Divalent cations induce protofibril gelation. 1988

G Marx
Magen David Adom Blood Services, Tel Hashomer Medical Center, Tel Aviv, Israel.

Soluble fibrin oligomers (protofibrils) undergo phase change merely by adding 1-2 mM Ca2+ or 25-100 microM Zn2+. The cation-induced "protofibrin" clots appear similar to normally formed fibrin gels. Maximal clot turbidity of protofibrin gels increases with cations in a concentration-dependent manner. Magnesium (less than 0.5 mM) is ineffective in inducing protofibril gelation. Turbidity and degree of polymerization (DP) [indirectly expressed as AT (activation time)] appear to be positively correlated, regardless of whether the divalent cation is Ca2+ or Zn2+. Cross sections of Ca2+-induced protofibrin fibers are approximately 6-18-fibrin-monomers-thick. With both Ca2+ and 40 microM Zn2+, fiber cross section increases to 30-50 monomers thick. Negatively stained Zn2+-and Ca2+-induced protofibrin gels exhibit banding periodicity of approximately 240 A, similar to that of normally generated fibrin gels. Regions of lateral merging of individual segments of the protofibrin leads to increased cross section of the fiber and forms a branch required for gelation. These findings indicate that the rate of coagulation and the ultimate thickness of the fibers both relate to lateral associative processes of protofibrils, which are augmented by physiologic concentrations of 2+ and Zn2+.

UI MeSH Term Description Entries
D008854 Microscopy, Electron Microscopy using an electron beam, instead of light, to visualize the sample, thereby allowing much greater magnification. The interactions of ELECTRONS with specimens are used to provide information about the fine structure of that specimen. In TRANSMISSION ELECTRON MICROSCOPY the reactions of the electrons that are transmitted through the specimen are imaged. In SCANNING ELECTRON MICROSCOPY an electron beam falls at a non-normal angle on the specimen and the image is derived from the reactions occurring above the plane of the specimen. Electron Microscopy
D009391 Nephelometry and Turbidimetry Chemical analysis based on the phenomenon whereby light, passing through a medium with dispersed particles of a different refractive index from that of the medium, is attenuated in intensity by scattering. In turbidimetry, the intensity of light transmitted through the medium, the unscattered light, is measured. In nephelometry, the intensity of the scattered light is measured, usually, but not necessarily, at right angles to the incident light beam. Turbidimetry,Nephelometry,Turbidimetry and Nephelometry
D001777 Blood Coagulation The process of the interaction of BLOOD COAGULATION FACTORS that results in an insoluble FIBRIN clot. Blood Clotting,Coagulation, Blood,Blood Clottings,Clotting, Blood
D002118 Calcium A basic element found in nearly all tissues. It is a member of the alkaline earth family of metals with the atomic symbol Ca, atomic number 20, and atomic weight 40. Calcium is the most abundant mineral in the body and combines with phosphorus to form calcium phosphate in the bones and teeth. It is essential for the normal functioning of nerves and muscles and plays a role in blood coagulation (as factor IV) and in many enzymatic processes. Coagulation Factor IV,Factor IV,Blood Coagulation Factor IV,Calcium-40,Calcium 40,Factor IV, Coagulation
D002413 Cations, Divalent Positively charged atoms, radicals or groups of atoms with a valence of plus 2, which travel to the cathode or negative pole during electrolysis. Divalent Cations
D005176 Factor XIII A fibrin-stabilizing plasma enzyme (TRANSGLUTAMINASES) that is activated by THROMBIN and CALCIUM to form FACTOR XIIIA. It is important for stabilizing the formation of the fibrin polymer (clot) which culminates the coagulation cascade. Coagulation Factor XIII,Factor XIII Transamidase,Fibrin Stabilizing Factor,Fibrinase,Laki-Lorand Factor,Blood Coagulation Factor XIII,Factor 13,Factor Thirteen,Laki Lorand Factor,Factor XIII, Coagulation,Stabilizing Factor, Fibrin,Transamidase, Factor XIII,XIII, Coagulation Factor
D005337 Fibrin A protein derived from FIBRINOGEN in the presence of THROMBIN, which forms part of the blood clot. Antithrombin I
D005340 Fibrinogen Plasma glycoprotein clotted by thrombin, composed of a dimer of three non-identical pairs of polypeptide chains (alpha, beta, gamma) held together by disulfide bonds. Fibrinogen clotting is a sol-gel change involving complex molecular arrangements: whereas fibrinogen is cleaved by thrombin to form polypeptides A and B, the proteolytic action of other enzymes yields different fibrinogen degradation products. Coagulation Factor I,Factor I,Blood Coagulation Factor I,gamma-Fibrinogen,Factor I, Coagulation,gamma Fibrinogen
D005782 Gels Colloids with a solid continuous phase and liquid as the dispersed phase; gels may be unstable when, due to temperature or other cause, the solid phase liquefies; the resulting colloid is called a sol.
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man

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