Thrombosis and Haemostasis, Inhaltsverzeichnis

Thromb Haemost 1993; 69(04): 351-360
DOI: 10.1055/s-0038-1651611

Original Article

Coagulation

Schattauer GmbH Stuttgart

Diversity of Primary Structures of the Carboxy-terminal Regions of Mammalian Fibrinogen Aα-Chains

Characterization of the Partial Nucleotide and Deduced Amino Acid Sequences in Five Mammalian Species; Rhesus Monkey, Pig, Dog, Mouse and Syrian Hamster

Masahiro Murakawa

The First Department of Internal Medicine, Faculty of Medicine, Kyushu University, Fukuoka, Japan

,

Takashi Okamura

The First Department of Internal Medicine, Faculty of Medicine, Kyushu University, Fukuoka, Japan

,

Takumi Kamura

The First Department of Internal Medicine, Faculty of Medicine, Kyushu University, Fukuoka, Japan

,

Tsunefumi Shibuya

The First Department of Internal Medicine, Faculty of Medicine, Kyushu University, Fukuoka, Japan

,

Mine Harada

The First Department of Internal Medicine, Faculty of Medicine, Kyushu University, Fukuoka, Japan

,

Yoshiyuki Niho

The First Department of Internal Medicine, Faculty of Medicine, Kyushu University, Fukuoka, Japan

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Summary

The partial amino acid sequences of fibrinogen Aα-chains from five mammalian species have been inferred by means of the polymerase chain reaction (PCR). From the genomic DNA of the rhesus monkey, pig, dog, mouse and Syrian hamster, the DNA fragments coding for α-C domains in the Aα-chains were amplified and sequenced. In all species examined, four cysteine residues were always conserved at the homologous positions. The carboxy- and amino-terminal portions of the α-C domains showed a considerable homology among the species. However, the sizes of the middle portions, which corresponded to the internal repeat structures, showed an apparent variability because of several insertions and/or deletions. In the rhesus monkey, pig, mouse and Syrian hamster, 13 amino acid tandem repeats fundamentally similar to those in humans and the rat were identified. In the dog, however, tandem repeats were found to consist of 18 amino acids, suggesting an independent multiplication of the canine repeats. The sites of the α-chain cross-linking acceptor and α₂-plasmin inhibitor cross-linking donor were not always evolutionally conserved. The arginyl-glycyl-aspartic acid (RGD) sequence was not found in the amplified region of either the rhesus monkey or the pig. In the canine α-C domain, two RGD sequences were identified at the homologous positions to both rat and human RGD S. In the Syrian hamster, a single RGD sequence was found at the same position to that of the rat. Triplication of the RGD sequences was seen in the murine fibrinogen α-C domain around the homologous site to the rat RGDS sequence. These findings are of some interest from the point of view of structure-function and evolutionary relationships in the mammalian fibrinogen Aα-chains.

References
1 Archer RK. Blood coagulation in animals other than man and animal models of human coagulation disorders. In: Recent Advances in Blood Coagulation 3. Poller L. (ed). London: Churchill Livingstone; 1981: 211-226
2 Doolittle RF. The evolution of vertebrate fibrinogen. Fed Proc 1976; 35: 2145-2149
3 Cierniewski CS, Krajewski T, Janiak A. Homology of polymerization domains in vertebrate fibrinogens. Thromb Res 1980; 19: 599-607
4 Doolittle RF. The structure and evolution of vertebrate fibrinogen. Ann NY Acad Sci 1983; 408: 13-27
5 Doolittle RF. Structural aspects of the fibrinogen to fibrin conversion. Adv Protein Chem 1973; 27: 1-109
6 Doolittle RF. The evolution of vertebrate fibrinogen. In: Protides of the Biological Fluids. Peeters H. (ed). Oxford: Pergamon Press; 1980: 41-46
7 Henschen A, Lottspeich F, Töpfer-Petersen E, Kehl M, Timple R. Fibrinogen evolution: Intra- and inter-species comparisons. In: Protides of the Biological Fluids. Peeters H. (ed). Oxford: Pergamon Press; 1980: 47-50
8 Doolittle RF, Blombäck B. Amino-acid sequence investigations of fibrinopep-tides from various mammals: Evolutionary implications. Nature 1964; 202: 147-152
9 Blombäk B. Selectional trends in the structure of fibrinogen of different species. In: Biochemical Evolution and the Origin of Life.Molecular Evolution II. Schoffeniels E. (ed). North-Holland, Amsterdam: 1971: l12-129
10 Henschen A, Lottspeich F, Kehl M, Southern C. Covalent structure of fibrinogen. Ann NY Acad Sci 1983; 408: 28-43
11 Gårdlund B, Hessel B, Marguerie G, Murano G, Blombäck B. Primary structure of human fibrinogen. Characterization of disulfide-containing cyanogen-bromide fragments. Eur J Biochem 1977; 77: 595-610
12 Henschen A, Lottspeich F, Hessel B. Amino acid sequence of human fibrin. Preliminary note on the completion of the intermediate part of the α-chain sequence. Hoppe-Seyler’s Z Physiol Chem 1979; 360: 1951-1956
13 Watt KWK, Cottrell BA, Strong DD, Doolittle RF. Amino acid sequence studies on the a chain of human fibrinogen.Overlapping sequences providing the complete sequence. Biochemistry 1979; 18: 5410-5416
14 Doolittle RF, Watt KWK, Cottrell BA, Strong DD, Riley M. The amino acid sequence of the α-chain of human fibrinogen. Nature 1979; 280: 464-468
15 Rixon MW, Chan WY, Davie EW, Chung DW. Characterization of a complementary deoxyribonucleic acid coding for the α chain of human fibrinogen. Biochemistry 1983; 22: 3237-3244
16 Kant JA, Lord ST, Crabtree GR. Partial mRNA sequences for human Aα, Bβ, and γ fibrinogen chains: Evolutionary and functional implications. Proc Natl Acad Sci USA 1983; 80: 3953-3957
17 Imam AMA, Eaton MAW, Williamson R, Humphries S. Isolation and characterization of cDNA clones for the Aα- and γ-chains of human fibrinogen. Nucl Acid Res 1983; 11: 7427-7434
18 Crabtree GR, Kant JA. Molecular cloning of cDNA for the α, β and γ chains of rat fibrinogen.A family of coordinately regulated genes. J Biol Chem 1981; 256: 9718-9723
19 Crabtree GR, Comeau CM, Fowlkes DM, Fornace AJ, Malley JD, Kant JA. Evolution and structure of the fibrinogen genes.Random insertion of introns or selective loss?. J Mol Biol 1985; 185: 1-19
20 Chung DW, Rixon MW, Davie EW. The biosynthesis of fibrinogen and the cloning of its cDNA. In: Proteins in Biology and Medicine. Bradshaw RA, Hill RL, Tang J, Liang CC, Tsao TC, Tsou CL. (eds). Academic Press; New York: 1982: 309-328
21 Krieglstein K, Henschen A. The primary structure of bovine fibrinogen and its functional implications. Thromb Haemost 1989; 62: 70 (Abstr)
22 Kant JA, Fornace AJ, Saxe D, Simon Ml, McBride OW, Crabtree GR. Evolution and organization of the fibrinogen locus on chromosome 4. Gene duplication accompanied by transposition and inversion. Proc Natl Acad Sci USA 1985; 82: 2344-2348
23 Henry I, Uzan G, Weil D, Nicolas H, Kaplan JC, Marguerie C, Kahn A, Junien C. The genes coding for Aα-, Bβ-, and γ-chains of fibrinogen map to 4q2. Am J Hum Genet 1984; 36: 760-768
24 Marino MW, Fuller GM, Elder FFB. Chromosomal localization of human and rat Aα, Bβ, and γ fibrinogen genes by in situ hybridization. Cytogenet Cell Genet 1986; 42: 36-41
25 Kant JA, Crabtree GR. The rat fibrinogen genes.Linkage of the Aα and γ chain genes. J Biol Chem 1983; 258: 4666-4667
26 Medved’ LV, Gorkun OV, Manyakov VF, Belitser VA. The role of fibrinogen α-C domains in the fibrin assembly process. FEBS Lett 1985; 181: 109-112
27 Shen LL, McDonagh RP, McDonagh J, Hermans J. Early events in the plasmin digestion of fibrinogen and fibrin. J Biol Chem 1977; 252: 6184-6189
28 McKee PA, Mattock P, Hill RL. Subunit Structure of human fibrinogen, soluble fibrin, and cross-linked insoluble fibrin. Proc Natl Acad Sci USA 1970; 66: 738-744
29 Marder VJ, Shulman NR, Carroll WR. High molecular weight derivatives of human fibrinogen produced by plasmin.I. Physicochemical and immunological characterization. J Biol Chem 1969; 244: 2111-2119
30 Sherman LA, Mosesson MW, Sherry S. Isolation and characterization of the clottable low molecular weight fibrinogen derived by limited plasmin hydrolysis of human fraction I-4. Biochemistry 1969; 8: 1515-1523
31 Hawiger J, Timmons S, Kloczewiak M, Strong DD, Doolittle RF. ϒ and β chains of human fibrinogen possess sites reactive with human platelet receptors. Proc Natl Acad Sci USA 1982; 79: 2068-2071
32 Hawiger J, Kloczewiak M, Bednarek MA, Timmons S. Platelet receptor recognition domains on the β chain of human fibrinogen. Structure-function analysis. Biochemistry 1989; 28: 2909-2914
33 Plow EF, Pierschbacher MD, Ruoslahti E, Marguerie GA, Ginsberg MH. The effect of Arg-Gly-Asp-containing peptides on fibrinogen and von Willebrand factor binding to platelets. Proc Natl Acad Sci USA 1985; 82: 8057-8061
34 Gartner TK, Bennet JS. The tetrapeptide analogue of the cell attachment site of fibronectin inhibits platelet aggregation and fibrinogen binding to activated platelets. J Biol Chem 1985; 260: 11891-11894
35 Peerschke EIB, Galanakis DK. The synthetic RGDS peptide inhibits the binding of fibrinogen lacking intact β chain carboxyterminal sequences to human bood platelets. Blood 1987; 69: 950-952
36 Ruoslahti E, Pierschbacher MD. New Perspectives in Cell Adhesion: RGD and integrins. Science 1987; 238: 491-497
37 Wang YZ, Patterson J, Gray JE, Yu C, Cottrell BA, Shimizu A, Graham D, Riley M, Doolittle FR. Complete sequence of the lamprey fibrinogen β chain. Biochemistry 1989; 28: 9801-9806
38 Weissbach L, Grieninger G. Bipartite mRNA for chicken β-fibrinogen potentially encodes an amino acid sequence homologous to β- and ϒ-fibrinogens. Proc Natl Acad Sci USA 1990; 87: 5198-5202
39 Saiki RK, Gelfand DH, Stoffel S, Scharf SJ, Higuchi R, Horn GT, Mullis KB, Erlich HA. Primer-directed enzymatic amplification of DNA with a thermostable DNA polymerase. Science 1988; 239: 487-491
40 Blin N, Stafford DW. Isolation of high molecular weight DNA. Nucleic Acid Res 1976; 3: 2303
41 Maniatis T, Fritsch EF, Sambrook J. Molecular Cloning. A Laboratory Manual. Cold Spring Harbor Laboratory Press; New York: 1982: 1-545
42 Innis MA, Gelfand DH, Sninski JJ, White TJ. PCR Protocols. A Guide to Methods and Applications. Academic Press; San Diego, CA: 1990: 1-459
43 Sanger F, Nicklen S, Coulson AR. DNA sequencing with chain-terminating inhibitors. Proc Natl Acad Sci USA 1977; 74: 5463-5467
44 Maizel JV, Lenk RP. Enhanced graphic matrix analysis of nucleic acid and protein sequences. Proc Natl Acad Sci USA 1981; 78: 7665-7669
45 Cottrell BA, Strong DD, Watt KWK, Doolittle RF. Amino acid sequence studies on the β chain of human fibrinogen. Exact localization of cross-linking acceptor sites. Biochemistry 1979; 18: 5405-10
46 Corcoran DH, Ferguson EW, Fretto LJ, McKee PA. Localization of a cross-link donor site in the β-chain of human fibrinogen. Thromb Res 1980; 19: 883-888
47 Kimura S, Aoki N. Cross-linking site in fibrinogen for β₂-plasminogen inhibitor. J Biol Chem 1986; 261: 15591-15595
48 De Serrano VS, Urano T, Gaffney PJ, Castellino FJ. Influence of various structural domains of fibrinogen and fibrin on the potentiation of plasminogen activation by recombinant tissue plasminogen activator. J Protein Chem 1989; 8: 61-77
49 Nieuwenhuizen W, Verheijen JH, Vermond A, Chang GTG. Plasminogen activation by tissue activator is accelerated in the presence of fibrin(ogen) cyanogen bromide fragment FCB-2. Biochim Biophys Acta 1983; 755: 531-533
50 Voskuilen M, Vermond A, Veeneman GH, Van Boom JH, Klasen EA, Zegers ND, Nieuwenhiuzen W. Fibrinogen lysine residue Aβ157 plays a crucial role in the fibrin-induced acceleration of plasminogen activation, catalyzed by tissue-type plasminogen activator. J Biol Chem 1987; 262: 5944-5946
51 Bosna PJ, Pijken DC, Nieuwenhuizen W. Binding of tissue-type plasminogen activator to fibrinogen fragments. Eur J Biochem 1988; 172: 399-404
52 Schielen WJG, Voskuilen M, Tesser GI, Nieuwenhuizen W. The sequence Aβ-(148-160) in fibrin, but not in fibrinogen, is accessible to monoclonal antibodies. Proc Natl Acad Sci USA 1989; 86: 8951-8954
53 Schielen WJG, Adams HPHM, Voskuilen M, Tesser GI, Nieuwenhuizen W. The sequence Aβ(154-159) of fibrinogen is capable of accelerating the t-PA catalysed activation of plasminogen. Blood Coagulation Fibrinolysis 1991; 2: 465-470
54 Henschen A. Disulfide bridges in the middle part of human fibrinogen. Hoppe-Seyler’s Z Physiol Chem 1978; 359: 1757-1770
55 Doolittle RF, Cottrell BA, Strong D, Watt KWK. Sequence of amino acids comprising the single intra-chain disulfide loop in the β-chain of human fibrinogen. Biochem Biophys Res Commun 1978; 84: 495-500
56 Pierschbacher MD, Ruoslahti E. Variants of the cell recognition site of fibronectin that retain attachment-promoting activity. Proc Natl Acad Sci USA 1984; 81: 5985-5988
57 Plow EF, Pierchbacher MD, Ruoslahti E, Marguerie G, Ginsberg MH. Arginyl-glycyl-aspartic acid sequences and fibrinogen binding to platelets. Blood 1987; 70: 110-115
58 Andrieux A, Hudry-Clergeon C, Ryckewaert JJ, Chapel A, Ginsberg MH, Plow EF, Marguerie G. Amino acid sequences in fibrinogen mediating its interaction with its platelet receptor, GPIIbIIIa. J Biol Chem 1989; 264: 9258-9265
59 Niewiarowski S, Budzynski AZ, Lipinski B. Significance of the intact polypeptide chains of human fibrinogen in ADP-induced platelet aggregation. Blood 1977; 49: 635-644
60 Amrani DL, Newman PJ, Meh D, Mosesson MW. The role of fibrinogen Aβ chains in ADP-induced platelet aggregation in the presence of fibrinogen molecules containing ϒ’ chains. Blood 1988; 72: 919-924