Kininogenases of Blood Cells (Alternate Kinin Generating Systems)

Greenbaum, Lowell M.

doi:10.1007/978-3-642-67301-6_2

Cited by 9 publications

(4 citation statements)

References 21 publications

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“…Previous studies have shown that polymorphonuclear (PMN) leucocytes contain two distinct types of kininogenases (Greenbaum & Kim, 1967: Greenbaum et (11, 1969Greenbaum, , 1979Melmon & Cline, 1967;Movat et al, 1976;Newballetal, 1975;Lupkeetal, 1982). Oneisafamily of neutral proteases that catalyse the formation of methionyllysyl-bradykinin or bradykinin from plasma kininogen (Melmon & Cline, 1967;Movat et al, 1973Movat et al, , 1976Newball et al, 1975;Lupke et al, 1982).…”

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“…Oneisafamily of neutral proteases that catalyse the formation of methionyllysyl-bradykinin or bradykinin from plasma kininogen (Melmon & Cline, 1967;Movat et al, 1973Movat et al, , 1976Newball et al, 1975;Lupke et al, 1982). The second group consists of the leucokinin-forming enzyme, which shows properties similar to cathepsins (Greenbaum, 1979); they act on leucokininogen to produce leucokinins, bioactive peptides of 2 1-25 amino acids (Chang et al, 1972;Freer et al, 1972). A further distinction between the two types of kininogenases is that leucokininogen and leucokinins are structurally distinct from plasma kininogens and kinins respectively (Greenbaum, , 1979.…”

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“…The second group consists of the leucokinin-forming enzyme, which shows properties similar to cathepsins (Greenbaum, 1979); they act on leucokininogen to produce leucokinins, bioactive peptides of 2 1-25 amino acids (Chang et al, 1972;Freer et al, 1972). A further distinction between the two types of kininogenases is that leucokininogen and leucokinins are structurally distinct from plasma kininogens and kinins respectively (Greenbaum, , 1979. Both types of kininogenases have so far been described in preparations of human PMN leucocytes isolated from blood (Melmon & Cline, 1967;Greenbaum et al, 1969;Movat et al, 1973;Newball et al, 1975;Lupke et al, 1982).…”

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Identification of a tissue kallikrein in human polymorphonuclear leucocytes

1989

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We have identified a tissue kallikrein in polymorphonuclear (PMN) leucocytes of normal human blood and bone marrow by immunocytochemistry, radioimmunoassay and enzymology. Immunoreactive tissue kallikrein was visualized in the mature neutrophil leucocytes and in immature forms such as metamyelocytes and myelocytes. No tissue kallikrein was detected in eosinophil leucocytes, lymphocytes, macrophages, megakaryocytes and platelets. So far, we have failed to observe immunoreactivity to tissue kallikrein in basophils. The presence of tissue kallikrein in extracts prepared from PMN leucocytes isolated from peripheral blood was demonstrated by immunodiffusion, dot-blotting and by radioimmunoassay. The kininogenase and amidase activity of the extracts resembled that of tissue kallikrein in being resistant to soya bean trypsin inhibitor and sensitive to trasylol. The amidase activity attributable to tissue kallikrein was completely inhibited by specific antisera.

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Identification of a tissue kallikrein in human polymorphonuclear leucocytes

1989

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“…Besides kallikreins, neutrophils contain a number of other enzymes which are stored intracellulary in cytoplasmic granules. These enzymes, similarly to tissue kallikreins, have the capacity to generate kinins from kininogens (Movat et al ., 1973; Greenbaum, 1979; Lupke et al ., 1982) and may be implicated in the inflammatory responses.…”

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Contribution of B₂ receptors for bradykinin in Arthus reaction‐induced plasma extravasation in wild‐type or B₂ transgenic knockout mice

Samadfam

Teixeira²,

Bkaily

et al. 2000

British J Pharmacology

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1 The aim of the present study was to investigate the contribution of bradykinin (BK) B 1 and B 2 receptors in a model of type III hypersensitivity, the reverse passive Arthus reaction (RPA), in wildtype mice and transgenic B 2 knockout littermates. 2 BK (10 mg mouse 71 ) or bovine serum albumin (0.5 mg mouse 71 ) induced a sustained Evans blue extravasation for more than 80 min in naive or rabbit anti-bovine serum albumin-treated mice (RPA model), respectively. The response to the two stimuli was prevented by the B 2 receptor antagonist, HOE-140, but not by [Leu 8 ]desArg 9 -BK (B 1 receptor antagonist). 3 In contrast to the wild-type littermates, RPA and bradykinin were unable to trigger an increase in plasma extravasation in B 2 knockout mice. 4 Furthermore, endothelin-1 (5 mg mouse 71 ) and a selective NK-1 receptor agonist [Sar 9 ,Met (O 2 ) 11 ]-SP (20 mg mouse 71 ), triggered a signi®cant increase in peritoneal plasma extravasation in both wild-type and B 2 knockout animals. 5 A pretreatment with indomethacin (200 mg mouse 71 ) signi®cantly reduced the RPA-induced but not the BK-induced increase in Evans blue extravasation. Furthermore, RPA, but not BK, triggered a signi®cant indomethacin-sensitive increase in peritoneal prostaglandin E 2 content. 6 Our results suggest a pivotal role for B 2 receptors in the mechanism of plasma extravasation which occurs during the reverse passive Arthus reaction in the mouse. Moreover, our results suggest an important contribution of prostanoids in the plasma leakage mechanisms triggered by RPA but not by bradykinin.

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Bradykinin receptor antagonists

Burch

Farmer

Steranka

1990

Medicinal Research Reviews

132

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Bradykinin and its active metabolites are produced at the sites of their actions by kallikreins. They potently elicit a variety of biological effects: hypotension, bronchoconstriction, gut and uterine contraction, epithelial secretion in airway, gut, and exocrine glands, vascular permeability, pain, connective tissue proliferation, and eicosanoid formation. These effects are mediated by at least two broad classes of receptors. The most common is the B2 subtype. The Stewart and Vavrek peptides characterized by a DPhe7 substitution have provided powerful tools for study of bradykinin's actions by competitively and specifically blocking bradykinin B2 receptors. The significance of kinins in certain human diseases is being explored using these new tools and potential therapeutic agents. At present, human clinical trials are underway to test the usefulness of bradykinin receptor antagonists in the symptoms of the common cold and in the pain associated with severe burns. Trials for use in asthma will be initiated in 1990.

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Kininogenases of Blood Cells (Alternate Kinin Generating Systems)

Cited by 9 publications

References 21 publications

Identification of a tissue kallikrein in human polymorphonuclear leucocytes

Identification of a tissue kallikrein in human polymorphonuclear leucocytes

Contribution of B₂ receptors for bradykinin in Arthus reaction‐induced plasma extravasation in wild‐type or B₂ transgenic knockout mice

Bradykinin receptor antagonists

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Kininogenases of Blood Cells (Alternate Kinin Generating Systems)

Cited by 9 publications

References 21 publications

Identification of a tissue kallikrein in human polymorphonuclear leucocytes

Identification of a tissue kallikrein in human polymorphonuclear leucocytes

Contribution of B2 receptors for bradykinin in Arthus reaction‐induced plasma extravasation in wild‐type or B2 transgenic knockout mice

Bradykinin receptor antagonists

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Contribution of B₂ receptors for bradykinin in Arthus reaction‐induced plasma extravasation in wild‐type or B₂ transgenic knockout mice