Orientation of the Carboxy-terminal Regions of Fibrin γ Chain Dimers Determined from the Crosslinked Products Formed in Mixtures of Fibrin, Fragment D, and Factor XIIIa

Kevin R Siebenlist; David A Meh; Joseph S Wall; James F Hainfeld; Michael W Mosesson

doi:10.1055/s-0038-1649890

Thrombosis and Haemostasis, Inhaltsverzeichnis

Thromb Haemost 1995; 74(04): 1113-1119
DOI: 10.1055/s-0038-1649890

Original Article

Coagulation

Schattauer GmbH Stuttgart

Orientation of the Carboxy-terminal Regions of Fibrin γ Chain Dimers Determined from the Crosslinked Products Formed in Mixtures of Fibrin, Fragment D, and Factor XIIIa

Kevin R Siebenlist

¹The University of Wisconsin Medical School Sinai Samaritan Medical Center, Milwaukee, WI, USA

²The Department of Basic Health Sciences, School of Dentistry, Marquette University, Milwaukee, WI, USA

,

David A Meh

¹The University of Wisconsin Medical School Sinai Samaritan Medical Center, Milwaukee, WI, USA

,

Joseph S Wall

³The Brookhaven National Laboratory, Biology Department, Upton, NY, USA

,

James F Hainfeld

³The Brookhaven National Laboratory, Biology Department, Upton, NY, USA

,

Michael W Mosesson

¹The University of Wisconsin Medical School Sinai Samaritan Medical Center, Milwaukee, WI, USA

› Institutsangaben

Abstract

als PDF herunterladen

Summary

There are two schools of thought regarding the orientation of the intermolecular ∈-amino-(γ-glutamyl) lysine isopeptide bonds formed between γ chains in the D domains of assembled fibrin fibers. Some investigators believe that these bonds are oriented parallel to the direction of fiber growth (longitudinally) at the contacting ends of fibrin D domains (‘DD-long’), whereas others believe that these bonds are oriented across the two-stranded fibril, between D domains in opposing strands (‘DD-transverse’). To distinguish between these two possibilities, the structure of crosslinked products formed in mixtures of fibrin, plasmic fragment D, and factor XIIIa were analyzed, based upon this rationale: Complex formation between D fragments and a fibrin template depends upon the non-covalent ‘D:E’ interaction between each fibrin E domain and two D fragments (‘D:fibrin:D’). If carboxy-terminal γ chains in the D:fibrin:D complex become aligned in a DD-long configuration, only crosslinked fragment D dimers (‘D-D’) will result and the fibrin ‘template’ will not become crosslinked to the associated D fragments. If instead, γ chain crosslinks form transversely between the D fragments and fibrin, covalently linked D-fibrin complexes will result.

SDS-PAGE of factor XIIIa crosslinked mixtures of fibrin and fragment D demonstrated products of a size and subunit composition indicating D-fibrin and D-fibrin-D formation. Small amounts of D dimers were also formed at the same levels as were formed in mixtures of fragment D and factor XIIIa alone. Electron microscopic images of D-fibrin-D complexes prepared under physiological buffer conditions demonstrated that the D fragments were associated with the central E domain of the fibrin molecule, but that they could be dissociated from this non-covalent association in 2% acetic acid. These findings indicate that γ chain crosslinks occur transversely in D:fibrin:D complexes and permit the extrapolated conclusion that γ chain crosslinks are also positioned transversely in an assembled fibrin polymer.

PDF (420 kb)

Referenzen

References
1 Kudryck B, Reuterby J, Blombäck B. Adsorption of plasmic fragment D to thrombin modified fibrinogen-sepharose. Thromb Res 1973; 2: 297-304
2 Kudryck B, Collen D, Woods KR, Blombäck B. Evidence for localization of polymerization sites in fibrinogen. J Biol Chem 1974; 249: 3322-3325
3 Kudryck B, Blombäck B, Blombäck M. Fibrinogen Detroit-An abnormal fibrinogen with non-functional NH₂-terminal polymerization domain. Thromb Res 1976; 9: 25-36
4 Blombäck B, Hessel D, Hogg D, Therkildsen L. A two-step fibrinogen-fibrin transition in blood coagulation. Nature 1978; 275: 501-505
5 Budzynski AZ, Olexa SA, Pandya BV. Fibrin polymerization sites in fibrinogen and fibrin fragments. Ann NY Acad Sci 1983; 408: 301-314
6 Pisano JJ, Finlayson JS, Peyton MP. Crosslink in fibrin polymerized by factor XIII: ∈-(γ-glutamyl) lysine. Science 1968; 160: 892-893
7 Matačic S, Loewy AG. The identification of isopeptide crosslinks in insoluble fibrin. Biochem Biophys Res Comm 1968; 30: 356-362
8 McKee PA, Mattock P, Hill R. Subunit structure of human fibrinogen, soluble fibrin, and cross-linked insoluble fibrin. Proc Nat Acad Sci USA 1970; 66: 738-744
9 Folk JE, Finlayson JS. The ∈-(γ-glutamyl) lysine crosslink and the catalytic role of transglutaminases. Adv Prot Chem 1977; 31: 1-133
10 Mosesson MW, Siebenlist KR, Amrani DL, DiOrio JP. Identification of covalently linked trimeric and tetrameric D domains in crosslinked fibrin. Proc Natl Acad Sci USA 1989; 86: 1113-1117
11 Shainoff JR, Urbanic DA, DiBello PM. Immunoelectrophoretic characterizations of the cross-linking of fibrinogen and fibrin by factor XIIIa and tissue transglutaminase. J Biol Chem 1991; 166: 6429-6437
12 Grøn B, Filion-Myklebust C, Bjørnsen S, Haidaris P, Brosstad F. Cross- linked α_sγ_t-chain hybrids in plasma clots studied by 1D- and 2D electrophoresis and western blotting. Thromb Haemost 1993; 70: 438-442
13 Siebenlist KR, Mosesson MW. Factors affecting γ-chain multimer formation in cross-linked fibrin. Biochemistry 1992; 31: 936-941
14 Chen R, Doolittle RF. Identification of the polypeptide chains involved in the cross-linking of fibrin. Proc Nat Acad Sci USA 1969; 63: 420-427
15 Chen R, Doolittle RF. γ-γ cross-linking sites in human and bovine fibrin. Biochemistry 1971; 10: 4486-4491
16 Doolittle RF, Chen R, Lau F. Hybrid fibrin: proof of the intermolecular nature of γ-γ crosslinking units. Biochem Biophys Res Comm 1971; 44: 94-100
17 Doolittle RF. Structural details of fibrin stabilization: implications for fibrinogen structure and initial fibrin formation. Thromb Diath Haemorrh 1973; 54 suppl 155-165
18 Fowler WR, Hantgan R, Hermans J, Erickson H. Structure of the fibrin protofibril. Proc Nat Acad. Sci USA 1981; 78: 4872-4876
19 Fowler WE, Erickson HP, Hantgan RR, McDonagh J, Hermans J. Cross- linked fibrinogen dimers demonstrate a feature of the molecular packing in fibrin fibers. Science 1981; 211: 287-289
20 Erickson HP, Fowler WE. Electron microscopy of fibrinogen, its plasmic fragments and small polymers. Ann NY Acad Sci 1983; 408: 146-163
21 Weisel JW, Francis CW, Nagaswami C, Marder VJ. Determination of the topology of factor XIIIa-induced fibrin γ-chain cross-links by electron microscopy of ligated fragments. J Biol Chem 1993; 268: 26618-26624
22 Selmayr E, Thiel W, Mϋller-Berghaus G. Crosslinking of fibrinogen to immobilized des AA-fibrin. Thromb Res 1985; 39: 459-465
23 Selmayr E, Bachmann L, Deffner M, Mϋller-Berghaus G. Chromatography and electron microscopy of cross-linked fibrin polymers-a new model describing the cross-linking at the DD-trans contact of the fibrin molecules. Biopolymers 1988 27: 1733-1748
24 Mosesson MW, Siebenlist KR, Hainfeld JF, Wall JS. The structure of factor Xllla-crosslinked fibrinogen fibrils: evidence for double strands interlinked transversely through covalent bonds between carboxy-terminal regions of γchains. J Sir Biol. submitted
25 Kazal LA, Amsel S, Miller OP, Tocantins LM. The preparation and some properties of fibrinogen precipitated from human plasma by glycine. Proc Soc Exp Biol Med 1963; 113: 989-994
26 Mosesson MW, Sherry S. The preparation and properties of human fibrinogen of relatively high solubility. Biochemistry 1966; 5: 2829-2835
27 Finlayson JS, Mosesson MW. Heterogeneity of human fibrinogen. Biochemistry 1963; 2: 42-46
28 Mosesson MW, Finlayson JS, Umfleet RA. Human fibrinogen heterogeneities III. Identification of γchain variants J Biol Chem 1972; 247: 5223-5227
29 Galanakis DK, Mosesson MW, Stathakis NE. Human fibrinogen heterogeneities: distribution and charge characteristics of chains of Aケ origin. J Lab Clin Med 1978; 92: 376-386
30 McFarlane AS. In vivo behavior of¹³¹l fibrinogen. J Clin Inv 1963; 42: 346-361
31 Belitser VA, Varetskaja TV, Malneva GV. Fibrinogen-fibrin interaction. Biochim Biophys Acta 1968; 154: 367-375
32 Mosesson MW, Finlayson JS. Subfractions of human fibrinogen-preparation and analysis. J Lab Clin Med 1963; 62: 663-674
33 Lorand L, Gotoh T. Fibrinoligase. The fibrin stabilizing factor Methods Enzymol 1970; 19: 770-782
34 Liewy AG, Dunathan K, Kriel R, Wolfinger HL, Fibrinase I. Purification of substrate and enzyme. J Biol Chem 1961; 236: 2625-2633
35 Kanaide H, Shainoff JR. Cross-linking of fibrinogen and fibrin by fibrin-stabilizing factor (factor XIIIa). J Lab Clin Med 1975; 85: 574-597
36 Robbins KC, Summaria L. Plasminogen and plasmin. Methods Enzymol 1976; 45: 257-273
37 Robbins KC, Summaria L. Human plasminogen and plasmin. Methods Enzymol 1970; 19: 184-199
38 Mosesson MW, Finlayson JS, Galanakis DK. The essential covalent structure of human fibrinogen evinced by analysis of derivatives formed during plasmic hydrolysis. J Biol Chem 1973; 248: 7913-7929
39 Marder VJ, Budzynski AZ, James HL. High molecular weight derivatives of human fibrinogen produced by plasmin: (III) Their Nil,-terminal amino acids and comparison with the NH,-terminal disulfide knot. J Biol Chem 1972; 244: 2120-2124
40 Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970; 227: 680-685
41 Mosesson MW, DiOrio JP, Siebenlist KR, Wall JS, Hainfeld JF. Evidence for a second type of fibril branch point in fibrin polymer networks, the trimolecular branch junction. Blood 1993; 82: 1517-1521
42 Mosesson MW, Hainfeld JF, Haschemeyer RH, Wall J. Identification and mass analysis of human fibrinogen molecules and their domains by scanning transmission electron microscopy. J Mol Biol 1981; 153: 695-718
43 Hainfeld JF, Wall JS, Desmond EJ. A small computer system for micrograph analysis. Ultramicroscopy 1982; 8: 263-270
44 Wall JS, Hainfeld JF. Mass mapping with the scanning transmission electron microscope. Ann Rev Biophys Chem 1986; 15: 355-376
45 Wall JS. Biological scanning transmission electron microscopy. In: Introduction to Analytical Electron Microscopy. Hren JJ, Goldstein JI, Joy DC. eds New York, NY: Plenum: 1979. pp 333-342
46 Wall JS. Limits on visibility of single heavy atoms in the scanning transmission electron microscope-anexperimental study. Chem Scripta 1979; 15: 271-278
47 Weisel JW, Stauffacher CV, Bullitt E, Cohen C. A model for fibrinogen: domains and sequence. Science 1985; 230: 1388-1391