A local kallikrein-kinin system is present in rat hearts.

Nolly, H; Carbini, Luis A.; Scicli, G; Carretero, Oscar A.; Scicli, A. G.

doi:10.1161/01.hyp.23.6.919

Cited by 132 publications

(55 citation statements)

References 12 publications

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“…Possible candidates for the prorenin-activating enzyme are kallikrein (37), prohormone convertases (51), and cathepsin B (45), although the latter seems unlikely in view of the absence of an inhibitory effect of E64. These enzymes have been demonstrated in the heart (6,41,49,55). Furthermore, Baba and colleagues (3) described a serine protease (mol mass 26 kDa) capable of activating prorenin in rat adrenal explant cultures.…”

Section: Discussionmentioning

confidence: 99%

High-affinity prorenin binding to cardiac man-6-P/IGF-II receptors precedes proteolytic activation to renin

Saris¹,

Derkx²,

Bruin³

et al. 2001

American Journal of Physiology-Heart and Circulatory Physiology

105

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Section: Discussionmentioning

confidence: 99%

High-affinity prorenin binding to cardiac man-6-P/IGF-II receptors precedes proteolytic activation to renin

Saris¹,

Derkx²,

Bruin³

et al. 2001

American Journal of Physiology-Heart and Circulatory Physiology

105

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“…24 Therefore, locally generated hormones could alter the tissue structure in an autocrine and/or paracrine manner. 25 Because we could not detect any conspicuous differences in LV geometry and systolic function between the 2 treatment groups, the effect of the ACEI on both the LV contractile state and geometry seems to be more closely related to the inhibition of Ang II rather than the potentiation of BK action.…”

Section: Discussionmentioning

confidence: 99%

Bradykinin Improves Left Ventricular Diastolic Function Under Long-Term Angiotensin-Converting Enzyme Inhibition in Heart Failure

et al. 2002

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Abstract-Both systolic and diastolic cardiac dysfunction coexist in various degrees in the majority of patients with heart failure. Although ACE inhibitors are useful in the treatment of heart failure, the roles of bradykinin in the systolic and diastolic properties of left ventricular function under long-term treatment of ACE inhibitor have not been fully elucidated. We therefore evaluated the changes in left ventricular function, histomorphometry, and the expression of several failing heart related genes, by use of an orally active specific bradykinin type 2 receptor antagonist, FR173657 (0.3 mg/kg per day), with an ACE inhibitor, enalapril (1 mg/kg per day), in dogs with tachycardia-induced heart failure (270 ppm, 22 days) and compared the effects to enalapril alone. Although there were no differences observed in blood pressure, left ventricular dimension, and percentage of fractional shortening, FR173657 significantly increased left ventricular filling pressure (PϽ0.01), prolonged the time constant of relaxation (PϽ0.05), and suppressed the expression of endothelial NO synthase and sarcoplasmic reticulum Ca 2ϩ -ATPase mRNA (PϽ0.05). FR173657 also upregulated collagen type I and III mRNA (PϽ0.05) and increased the total amount of cardiac collagen deposits (PϽ0.05) in left ventricle compared with that in the enalapril-treated group. In conclusion, endogenous bradykinin contributes to the cardioprotective effect of ACE inhibitor, improving left ventricular diastolic dysfunction rather than systolic dysfunction, via modification of NO release and Ca 2ϩ handling and suppression of collagen accumulation. Key Words: angiotensin-converting enzyme Ⅲ bradykinin Ⅲ Ca 2ϩ -transponding ATPase Ⅲ diastole Ⅲ fibrosis Ⅲ heart failure Ⅲ ventricular function, left A ngiotensin-converting enzyme inhibitors (ACEIs) exert beneficial effects on cardiac contractile function and are useful in improving both the symptoms and survival rate of a broad spectrum of patients with congestive heart failure (CHF). 1 In addition to suppressing the formation of angiotensin (Ang) II, the agents also prevent the breakdown of the potent vasodilator bradykinin (BK), which exerts its vasodilative action through BK type 2 (B 2 ) receptors. 2 Cardiomyocytes and cardiac fibroblasts have the capacity to generate BK, and they express functional B 2 receptors. BK possesses not only vasodilative action but also inotropic and antiproliferative properties. 3 Indeed, an ACEI increased the left ventricular (LV) ejection fraction and reduced LV chamber dimension and mass, but these effects were attenuated in B 2 receptor knockout mice. 4 In the clinical setting, however, the majority of patients with what is currently called "systolic heart failure" also have diastolic dysfunction of various degrees. 5 Ang II affects diastolic LV function through the changed composition of the LV wall (ie, increased interstitial fibrosis or fibrous content) and by virtue of the altered activity of the myofibroblasts in CHF. Because BK also possesses antiproliferative propertie...

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“…In rat cardiac atria and ventricles glandular KLK, its mRNA (2) and low-molecularweight kininogens could be detected (3,4). Coronaries also contain and release KLK (2). Binding sites for BK have been described in myocytes as well as in cardiac fibroblasts (2,5).…”

Section: The Kallikrein-kinin Systemmentioning

confidence: 99%

“…Coronaries also contain and release KLK (2). Binding sites for BK have been described in myocytes as well as in cardiac fibroblasts (2,5). Thus, cardiac kinins may be generated continuously by a local KKS.…”

Section: The Kallikrein-kinin Systemmentioning

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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A local kallikrein-kinin system is present in rat hearts.

Cited by 132 publications

References 12 publications

High-affinity prorenin binding to cardiac man-6-P/IGF-II receptors precedes proteolytic activation to renin

High-affinity prorenin binding to cardiac man-6-P/IGF-II receptors precedes proteolytic activation to renin

Bradykinin Improves Left Ventricular Diastolic Function Under Long-Term Angiotensin-Converting Enzyme Inhibition in Heart Failure

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

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