Molecular cloning of Limulus α2-macroglobulin

European Journal of Biochemistry

Volumn 242, Issue 3, 1996, Pages 822-831

  Iwaki, Daisuke ^a   Kawabata, Shun Ichiro ^a   Miura, Yoshiki ^a   Kato, Atsuko ^a   Armstrong, Peter B ^b,c   Quigley, James P ^c,d   Nielsen, Kåre Lehmann ^e   Dolmer, Klavs ^e   Sottrup Jensen, Lars ^e   Iwanaga, Sadaaki ^a  

^a KYUSHU UNIVERSITY   (Japan)

^b UNIVERSITY OF CALIFORNIA   (United States)

^c MARINE BIOLOGICAL LABORATORY   (United States)

^d STATE UNIVERSITY OF NEW YORK   (United States)

^e AARHUS UNIVERSITY   (Denmark)

Author keywords

cDNA; Horseshoe crab; Invertebrate; 2 Macroglobulin

Indexed keywords

ALPHA 2 MACROGLOBULIN;

AMINO ACID SEQUENCE; ANIMAL CELL; ANIMAL TISSUE; ARTICLE; BLOOD CELL; BLOOD CLOTTING; CARBOHYDRATE ANALYSIS; CONTROLLED STUDY; DNA LIBRARY; GENE EXPRESSION; HEMOLYMPH; IMMUNOBLOTTING; LIMULUS; MOLECULAR CLONING; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS;

ANIMALIA; ARTHROPODA; DECAPODA (CRUSTACEA); INVERTEBRATA; LIMULUS; LIMULUS POLYPHEMUS; MAMMALIA; MEROSTOMATA; POLYPHEMUS;

EID: 8044252161     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1996.0822r.x     Document Type: Article

References (73)

1. Aimes, R. T., Quigley, J. P., Swarnakar, S., Strickland, D. K. & Armstrong, P. B. (1995) Preliminary investigations on the scavenger receptors of the amebocyte of the American horseshoe crab, Limulus polyphemus, Biol. Bull. 189, 225-226.
2. Armstrong, P. B., Levin, J. & Quigley, J. P. (1984) Role of endogenous proteinase inhibitors in the regulation of the blood clotting system of the horseshoe crab, Limulus polyphemus, Thromb. Haemostasis (Stuttgart) 52, 117-120.
3. 2-macroglobulinlike activity in the blood of chelicerate and mandibulate arthropods, J. Exp. Zool. 236, 1-9.
4. 2-macroglobulin when activated, Biol. Bull. 178, 137-143.
5. 2-macroglobulin from the arthropod Limulus polyphemus, J. Biol. Chem. 266, 2526-2530.
6. 2M in the horseshoe crab: A structural and functional invertebrate homologue, Ann. NY Acad. Sci. 737, 188-201.
7. Armstrong, P. B., Misquith, S., Srimal, S., Melchior, R. & Quigley, J. P. (1994b) Identification of limulin as a major cytolytic protein in the plasma of the American horseshoe crab, Limulus polyphemus, Biol. Bull. 187, 227-228.
8. Armstrong, P. B., Melchior, R. & Quigley, J. P. (1996a) Humoral immunity in long-lived arthropods, J. Insect Physiol. 42, 53-64.
9. Armstrong, P. B., Swarnakar, S., Srimal, S., Misquith, S., Hahn, E. A., Aimes R. T. & Quigley, J. P. (1996b) A cytolytic function for a sialic acid-binding lectin that is a member of the pentraxin family of proteins, J. Biol. Chem. 271, 14717-14721.
10. 2-macroglobulin with proteinases: Characteristics and specifity of the reaction, and a hypothesis concerning its molecular mechanism, Biochem. J. 133, 709-724.
11. 2-macroglobulin molecule, Biochem. J. 181, 401-418.
12. Belt, K. T., Carroll, M. C. & Porter, P. R. (1984) The structural basis of the multiple forms of human complement component C4, Cell 36, 907-914.
13. 2-macroglobulin on reaction with primary amines or proteolytic enzymes, Biochem. J. 207, 347-356.
14. 1-inhibitor III messenger RNA, J. Biol. Chem. 263, 3999-4012.
15. 2-macroglobulin-protease complexes. Methylamine competition shows that proteases bridge two disulfide-bonded half-molecules, Biochemistry 31, 8960-8966.
16. Chomczynski, P. & Sacchi, N. (1987) Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction, Anal. Biochem. 162, 156-159.
17. De Bruijn, M. H. L. & Fey, G. H. (1985) Human complement component C3: cDNA coding sequence and derived primary structure, Proc. Natl Acad. Sci. USA 82, 708-712.
18. Edwards, J. B. D. M., Delort, J. & Mallet, J. (1991) Oligodeoxyribo-nucleotide ligation to single-stranded cDNAs: a new tool for cloning 5′ ends of mRNAs and for constructing cDNA libraries by in vitro amplification, Nucleic Acids Res. 19, 5227-5232.
19. Enghild, J. J., Thøgersin, I. B., Roche, P. A. & Pizzo, S. V. (1989) A conserved region in α-macroglobulins participates in binding to the mammalian α-macroglobulin receptor, Biochemistry 28, 1406-1412.
20. Enghild, J. J., Thøgersin, I. B., Salvesen, G., Fey, G. H., Figler, N. L., Gonias, S. L. & Pizzo, S. V. (1990) α-macroglobulin from Limulus polyphemus exhibits proteinase inhibitory activity and participates in a hemolytic system, Biochemistry 29, 10070-10080.
21. 2-macroglobulin as trypsin-protein esterase, Clin. Chim. Acta 14, 493-501.
22. 2-macroglobulin concentration and its variation with age and sex, Clin. Chim. Acta 15, 113-120.
23. 2-macroglobulin and acute phase control of its messenger RNA, J. Biol. Chem. 262, 446-454.
24. 2-macroglobulin following reaction with methylamine and trypsin, Biochim. Biophys. Acta 705, 306-314.
25. 2-macroglobulin, Biochem. J. 173, 27-38.
26. 2-macroglobulins, potent inhibitors of influenza virus infection, J. Biol. Chem. 264, 9842-9849.
27. Hara, S., Takemori, Y., Yamaguchi, M. Nakamura, M. & Ohkura, Y. (1987) Fluorometric high-performance liquid chromatography of N-acetyl- and N-glycolylneuraminic acids and its application to their microdetermination in human and animal sera, glycoproteins, and glycolipids, Anal. Biochem. 164, 138-145.
28. 2-macroglobulin-enzyme interactions, J. Exp. Med. 138, 508-521.
29. 2-macroglobulin: Expression, folding and biochemical characterization of a high-affinity recombinant derivative, FEBS Lett. 344, 242-246.
30. Iwanaga, S., Miyata, T., Tokunaga, F. & Muta, T. (1992) Molecular mechanism of hemolymph clotting system in Limulus, Thromb. Res. 68, 1-32.
31. 2-macroglobulin: Complete disulfide bridge assignment and locarization of two interchain bridges in the dimeric proteinase binding unit, J. Biol. Chem. 261, 15863-15869.
32. 2-macroglobulin and assignment of the chromosomal locus, Proc. Natl Acad. Sci. USA 82, 2282-2286.
33. Kolb, W. P. & Müller-Eberhard, H. J. (1976) The membrane attack mechanism of complement: The three polypeptide chain structure of the eighth component (C8), J. Exp. Med. 143, 1131-1139.
34. Krieger, M. & Herz, J. (1994) Structures and functions of multiligand lipoprotein receptors: Macrophage scavenger receptors and LDL receptor-related protein (LRP), Annu. Rev. Biochem. 63, 601-637.
35. 2-macroglobulin receptor, FEBS Lett. 276, 151-155.
36. Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature 227, 680-685.
37. Laskowski, M. Jr & Kato, I. (1980) Protein inhibitors of proteinases, Annu. Rev. Biochem. 49, 593-626.
38. Liang, Z., Lindblad, P., Beauvais, A., Johansson, M. W., Latgé, J.-P., Hall, M., Cerenius, L. & Söderhäll, K. (1992) Crayfish α-macroglobulin and 76 kDa protein; their biosynthesis and subcellular locarlization of the 76 kDa protein, J. Insect. Physiol. 38, 987-995.
39. 2-macroglobulin-mediated clearance of proteases from the plasma of the American horseshoe crab, Limulus Polyphemus, J. Biol. Chem. 270, 13496-13502.
40. Miura, Y., Tokunaga, F., Miyata, T., Moriyasu, M., Yoshikawa, K. & Iwanaga, S. (1992) Preparation and properties of monoclonal antibodies against lipopolysaccharide-sensitive serine protease zymogen, factor C, from horseshoe crab (Tachypleus tridentatus)hemocytes, J. Biochem. (Tokyo) 112, 476-481.
41. Miura, Y., Kawabata, S. & Iwanaga, S. (1994) A Limulus intracellular coagulation inhibitor with characteristics of the serpin superfamily: Purification, characterization, and cDNA cloning, J. Biol. Chem. 269, 542-547.
42. Miura, Y., Kawabata, S., Wakamiya, Y., Nakamura, T. & Iwanaga, S. (1995) A limulus intracellular coagulation inhibitor type 2: Purification, characterization, cDNA cloning, and tissue localization, J. Biol. Chem. 270, 558-565.
43. 2-macroglobulin-proteinase complex is achieved by binding to adjacent receptors, J. Biol. Chem. 266, 14011-14017.
44. Muta, T., Seki, N., Takaki, Y., Hashimoto, R., Oda, T., Iwanaga, A., Tokunaga, F. & Iwanaga, S. (1995) Purified horseshoe crab factor G: Reconstitution and characterization of the (1→3)-β-D-glucan-sensitive serine protease cascade, J. Biol. Chem. 270, 892-897.
45. 1-antitrypsin, J. Biol. Chem. 251, 4514-4521.
46. Nakamura, T., Morita, T. & Iwanaga, S. (1985) Intracellular proclotting enzyme in limulus (Tachypleus tridentatus) hemocytes: Its purification and properties, J. Biochem. (Tokyo) 97, 1561-1574.
47. Ng, S. C., Rao, A. G., Howard, O. M. Z. & Sodetz, J. M. (1987) The eighth component of human complement: Evidence that it is an oligomeric serum protein assembled from products of three different genes, Biochemistry 26, 5229-5233.
48. Nielsen, K. L., Holtet, T. L., Etzerodt, M., Moestrup, S. K., Gliemann, J., Sottrup-Jensen, L. & Thøgersen, H. C. (1996) Identification of residues in α-macroglobulins important for binding to the «,-macroglobulin receptor/low density lipoprotein receptor-related protein, J. Biol. Chem. 271, 12909-12912.
49. Nishimura, H., Takao, T., Hase, S., Shimonishi, Y. & Iwanaga, S. (1992) Human factor IX has a tetrasaccharide O-glycosidically linked to serine 61 through the fucose residue, J. Biol. Chem. 267, 17520-17525.
50. Overbergh, L., Torrekens, S., Van Leuven, F. & Van Den Berghe, H. (1991) Molecular characterization of the murinoglobulins, J. Biol. Chem. 266, 16903-16910.
51. 2-macroglobulin purified from the hemolymph of the horseshoe crab Limulus polyphemus, J. Biol. Chem. 260, 12715-12719.
52. 2-macroglobulin from the American horseshoe crab, Limulus, J. Biol. Chem. 266, 19426-19431.
53. 2-macroglobulin, J. Biol. Chem. 260, 15723-15735.
54. Seki, N., Muta, T., Oda, T., Iwaki, D., Kuma, K., Miyata, T. & Iwanaga, S. (1994) Horseshoe crab (1,3)-β-D-glucan-sensitive coagulation factor G: A serine protease zymogen heterodimer with similarities to β-glucan-binding proteins, J. Biol. Chem. 269, 1370-1374.
55. Shigenaga, T., Takaenoki, Y. Kawasaki, S., Seki, N., Muta, T., Toh, Y., Ito, A. & Iwanaga, S. (1993) Separation of large and small granules from horseshoe crab (Tachypleus tridentatus) hemocytes and characterization of their components, J. Biochem. (Tokyo) 114, 307-316.
56. Sodetz, J. M. (1989) Structure and function of C8 in the membrane attack sequence of complement, Curr. Top. Microbiol. Immunol. 140, 19-31.
57. 2-macroglobulin: Nature of the complex, FEBS Lett. 127, 167-173.
58. 2-macroglobulin: V. The complete structure, J. Biol. Chem. 259, 8318-8327.
59. 2-macroglobulin: Characterization of a receptor-binding domain obtained by digestion with papain, FEBS Lett. 205, 20-24.
60. Sottrup-Jensen, L. (1987) in The plasma proteins. Structure, function, and genetic control (Putnam, F. W., ed.) 2nd edn, vol. 5, pp. 191-291, Academic Press, Inc., Orlando FL.
61. Sottrup-Jensen, L. (1989) α-macroglobulins: Structure, shape, and mechanism of proteinase complex formation, J. Biol. Chem. 264, 11539-11542.
62. Sottrup-Jensen, L., Sand, O., Kristensen, L. & Fey, G. H. (1989) The α-macroglobulin bait region: Sequence diversity and localization of cleavage sites for proteinases in five mammalian α-macroglobulins, J. Biol. Chein. 264, 15781-15789.
63. 2-macroglobulin family from mammals, Comp. Biochem. Physiol. 96B, 621-625.
64. 2-macroglobulin-proteinase complexes: Nature of the high molecular mass cross-linked products, J. Biol. Chem. 265, 17727-17737.
65. Starkey, P. M. & Barrett, A. J. (1977) in Proteinases in mammalian cells and tissues (Barrett, A. J., ed.) pp. 663-696, Elsevier/North-Holland Biomedical Press, Amsterdam.
66. Steckel, E. W., York, R. G., Monahan, J. B. & Sodetz, J. M. (1980) The eighth component of human complement: Purification and physicochemical characterization of its unusual subunit structure, J. Biol. Chem. 255, 11997-12005.
67. 2-macroglobulin receptor and low density lipoprotein receptor-related protein suggests that this molecule is a multifunctional receptor, J. Biol. Chem. 265, 17401-17404.
68. 2-macroglobulin, Biol. Bull 189, 226-227.
69. 2-macroglobulin: Primary amines and the molecular mechanisms of endoprotease inhibition and receptor-mediated endocytosis, Mol. Cell. Biochem. 58, 121-128.
70. 2-macroglobulin: Isolation after limited proteolysis with a bacterial proteinase, J. Biol. Chem. 261, 11369-11373.
71. Van Leuven, F., Torrekens, S., Overbergh, L., Lorent, K., de Strooper, B. & Van Den Berghe, H. (1992) The primary sequence and the subunit structure of mouse α-2-macroglobulin, deduced from protein sequencing of the isolated subunits and from molecular cloning of the c-DNA, Eur. J. Biochem. 210, 319-327.
72. 1-macroglobulin, Biochemistry 31, 2346-2352.
73. Wetsel, R. A., Lemons, R. S., Le Beau, M. M., Barnum, S. R., Noack, D. & Tack, B. F. (1988) Molecular analysis of human complement component C5: Localization of the structural gene to chromosome 9, Biochemistiy 27, 1474-1482.