Kallikrein release by vascular tissue

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

doi:10.1152/ajpheart.1993.265.4.h1209

Cited by 35 publications

(33 citation statements)

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“…On the other hand, we and others have shown that components of the kallikrein-kinin system are found in the heart (11,54,55), while kinins are found in the effluent of isolated perfused hearts and are increased by ACEi as well as by ischemia (56, 57). Furthermore, ACEi significantly increase kinin concentrations in the heart and vascular tissue (58).…”

Section: Discussionmentioning

confidence: 96%

Effects of angiotensin-converting enzyme inhibitors and angiotensin II type 1 receptor antagonists in rats with heart failure. Role of kinins and angiotensin II type 2 receptors.

Liu¹,

Yang²,

Sharov³

et al. 1997

J. Clin. Invest.

567

407

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Angiotensin-converting enzyme inhibitors (ACEi) improve cardiac function and remodeling and prolong survival in patients with heart failure (HF). Blockade of the renin-angiotensin system (RAS) with an angiotensin II type 1 receptor antagonist (AT 1 -ant) may have a similar beneficial effect. In addition to inhibition of the RAS, ACEi may also act by inhibiting kinin destruction, whereas AT 1 -ant may block the RAS at the level of the AT 1 receptor and activate the angiotensin II type 2 (AT 2 ) receptor. Using a model of HF induced by myocardial infarction (MI) in rats, we studied the role of kinins in the cardioprotective effect of ACEi. We also investigated whether an AT 1 -ant has a similar effect and whether these effects are partly due to activation of the AT 2 receptor. Two months after MI, rats were treated for 2 mo with: (

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Section: Discussionmentioning

confidence: 96%

Effects of angiotensin-converting enzyme inhibitors and angiotensin II type 1 receptor antagonists in rats with heart failure. Role of kinins and angiotensin II type 2 receptors.

Liu¹,

Yang²,

Sharov³

et al. 1997

J. Clin. Invest.

567

407

View full text Add to dashboard Cite

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“…its action as an antioxidant, as a mitogen, or as an antiinflammatory agent (57-60)? Second, do other proteases present in the aortic intima that are capable of cleaving apoA-I, such as plasmin, thrombin, kallikrein, and elastase (42,61,62), also block cholesterol efflux? Interestingly, SDS-PAGE analysis of a major fibril protein purified from amyloid deposits in the aortic intima revealed two broad bands corresponding to ϳ14 and Ͻ10 kDa, which were shown to be NH 2 -terminal fragments of apoA-I (63).…”

Section: Fig 6 Proteolytic Degradation Of Hdlmentioning

confidence: 99%

Matrix Metalloproteinases-3, -7, and -12, but Not -9, Reduce High Density Lipoprotein-induced Cholesterol Efflux from Human Macrophage Foam Cells by Truncation of the Carboxyl Terminus of Apolipoprotein A-I

Lindstedt

Saarinen

Kalkkinen

et al. 1999

Journal of Biological Chemistry

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Matrix metalloproteinases (MMPs) have been suggested to function in remodeling of the arterial wall, but no information is available on their possible role in early atherogenesis, when cholesterol accumulates in the cells of the arterial intima, forming foam cells. Here, we incubated the major component responsible for efflux of cholesterol from foam cells, high density lipoprotein 3 (HDL 3 ), with MMP-1, -3, -7, -9, or -12 at 37°C before adding it to cholesterol-loaded human monocyte-derived macrophages. After incubation with MMP-3, -7, or -12, the ability of HDL 3 to induce the high affinity component of cholesterol efflux from the macrophage foam cells was strongly reduced, whereas preincubation with MMP-1 reduced cholesterol efflux only slightly and preincubation with MMP-9 had no effect. These differential effects of the various MMPs were reflected in their differential abilities to degrade the small pre-␤ migrating particles present in the HDL 3 fraction. NH 2 -terminal sequence and mass spectrometric analyses of the apolipoprotein (apo) A-I fragments generated by MMPs revealed that those MMPs that strongly reduced cholesterol efflux (MMPs-3, -7, and -12) cleaved the COOH-terminal region of apoA-I and produced a major fragment of about 22 kDa, whereas MMPs-1 and -9, which had little and no effect on cholesterol efflux, degraded apoA-I only slightly and not at all, respectively. These results show, for the first time, that some members of the MMP family can degrade the apoA-I of HDL 3 , so blocking cholesterol efflux from macrophage foam cells. This expansion of the substrate repertoire of MMPs to include apoA suggests that these proteinases are directly involved in the accumulation of cholesterol in atherosclerotic lesions.

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“…In addition, the expression of a kiningenerating member of mouse glandular kallikrein was detected in mouse kidney (28). We performed our studies in the presence of soybean trypsin inhibitor, which, at a concentration of 2 mg/ml, caused 73.3% of inhibition of the amidase activity of human leukocyte extracts (20) and which did not inhibit glandular (renal) kallikreins (29). Thus, we cannot rule out the possibility that our results could probably represent additive activities of both renal and leukocyte enzymes.…”

Section: Discussionmentioning

confidence: 96%

“…Thus, we cannot rule out the possibility that our results could probably represent additive activities of both renal and leukocyte enzymes. Future studies in the presence of SBTI + EDTA + aprotinin should be performed to evaluate independently renal kallikrein-like amidase activities from leukocyte or other proteases (29).…”

Section: Discussionmentioning

confidence: 99%

Kallikrein-like amidase activity in renal ischemia and reperfusion

Carattino

Cueva²,

Fonovich-de-Schroeder

et al. 2000

Braz J Med Biol Res

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We assessed a kallikrein-like amidase activity probably related to the kallikrein-kinin system, as well as the participation of leukocyte infiltration in renal ischemia and reperfusion. Male C57BL/KSJmdb mice were subjected to 20 or 60 min of ischemia and to different periods of reperfusion. A control group consisted of sham-operated mice, under similar conditions, except for ischemia induction. Kallikrein-like amidase activity, Evans blue extravasation and myeloperoxidase activity were measured in kidney homogenates, previously perfused with 0.9% NaCl. Plasma creatinine concentration increased only in the 60-min ischemic group. After 20 min of ischemia and 1 or 24 h of reperfusion, no change in kallikrein-like amidase activity or Evans blue extravasation was observed. In the mice subjected to 20 min of ischemia, edema was evident at 1 h of reperfusion, but kidney water content returned to basal levels after 24 h of reperfusion. In the 60-min ischemic group, kallikrein-like amidase activity and Evans blue extravasation showed a similar significant increase along reperfusion time. Kallikrein-like amidase activity increased from 4 nmol PNA mg protein -1 min -1 in the basal condition to 15 nmol PNA mg protein -1 min -1 at 10 h of reperfusion. For dye extravasation the concentration measured was near 200 µg of Evans blue/g dry tissue in the basal condition and 1750 µg of Evans blue/g dry tissue at 10 h of reperfusion. No variation could be detected in the control group. A significant increase from 5 to 40 units of DAbs 655 nm g wet tissue -1 min -1 in the activity of the enzyme myeloperoxidase was observed in the 60-min ischemic group, when it was evaluated after 24 h of reperfusion. Histological analysis of the kidneys showed migration of polymorphonuclear leukocytes from the vascular bed to the interstitial tissue in the 60-min ischemic group after 24 h of reperfusion. We conclude that the duration of ischemia is critical for the development of damage during reperfusion and that the increase in renal cortex kallikrein-like amidase activity probably released from both the kidney and leukocytes may be responsible, at least in part, for the observed effects, probably through direct induction of increased vascular permeability.

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Kallikrein release by vascular tissue

Cited by 35 publications

References 0 publications

Effects of angiotensin-converting enzyme inhibitors and angiotensin II type 1 receptor antagonists in rats with heart failure. Role of kinins and angiotensin II type 2 receptors.

Effects of angiotensin-converting enzyme inhibitors and angiotensin II type 1 receptor antagonists in rats with heart failure. Role of kinins and angiotensin II type 2 receptors.

Matrix Metalloproteinases-3, -7, and -12, but Not -9, Reduce High Density Lipoprotein-induced Cholesterol Efflux from Human Macrophage Foam Cells by Truncation of the Carboxyl Terminus of Apolipoprotein A-I

Kallikrein-like amidase activity in renal ischemia and reperfusion

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