Individual differences |
Methods | Statistics | Clinical | Educational | Industrial | Professional items | World psychology |
Biological: Behavioural genetics · Evolutionary psychology · Neuroanatomy · Neurochemistry · Neuroendocrinology · Neuroscience · Psychoneuroimmunology · Physiological Psychology · Psychopharmacology (Index, Outline)
|style="background: #F8EABA; text-align: center;" colspan="2"||Bradykinin|
|style="background: #F8EABA; text-align: center;" colspan="2"||Except where noted otherwise, data are given for|
materials in their standard state
(at 25 °C, 100 kPa)
Infobox disclaimer and references
Structure[edit | edit source]
Synthesis[edit | edit source]
Metabolism[edit | edit source]
In humans, bradykinin is broken down by three kininases: angiotensin-converting enzyme (ACE), aminopeptidase P (APP), and carboxypeptidase N (CPN), which cleave the 7-8, 1-2, and 8-9 positions, respectively .
Physiological role[edit | edit source]
Effects[edit | edit source]
Bradykinin is a potent endothelium-dependent vasodilator, causes contraction of non-vascular smooth muscle, increases vascular permeability and also is involved in the mechanism of pain. In some aspects, it has similar actions to that of histamine, and like histamine is released from venules rather than arterioles.
Bradykinin is also thought to be the cause of the dry cough in some patients on angiotensin converting enzyme (ACE) inhibitor drugs. This refractory cough is a common cause for stopping ACE-inhibitor therapy.
Receptors[edit | edit source]
- The B1 receptor is only expressed as a result of tissue injury, and is presumed to play a role in chronic pain. Most recently, this receptor has been described to play a role in inflammation. 
- The B2 receptor is constitutively active and participates in bradykinin's vasodilatory role.
The kinin B1 and B2 receptors belong to G protein coupled receptor (GPCR) family.
History[edit | edit source]
Bradykinin was discovered by three Brazilian physiologists and pharmacologists working at the Instituto de Biologia de São Paulo, in São Paulo city, led by Dr. Maurício Rocha e Silva. Together with colleagues Wilson Teixeira Beraldo and Gastão Rosenfeld they discovered in 1948 its powerful hypotensive effects in animal preparations. Bradykinin was detected in the blood plasma of animals after the addition of venom of Bothrops jararaca (Brazilian lancehead snake), which was brought by Rosenfeld from the Butantan Institute. This discovery was part of a continuing study on circulatory shock and proteolytic enzymes related to the toxicology of snake bites, started by Rocha e Silva as early as 1939. Bradykinin was to prove a new autopharmacological principle, i.e., a substance that is released in the body by a metabolic modification from precursors, which are pharmacologically active. According to B.J. Hagwood, Rocha e Silva's biographer, "The discovery of bradykinin has led to a new understanding of many physiological and pathological phenomena including circulatory shock induced by venoms and toxins."
Applications[edit | edit source]
The practical importance of the discovery of bradykinin became apparent when one of his collaborators at the Medical School of Ribeirão Preto at the University of São Paulo, Dr. Sérgio Henrique Ferreira, discovered a bradykinin potentiating factor (BPF) in the bothropic venom which increases powerfully both the duration and magnitude of its effects on vasodilation and the consequent fall in blood pressure. On the basis of this finding, Squibb scientists developed the first of a new generation of highly-effective anti-hypertensive drugs, the so-called ACE inhibitors, such as captopril (trademarked Capoten).
References[edit | edit source]
- Dendorfer A, Wolfrum S, Wagemann M, Qadri F, Dominiak P. Pathways of bradykinin degradation in blood and plasma of normotensive and hypertensive rats. Am J Physiol Heart Circ Physiol 2001;280:H2182-8. Fulltext. PMID 11299220.
- Kuoppala A, Lindstedt KA, Saarinen J, Kovanen PT, Kokkonen JO. Inactivation of bradykinin by angiotensin-converting enzyme and by carboxypeptidase N in human plasma. Am J Physiol Heart Circ Physiol 2000;278(4):H1069-74. Fulltext. PMID 10749699.
- Parpura et al., Glutamate-mediated astrocyte−neuron signalling, Nature 1994 Article
- Peter G. McLean et al., Association between Kinin B1 Receptor Expression and Leukocyte Trafficking across Mouse Mesenteric Postcapillary Venules, The Journal of Experimental Medicine 2000 Article
Angiotensin - Bombesin/Neuromedin B - Calcitonin gene-related peptide - Carnosine - Delta sleep-inducing peptide - FMRFamide - Galanin - Gastrin releasing peptide - Kinins (Bradykinin, Tachykinins ) - Neuromedin (B, N, U) - Neuropeptide Y - Neurophysins - Neurotensin - Opioid peptide - Pancreatic polypeptide - Pituitary adenylate cyclase activating peptide
|This page uses Creative Commons Licensed content from Wikipedia (view authors).|