Studies of the digestion of bradykinin, lysyl bradykinin, and kinin-degradation products by carboxypeptidases A, B, and N

Sheikh, Ijaz; Kaplan, Allen P.

doi:10.1016/0006-2952(86)90727-6

Cited by 56 publications

(28 citation statements)

References 18 publications

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“…These results suggest that in chronic bronchitis, kinin generation may be mainly due to t-Kal. Studying the BALF of asthma patients, CHRISTIANSEN et al [33] found the highest kininogenase activity in small molecules after gel filtration chromatography (20)(21)(22)(23)(24)(25)(26)(27)(28)(29)(30)(31)(32)(33)(34). This kininogenase profile appears similar to the profile we found in patients with chronic bronchitis.…”

Section: Discussionsupporting

confidence: 82%

“…Theoretically, pl-Kal and t-Kal activity could be further differentiated with the direct measurement of bradykinin (as product of the pl-Kal activity) and lysyl-bradykinin (as product of the t-Kal activity). However, we believe that the catalytic activity of aminopeptidase N, degrading lysyl-bradykinin to bradykinin, would influence the lysyl-bradykinin measurement [34,35].…”

Section: Discussionmentioning

confidence: 98%

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Kinin generation in acute pneumonia and chronic bronchitis

Zhang¹,

Peng²,

Niehus³

et al. 1997

Eur Respir J

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Kinins are potent inflammatory mediators, liberated from kininogens by different kininogenases. The aim of this study was to investigate the kinin generation pathways in acute and chronic inflammation of the lower airways.We studied bronchoalveolar lavage fluid (BALF) of patients with acute pneumonia, patients with chronic bronchitis and healthy controls. Kinins were determined by radioimmunoassay (RIA). Plasma kallikrein (pl-Kal), α 2 -macroglobulin (α 2 -M) and toluenesulphonylarginine methyl ester (TAME) esterase activity (TAMEea) were studied in BALF before and after gel filtration chromatography. Plasma kallikrein and α 2 -M were measured using two newly developed sandwich enzymelinked immunosorbent assays (ELISAs). TAME-ea was measured by a radiochemical assay. After gel filtration, inhibition of TAME-ea with benzamidine, soy-beantrypsin inhibitor (SBTI) and aprotinin was performed.Kinins and TAME-ea did not differ significantly between acute pneumonia and chronic bronchitis, whereas pl-Kal and α 2 -M values were significantly higher in acute pneumonia. Gel filtration revealed the highest TAME-ea peak in acute pneumonia corresponding with the first α 2 -M peak at ~800 kDa, whereas in chronic bronchitis the highest peak was found at ~40 kDa. The inhibition test showed that the TAME-ea peak at ~800 kDa was due to pl-Kal and the TAME-ea peak at ~40 kDa was mainly due to tissue kallikrein. High peaks of α 2 -M and pl-Kal were found in pneumonia and only small peaks were seen in chronic bronchitis.We conclude that in acute airway inflammation kinins seem to be mainly generated by plasma kallikrein whereas in chronic inflammation, kininogenases other than plasma kallikrein, such as tissue kallikrein, seem to be more important.

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Section: Discussionsupporting

confidence: 82%

Section: Discussionmentioning

confidence: 98%

Kinin generation in acute pneumonia and chronic bronchitis

Zhang¹,

Peng²,

Niehus³

et al. 1997

Eur Respir J

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“…The second enzyme in plasma, kininase II, on the other hand is concentrated along the pulmonary vascular endothelial cell surface, and is identical to angiotensin-converting enzyme (ACE) (Sheikh and Kaplan, 1986b). This enzyme removes the dipeptide phe-arg from the C-terminus of bradykinin to yield a heptapeptide and a second cleavage removes ser-pro to leave a pentapeptide (Sheikh and Kaplan, 1986b).…”

Section: Bradykinin Generationmentioning

confidence: 99%

The contribution of gC1qR/p33 in infection and inflammation

Peerschke

Ghebrehiwet

2007

Immunobiology

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Human gC1qR/p33 is a multi-compartmental and multi-functional cellular protein expressed on a wide range of tissues and cell types including lymphocytes, endothelial cells, dendritic cells, and platelets. Although originally isolated as a receptor for C1q by virtue of its affinity (K d = 15-50 nM), and specificity for the globular heads of this molecule, a large body of evidence has now been accumulated which shows that in addition to C1q, gC1qR can serve as a receptor for diverse proinflammatory ligands including proteins of the plasma kinin-forming system, most notably high molecular weight kininogen (HK; K d = 9 nM). In addition, gC1qR has been reported to recognize and bind a number of functional antigens of viral and bacterial origin. It is its ability to interact with microbial antigens and its potential to serve as a cellular protein for bacterial attachment and/or entry that has been the focus of our laboratory in the past few years. On the surface of activated platelets, gC1qR has been shown to serve as a binding site for S. aureus and this binding is mediated by protein A. Since the binding of S. aureus to platelets is postulated to play a major role in the pathogenesis of endocarditis, gC1qR may provide a suitable surface for the initial adhesion of the bacterium. Recent data also demonstrate that the exosporium of B. cereus, a member of a genus of aerobic, gram-positive, spore-forming rod-like bacilli, which includes the deadly B. anthracis, contains a binding site for gC1qR. Therefore, by virtue of its ability to recognize plasma proteins such as C1q and HK, as well as bacterial and viral antigens, cell surface gC1qR not only is able to generate proinflammatory byproducts from the complement and kinin/kallikrein systems, but also can be an efficient vehicle and platform for a plethora of pathogenic microorganisms.

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“…The effect of prolonged ACE inhibition on kininase I activity is also reported. This enzyme represents one possible pathway of bradykinin metabolism during kininase II inhibition (Sheikh & Kaplan, 1986). The kallikrein-kinin system The basic elements of the kallikrein-kinin system are illustrated in Figure 1.…”

Section: Introductionmentioning

confidence: 99%

“…Effect of ACE inhibition on kininase I activity Kininase II is not the only enzyme capable of degrading bradykinin. This vasodilating peptide can also be metabolized in human plasma by carboxypeptidase N (= kininase I) (Sheikh & Kaplan, 1986), an enzyme which, like ACE, is located on the surface of endothelial cells (Ryan et al, 1982). We therefore studied in normal volunteers the effect of repeated doses of an ACE inhibitor on the plasma activity of kininase I.…”

Section: Introductionmentioning

confidence: 99%

Involvement of the kallikrein‐kinin system in the antihypertensive effect of the angiotensin converting enzyme inhibitors.

Waeber

Juillerat‐Jeanneret

Aubert

et al. 1989

Brit J Clinical Pharma

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1 Studies were performed in normal subjects and in rats to assess the effect of angiotensin converting enzyme (ACE) inhibition on the kallikrein-kinin system. As ACE is identical to kininase II, one of the enzymes physiologically involved in bradykinin degradation, bradykinin may be expected to accumulate during ACE inhibition. 2 A competitive antagonist of bradykinin was used to explore in unanaesthetized rats the contribution of circulating bradykinin to blood pressure control under ACE inhibition. 3 No evidence was found for a role of this vasodilating peptide in the blood pressure lowering effect of acute ACE inhibition. 4 The plasma activity of carboxypeptidase N (= kininase I), another pathway of bradykinin degradation, remained intact during a 1 week course of treatment with an ACE inhibitor in normal subjects. This therefore indicates that bradykinin formed during ACE inhibition can still be metabolized.

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Studies of the digestion of bradykinin, lysyl bradykinin, and kinin-degradation products by carboxypeptidases A, B, and N

Cited by 56 publications

References 18 publications

Kinin generation in acute pneumonia and chronic bronchitis

Kinin generation in acute pneumonia and chronic bronchitis

The contribution of gC1qR/p33 in infection and inflammation

Involvement of the kallikrein‐kinin system in the antihypertensive effect of the angiotensin converting enzyme inhibitors.

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