Comparative studies of plasma kinins: The kallikrein-kinin system in poikilotherm and other vertebrates

Plasma kinins were studied throughout a wide-range of vertebrates. In all mammals, birds, and reptiles investigated, trypsin liberated kinins from whole blood preparations, from heat-treated plasma, and from intact plasma treated with 8-HQSO 4 (overall range of kinins = 0.7–4.4 μg/ml plasma, BK-equi...

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Veröffentlicht in:General and comparative endocrinology 1975-06, Vol.26 (2), p.165-178
Hauptverfasser: Dunn, K.S., Perks, A.M.
Format: Artikel
Sprache:eng
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Zusammenfassung:Plasma kinins were studied throughout a wide-range of vertebrates. In all mammals, birds, and reptiles investigated, trypsin liberated kinins from whole blood preparations, from heat-treated plasma, and from intact plasma treated with 8-HQSO 4 (overall range of kinins = 0.7–4.4 μg/ml plasma, BK-equivalent). Trypsin failed to produce kinins from similar preparations of amphibian, teleost, holocephalian, and elasmobranch blood, except for traces of activity in heat-treated amphibian plasma. A glass surface generated kinins in mammalian and turtle plasmas (averages: rat, 2.5; dog, 1.6; turtle, 1.3 μg/ml plasma, BK-equivalent); however, it was apparently without effect on any amphibian or teleost plasma tested. Kininase activity was found throughout all vertebrate plasmas investigated. The results suggested that plasma kinins could exist in the blood of various reptiles, birds, and mammals, and that a glass-activatable kallikrein-kinin system was present in the mammals and the turtle. A kinin-generating system could not be demonstrated in fish and amphibian plasmas. However, hog pancreas kallikrein liberated an oxytocic agent from the heattreated plasmas of fish and amphibians, as well as from all other vertebrate plasmas; the highest activity was found in the urodele, Amphiuma tridactylum (2.9 μg/ml plasma, BK-equivalent). Therefore, despite the apparent absence of the classical kallikrein-kinin system, oxytocic agents with some similarities to kinins can be produced in lower vertebrate plasmas by the action of specific kallikreins.
ISSN:0016-6480
1095-6840
DOI:10.1016/0016-6480(75)90132-X