Characterization of a kininogenase from rat vascular tissue resembling tissue kallikrein.

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

doi:10.1161/01.res.56.6.816

Cited by 84 publications

(53 citation statements)

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“…The vascular kininogenase is inhibited by aprotinin and phenylmethylsulfonyl fluoride (PMSF) but is resistant to SBTI, 4 which is characteristic of glandular kallikrein. 5 SBTI was included in the incubation buffer to inhibit plasma kallikrein and trypsin-like enzymes that could contaminate the homogenates.…”

Section: Methodsmentioning

confidence: 99%

“…It was inhibited by aprotinin and by polyclonal and monoclonal antibodies against glandular kallikrein and was resistant to soybean trypsin inhibitor (SBTI). 4 Although the function of this vascular kininogenase is not known, it could participate in circulatory homeostasis through local generation of kinins. The present study was designed to determine whether one-kidney, one clip renovascular hypertension alters the concentration of vascular kininogenase.…”

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A kallikrein-like enzyme in blood vessels of one-kidney, one clip hypertensive rats.

et al. 1990

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Active and inactive kallikrein or a kallikrein-like enzyme are found in the aorta, vena cava, and tail artery and veins of the rat We studied the concentration of vascular ldninogenase in rats with one-kidney, one clip renovascular hypertension and in unilaterally nephrectomized normotensive rats. Six weeks after surgery, active and total vascular kininogenase activity (active plus trypsin-activated) was measured. Blood pressure was 212±4 mm Hg in the hypertensive rats (n=33) and 120±l mm Hg in the normotensive rats (n=32) (p<0.001). Active kininogenase was lower in the hypertensive rats; although the difference was not significant in the thoracic aorta (56±8 versus 77±15), it was highly significant in the abdominal aorta (63±13 versus 167±17, p<0.001) and tail artery (48±8 versus 197±31, p< 0.003). Total vascular kininogenase activity (active plus trypsin-activated) was lower in the hypertensive rats in all arteries examined: thoracic aorta (183±16 versus 380±38, p<0.003), abdominal aorta (565+61 versus 1,093±74, p<0.001), and tail artery (532±112 versus 1,243 ± 135, p< 0.003). Active kininogenase in the vena cava was higher in the hypertensive rats (213±56 versus 131±31); however, this difference was not statistically significant, whereas in the tail veins it was highly significant (l,803±221 versus 771 ±79, p<0.003). Total venous kininogenase activity was significantly higher in the hypertensive rats (vena cava, l,850±171 versus 998±149,p<0.01; tail vein, 4,261 ±261 versus 2,521±212, p<0.001). In conclusion, we found that in rats with one-kidney, one clip renovascular hypertension both active and total vascular kininogenase are decreased in the arteries and increased in the veins. These changes may contribute to the pathogenesis of hypertension. (Hypertension 1990;16:436-440) T he kallikrein-kinin system has been implicated in the regulation of renal function and blood pressure and in the pathogenesis of various forms of hypertension. "3 We found that kallikrein or a kallikrein-like enzyme is present in the tail arteries and veins of the rat in both active and inactive (trypsin-activated) forms. Both its molecular weight and inhibition profile were similar to glandular kallikrein. It was inhibited by aprotinin and by polyclonal and monoclonal antibodies against glandular kallikrein and was resistant to soybean trypsin inhibitor (SBTI). 4 Although the function of this vascular kininogenase is not known, it could participate in circulatory homeostasis through local generation of kinins. The present study was designed to determine whether one-kidney, one clip renovascular hypertension alters the concentration of vascular kininogenase. We measured active and total kininogenase activity in the thoracic and abdominal aorta, vena cava, and tail artery and veins of rats with onekidney, one clip renovascular hypertension and in unilaterally nephrectomized normotensive rats. MethodsMale Sprague-Dawley rats weighing 200-250 g were housed in a room under conditions of constant temperature and a 12-hour light/dark cycle; ...

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Section: Methodsmentioning

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A kallikrein-like enzyme in blood vessels of one-kidney, one clip hypertensive rats.

et al. 1990

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“…While the kallikrein gene is expressed mainly in the submandibular gland, pancreas and kidney, we detected small amounts of kallikrein mRNA in the heart, vascular tissue, and adrenal glands on polymerase chain reaction (PCR) (189,237). Kallikrein and similar enzymes have been found in the arteries and veins (190), heart (188), brain (58), spleen (57), adrenal glands (255), and blood cells (189); they have also been observed in the pituitary gland (66,216), pancreas (84), large and small intestines (242,320), and salivary and sweat glands (106) along with their exocrine secretions. Some of these enzymes were probably true kallikrein, while others may represent separate members of the kallikrein family.…”

Section: Introductionmentioning

confidence: 86%

“…The kallikrein-kinin system in the vasculature and regulation of local blood flow-Arteries and veins contain a kallikrein-like enzyme, and both vascular tissue and smooth muscle cells in culture contain kallikrein mRNA (190,237). Vascular smooth muscle cells in culture release both kallikrein and kininogen (200).…”

Section: The Kallikrein-kinin System In Inflammationmentioning

confidence: 99%

The Kallikrein-Kinin System as a Regulator of Cardiovascular and Renal Function

Carretero¹,

Yang²,

Rhaleb³

2005

Hypertension

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“…78 We do not know which enzymes release tissue kinins. We have reported that vascular tissue contains a kininogenase that has the same properties as glandular kallikrein 9 and that messenger RNA for kallikrein is present in vascular tissue and smooth muscle cells in culture. 10 Oza et al n reported that vascular smooth muscle cells in culture release both kallikrein and kininogen (kallikrein substrate).…”

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Zinc metallopeptidase inhibitors. A novel antihypertensive treatment.

Carretero

Scicli

1991

Hypertension

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Inhibitors of two zinc metallopeptidases, angiotensin I converting enzyme (ACE) and neutral metalloendopeptidase-24.11 (EP-24.11), are antihypertensive agents. In this issue of Hypertension, Genden and Molineaux report that yet another peptidase inhibitor, metalloendopeptidase-24.15, EC 3.4.24.15 (EP-24.15), lowers blood pressure in normotensive rats. In this editorial we discuss the possible role of kinins as common mediators of part of the vasodepressor action of these peptidase inhibitors. Genden and Molineaux report that the marked fall in blood pressure caused by the EP-24.15 inhibitor is almost abolished by a kinin receptor antagonist, supporting the hypothesis that kinins play a role in the regulation of normal blood pressure. We have confirmed that the EP-24.15 inhibitor used by these investigators lowers blood pressure. Up to now, EP-24.15 has not been implicated in in vivo metabolism of kinins. Although a number of kininases have been identified, our own previous work indicated that the metabolic pathway responsible for clearing kinins from the circulation involves the action of kininase II (angiotensin I converting enzyme) and renal peptidases. Nevertheless, the main metabolic pathway involved some other unidentified enzyme, since in these experiments disappearance of kinins from the circulation was only marginally reduced by a "cocktail" of inhibitors of ACE, EP-24.11, and carboxypeptidase N. It could be that EP-24.15 is involved in kinin metabolism. However, a number of questions need to be answered with regard to the mechanism by which the EP-24.15 inhibitor lowers blood pressure. The data obtained with the EP-24.15, NE-24.11, and ACE inhibitors suggest that potentiation of vasodilator peptides is yet another possible relevant therapeutic approach to hypertension and perhaps heart failure. (Hypertension 1991;68:366-371)

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Characterization of a kininogenase from rat vascular tissue resembling tissue kallikrein.

Cited by 84 publications

References 11 publications

A kallikrein-like enzyme in blood vessels of one-kidney, one clip hypertensive rats.

A kallikrein-like enzyme in blood vessels of one-kidney, one clip hypertensive rats.

The Kallikrein-Kinin System as a Regulator of Cardiovascular and Renal Function

Zinc metallopeptidase inhibitors. A novel antihypertensive treatment.

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