Characterization of a Monoclonal Antibody Directed Against the Carboxyl-Terminus of Human Factor XIII

Yeqing Song; Stephen M Taubenfeld; DeQuan Sheng; Gary R Matsueda

doi:10.1055/s-0038-1642385

Thrombosis and Haemostasis, Table of Contents

Thromb Haemost 1994; 71(01): 062-067
DOI: 10.1055/s-0038-1642385

Review Article

Schattauer GmbH Stuttgart

Characterization of a Monoclonal Antibody Directed Against the Carboxyl-Terminus of Human Factor XIII

An Epitope Exposed Upon Denaturation and Conserved Across Species Lines

Yeqing Song

The Department of Molecular Biology, Princeton University and Macromolecular Biochemistry, Bristol-Myers Squibb Pharmaceutical Research Institute, Princeton, NJ, USA

,

Stephen M Taubenfeld

The Department of Molecular Biology, Princeton University and Macromolecular Biochemistry, Bristol-Myers Squibb Pharmaceutical Research Institute, Princeton, NJ, USA

,

DeQuan Sheng

The Department of Molecular Biology, Princeton University and Macromolecular Biochemistry, Bristol-Myers Squibb Pharmaceutical Research Institute, Princeton, NJ, USA

,

Gary R Matsueda

The Department of Molecular Biology, Princeton University and Macromolecular Biochemistry, Bristol-Myers Squibb Pharmaceutical Research Institute, Princeton, NJ, USA

› Author Affiliations

Abstract

PDF Download

Summary

By deriving an anti-peptide monoclonal antibody, mAb 7A4, we characterized the relatively unstudied carboxyl-terminal end of the α-chain of human factor XIII, the plasma transglutaminase. MAb 7A4 was directed against the last eight amino acids (Gln-Ile-Gln-Arg-Arg-Pro-Ser-Met) and bound with a dissociation constant of 3.4 × 10⁻⁸ M. In a solid assay format, mAb 7A4 bound equally well to factor XIII obtained from human plasma, platelets or placenta. However, in a solution-phase assay format, the epitope was largely unavailable but could be readily exposed by heat denaturation. Tmmunoblotting showed that this epitope is conserved among all species of plasma factor XIII tested except rabbit suggesting that the carboxyl-terminus might be an important structural element. Other competitive binding experiments with synthetic peptides as inhibitors pointed toward the final carboxyl-terminal amino acid, Met-731, as an immunochemically important determinant. This was used advantageously to confirm the finding that the caiboxyl-leiminal Mel-731 is largely absent from placental factor XIII (1) as compared to platelet or plasma factor XIII.

PDF (277 kb)

References

References
1 Takahashi N, Takahashi Y, Putnam FW. Primary structure of blood coagulation factor XIII a (fibrinoligase, transglutaminase) from human placenta. Proc Natl Acad Sci USA 1986; 83: 8019-23
2 Greenberg CS, Birckbichler PJ, Rice RH. Transglutaminases: multifunctional cross-linking enzymes that stabilize tissues. FASEB J 1991; 5: 3071-7
3 Chen R, Doolittle RF. Isolation, characterization, and location of a donor-acceptor unit from cross-linked fibrin. Proc Natl Acad Sci USA 1970; 66: 472-9
4 Pisano JJ, Bronzert TJ, Peyton MP, Finlayson JS. ε-(γ-Glutamyl)ly-sine cross-links: determination in fibrin from normal and factor XIII-deficient individuals. Ann NY Acad Sci USA 1972; 87: 1114-8
5 Lorand L, Jacobsen A. Accelerated lysis of blood clots. Nature 1962; 195: 911-2
6 Folk JE, Chung SI. Transglutaminases. Methods Enzymol 1985; 113: 358-75
7 Pisano JJ, Finlayson JS, Peyton MP. Cross-link in fibrin polymerized by factor XIII: ε-(γ-glutamyl)lysine. Science 1968; 160: 892-3
8 Mosher DF. Cross-linking of plasma and cellular fibronectin by plasma transglutaminase. Ann NY Acad Sci 1978; 312: 38-42
9 Sakata Y, Aoki N. Cross-linking of a2-plasmin inhibitor to fibrin-stabilizing factor. J Clin Invest 1980; 65: 290-7
10 Sakata Y, Aoki N. Significance of cross-linking of a2-plasmin inhibitor to fibrin in inhibition of fibrinolysis and in hemostasis. J Clin Invest 1982; 69: 536-42
11 Bale MD, Westrick LG, Mosher DF. Incorporation of thrombospondin into fibrin clots. J Biol Chem 1985; 260: 7502-8
12 Gorman JJ, Folk JE. Structural features of glutamine substrates for human plasma factor XIIIa. J Biol Chem 1980; 255: 419-27
13 Schwartz ML, Pizzo SV, Hill RL, Mc Kee PA. Human factor XIII from plasma and platelets. J Biol Chem 1973; 248: 1395-1407
14 Lopaciuk S, Lovette KM, Mc Donagh J, Chuang HY K, Mc Donagh RP. Subcellular distribution of fibrinogen and factor XIII in human blood platelets. Thromb Res 1976; 8: 453-65
15 Duckert F. Documentation of the plasma factor XIII deficiency in man. Ann NY Acad Sci 1972; 202: 190-9
16 Bohn H. Comparative studies on the fibrin-stabilizing factors from human plasma, platelets and placentas. Ann NY Acad Sci 1972; 202: 256-72
17 Ichinose A, Hendrickson LE, Fujikawa K, Davie EW. Amino acid sequence of the a subunit of human factor XIII. Biochemistry 1986; 25: 6900-6
18 Tagaki T, Doolittle RF. Amino acid sequence studies on factor XIII and the peptide released during its activation by thrombin. Biochemistry 1974; 13: 750-6
19 Bishop PD, Lasser GW, Teller DC, Lc Trong I, Stenkamp RE. Crystallization and preliminary electron density map for human recombinant factor XIII from Saccharomyces cerevisiae. Second International Conference on Factor XIII. Marburg, Germany: July 9-10 1991: 102-5
20 Hilgenfeld R, Liesum A, Mausil D, Metzner HJ, Karges HE. Towards a high-resolution crystal structure of the factor XIII α-chain dimer. Second International Conference on Factor XIII. Marburg, Germany: July 9-10 1991: 106-9
21 Greenberg CS, Enghild JJ, Mary A, Dobson JV, Achyuthan KE. Isolation of a fibrin-binding fragment from blood coagulation factor XIII capable of cross-linking fibrin(ogen). Biochem J 1988; 256: 1013-9
22 Stewart JM, Young JD. Solid-Phase Peptide Synthesis. 2nd. edn Pierce Chemical Co.; Rockford, IL: 1984
23 Harlow E, Lane D. Antibodies: A Laboratory Manual. Cold Spring Harbor Laboratory. Cold Spring Harbor, NY: 1988
24 Bernatowicz MS, Matsueda GR. Preparation of peptide-protein immunogens using N-succinimidyl bromoacetate as a heterobifunctional crosslinking reagent. Anal Biochem 1986; 155: 95-102
25 Friguct B, Chaffotte AF, Djavadi-Ohaniance L, Goldberg ME. Measurements of the true affinity constant in solution of antigen-antibody complexes by enzyme-linked immunosorbent assay. J Immunol Methods 1985; 77: 305-19
26 Lukacova D, Matsueda GR, Haber E, Reed GL. Inhibition of factor XIII activation by an anti-peptide monoclonal antibody. Biochemistry 1991; 30: 10164-70
27 Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970; 227: 680-5
28 Towbin H, Staehelin T, Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci USA 1979; 76: 4350-4
29 Kyhse-Anderson J. Electroblotting of multiple gels: a simple apparatus without buffer tank for rapid transfer of proteins from polyacrylamide to nitrocellulose. J Biochem and Biophys Meth 1984; 10: 203-9
30 Godal HC. An inhibitor to fibrin stabilizing factor (FSF, factor XIII). Scand J Haemat 1970; 7: 43-8
31 Mc Donagh J, Waggoner WG, Hamilton EG, Hindenach B, Mc Donagh RP. Affinity chromatography of human plasma and platelet factor XIII on organomercurial agarose. Biochim Biophys Acta 1976; 445: 345-57
32 Lopaciuk S, Bykowska K, Mc Donagh JM, Mc Donagh RP, Yount WJ, Fuller CR, Cooperstein L, Gray A, Lorand L. Differences between type I autoimmune inhibitors of fibrin stabilization in two patients with severe hemorrhagic disorder. J Clin Invest 1978; 61: 1196-202
33 Lorand L, Velasco PT, Rinne JR, Amare M, Miller LK, Zucker ML. Autoimmune antibody (IgG Kansas) against the fibrin stabilizing factor (factor XIII) system. Proc Natl Acad Sci USA 1988; 85: 232-6
34 Fukue H, Anderson K, Mc Phedran P, Clyne L, Me Donagh J. A unique factor XIII inhibitor to a fibrin-binding site on factor XIII A. Blood 1992; 79: 65-74
35 Lukacova D, Reed GL. Single step purification of platelet factor XIII using an immobilized factor XIII a-subunit monoclonal antibody. Thromb Haemost 1993; 69: 397-400