Cardiac myosin adenosinetriphosphatase of rat and mouse. Distinctive enzymatic properties compared with rabbit and dog cardiac myosin.
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Biomedical subjects
Publications and source records attributed to Y Yazaki.
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Constriction of one renal artery in the presence of the opposite kidney can produce persistent hypertension which is often associated with increase in plasma renin activity, decrease in serum potassium and increase in water intake. In the present study the clipped kidney was removed in 15 hypertensive rabbits 12 to 54 weeks after the constriction. Blood pressure showed a prompt and transient fall which was followed by a slight rebound and subsequently a gradual decline. However, it still remained above the normal 5 weeks after removal. Removal of the clipped kidney resulted in return to normal of increased plasma renin activity, decreased serum potassium and increased water intake at the end of the postoperative first week.
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To elucidate the signal transduction pathway from external stimuli to nuclear gene expression in mechanical stress-induced cardiac hypertrophy, we examined the time course of activation of protein kinases such as Raf-1 kinase (Raf-1), mitogen-activated protein kinase kinase (MAPKK), MAP kinases (MAPKs) and 90-kDa ribosomal S6 kinase (p90rsk) in neonatal rat cardiomyocytes. Mechanical stretch rapidly activated Raf-1 and its maximal activation was observed at 1-2 min after stretch. The activity of MAPKK was also increased by stretch, with a peak at 5 min after stretch. In addition, MAPKs and p90rsk were maximally activated at 8 min and at 10-30 min after stretch, respectively. Next, the relationship between mechanical stress-induced hypertrophy and the cardiac renin-angiotensin system was investigated. When the stretch-conditioned culture medium was transferred to the culture dish of non-stretched cardiac myocytes, the medium activated MAPK activity slightly but significantly, and the activation was completely blocked by the type 1 angiotensin II receptor antagonist, CV-11974. However, activation of Raf-1 and MAPKs provoked by stretching cardiomyocytes was only partially suppressed by pretreatment with CV-11974. These results suggest that mechanical stress activates the protein kinase cascade of phosphorylation in cardiac myocytes in the order of Raf-1, MAPKK, MAPKs and p90rsk, and that angiotensin II, which is secreted from stretched myocytes, activates a part of these protein kinases.
Cardiac myxomas are benign tumors which sometimes secrete interleukin-6 (IL-6), however, the pathogenesis and the IL-6 secreting cells are not clear. There are vascular myosin heavy chain isoforms; SM2 expression is specific to mature smooth muscle cells, while SMemb is a nonmuscle-type isoform which is expressed in immature mesenchyme cells. We hypothesized that immature mesenchyme cells play pivotal roles in the secretion of IL-6; we studied these expression in resected samples of myxoma. SMemb expression was increased but SM2 expression was not in the channels of myxoma. Increased IL-6 transcription was observed in the SMemb expressing cells in the channel. Therefore, mesenchyme cells with immature phenotype in the channel play pivotal roles of inflammation and pathogenesis of cardiac myxoma.
BACKGROUND/AIMS: Histamine H(2) receptor antagonists are widely used for the treatment of peptic ulcer disorders. However, whether the H(2) receptor is present in parietal or immune cells in the lamina propria remains controversial. This study is designed to determine the H(2) receptor localization immunohistochemically using an antibody against the newly cloned mouse histamine H(2) receptor. METHODS: We cloned the mouse histamine H(2) receptor gene and generated a specific antipeptide antibody against the C terminus. Immunohistochemical studies were performed with this antibody and with a monoclonal antibody against H(+)/K(+) adenosine triphosphatase (ATPase). RESULTS: Histamine H(2) receptors were localized on the plasma membrane and on the cytoplasm just beneath the plasma membrane on the basolateral sides of gastric cells. Confocal microscopy of double-stained sections using the monoclonal antibody against H(+)/K(+) ATPase, a specific parietal cell marker, showed that histamine H(2) receptors colocalized with H(+)/K(+) ATPase. No specific histamine H(2) receptor immunoreactivities were observed in the submucosal regions. CONCLUSION: The H(2) receptor is localized in the gastric parietal cell.
We have previously shown that smooth muscle contains three types of myosin heavy chains: SM1, SM2, and SMemb. The present study was designed to assess how glomerular expression of mRNA for these isoforms is regulated and whether their expression is affected by enalapril treatment in diabetic rats. Animals were divided into 4 groups: (1) untreated diabetic rats; (2) enalapril-treated diabetic rats; (3) untreated control rats, and (4) enalapril-treated control rats. Enalapril treatment was continued for 24 weeks. The glomerular mRNA levels for SM1 and SM2 showed little change in all groups throughout the experimental period. In contrast, SMemb mRNA in group 1 increased significantly with age compared to levels found in untreated controls (4.6-fold higher at 4 weeks, p < 0.01; 6.8-fold higher at 12 weeks, p < 0.01, and 10.6-fold higher at 24 weeks, p < 0.001). Enalapril reduced both creatinine clearance (p < 0.01) and urinary protein excretion (p < 0.01) in diabetic rats. Moreover, enalapril significantly attenuated the increase in the glomerular SMemb mRNA level in diabetic rats (the difference between treated and untreated rats was significant at p < 0.01 from week 4 to 24). However, enalapril had no effect on SMemb mRNA levels in controls. These data suggest that SMemb is a molecular marker for phenotypic alteration and that the beneficial effect of enalapril on proteinuria and renal function may be, at least in part, associated with reducing SMemb mRNA expression in diabetic glomeruli.