schuchertellopsis durbutensis has proved difficult to classify and its possible taxonomic relationships are unknown. Morphologically Schuchertellopsis resembles more closely members of the Orthotetidina than the Davidsoniidina. Examination of the shell structure, a key diagnostic feature of the Orthotetidina, shows that Schuchertellopsis has the cross laminar secondary shell typical of all orthotetidines. However, the presence of both pseudopunctate and incipient an extropunctate fabric within the ventral valve is unique amongst orthotetidine brachiopods and is thought to represent a phase of shell fabric experimentation. Schuchertellopsis probably fits most comfortably within the Schuchertellidae, and is the earliest representative of that family. 相似文献
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Summary The actions of cyclic AMP are subject to several levels of post-receptor modulation in cardiac tissue. Isoproterenol and prostaglandin E1 both stimulate cAMP accumulation, but only isoproterenol causes activation of particulate cAMP-dependent protein kinase, leading to activation of phosphorylase kinase and glycogen phosphorylase, and inhibition of glycogen synthase. Through the use of isolated, adult ventricular myocytes, we have determined that the hormone-specific activation of glycogen phosphorylase is due to subcellular compartmentation of cAMP. There is some evidence that cyclic nucleotide phosphodiesterases, whose activity is stimulated by alpha1-adrenergic agonists in isolated myocytes, may have a role in compartmentation. Phosphoinositide hydrolysis is stimulated by alpha, and muscarinic agonists, presumably leading to activation of protein kinase C, which in turn has multiple effects on hormone-sensitive adenylate cyclase.Abbreviations cAMP
Adenosine-3,5-Cyclic Monophosphate
- cGMP
Guanosine-3,5-Cyclic Monophosphate
- Gi, GS
Guanine nucleotide-binding proteins linked to inhibition and stimulation, respectively, of adenylate cyclase
- GTP
Guanosine-5-triphosphate
- PDE
Cyclic Nucleotide Phosphodiesterase
- PGE1
Prostaglandin E1 相似文献
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Putative inhibitor of cyclic AMP efflux: chromatography, amino acid composition, and identification as a prostaglandin A1-glutathione adduct 总被引:2,自引:0,他引:2
Avian red cells rapidly and extensively metabolize prostaglandin A1 (PGA1) to a polar form that extracts into 80% ethanol and is quantitatively desalted and recovered over a Waters C18 Sep-Pak. This material co-chromatographs with synthetic PGA1-GSH and with the human red cell PGA1 metabolite on cellulose and silica gel thin layer plates and on normal phase high performance liquid chromatography. Quantitation of the amino acid composition by [35S]cysteine incorporation and by fluorometric amino acid analysis of the material eluting from high performance liquid chromatography indicates the presence of PGA1, cysteine, glutamate, and glycine in equimolar ratios. Base sensitivity of the metabolite indicates that it exists largely (80%) in the 9-hydroxyl form. We conclude that the polar metabolite of PGA1 that acts intracellularly to inhibit cyclic AMP efflux by avian red cells is a glutathione conjugate of PGA1. 相似文献
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Action of the cardiac alpha 1-adrenergic receptor. Activation of cyclic AMP degradation 总被引:3,自引:0,他引:3
Using purified rat ventricular myocytes and membranes prepared from them, we have previously found that alpha 1-adrenergic stimulation causes decreased cyclic AMP accumulation and decreased activation of cyclic AMP-dependent protein kinase. We have now analyzed the mechanism by which alpha 1 stimulation is linked to cyclic AMP metabolism. In an adenylate cyclase assay in which carbachol inhibits the stimulatory effect of norepinephrine, the addition of prazosin (alpha 1-antagonist) has no effect on the response to norepinephrine. In membranes prepared from myocytes treated with pertussis toxin, norepinephrine competes for alpha 1-receptors (assessed by [3H]prazosin binding) with two components, binding to the high affinity component being sensitive to exogenous GTP, exactly as in membranes prepared from control myocytes. In intact cells labeled with [3H]adenine in which carbachol antagonizes the norepinephrine response, prazosin enhances accumulation of [3H]cyclic AMP due to norepinephrine. Treatment of cells with pertussis toxin eliminates inhibition by carbachol but does not alter prazosin's capacity to enhance the norepinephrine response. Addition of phosphodiesterase inhibitors eliminates this effect of alpha 1 blockade. In [3H]adenine-labeled cells loaded with [3H]cyclic AMP by prior treatment with isoproterenol, alpha 1-adrenergic stimulation enhances disappearance of [3H]cyclic AMP. Measurements of cellular cyclic AMP give results similar to those obtained with the adenine labeling technic. We conclude that occupation of the myocyte alpha 1-receptor results in stimulation of cyclic AMP phosphodiesterase activity. 相似文献
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