Primitive Coagulation Systems and their Message to Modern Biology

Sadaaki Iwanaga

doi:10.1055/s-0038-1646158

Thrombosis and Haemostasis, Table of Contents

Thromb Haemost 1993; 70(01): 048-055
DOI: 10.1055/s-0038-1646158

Plenary Lecture

Schattauer GmbH Stuttgart

Primitive Coagulation Systems and their Message to Modern Biology

Sadaaki Iwanaga

Department of Biology, Faculty of Science, Kyushu University, Fukuoka 812, JAPAN

› Author Affiliations

Abstract

PDF Download

PDF (1561 kb)

References

References
1 Marcus A, Zucker M. The Physiology of Blood Platelets: Recent Biochemical, Morphologic and Clinical Research. 1965. Grune & Stratton, Inc; New York and London:
2 Jackson CM, Nemerson Y. Blood Coagulation. Annu Rev Biochem 1980; 49: 765-811
3 Mann KG, Jenny RJ, Krishnaswamy S. Cofactor proteins in the assembly and expression of blood clotting enzyme complexes. 1988; Annu Rev Biochem 57: 915-956
4 Furie B, Furie BC. The molecular basis of blood coagulation. 1988; Cell 53: 508-518
5 Davie EW, Fujikawa K, Kisiel W. The coagulation cascade: initiation, maintenance and regulation. 1991; Biochemistry 30: 10363-10370
6 Heilbrunn LV. The evolution of the haemostatic mechanism. In: Functions of the Blood Macfarlane RG, Robb-Smith ATH. (eds). Academic Press; New York and London: 1961
7 Macfarlane RG. The Haemostatic Mechanism in Man and Other Animals.. Symp Zool Soc Lond. Academic Press. New York and London: 1970 27. 283-301
8 Belamarich FA. Hemostasis in animals other than mammals: The role of cells.. In: Progress in Hemostasis and Thrombosis. Spaet TH. (ed) Grune & Stratton; New York and San Francisco: 1976. pp. 191-209
9 Archer PK. Blood coagulation in animals other than man and animal models of human coagulation disorders. In: Recent Advances in Blood Coagulation. Poller L. (ed). Churchill Livingstone; Edinburgh & London: 1981. pp. 211-226
10 Ravindranath MH. Hemocytes in hemolymph coagulation of arthropods. Biol. Rev. 1980; 55: 139-170
11 Levin J, Bang FB. The role of endotoxin in the extracellular coagulation of Limulus blood.. Bull. Johns Hopkins Hosp 1964; 115: 265-274
12 Söderhäll k, Cerenius L. Crustacean immunity. Annu Rev Fish Dis 1992; 1: 3-23
13 Mürer EH, Levin J, Holm R. Isolation and studies of the granules of the amebocytes of Limulus polyphemus, the horseshoe crab. J Cell Physiol 1975; 86: 533-542
14 Doolittle RF, Riley M. The amino-terminal sequence of lobster fibrinogen reveals common ancestry with vitellogenins. Biochem Bio-phys Res Commun 1990; 167: 16-19
15 Fuller GM, Doolittle RF. Studies of invertebrate fibrinogen II. Transformation of lobster fibrinogen into fibrin. Biochemistry 1971; 10: 1311-1315
16 Iwanaga S, Morita T, Miyata T, Nakamura T, Aketagawa J. The hemolymph coagulation system in invertebrate animals. J Protein Chem 1986; 5: 225-268
17 Armstrong PB. Cellular and humoral immunity in the horseshoe crab, Limulus polyphemus. In: Immunology of Insects and Other Arthropods. Gupta AP. (ed). CRC Press; Boca Raton: 1991. pp. 3-17
18 Ornberg RL, Reese TS. Beginning of exocytosis captured by rapid-freezing of Limulus amebocytes. J Cell Biol 1981; 90: 40-54
19 Armstrong PB, Rickles FR. Endotoxin-induced degranulation of the Limulus amebocyte. Exp Cell Res 1982; 140: 15-24
20 Toh Y, Mizutani A, Tokunaga F, Muta T, Iwanaga S. Structure of hemocytes of the Japanese horseshoe crab Tachypleus tridentatus: Fine structure, morphological changes during coagulation and localization of clotting factors and antimicrobial substances. Cell Tissue Res 1991; 266: 137-147
21 Miyata T, Hiranaga M, Umezu M, Iwanaga S. Amino acid sequence of the coagulogen from Limulus polyphemus hemocytes. J Biol Chem 1984; 259: 8924-8933
22 Miyata T, Matsumoto H, Hattori M, Sakaki Y, Iwanaga S. Two types of coagulogen mRNAs found in horseshoe crab (Tachypleus tridentatus) hemocytes: Molecular cloning and nucleotide sequences. J Biochem (Tokyo) 1986; 100: 213-220
23 Cheng SM, Suzuki A, Zon G, Liu TY. Characterization of a complementary deoxyribonucleic acid for the coagulogen of Limulus polyphemus. Biochim Biophys Acta 1986; 868: 1-8
24 Muta T, Hashimoto R, Miyata T, Nishimura H, Toh Y, Iwanaga S. Proclotting enzyme from horseshoe crab hemocytes: cDNA cloning, disulfide locations, and subcellular localization. J Biol Chem 1990; 265: 22426-22433
25 Chasan R, Anderson KV. The role of easter, an apparent serine protease, in organizing the dorsal-ventral pattern of the Drosophila embryo. Cell 1989; 56: 391-400
26 Nakamura T, Horiuchi T, Morita T, Iwanaga S. Purification and properties of intracellular clotting factor, factor B, from horseshoe crab (Tachypleus tridentatus) hemocytes. J Biochem (Tokyo) 1986; 99: 847-857
27 Tokunaga F, Miyata T, Nakamura T, Morita T, Kuma K, Miyata T, Iwanaga S. Lipopolysaccharide-sensitive serine-protease zymogen (factor C) of horseshoe crab hemocytes: Identification and alignment of proteolytic fragment produced during the activation show that it is a novel type of serine protease. Eur J Biochem 1987; 167: 405-416
28 Nakamura T, Tokunaga F, Morita T, Iwanaga S, Kusumoto S, Shiba T, Kobayashi T, Inoue K. Intracellular serine-protease zymogen, factor C from horseshoe crab hemocytes: Its activation by synthetic lipid A analogues and acidic phospholipids. Eur J Biochem 1988; 176: 89-94
29 Nakamura T, Tokunaga F, Morita T, Iwanaga S. Interaction between lipopolysaccharide and intracellular serine protease zymogen, factor Cfrom horseshoe crab (Tachypleus tridentatus) hemocytes. J Biochem (Tokyo) 1988; 103: 370-374
30 Muta T, Miyata T, Misumi Y, Tokunaga F, Nakamura T, Toh Y, Ikehara Y, Iwanaga S. Limulus factor C: An endotoxin sensitive serine protease zymogen with a mosaic structure of complement-like, epidermal growth factor-like, and lectin-like domains. J Biol Chem 1991; 266: 6554-6561
31 Tokunaga F, Nakajima H, Iwanaga S. Purification and characterization of lipopolysaccharide-sensitive serine protease zymogen (factor C) isolated from Limulus polyphemus hemocytes: A newly identified intracellular zymogen activated by α-chymotrypsin, not by trypsin.. J Biochem (Tokyo) 1991; 109: 150-157
32 Morita T, Tanaka S, Nakamura T, Iwanaga S. A new (1, 3)-β-D-glu-can- mediated coagulation pathway found in Limulus amebocytes.. FEBS Lett 1981; 129: 318-321
33 Kakinuma A, Asano T, Torii H, Sugino Y. Gelation of Limulus amebocyte lysate by an antitumor (1, 3)-β-D-glucan. Biochem Biophys Res Commun 1981; 101: 433-439
34 Doolittle RF. Fibrinogen and fibrin. Annu Rev Biochem 1984; 53: 195-229
35 Blomback B, Banerjee D, Carlsson K, Hamsten A, Hessel B, Procyk R, Silveria A, Zacharski L. Native fibrin gel networks and factors influencing their formation in health and disease. Adv Exp Med Biol 1990; 281: 1-23
36 Wilson J, Rickles FR, Armstrong PB, Lorand L. Nε (γ-glutamyl) lysine crosslinks in the blood clot of the horseshoe crab, Limulus polyphemus. Biochem Biophys Res Commun 1992; 188: 655-661
37 Tokunaga F, Yamada M, Miyata T, Ding YL, Hiranaga-Kawabata M, Muta T, Iwanaga S, Ichinose A, Davie EW. Limulus hemocyte transglutaminase: Its purification and characterization, and identification of the intracellular substrates. J Biol Chem 1993; 268: 252-261
38 Tokunaga F, Muta T, Iwanaga S, Ichinose A, Davie EW, Kuma K, Miyata T. Limulus hemocyte transglutaminase: cDNA cloning, amino acid sequence, and tissue localization. J Biol Chem 1993; 268: 262-268
39 Aketagawa J, Miyata T, Ohtsubo S, Nakamura T, Hayashida H, Miyata T, Iwanaga S. Primary structure of Limulus anticoagulant anti-lipopolysaccharide factor. J Biol Chem 1986; 261: 7357-7365
40 Muta T, Miyata T, Tokunaga F, Nakamura T, Iwanaga S. Primary structure of anti-lipopolysaccharide factor from American horseshoe crab, Limulus polyphemus. J Biochem (Tokyo) 1987; 101: 1321-1330
41 Ohashi K, Niwa M, Nakamura T, Morita T, Iwanaga S. Anti-LPS factor in the horseshoe crab, Tachypleus tridentatus: Its hemolytic activity on the red blood cell sensitized with lipopolysaccharide. FEBS Lett 1984; 176: 207-210
42 Nakamura T, Furunaka H, Miyata T, Tokunaga F, Muta T, Iwanaga S, Niwa M, Takao T, Shimonishi Y. Tachyplesin, a class of antimicrobial peptide from hemocytes of the horseshoe crab, (Tachypleus tridentatus). J Biol Chem 1988; 263: 16709-16713
43 Miyata T, Tokunaga F, Yoneya Y, Yoshikawa K, Iwanaga S, Niwa M, Takao T, Shimonishi Y. Antimicrobial peptides isolated from horseshoe crab hemocytes, tachyplesin II and polyphemusins I and II: Chemical structures and biological activity. J Biochem (Tokyo) 1989; 106: 663-668
44 Kawano K, Yoneya T, Miyata T, Yoshikawa K, Tokunaga F, Terada Y, Iwanaga S. Antimicrobial peptide, tachyplesin I isolated from hemocytes of the horseshoe crab (Tachypleus tridentatus): NMR determination of the β-sheet structure. J Biol Chem 1990; 265: 15365-15367
45 Shigenaga T, Muta T, Toh Y, Tokunaga F, Iwanaga S. Antimicrobial tachyplesin peptide precursor: cDNA cloning and cellular localization in horseshoe crab (Tachypleus tridentatus). J Biol Chem 1990; 265: 21350-21354
46 Nakamura T, Hirai T, Tokunaga F, Kawabata S, Iwanaga S. Purification and amino acid sequence of Kunitz-type protease inhibitor found in the hemocytes of the horseshoe crab (Tachypleus tridentatus). J Biochem (Tokyo) 1987; 101: 1297-1306
47 Armstrong PB, Quigley JP, Rickles FR. The Limulus blood cell secretes α2-macroglobulin when activated. Biol Bull (Woods Hole, Mass.) 1990; 178: 137-143
48 Nguyen NY, Suzuki A, Cheng SM, Zon G, Liu TY. The amino acid sequence of Limulus C-reactive protein. J Biol Chem 1986; 261: 10450-10455
49 Liang SM, Sakmar TP, Liu TY. Studies on Limulus amebocyte lysate III: Purification of an endotoxin-binding protein from Limulus amebocyte membranes. J Biol Chem 1980; 255: 5586-5590
50 Liang SM, Liang CM, Liu TY. Studies on Limulus amebocytes. Isolation and identification of a membrane-bound protein activator of cyclic nucleotide phosphodiesterase from Limulus amebocytes. J Biol Chem 1981; 256: 4968-4972
51 Minetti CASA, Lin Y, Cislo T, Liu TY. Purification and characterization of an endotoxin-binding protein with protease inhibitory activity from Limulus amebocytes. J Biol Chem 1991; 266: 20773-20780
52 Liu T, Lin Y, Cislo T, Minetti CASA, Baba JMK, Liu TY. Limunectin: A phosphocholine-binding protein from Limulus amebocytes with adhesion-promoting properties. J Biol Chem 1991; 266: 14813-14821