kallidin has been researched along with Coronary-Disease* in 3 studies
2 review(s) available for kallidin and Coronary-Disease
Article | Year |
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[Plasma kinins and the cardiovascular system].
Topics: Animals; Arteriosclerosis; Blood Pressure; Bradykinin; Cardiovascular Physiological Phenomena; Coronary Circulation; Coronary Disease; Coronary Vessels; Dogs; Guinea Pigs; Heart; Heart Diseases; Humans; Hypersensitivity; Hypertension; Kallidin; Kinins; Myocarditis; Rheumatic Heart Disease | 1974 |
[Vasoactive kinins in the physiology and pathology of the cardiovascular system].
Topics: Animals; Arteries; Arteriovenous Anastomosis; Blood Circulation; Blood Vessels; Bradykinin; Cardiovascular Diseases; Cardiovascular Physiological Phenomena; Coronary Disease; Dogs; Guinea Pigs; Heart; Hemodynamics; Humans; Hypertension; Kallidin; Kallikreins; Kidney; Kinins; Models, Chemical; Myocardial Infarction; Pancreas; Salivary Glands; Shock | 1969 |
1 other study(ies) available for kallidin and Coronary-Disease
Article | Year |
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Kinins in humans.
The kinin peptide system in humans is complex. Whereas plasma kallikrein generates bradykinin peptides, glandular kallikrein generates kallidin peptides. Moreover, a proportion of kinin peptides is hydroxylated on proline(3) of the bradykinin sequence. We established HPLC-based radioimmunoassays for nonhydroxylated and hydroxylated bradykinin and kallidin peptides and their metabolites in blood and urine. Both nonhydroxylated and hydroxylated bradykinin and kallidin peptides were identified in human blood and urine, although the levels in blood were often below the assay detection limit. Whereas kallidin peptides were more abundant than bradykinin peptides in urine, bradykinin peptides were more abundant in blood. Bradykinin and kallidin peptide levels were higher in venous than arterial blood. Angiotensin-converting enzyme inhibition increased blood levels of bradykinin, but not kallidin, peptides. Reactive hyperemia had no effect on antecubital venous levels of bradykinin or kallidin peptide levels. These studies demonstrate differential regulation of the bradykinin and kallidin peptide systems, and indicate that blood levels of bradykinin peptides are more responsive to angiotensin-converting enzyme inhibition than blood levels of kallidin peptides. Topics: Adult; Angiotensin-Converting Enzyme Inhibitors; Antibody Specificity; Arteries; Bradykinin; Chromatography, High Pressure Liquid; Coronary Disease; Cross Reactions; Endothelium, Vascular; Female; Humans; Hydroxylation; Hyperemia; Jugular Veins; Kallidin; Male; Middle Aged; Peptidyl-Dipeptidase A; Radioimmunoassay; Renal Veins; Vasodilation | 2000 |