WO1991017444A1 - PROCEDE POUR EVALUER QUANTITATIVEMENT LA CONCENTRATION DE FIBRINOGENE, DE FIBRONECTINE, D'α2-ANTIPLASMINE OU D'UNE TRANSGLUTAMINASE - Google Patents

PROCEDE POUR EVALUER QUANTITATIVEMENT LA CONCENTRATION DE FIBRINOGENE, DE FIBRONECTINE, D'α2-ANTIPLASMINE OU D'UNE TRANSGLUTAMINASE Download PDF

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Publication number
WO1991017444A1
WO1991017444A1 PCT/SE1991/000318 SE9100318W WO9117444A1 WO 1991017444 A1 WO1991017444 A1 WO 1991017444A1 SE 9100318 W SE9100318 W SE 9100318W WO 9117444 A1 WO9117444 A1 WO 9117444A1
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Prior art keywords
fibrinogen
fibronectin
antibody
factor xiii
peroxidase
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PCT/SE1991/000318
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English (en)
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Birger Blombäck
Birgitta Hessel
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    • G—PHYSICS
    • G01—MEASURING; TESTING
    • G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N33/00—Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
    • G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
    • G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
    • G01N33/86—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving blood coagulating time or factors, or their receptors
    • G—PHYSICS
    • G01—MEASURING; TESTING
    • G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N2333/00—Assays involving biological materials from specific organisms or of a specific nature
    • G01N2333/435—Assays involving biological materials from specific organisms or of a specific nature from animals; from humans
    • G01N2333/745—Assays involving non-enzymic blood coagulation factors
    • G01N2333/75—Fibrin; Fibrinogen
    • G—PHYSICS
    • G01—MEASURING; TESTING
    • G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N2333/00—Assays involving biological materials from specific organisms or of a specific nature
    • G01N2333/435—Assays involving biological materials from specific organisms or of a specific nature from animals; from humans
    • G01N2333/78—Connective tissue peptides, e.g. collagen, elastin, laminin, fibronectin, vitronectin, cold insoluble globulin [CIG]
    • G—PHYSICS
    • G01—MEASURING; TESTING
    • G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N2333/00—Assays involving biological materials from specific organisms or of a specific nature
    • G01N2333/81—Protease inhibitors
    • G—PHYSICS
    • G01—MEASURING; TESTING
    • G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N2333/00—Assays involving biological materials from specific organisms or of a specific nature
    • G01N2333/90—Enzymes; Proenzymes
    • G01N2333/91—Transferases (2.)
    • G01N2333/91045—Acyltransferases (2.3)
    • G01N2333/91074—Aminoacyltransferases (general) (2.3.2)
    • G01N2333/9108—Aminoacyltransferases (general) (2.3.2) with definite EC number (2.3.2.-)
    • G—PHYSICS
    • G01—MEASURING; TESTING
    • G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N2333/00—Assays involving biological materials from specific organisms or of a specific nature
    • G01N2333/90—Enzymes; Proenzymes
    • G01N2333/91—Transferases (2.)
    • G01N2333/91045—Acyltransferases (2.3)
    • G01N2333/91074—Aminoacyltransferases (general) (2.3.2)
    • G01N2333/9108—Aminoacyltransferases (general) (2.3.2) with definite EC number (2.3.2.-)
    • G01N2333/91085—Transglutaminases; Factor XIIIq (2.3.2.13)

Definitions

  • the present invention to a method of determining quan- titatively fibrinogen, fibronectin, ⁇ _-antiplasmin or a transglutaminase.
  • a known and important transglutamin ⁇ ase is Factor XIII.
  • Fibrinogen, fibronectin, ⁇ _-antiplasmin and Factor XIII are all important blood constituents and it is essen ⁇ tial to be able to determine the concentration of these constituents in blood and in other tissues. It has been found that Factor XIII is a transglutaminase in blood, the primary role of which is to cross-link protein chains in the fibrin network subsequent to its formation. This results partly in cross-linking bet ⁇ ween the ⁇ -chains in the fibrin and partly also be ⁇ tween the ⁇ -chains themselves. Factor XIII is also able to catalyse specifically the incorporation of certain plasma proteins in the fibrin network. For instance, fibronectin and ⁇ -antiplasmin are linked to the fibrin by Factor XIII catalysis; a ino groups in the fibrin fulfil a donator function in both cases.
  • Fibronectin is a protein which is apparently essential to cell proliferation and wound healing. The concentration of fibronectin is also lowered with infectious conditions, such as sepsis.
  • ⁇ _-antiplasmin is the most important inhibitor of fibrinolysis in blood. Increased con ⁇ centrations of this inhibitor or increased incorpora- tion in the fibrin coagulum has been observed in throm- botic conditions.
  • Factor Xllla on polystyrene spheres in the presence of fibro ⁇ nectin is not able to bind fibrin to the spheres; but that fibronectin is able to cross-link to cellular locations on a matrix with Factor Xllla acting as a catalyst. It is also shown that Factor XIII cross ⁇ links fibrin on itself and a limited number of sub ⁇ strates. Factor XIII also has a catalyzing effect in solutions containing fibrinogen and fibronectin, forming two types of cross-linked polymers, namely hybridoligomers and fibrinogenoligomers.
  • fragments of the fibrinogen molecule will not disturb the surface- bound reaction.
  • fibrinolytic fragment of the fibrinogen molecule has had a disturbing effect on the assay analysis. This disturbance is not found when practicing the present method, despite the fact that potential cross-linking locations are found in such fragments as Ds. Heparin can also have a disturbing effect in several known assaying methods. This is not the case when practicing the present invention, how ⁇ ever.
  • fibrinogen, fibronectin, ⁇ _- antiplasmin or a transglutaminase, particularly Factor XIII can be assayed functionally in a simple, but very precise fashion by means of a reaction which involves:
  • Figure 1 is a schematic illustration of the course followed by the reaction when determining, or assaying, fibrinogen
  • Figure 2 is a diagramme which illustrates the relation- ship between colour intensity and fibrinogen concentra ⁇ tion
  • Figure 3 is a diagramme which shows the relationship between colour intensity and fibronectin concentration, and also the effect of iodo acetamide on the reaction with Factor XIII;
  • Figure 4 is a diagramme which shows the relationship between colour intensity and activity for Factor Xllla
  • Figure 5 is a diagramme which shows the relationship between the colour intensity and the activity of Factor Xllla.
  • Figure 6 illustrates the relationship between absorb- ency and fibrinogen concentration in plasma
  • Figure 7 illustrates the relationship between absorb- ency and fibronectin concentration in plasma and serum
  • Figure 8 illustrates the activity of Factor XIII after different reaction times.
  • fibronectin When carrying out the analysis, fibronectin is adsorbed on a surface in a known manner (see Figure la) .
  • This surface may consist of a plastic material, such as polystyrene. Materials that are suitable for this purpose are available commercially, for example "Titer- tecplattor", latex spheres, etc.
  • a sample solution containing fibrinogen is then added ( Figure lb) ) .
  • a calcium chloride solution and Factor XIII suitably in an activated form, for instance a thrombin activated form, is then added.
  • a thrombin-activity inhibitor, for instance hirudin is then added to inhibit the thrombin excess used in the activating process or possibly generated in the sample.
  • Factor Xllla activated Factor XIII now catalyses the incorporation of the fibrinogen into the surface-bound fibronectin
  • HRP "horse-radish-peroxidase"
  • the fibrinogen-bound peroxidase (HRP) splits or cleaves the substrate, therewith producing a yellowish colour.
  • This part-stage of the process involving the use of an enzyme-labelled antibody and its visibilisation, is known as the enzyme immunosorption technique and is
  • Fibrinogen that is essentially free from fibronectin and Factor XIII is adsorbed on a surface of the kind described with reference to the quantitative determin ⁇ ation of fibrinogen.
  • a fibronectin-containing solution is applied to the surface, together with calcium chlor ⁇ ide, thrombin-activated Factor XIII and hirudin, this latter to neutralize excess thrombin.
  • Factor Xllla catalyses the incorporation of fibronectin into the surface-bound fibrinogen, analogously with that described with reference to the quantitative determination of fibrinogen.
  • the fibrinogen-bound fibronectin is then caused to react with an antibody (e.g.
  • Fibrinogen is caused to be adsorbed on a surface in the
  • sample solution contain fibrinogen and fibronectin, as is the case with blood plasma, it is necessary to remove the fibrinogen by coagulation with a snake—venom enzyme, and to remove fibronectin by adsorption on gelatine coupled to an appropriate poly- mer matrix, e.g. Sepharos ® , in a known manner.
  • an appropriate poly- mer matrix e.g. Sepharos ®
  • Fibrinogen that is essentially free from fibronectin and Factor XIII is adsorbed on a surface, analogous with the method described with reference to the quant ⁇ itative determination of fibronectin and Q._-anti- plasmin. An excess quantity of fibronectin is then added, together with calcium chloride and hirudin. A sample solution containing Factor XIII is then added. If active Factor XIII is present in the sample, the fibronectin will be incorporated on the surface of the fibrinogen and can be visibilised with a specific anti ⁇ body against fibronectin and a secondary antibody labelled with peroxidase, e.g. HRP, as described with reference to the quantitative determination of fibro ⁇ nectin. The total activity of Factor XIII can be determined by first treating the sample solution with batroxobin, to remove the fibrinogen by coagulation.
  • peroxidase e.g. HRP
  • a labelled fibronectin antibody when quantitatively determining the fibronectin concentration a labelled fibronectin antibody, while when determining the con ⁇ centration of ⁇ _-antiplasmin, there is used a labelled ⁇ _-antiplasmin antibody.
  • a primary labelled antifibronectin antibody when determining the activity of Factor XIII, there is preferably used a primary labelled antifibronectin antibody.
  • the primary antibody is preferably a HRP-labelled antibody.
  • a fibronectin solution 10 ⁇ g/ml
  • a fibronectin solution 10 ⁇ g/ml
  • the plates were allowed to stand overnight at room temperature.
  • the wells were then emptied and washed repeatedly with a solution of TNE-BSA-buffer 0 (0.05 M-tris-0.10 M NaCl-l mM EDTA, pH 7.4, containing 0.1% bovine serum albumin) .
  • a solution of bovine albumin (30 mg/ml) was then poured into the wells with the intention of blocking those locations on the well surfaces not saturated with fibronectin.
  • Microtitre plates were treated with fibrinogen in the same manner as that described in Example 2. The plates were also blocked and washed in the same manner as that described in Example 2. 150 ⁇ l of fibronectin solution
  • the blood was introduced into a vessel containing an anticoagulant substance, for example 3.8% trisodiu citrate or 0.1 M EDTA.
  • the anticoagulant is normally present in a proportion of 1 part coagulant to 9 parts of blood.
  • the blood was centrifuged (room temperature, 30 minutes, 1500 rpm) and blood plasma removed by suction. Prior to the analysis, the plasma was diluted with a TNE-BSA-buffer, (1:1000, 1:2000 and so on) (see Example 1).
  • Example 7 Analysis of the fibrinogen concentration in the same plasma on mutually different occasions.
  • Plasma from one single individual was treated in the manner described in Example 5 and analyzed (also in accordance with Example 5) on nine different occasions.
  • Plasma was treated in the manner described in Example 5. Serum was treated by treating a part of said plasma with the snake venom enzyme batroxobin (final concentration 0,5 E/ml for 60 minutes at 37°C) at room temperature, whereafter the fibrin coagulum was removed.
  • Plasma standard is a mixed plasma from several individuals, plasma B.J. is plasma from a single individual. Fragment Ds and heparin were added to plasma and these plasmas were compared with intact plasma. Fragment Ds and fibrinogen were added to serum.
  • Plasma was treated in the manner -described in Example 5.
  • the anticoagulant used comprised 0.1 M EDTA.
  • Fibrinogen was extracted from this plasma by coagula ⁇ tion with the snake venom enzyme batroxobin (final concentration 0,5 E/ml, 37°C, for 60 minutes). The fibrin coagulum was removed and the supernatant
  • fibronectin was effected essentially in the same manner as that described in Example 2. Microtitre plates were treated with fibrinogen and the plates blocked and washed in the manner described in Example 2. 150 ⁇ l of diluted plasma 20 ⁇ l of calcium chloride and 5 ⁇ l of hirudin were then added. 25 ⁇ l of thrombin- activated Factor XIII (final concentrations between 0.001 and 0.1 E/ml) were then added and the plates incubated for one hour at 37°C, while shaking the plates slowly.
  • Microtitre plates were treated with fibrinogen, in the manner described in Example 2. Blocking and washing of the plates was also effected in the manner described in Example 2. 150 ⁇ l of fibronectin solution (10.0 ⁇ g/ml), 20 ⁇ l of calcium chloride (0.2 M) and 5 ⁇ l of hirudin (2 ATU/ml) were then added. Finally, 25 ⁇ l of thrombin- activated Factor XIII (concentrations between 0.001 and 0.1 E/ml) were added and the plates incubated over different time periods, namely 1, 1.5 and 4 hours at 37°C, while slowly shaking the plates.
  • Plasma from a number of individuals (12 persons) was treated in accordance with Example 5.
  • the anticoagulant used consisted of 0.1 M EDTA.
  • the plasmas were caused to coagulate by adding the snake venom enzyme batroxo- bin (0.5 E/ml in final concentration) over one hour at 37°. The coagulum was removed. These samples were analyzed with respect to the spontaneous activity of factor XIII in the manner described in Example 3.
  • Plasma from a girl suffering from a Factor XIII defi ⁇ ciency and from her father were treated in the manner described in Example 5.
  • the anticoagulant used con ⁇ sisted of 0.1 M EDTA.
  • the girl received transfusion with plasma from the father and samples were subsequently taken.
  • the plasmas were caused to coagu ⁇ late and were activated in the same manner as that described in Example 11.
  • the fibrinogen concentration was determined in the manner described in Example 5 and Factor XIII was determined in the manner described in Examples 3 and 11.

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Abstract

Le fibrinogène, la fibronectine, l'α2-antiplasmine et le Facteur XIII sont évalués quantitativement par un procédé de réaction qui consiste à: faire réagir du fibrinogène avec de la fibronectine ou de l'α2-antiplasmine, le Facteur XIII fonctionnant comme catalyseur; pré-évaluer les quantités de tous les constituants de réaction utilisés à l'exception de la quantité recherchée; et évaluer la quantité recherchée à l'aide d'une technique d'immunoadsorption connue, en particulier par l'adsorption du fibrinogène ou de la fibronectine sur une surface et par la réaction dutit fibrinogène ou de ladite fibronectine avec l'autre constituant de réaction et ensuite avec un anticorps agissant spécifiquement contre la substance devant être évaluée, lequel anticorps peut être marqué; après quoi la quantité dudit anticorps est mesurée selon une technique connue, éventuellement par la réaction avec un anticorps secondaire marqué.
PCT/SE1991/000318 1990-05-03 1991-05-03 PROCEDE POUR EVALUER QUANTITATIVEMENT LA CONCENTRATION DE FIBRINOGENE, DE FIBRONECTINE, D'α2-ANTIPLASMINE OU D'UNE TRANSGLUTAMINASE Ceased WO1991017444A1 (fr)

Applications Claiming Priority (2)

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SE9001582-7 1990-05-03
SE9001582A SE9001582D0 (sv) 1990-05-03 1990-05-03 Saett vid kvantitativ bestaemning av fibrinogen, fibronektin, alfa-2-antiplasmin eller faktor xiii

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Cited By (6)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO2001029090A1 (fr) * 1999-10-20 2001-04-26 Immco Diagnostics Methode de dosage immunologique servant a detecter des anticorps d'une maladie coeliaque
US6703208B1 (en) 1999-10-20 2004-03-09 Immco Diagnostics Immunological assay for detection of antibodies in celiac disease
WO2012110253A3 (fr) * 2011-02-18 2013-02-07 Cavadis B.V. Biomarqueurs exosomaux pour des événements cardiovasculaires
WO2020092531A1 (fr) * 2018-10-30 2020-05-07 The Research Institute At Nationwide Children's Hospital Immunoessai du facteur xiii
CN114736948A (zh) * 2022-06-10 2022-07-12 深圳市帝迈生物技术有限公司 一种α2-抗纤溶酶活性测定试剂盒
CN118010469A (zh) * 2024-04-08 2024-05-10 中国人民解放军军事科学院军事医学研究院 一种纤维蛋白原浓度定量检测稀释液及其制备方法与应用

Families Citing this family (1)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US8900822B2 (en) * 2011-11-21 2014-12-02 Ethicon, Inc. Fibrinogen assay

Citations (1)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US4624927A (en) * 1983-04-15 1986-11-25 The Green Cross Corporation Reagent for determination of blood coagulation factor XIII

Patent Citations (1)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US4624927A (en) * 1983-04-15 1986-11-25 The Green Cross Corporation Reagent for determination of blood coagulation factor XIII

Non-Patent Citations (4)

* Cited by examiner, † Cited by third party
Title
Medline (NLM Database), Accession Number 86243695, Blood 1986 Jul; 68(1):95-101 (M. HADA et al.) "Covalent crosslinking of von Willebrand factor to fibrin". *
Medline (NLM Database), Accession Number 87299006, Biol Chem Hoppe Seyler 1987 Jun; 368(6):669-74 (H. HORMANN et al.) "N-terminal fibronectin 30-kDa fragment mediates the immobilization of soluble fibrin by factor XIIIa-coated polystyrene beads". *
Medline (NLM Database), Accession Number 88273153, J Biol Chem 1988 Jul 25; 263(21):10464-9 (E.L. BARRY et al.) "Factor XIII cross-linking of fibronectin at cellular matrix assembly sites". *
Medline (NLM Database), Accession Number 89051068, Biochim Biophys Acta 1988 Nov 17; 967(2):304-13 (R. PROCYK et al.) "Factor XIII-induced crosslinking in solutions of fibrinogen and fibrinonectin". *

Cited By (9)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO2001029090A1 (fr) * 1999-10-20 2001-04-26 Immco Diagnostics Methode de dosage immunologique servant a detecter des anticorps d'une maladie coeliaque
US6703208B1 (en) 1999-10-20 2004-03-09 Immco Diagnostics Immunological assay for detection of antibodies in celiac disease
WO2012110253A3 (fr) * 2011-02-18 2013-02-07 Cavadis B.V. Biomarqueurs exosomaux pour des événements cardiovasculaires
WO2020092531A1 (fr) * 2018-10-30 2020-05-07 The Research Institute At Nationwide Children's Hospital Immunoessai du facteur xiii
US20210405073A1 (en) * 2018-10-30 2021-12-30 The Research Institute At Nationwide Children's Hospital Factor xiii immunoassay
EP3874267A4 (fr) * 2018-10-30 2022-07-27 The Research Institute at Nationwide Children's Hospital Immunoessai du facteur xiii
US12216130B2 (en) * 2018-10-30 2025-02-04 The Research Institute At Nationwide Children's Hospital Factor XIII immunoassay
CN114736948A (zh) * 2022-06-10 2022-07-12 深圳市帝迈生物技术有限公司 一种α2-抗纤溶酶活性测定试剂盒
CN118010469A (zh) * 2024-04-08 2024-05-10 中国人民解放军军事科学院军事医学研究院 一种纤维蛋白原浓度定量检测稀释液及其制备方法与应用

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JPH05508472A (ja) 1993-11-25
EP0527197A1 (fr) 1993-02-17

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