10.1016/S0006-8993(00)02118-1

10.1016/S0006-8993(00)02118-1 1 <h5>Introduction</h5> Tissue kallikrein (EC 3.4.21.35) is a serine protease which liberates a physiologically active peptide, kinin, from kininogens which mainly exist in the plasma and are widely distributed in the body. Although its physico-chemical properties have been extensively investigated [1,16,21] , little is known about the biological significance in the body. Tissue kallikrein has an extremely high substrate specificity for kininogens, but the enzyme also can hydrolyze proinsulin [24] , atrial natriuretic peptide [2] , apolipoprotein B-100 [3] , procollagenase [5] and vasoactive intestinal polypeptide (VIP) [14] in vitro. In addition, the presence of kallikrein mRNA and immunoreactive kallikrein has been reported in the various regions of the brains of mammals, such as pituitaries of rat [4,10,12,23] , pig [20] and human [9] , and pineal gland of rat [11] , although their contents are extremely low. Furthermore, the immunoreactive kallikrein has found in the neuronal cell bodies and processes of adult rat brains [13] . These suggest that wide varieties of proteins and/or polypeptides could be hydrolyzed by tissue kallikrein in vivo, too, and the enzyme plays an important role in neuronal functions besides the liberation of kinin. In the present paper, we investigated biochemically the http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png

10.1016/S0006-8993(00)02118-1

Elsevier — Jun 11, 2020

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Abstract

1 <h5>Introduction</h5> Tissue kallikrein (EC 3.4.21.35) is a serine protease which liberates a physiologically active peptide, kinin, from kininogens which mainly exist in the plasma and are widely distributed in the body. Although its physico-chemical properties have been extensively investigated [1,16,21] , little is known about the biological significance in the body. Tissue kallikrein has an extremely high substrate specificity for kininogens, but the enzyme also can hydrolyze proinsulin [24] , atrial natriuretic peptide [2] , apolipoprotein B-100 [3] , procollagenase [5] and vasoactive intestinal polypeptide (VIP) [14] in vitro. In addition, the presence of kallikrein mRNA and immunoreactive kallikrein has been reported in the various regions of the brains of mammals, such as pituitaries of rat [4,10,12,23] , pig [20] and human [9] , and pineal gland of rat [11] , although their contents are extremely low. Furthermore, the immunoreactive kallikrein has found in the neuronal cell bodies and processes of adult rat brains [13] . These suggest that wide varieties of proteins and/or polypeptides could be hydrolyzed by tissue kallikrein in vivo, too, and the enzyme plays an important role in neuronal functions besides the liberation of kinin. In the present paper, we investigated biochemically the

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