L Herbette, C A Napolitano, F C Messineo, A M Katz
{"title":"Interaction of amphiphilic molecules with biological membranes. A model for nonspecific and specific drug effects with membranes.","authors":"L Herbette, C A Napolitano, F C Messineo, A M Katz","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The nonspecific interactions of propranolol, timolol, and ethanol with model and sarcoplasmic reticulum membranes were determined utilizing radioisotopic association differential scanning calorimetry, and neutron diffraction. Differential scanning calorimetry performed on mixtures of these amphiphilic compounds and model membrane bilayers composed of dimyristoyllecithin showed that propranolol was approximately 25 times more lipid-soluble than timolol and at least 100 times more lipid-soluble than ethanol. Neutron diffraction showed that the solvation of propranolol was within the fatty acyl chain region of the lipid bilayer. This solvation correlated with the effect of propranolol to inhibit ATP-dependent calcium transport in isolated rabbit skeletal muscle sarcoplasmic reticulum, a membrane that lacks beta-adrenergic receptors. In contrast, the major site of interaction of ethanol was within the aqueous compartment hydrating the sarcoplasmic reticulum membrane. A model for nonspecific drug interaction with the sarcoplasmic reticulum membrane based on the site of interaction of these amphiphiles and their relative potencies to inhibit calcium transport by these membranes is proposed. In principle, this model could be extended to specific drug interactions with membranes.</p>","PeriodicalId":77831,"journal":{"name":"Advances in myocardiology","volume":"5 ","pages":"333-46"},"PeriodicalIF":0.0,"publicationDate":"1985-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"15082604","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"The effects of hormonal factors on cardiac protein turnover.","authors":"P H Sugden","doi":"10.1007/978-1-4757-1287-2_8","DOIUrl":"https://doi.org/10.1007/978-1-4757-1287-2_8","url":null,"abstract":"","PeriodicalId":77831,"journal":{"name":"Advances in myocardiology","volume":"5 ","pages":"105-21"},"PeriodicalIF":0.0,"publicationDate":"1985-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14998695","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Ethanol and cardiac protein synthesis.","authors":"S S Schreiber, C D Evans, M Oratz, M A Rothschild","doi":"10.1007/978-1-4757-1287-2_9","DOIUrl":"https://doi.org/10.1007/978-1-4757-1287-2_9","url":null,"abstract":"<p><p>Acute exposure of the heart to ethanol does not appear to alter the rate of young guinea pig cardiac protein synthesis when assayed in vitro. In contrast, the primary metabolite of ethanol, acetaldehyde, markedly diminishes synthesis despite its chronotropic and inotropic effects. On the other hand, after 11-13 weeks of ethanol-drinking during growth and maturation, the synthetic capacity of the working right ventricle was decreased when measured in vitro with normal perfusate. Assay of synthesis of the contractile proteins myosin heavy and light chains, actin and tropomyosin suggests a change in synthesis or pool size of actin reflected in an alteration of relative synthesis of this protein compared to that of heavy chains. The relative synthesis of the other proteins remained at control levels. When hearts from ethanol-drinking and matched control animals were perfused under conditions of severe ischemia, there was a profound fall in protein synthesis in all hearts, and ethanol did not enhance the inhibition of synthesis. However, the hearts from ethanol-drinking animals showed a more marked and significant impairment of maintaining ejection pressure with a marked increase in coronary resistance as the perfusion progressed. It is postulated that some impairment of protein metabolism may occur during prolonged ethanol exposure, which may influence the cardiac response of another induced stress, e.g., ischemia.</p>","PeriodicalId":77831,"journal":{"name":"Advances in myocardiology","volume":"5 ","pages":"123-35"},"PeriodicalIF":0.0,"publicationDate":"1985-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"15032121","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
V E Koteliansky, V P Shirinsky, G N Gneushev, M A Chernousov
{"title":"The role of actin-binding proteins vinculin, filamin, and fibronectin in intracellular and intercellular linkages in cardiac muscle.","authors":"V E Koteliansky, V P Shirinsky, G N Gneushev, M A Chernousov","doi":"10.1007/978-1-4757-1287-2_17","DOIUrl":"https://doi.org/10.1007/978-1-4757-1287-2_17","url":null,"abstract":"<p><p>The localization in cardiac muscle and the biochemical properties of fibronectin, filamin, and vinculin were studied. Fibronectin was localized between cardiomyocytes. Filamin was identified in the Z-line region of sarcomers and in the intercalated disks of heart muscle. Vinculin was found to be present in intercalated disks and near the plasma membrane at the cell periphery between external myofibrils and sarcolemma. It was suggested that fibronectin, filamin, and vinculin play an important role in intercellular and intracellular linkages in cardiac muscle.</p>","PeriodicalId":77831,"journal":{"name":"Advances in myocardiology","volume":"5 ","pages":"215-21"},"PeriodicalIF":0.0,"publicationDate":"1985-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"15032122","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
S C Dennis, M C Kohn, M B Slegowski, G J Anderson, D Garfinkel
{"title":"Monocarboxylate-uptake kinetics in perfused rat heart.","authors":"S C Dennis, M C Kohn, M B Slegowski, G J Anderson, D Garfinkel","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>While there is considerable evidence to suggest that lactate and pyruvate transport across the cell membrane is controlled, virtually nothing is known about the mechanisms. To test a prediction that sarcolemmal monocarboxylate transport is mediated by a specific carrier, we have examined the kinetics of pyruvate and lactate uptake into aerobically perfused rat hearts. In preparations depleted of intracellular lactate and pyruvate by a 30-min pre-perfusion in the absence of substrates, various concentrations of [14C]lactate or pyruvate (0.02 Ci/mole), together with [3H]mannitol (50 nCi/ml), were transiently (2 min) infused into the mainstream perfusate immediately above the heart. Uptake was calculated from the difference between the level of 14C-labeled substrate predicted from the extracellular distribution of [3H]mannitol and the actual level (corrected for 14CO2 contamination) measured in successive 20-sec samples of effluent perfusate. Computer optimization analysis of the initially rapid (first 60 sec) uptake rates revealed that monocarboxylate transport is not simply a question of diffusion. On the contrary, the observation of typical saturation kinetics (Vmax 7.7-8.4 mumoles/min per g wet wt.) and cross-inhibition (Ki pyr, 2.3 +/- 0.5 mM; Ki lac, 0.16 +/- 0.02 mM) suggest that transsarcolemmal movement of monocarboxylate may be mediated by a high-affinity lactate (km 3.9 +/- 0.9 mM), low-affinity pyruvate (Km 8.6 +/- 1.1 mM), translocase.</p>","PeriodicalId":77831,"journal":{"name":"Advances in myocardiology","volume":"6 ","pages":"259-72"},"PeriodicalIF":0.0,"publicationDate":"1985-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"15037970","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Evolution, cardiac failure, and water metabolism. Presidential address.","authors":"P Harris","doi":"10.1007/978-1-4757-1287-2_1","DOIUrl":"https://doi.org/10.1007/978-1-4757-1287-2_1","url":null,"abstract":"<p><p>In this essay, I take the liberty of doubting the widely held view that congestive cardiac failure is due to an inability of the heart to provide enough oxygen for the needs of the body. Instead, the syndrome is best explained by an inappropriate and prolonged stimulation of the neurohumoral defense reaction that developed during evolution to support exercise and preserve life.</p>","PeriodicalId":77831,"journal":{"name":"Advances in myocardiology","volume":"5 ","pages":"1-11"},"PeriodicalIF":0.0,"publicationDate":"1985-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/978-1-4757-1287-2_1","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"15085722","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Characterization of a partially purified Na+,K+-ATPase from dog heart.","authors":"P. Sulakhe, V. Elimban, N. Dhalla","doi":"10.1016/0022-2828(83)91031-3","DOIUrl":"https://doi.org/10.1016/0022-2828(83)91031-3","url":null,"abstract":"","PeriodicalId":77831,"journal":{"name":"Advances in myocardiology","volume":"6 1","pages":"249-57"},"PeriodicalIF":0.0,"publicationDate":"1985-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0022-2828(83)91031-3","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"53279167","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
W B Weglicki, J H Kramer, F F Kennett, T E Knauer, K Owens
{"title":"Perturbations of sarcolemmal and microsomal enzymes by amphiphilic lipids and drugs.","authors":"W B Weglicki, J H Kramer, F F Kennett, T E Knauer, K Owens","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Sarcolemmal (SL) and microsomal (MC) membranes were prepared from adult canine cardiocytes. SL Na+, K+-ATPase (2.35 mumole/min per mg) was enriched 117-fold over the homogenate and MC rotenone-insensitive NADH cytochrome c reductase (RINCR) was enriched 41-fold. Preincubation of SL with 50 microM arachidonyl-CoA (20:4 CoA) stimulated Na+, K+-ATPase almost 2-fold; 250 microM 20:4 CoA inhibited the enzyme by 85%. However, RINCR was inhibited 80% by only 0.2 microM 20:4 CoA. Thus, each of these myocardial lipid-dependent enzymes showed a different sensitivity to perturbation by lipid amphiphiles. In further experiments, SL preincubated with 50 microM 20:4 CoA + 2.5 mM propranolol (which had no effect alone) exhibited a synergistic inhibition of the Na+, K+-ATPase: The enzymatic activity declined 8.5-fold when compared to sarcolemma treated with 50 microM 20:4 CoA alone. Thus, the presence of lipid amphiphiles may result in greater inhibition of the Na+, K+-ATPase when propranolol is present in the membrane.</p>","PeriodicalId":77831,"journal":{"name":"Advances in myocardiology","volume":"6 ","pages":"127-36"},"PeriodicalIF":0.0,"publicationDate":"1985-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14119803","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Dependence of protein synthesis on aortic pressure and calcium availability.","authors":"E E Gordon, Y Kira, H E Morgan","doi":"10.1007/978-1-4757-1287-2_11","DOIUrl":"https://doi.org/10.1007/978-1-4757-1287-2_11","url":null,"abstract":"<p><p>Increased aortic pressure accelerated protein synthesis in control-beating and arrested-drained hearts supplied with either glucose or pyruvate. Elevation of perfusion pressure from 60 to 120 mm Hg increased oxygen consumption in control-beating but not in arrested-drained preparations. Energy availability, as assessed by adenylate energy charge or creatine phosphate/creatine ratio, or both, was increased in arrested-drained hearts supplied with glucose and perfused at 60 and 120 mm Hg aortic pressure. In control-beating or arrested-drained hearts supplied with pyruvate, energy availability was not improved by elevation of aortic pressure from 60 to 120 mm Hg. An increase of perfusate calcium concentration from 0.5 to 5.0 mM in control-beating Langendorff preparations supplied with glucose and perfused at an aortic pressure of 90 mm Hg doubled oxygen consumption and decreased energy availability, but had no effect on the rate of protein synthesis. In arrested-drained hearts supplied with either glucose or pyruvate and calcium concentrations ranging from 0.5 to 5.0 mM, the rates at 120 mm Hg aortic pressure were 11-25% higher than at 60 mm Hg. These findings provide no evidence to implicate increased oxidative metabolism, energy availability, or extracellular calcium concentration as important factors in the mechanism that accounts for the effects of increased aortic pressure on protein synthesis.</p>","PeriodicalId":77831,"journal":{"name":"Advances in myocardiology","volume":"5 ","pages":"145-56"},"PeriodicalIF":0.0,"publicationDate":"1985-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"15085723","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Adenosine deaminase inhibition and myocardial adenosine metabolism during ischemia.","authors":"P W Achterberg, J W de Jong","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>It is generally assumed that myocardial adenine nucleotides are broken down (e.g., during ischemia) via AMP----adenosine----inosine, but contribution of the pathway AMP----IMP----inosine cannot be excluded. The catabolism of exogenously added adenosine (1-20 microM) was studied in isolated rat hearts. All catabolites (i.e., inosine, hypoxanthine, xanthine, and uric acid) were measured together with nonmetabolized adenosine. Even at low (1 microM) adenosine concentrations, deamination accounted for 60% of adenosine disappearing from the perfusate. The adenosine deaminase inhibitor erythro-9-(2-hydroxy-3-nonyl)adenine (EHNA) (5 and 50 microM) was infused together with adenosine (5 microM). These two concentrations of EHNA inhibited deamination of exogenous adenosine by 65 and 91%, respectively. When hearts were made ischemic by reduction of perfusion pressure, addition of EHNA raised the adenosine release from 1.4 to 9.8 nmole/min per gram wet wt., but surprisingly, the release of inosine and oxypurines (8 nmole/min per g wet wt.) did not change. These results suggest that considerable breakdown of myocardial adenine nucleotides can occur via the AMP----IMP----inosine pathway instead of AMP----adenosine----inosine. The rate of total purine release is probably not a good measure of intracellular adenosine formation.</p>","PeriodicalId":77831,"journal":{"name":"Advances in myocardiology","volume":"6 ","pages":"465-72"},"PeriodicalIF":0.0,"publicationDate":"1985-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"15103988","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}