Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0018799 (heart disease)
 34,133 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The factors influencing the decision to initiate resuscitation in prehospital cardiac arrest patients encountered in bradyasystole due to presumed heart disease were studied. For this purpose, the characteristics and circumstances of arrest of the patients encountered in asystole and electromechanical dissociation, seen by a physician-staffed prehospital emergency care unit in a tiered emergency medical system, were reviewed. During the study period, resuscitation was initiated in 83 bradyasytolic patients. The characteristics of these patients were compared with those of 72 patients in asystole or electromechanical dissociation declared dead on the scene without resuscitation. The presence of EMD was the most important factor influencing the decision to resuscitate (P less than 0.001), even if the arrest was unwitnessed, while the patient's age was of less importance. For the patients with a witnessed arrest, the delay before treatment was initiated also affected the decision. Successful resuscitation and survival of the patients was similar to earlier reports. The results provide guidelines in the decision making of initiation of resuscitation when developing our emergency care system into one with non-physicians as advanced life support providers.
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PMID:Initiation of resuscitation in patients with prehospital bradyasystolic cardiac arrest in Helsinki. 216 Jul 11

The authors, on a basis of experience acquisted since 1984 on two groups of patients, respectively 55 and 174 subjects with angina like chest-pain, individuated in the first group 45%, and 66.1% in the second group, the presence of GER-EMD with the execution of functional stationary manometric and 24 hour pH-metrical exams, without undergoing chemical, pharmacological, mechanical stimulation. They make note that 43 patients out of the second group, underwent, after a certain time, another cardiological study (negative for heart disease when recluted) due to graveness of the symptoms and 33 risulted holders of heart disease, 24 of whom also affected with EMD. The treatment with anti-H2 and procinethycs had succes in 39 patients out of 59, with GER; 10 patients underwent, with success, Nissen-Rossetti funduplication. Medical treatment with sublingual nifedipine was successful in 17 cases out of 56, with EMD; 19 underwent esophageal miotomy surgery commisurated on manometrical dates, with excellent results; 8 patients with hypertension of LES underwent pneumatic dilation with good results; 12 patients live, tolleratig angina like chest-pain. The final considerations are the following: it is not indispensable to look for contemperaly EMD and pain to afferm that pain is of esophageal origin; EMD must be clearly defined; the exclusion primarily of heart pathology must not exclude the possibility of the insorgence of heart desease, in the presence of EMD; the medical therapy, satisfactory in GER, is scarsely efficent in EMD, the decision for surgery must be taken on the gravity of pain associated with an esophageal pathology well defined with numerous diagnostic exams.
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PMID:[Clinical and therapeutic approaches in angina pectoris of esophageal origin]. 894 2

Emery-Dreifuss muscular dystrophy (EDMD) was delineated as a separate form of muscular dystrophy nearly 40 years ago, based on the distinctive clinical features of early contractures and humero-peroneal weakness, and cardiac conduction defects. The gene, STA at Xq28, for the commoner X-linked EDMD encodes a 34 kD nuclear membrane protein designated 'emerin', and in almost all cases on immunostaining is absent in muscle, skin fibroblasts, leucocytes and even exfoliative buccal cells, and a mosaic pattern in female carriers. The gene, LMNA at 1q21, for the autosomal dominant Emery-Dreifuss muscular dystrophy encodes other nuclear membrane proteins, lamins A/C. The diagnosis (at present) depends on mutation analysis rather than protein immunohistochemistry. It is still not at all clear how defects in these nuclear membrane proteins are related to the phenotype, even less clear that LMNA mutations can also be associated with familial dilated cardiomyopathy with no weakness, and even familial partial lipodystrophy with diabetes mellitus and coronary heart disease! What began as clinical studies in a relatively rare form of dystrophy has progressed to detailed research into the functions of nuclear membrane proteins particularly in regard to various forms of heart disease.
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PMID:Emery-Dreifuss muscular dystrophy - a 40 year retrospective. 1083 46

We used the relation between intracellular Ca(2+) concentration ([Ca(2+)](i)) and cell shortening during tetanus to evaluate the endogenous characteristics of Ca(2+) responsiveness of myofibrils in mouse ventricular myocytes. Enzymatically isolated myocytes were loaded with fura-2 AM (4 microM for 10 min), and the fura-2 fluorescence ratio at 340 and 380 nm excitation wave length [F(340)/F(380)] and cell length were measured simultaneously. Following treatment with thapsigargin (0.2 microM) (an inhibitor of the Ca(2+) pump of sarcoplasmic reticulum), myocytes were stimulated at 10 Hz for 10 s to produce a tetanic contraction and an instantaneous plot of the fluorescence ratio signal versus cell length (R-L trajectory) was constructed. An increase in the extracellular Ca(2+) concentration ([Ca(2+)](o)) from 0.5 to 2 mM extended the R-L trajectory without a substantial shift of the relation. The R-L trajectory was shifted rightward by the nonselective phosphodiesterase inhibitor, 3-isobutyl-1-methyl-xantine (IBMX, 200 microM) (desensitization of the myofibrils to Ca(2+)), and shifted leftward by the Ca(2+) sensitizing thiadiazinone derivative, EMD-57033 (0.5 microM) (sensitization of the myofibrils to Ca(2+)). Beta-adrenergic stimulant, isoproterenol (5 nM), also shifted the R-L trajectory to the right, suggesting that the membrane receptor could be preserved. These results suggest that the R-L trajectory is a useful method to estimate the myofibrillar responsiveness to Ca(2+) in isolated mouse myocytes and can be applied to various mouse models of heart disease.
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PMID:Use of tetanus to investigate myofibrillar responsiveness to Ca(2+) in isolated mouse ventricular myocytes. 1204 10

Emery-Dreifuss muscular dystrophy (EDMD) is an inherited disorder characterized by slowly progressive skeletal muscle weakness in a humero-peroneal distribution, early contractures and prominent cardiomyopathy with conduction block. Mutations in EMD, encoding emerin, and LMNA, encoding A-type lamins, respectively, cause X-linked and autosomal dominant EDMD. Emerin and A-type lamins are proteins of the inner membrane of the nuclear envelope. Whereas the genetic cause of EDMD has been described and the proteins well characterized, little is known on how abnormalities in nuclear envelope proteins cause striated muscle disease. In this study, we analyzed genome-wide expression profiles in hearts from Emd knockout mice, a model of X-linked EDMD, using Affymetrix GeneChips. This analysis showed a molecular signature similar to that we previously described in hearts from Lmna H222P knock-in mice, a model of autosomal dominant EDMD. There was a common activation of the ERK1/2 branch of the mitogen-activated protein kinase (MAPK) pathway in both murine models, as well as activation of downstream targets implicated in the pathogenesis of cardiomyopathy. Activation of MAPK signaling appears to be a cornerstone in the development of heart disease in both X-linked and autosomal dominant EDMD.
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PMID:Activation of MAPK in hearts of EMD null mice: similarities between mouse models of X-linked and autosomal dominant Emery Dreifuss muscular dystrophy. 1756 79

The human genome is contained within the nucleus and is separated from the cytoplasm by the nuclear envelope. Mutations in the nuclear envelope proteins emerin and lamin A cause a number of diseases including premature aging syndromes, muscular dystrophy, and cardiomyopathy. Emerin and lamin A are implicated in regulating muscle- and heart-specific gene expression and nuclear architecture. For example, lamin A regulates the expression and localization of gap junction and intercalated disc components. Additionally, emerin and lamin A are also required to maintain nuclear envelope integrity. Demonstrating the importance of maintaining nuclear integrity in heart disease, atrioventricular node cells lacking lamin A exhibit increased nuclear deformation and apoptosis. This review highlights the present understanding of lamin A and emerin function in regulating nuclear architecture, gene expression, and cell signaling and discusses putative mechanisms for how specific mutations in lamin A and emerin cause cardiac- or muscle-specific disease.
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PMID:Emerin and the nuclear lamina in muscle and cardiac disease. 1859 64

Heart muscle contraction is regulated by Ca(2+) binding to the thin filament protein troponin C. In cardiovascular disease, the myofilament response to Ca(2+) is often altered. Compounds that rectify this perturbation are of considerable interest as therapeutics. Plant flavonoids have been found to provide protection against a variety of human illnesses such as cancer, infection, and heart disease. (-)-Epigallocatechin gallate (EGCg), the prevalent flavonoid in green tea, modulates force generation in isolated guinea pig hearts (Hotta, Y., Huang, L., Muto, T., Yajima, M., Miyazeki, K., Ishikawa, N., Fukuzawa, Y., Wakida, Y., Tushima, H., Ando, H., and Nonogaki, T. (2006) Eur. J. Pharmacol. 552, 123-130) and in skinned cardiac muscle fibers (Liou, Y. M., Kuo, S. C., and Hsieh, S. R. (2008) Pflugers Arch. 456, 787-800; and Tadano, N., Yumoto, F., Tanokura, M., Ohtsuki, I., and Morimoto, S. (2005) Biophys. J. 88, 314a). In this study we describe the solution structure of the Ca(2+)-saturated C-terminal domain of troponin C in complex with EGCg. Moreover, we show that EGCg forms a ternary complex with the C-terminal domain of troponin C and the anchoring region of troponin I. The structural evidence indicates that the binding site of EGCg on the C-terminal domain of troponin C is in the hydrophobic pocket in the absence of troponin I, akin to EMD 57033. Based on chemical shift mapping, the binding of EGCg to the C-terminal domain of troponin C in the presence of troponin I may be to a new site formed by the troponin C.troponin I complex. This interaction of EGCg with the C-terminal domain of troponin C.troponin I complex has not been shown with other cardiotonic molecules and illustrates the potential mechanism by which EGCg modulates heart contraction.
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PMID:Solution structure of human cardiac troponin C in complex with the green tea polyphenol, (-)-epigallocatechin 3-gallate. 1954 63