[State of the kinin system in burn shock and early toxemia]. 1976

T S Paskhina, and V F Nartikova, and V L Dotsenko, and T M Maslova, and N A Morozova

State of kinin system was studied in blood serum of patients with burns of II, III, IIIb and IV degrees during shock and early toxemia. Content or activity of main components of kinin system (kininogen, kallikreinogen, kallikrein, kininase I (carboxypeptidase N)) were repeatedly estimated at 4-6 hrs intervals; BAEE-esterase and antitryptic activities were also studied within 48-72 hrs after the trauma. At the same period plasminogen and plasmin were estimated in 8 patients. The activation of kinin system in burn shock was demonstrated: content of kininogen was decreased on 30-50% (independently on alteration of total protein in blood serum), the kininase activity was decreased, appearance of free kallikrein was observed and content of kallikreinogen was distinctly lowered already within 10-24 hrs after the trauma. Within 24 hrs after the burn the total decrease of kininogen in circulation accounted for 50-70% of the theoretical content. Fibrinolytic system was also activated during the burn shock. Increase in the antitryptic activity within 30-40 hrs after the trauma, which was previously established, is corroborated; the effect correlated with development of burn intoxication. The data obtained suggest that massive production of free kinins occur apparently within 24-48 hrs after burn.

UI MeSH Term Description Entries
D007610 Kallikreins Proteolytic enzymes from the serine endopeptidase family found in normal blood and urine. Specifically, Kallikreins are potent vasodilators and hypotensives and increase vascular permeability and affect smooth muscle. They act as infertility agents in men. Three forms are recognized, PLASMA KALLIKREIN (EC 3.4.21.34), TISSUE KALLIKREIN (EC 3.4.21.35), and PROSTATE-SPECIFIC ANTIGEN (EC 3.4.21.77). Kallikrein,Kininogenase,Callicrein,Dilminal,Kallidinogenase,Kalliginogenase,Kallikrein A,Kallikrein B',Kallikrein Light Chain,Kinin-Forming Enzyme,Padutin,alpha-Kallikrein,beta-Kallikrein,beta-Kallikrein B,Enzyme, Kinin-Forming,Kinin Forming Enzyme,Light Chain, Kallikrein,alpha Kallikrein,beta Kallikrein,beta Kallikrein B
D007704 Kininogens Endogenous peptides present in most body fluids. Certain enzymes convert them to active KININS which are involved in inflammation, blood clotting, complement reactions, etc. Kininogens belong to the cystatin superfamily. They are cysteine proteinase inhibitors. HIGH-MOLECULAR-WEIGHT KININOGEN; (HMWK); is split by plasma kallikrein to produce BRADYKININ. LOW-MOLECULAR-WEIGHT KININOGEN; (LMWK); is split by tissue kallikrein to produce KALLIDIN. Cystatins, Kininogen,Kininogen,Prekinins,Prokinins,T-Kininogen,Thiostatin,Kininogen Cystatins,T Kininogen
D007705 Kinins A generic term used to describe a group of polypeptides with related chemical structures and pharmacological properties that are widely distributed in nature. These peptides are AUTACOIDS that act locally to produce pain, vasodilatation, increased vascular permeability, and the synthesis of prostaglandins. Thus, they comprise a subset of the large number of mediators that contribute to the inflammatory response. (From Goodman and Gilman's The Pharmacologic Basis of Therapeutics, 8th ed, p588) Kinin
D008297 Male Males
D001798 Blood Proteins Proteins that are present in blood serum, including SERUM ALBUMIN; BLOOD COAGULATION FACTORS; and many other types of proteins. Blood Protein,Plasma Protein,Plasma Proteins,Serum Protein,Serum Proteins,Protein, Blood,Protein, Plasma,Protein, Serum,Proteins, Blood,Proteins, Plasma,Proteins, Serum
D002056 Burns Injuries to tissues caused by contact with heat, steam, chemicals (BURNS, CHEMICAL), electricity (BURNS, ELECTRIC), or the like. Burn
D004950 Esterases Any member of the class of enzymes that catalyze the cleavage of an ester bond and result in the addition of water to the resulting molecules. Esterase
D005260 Female Females
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D001121 Lysine Carboxypeptidase A metallocarboxypeptidase that removes C-terminal basic amino acid from peptides and proteins, with preference shown for lysine over arginine. It is a plasma zinc enzyme that inactivates bradykinin and anaphylatoxins. Carboxypeptidase N,Kininase I,Anaphylatoxin Inactivator,Bradykininase,Carboxypeptidase, Lysine,Inactivator, Anaphylatoxin

Related Publications

T S Paskhina, and V F Nartikova, and V L Dotsenko, and T M Maslova, and N A Morozova
January 1977, Patologicheskaia fiziologiia i eksperimental'naia terapiia,
T S Paskhina, and V F Nartikova, and V L Dotsenko, and T M Maslova, and N A Morozova
January 1972, Voprosy meditsinskoi khimii,
T S Paskhina, and V F Nartikova, and V L Dotsenko, and T M Maslova, and N A Morozova
January 1992, Agents and actions. Supplements,
T S Paskhina, and V F Nartikova, and V L Dotsenko, and T M Maslova, and N A Morozova
August 1978, Nihon rinsho. Japanese journal of clinical medicine,
T S Paskhina, and V F Nartikova, and V L Dotsenko, and T M Maslova, and N A Morozova
April 1982, Zeitschrift fur medizinische Laboratoriumsdiagnostik,
T S Paskhina, and V F Nartikova, and V L Dotsenko, and T M Maslova, and N A Morozova
January 1972, Zhurnal eksperimental'noi i klinicheskoi meditsiny,
T S Paskhina, and V F Nartikova, and V L Dotsenko, and T M Maslova, and N A Morozova
January 1986, Voprosy meditsinskoi khimii,
T S Paskhina, and V F Nartikova, and V L Dotsenko, and T M Maslova, and N A Morozova
May 1970, Die Medizinische Welt,
T S Paskhina, and V F Nartikova, and V L Dotsenko, and T M Maslova, and N A Morozova
January 1984, Voprosy meditsinskoi khimii,
T S Paskhina, and V F Nartikova, and V L Dotsenko, and T M Maslova, and N A Morozova
June 1978, Problemy gematologii i perelivaniia krovi,
Copied contents to your clipboard!