Reduced transcoronary exchange and prostaglandin synthesis in diabetic rat heart

Rösen, P.; Rösen, R.; Hohl, Christopher M; Reinauer, H.; Klaus, W.

doi:10.1152/ajpheart.1984.247.4.h563

Cited by 20 publications

(12 citation statements)

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“…Several car-dioprotective effects of BK have been found by various authors after induction of myocardial ischemia. In isolated working rat hearts, BK improved cardiac performance and metabolism during ischemia and reperfusion (17,30). Recent emerging concepts propose also an anti-trophic role for kinins in attenuating the process of cardiac and vascular remodeling (31).…”

Section: Regulation Of B1r and B2r After Induction Of Myocardial Infamentioning

confidence: 99%

Regulation of the kinin receptors after induction of myocardial infarction: a mini-review

Tschöpe

Heringer-Walther

Walther

2000

Braz J Med Biol Res

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It is well known that the responses to vasoactive kinin peptides are mediated through the activation of two receptors termed bradykinin receptor B1 (B1R) and B2 (B2R). The physiologically prominent B2R subtype has certainly been the subject of more intensive efforts in structure-function studies and physiological investigations. However, the B1R activated by a class of kinin metabolites has emerged as an important subject of investigation within the study of the kallikreinkinin system (KKS). Its inducible character under stress and tissue injury is therefore a field of major interest. Although the KKS has been associated with cardiovascular regulation since its discovery at the beginning of the last century, less is known about the B1R and B2R regulation in cardiovascular diseases like hypertension, myocardial infarction (MI) and their complications. This mini-review will summarize our findings on B1R and B2R regulation after induction of MI using a rat model. We will develop the hypothesis that differences in the expression of these receptors may be associated with a dual pathway of the KKS in the complex mechanisms of myocardial remodeling. Key wordsThe kallikrein-kinin system Kinins are biologically active peptides which exert a broad spectrum of physiological effects, including vasodilation, smooth muscle contraction and pain induction. Several kinin peptides have been identified in mammalian species: the nonapeptide bradykinin (BK) and the decapeptide Lys-bradykinin (kallidin) belong to the best investigated members of the kinin family. Kinins are formed by cleavage from precursor kininogens by kallikreins (KLK). They are rapidly degraded by several kininases, including kininase II which is identical to angiotensinconverting enzyme. Kinins exert their effect after stimulation of their cell surface receptors: BK B1 receptor (B1R) and B2 receptor (B2R). Whereas the B2R is responsive to the intact kinins, BK and kallidin, the B1R has a higher affinity for the carboxypeptidase metabolites of kinins, des-Arg 9 -BK and des-

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Section: Regulation Of B1r and B2r After Induction Of Myocardial Infamentioning

confidence: 99%

Regulation of the kinin receptors after induction of myocardial infarction: a mini-review

Tschöpe

Heringer-Walther

Walther

2000

Braz J Med Biol Res

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“…Five rats were treated for inducing diabetes. We have applied the STZ model for rats (Rösen et al 1984) which we have already used in our previous studies (see, for example, Punkt et al 2001). In brief, diabetes was induced by intraperitoneal administration of 60 mg/kg body weight STZ (Boehringer, Mannheim, Germany) dissolved in 0.1 M citrate buffer pH 4.5 immediately before use.…”

Section: Animals and Processing Of Tissuementioning

confidence: 99%

Nitric oxide synthase�II in rat skeletal muscles

Punkt

Naupert

Wellner

et al. 2002

Histochemistry and Cell Biology

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Constitutive expression of nitric oxide synthase (NOS) II was found in rat hindlimb muscles by immunohistochemistry and western blotting during development from embryonic day 21 to the adult stage of 75 days. The immunohistochemical NOS II expression pattern was related to the physiological metabolic fibre types SO (slow-oxidative), FOG I, II (fast-oxidative glycolytic; I more glycolytic, II more oxidative) and FG (fast-glycolytic) and to the myosin-based fibre types I and IIA, IIB (IIX not separated) identified in serial sections by enzyme histochemistry and immunohistochemistry. In adult muscles only the small population of FOG II fibres, which is a part of both IIA and IIB fibre population, showed NOS II immunoreactivity. This is the reason that only weak NOS II expression in adult hindlimb muscles has been detected by western blotting. Hindlimb muscles of embryonic, neonatal and young rats of 8 days expressed more NOS II as compared with adult rat hindlimb muscles. This can be explained by the findings that before the age of 21 days fast fibres were metabolically undifferentiated, all of them were NOS II positive and contribute to the NOS II expression of the muscle. In muscles of diabetic rats the NOS II expression was elevated indicating an inhibition of glucose uptake into the muscle fibres of diabetic muscles. Our findings suggest that the NOS II may be designated both as constitutive and inducible.

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“…Diabetes was induced by streptozotocin (Boehringer ; 60 mg\kg body weight) dissolved in 0.1 ml of citrate buffer, pH 4.5, immediately before use, injected intraperitoneally as previously described [25]. Blood glucose was routinely checked, and was 34p6 mM at the time the animals were killed for experimentation.…”

Section: Induction Of Diabetesmentioning

confidence: 99%

Glucose transport and glucose transporter GLUT4 are regulated by product(s) of intermediary metabolism in cardiomyocytes

Fischer

Böttcher

Eblenkamp

et al. 1997

Biochemical Journal

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Alternative substrates of energy metabolism are thought to contribute to the impairment of heart and muscle glucose utilization in insulin-resistant states. We have investigated the acute effects of substrates in isolated rat cardiomyocytes. Exposure to lactate, pyruvate, propionate, acetate, palmitate, β-hydroxybutyrate or α-oxoglutarate led to the depression of glucose transport by up to 50 %, with lactate, pyruvate and propionate being the most potent agents. The percentage inhibition was greater in cardiomyocytes in which glucose transport was stimulated with the α-adrenergic agonist phenylephrine or with a submaximal insulin concentration than in basal or fully insulin-stimulated cells. Cardiomyocytes from fasted or diabetic rats displayed a similar sensitivity to substrates as did cells from control animals. On the other hand, the amination product of pyruvate (alanine), as well as valine and the aminotransferase inhibitors cycloserine and amino-oxyacetate, stimulated glucose transport about 2-fold. In addition, the effect of pyruvate was counteracted by cycloserine. Since reversible transamination reactions are known to affect the pool size of the citrate cycle, the influence of substrates, amino acids and aminotransferase

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Reduced transcoronary exchange and prostaglandin synthesis in diabetic rat heart

Cited by 20 publications

References 0 publications

Regulation of the kinin receptors after induction of myocardial infarction: a mini-review

Regulation of the kinin receptors after induction of myocardial infarction: a mini-review

Nitric oxide synthase�II in rat skeletal muscles

Glucose transport and glucose transporter GLUT4 are regulated by product(s) of intermediary metabolism in cardiomyocytes

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