메뉴 건너뛰기




Volumn 44, Issue 6, 2007, Pages 1065-1074

Molecular cloning and characterisation of a proteinase inhibitor, alpha 2-macroglobulin (α2-M) from the haemocytes of tiger shrimp Penaeus monodon

Author keywords

Alpha 2 macroglobulin; Bait region; Innate immunity; Penaeus monodon; Peptidoglycan; Protease inhibitor; Thioester containing protein

Indexed keywords

ALPHA 2 MACROGLOBULIN; COMPLEMENTARY DNA; MESSENGER RNA; PEPTIDOGLYCAN; PROTEINASE INHIBITOR; THIOESTER;

EID: 33748758437     PISSN: 01615890     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molimm.2006.08.002     Document Type: Article
Times cited : (58)

References (53)
  • 3
    • 0032586674 scopus 로고    scopus 로고
    • α2-Macroglobulin: an evolutionarily conserved arm of the innate immune system
    • Armstrong P.B., and Quigley J.P. α2-Macroglobulin: an evolutionarily conserved arm of the innate immune system. Dev. Comp. Immunol. 23 (1999) 375-390
    • (1999) Dev. Comp. Immunol. , vol.23 , pp. 375-390
    • Armstrong, P.B.1    Quigley, J.P.2
  • 4
    • 0029849796 scopus 로고    scopus 로고
    • Purification and characterization of a tetrameric α-macroglobulin proteinase inhibitor from the gastropod mollusc Biomphalaria glabrata
    • Bender R.C., and Bayne C.J. Purification and characterization of a tetrameric α-macroglobulin proteinase inhibitor from the gastropod mollusc Biomphalaria glabrata. Biochem. J. 316 (1996) 893-900
    • (1996) Biochem. J. , vol.316 , pp. 893-900
    • Bender, R.C.1    Bayne, C.J.2
  • 6
    • 0026735749 scopus 로고
    • Biochemical evidence of phenoloxidase activity (pro-PO system) in larvae of Allogamus auricollis (Insecta Trichoptera)
    • Brivio M.F., Pagani M., and Scarí G. Biochemical evidence of phenoloxidase activity (pro-PO system) in larvae of Allogamus auricollis (Insecta Trichoptera). Comp. Biochem. Physiol. Part B 102 (1992) 867-871
    • (1992) Comp. Biochem. Physiol. Part B , vol.102 , pp. 867-871
    • Brivio, M.F.1    Pagani, M.2    Scarí, G.3
  • 7
    • 0033775615 scopus 로고    scopus 로고
    • Absolute quantification of mRNA using real-time reverse transcription polymerase chain reaction assays
    • Bustin S.A. Absolute quantification of mRNA using real-time reverse transcription polymerase chain reaction assays. J. Mol. Endocrinol. 25 (2000) 169-193
    • (2000) J. Mol. Endocrinol. , vol.25 , pp. 169-193
    • Bustin, S.A.1
  • 8
    • 1642463826 scopus 로고    scopus 로고
    • The prophenoloxidase activating system in invertebrates
    • Cerenius L., and Söderhäll K. The prophenoloxidase activating system in invertebrates. Immunol. Rev. 198 (2004) 72-82
    • (2004) Immunol. Rev. , vol.198 , pp. 72-82
    • Cerenius, L.1    Söderhäll, K.2
  • 9
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • Chomczynski P., and Sacchi N. Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 162 (1987) 156-159
    • (1987) Anal. Biochem. , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 10
    • 0002764047 scopus 로고
    • The phylogeny and evolution of the complement system
    • Whaley M.L., and Weiler J.M. (Eds), Boston, USA
    • Dodds A.W., and Day A. The phylogeny and evolution of the complement system. In: Whaley M.L., and Weiler J.M. (Eds). Complement in Health and Disease (1993), Boston, USA
    • (1993) Complement in Health and Disease
    • Dodds, A.W.1    Day, A.2
  • 11
    • 0030577021 scopus 로고    scopus 로고
    • Localisation of the major reactive lysine residue involved in the self-crosslinking of proteinase-activated Limulus alpha2-macroglobulin
    • Dolmer K., Husted L.B., Armstrong P.B., and Sottrup-Jensen L. Localisation of the major reactive lysine residue involved in the self-crosslinking of proteinase-activated Limulus alpha2-macroglobulin. FEBS Lett. 393 (1996) 37-40
    • (1996) FEBS Lett. , vol.393 , pp. 37-40
    • Dolmer, K.1    Husted, L.B.2    Armstrong, P.B.3    Sottrup-Jensen, L.4
  • 12
    • 0024990650 scopus 로고
    • α2-Macroglobulin from Limulus polyphemus exhibits proteinase inhibitory activity and participates in a hemolytic system
    • Enghild J.J., Thøgersen I.B., Salvesen G., Fey G.H., Figler N.L., Gonias S.L., and Pizzo S.V. α2-Macroglobulin from Limulus polyphemus exhibits proteinase inhibitory activity and participates in a hemolytic system. Biochem. J. 29 (1990) 10070-10080
    • (1990) Biochem. J. , vol.29 , pp. 10070-10080
    • Enghild, J.J.1    Thøgersen, I.B.2    Salvesen, G.3    Fey, G.H.4    Figler, N.L.5    Gonias, S.L.6    Pizzo, S.V.7
  • 14
    • 0037297165 scopus 로고    scopus 로고
    • Stimulation of peripheral blood mononuclear cells with lipopolysaccharide induces expression of the plasma protein α2-macroglobulin
    • Gunnarsson M., Frangsmyr L., Stigbrand T., and Jensen P.E.H. Stimulation of peripheral blood mononuclear cells with lipopolysaccharide induces expression of the plasma protein α2-macroglobulin. Protein Expr. Purif. 27 (2003) 238-243
    • (2003) Protein Expr. Purif. , vol.27 , pp. 238-243
    • Gunnarsson, M.1    Frangsmyr, L.2    Stigbrand, T.3    Jensen, P.E.H.4
  • 15
    • 0024980237 scopus 로고
    • Amino acid sequence around the thiolester of α2-macroglobulin from plasma of the crayfish, Pacifastacus leniusculus
    • Hall M., Söderhäll K., and Sottrup-Jensen L. Amino acid sequence around the thiolester of α2-macroglobulin from plasma of the crayfish, Pacifastacus leniusculus. FEBS Lett. 54 (1989) 111-114
    • (1989) FEBS Lett. , vol.54 , pp. 111-114
    • Hall, M.1    Söderhäll, K.2    Sottrup-Jensen, L.3
  • 16
    • 15244354178 scopus 로고    scopus 로고
    • Cloning of a glycosylphosphatidylinositol-anchored alpha-2-macroglobulin cDNA from the ascidian, Ciona intestinalis, and its possible role in immunity
    • Hammond J.A., Nakao M., and Smith V.J. Cloning of a glycosylphosphatidylinositol-anchored alpha-2-macroglobulin cDNA from the ascidian, Ciona intestinalis, and its possible role in immunity. Mol. Immunol. 42 (2005) 683-694
    • (2005) Mol. Immunol. , vol.42 , pp. 683-694
    • Hammond, J.A.1    Nakao, M.2    Smith, V.J.3
  • 17
    • 0023684972 scopus 로고
    • Purification and characterization of an α2-macroglobulin-like proteinase inhibitor from plasma of the crayfish Pacifastacus leniusculus
    • Hergenhahn H.G., Hall M., and Söderhäll K. Purification and characterization of an α2-macroglobulin-like proteinase inhibitor from plasma of the crayfish Pacifastacus leniusculus. Biochem. J. 255 (1988) 801-806
    • (1988) Biochem. J. , vol.255 , pp. 801-806
    • Hergenhahn, H.G.1    Hall, M.2    Söderhäll, K.3
  • 18
    • 0024234855 scopus 로고
    • CLUSTAL: a package for performing multiple alignments on a microcomputer
    • Higgins D.G., and Sharp P.M. CLUSTAL: a package for performing multiple alignments on a microcomputer. Gene 73 (1988) 237-244
    • (1988) Gene , vol.73 , pp. 237-244
    • Higgins, D.G.1    Sharp, P.M.2
  • 19
    • 0031673224 scopus 로고    scopus 로고
    • Localization of basic residues required for receptor binding to the single alpha-helix of the receptor binding domain of human alpha2-macroglobulin
    • Huang W., Dolmer K., Liao X., and Guttins P.G. Localization of basic residues required for receptor binding to the single alpha-helix of the receptor binding domain of human alpha2-macroglobulin. Protein Sci. 7 (1998) 2602-2612
    • (1998) Protein Sci. , vol.7 , pp. 2602-2612
    • Huang, W.1    Dolmer, K.2    Liao, X.3    Guttins, P.G.4
  • 20
    • 0347722697 scopus 로고    scopus 로고
    • Localization of carbohydrate attachment sites and disulfide bridges in Limulus α2-macroglobulin. Evidence for two forms differing primarily in their bait region sequences
    • Husted L.B., Sorensen E.S., Armstrong P.B., Quigley J.P., Kristensen L., and Sottrup-Jensen L. Localization of carbohydrate attachment sites and disulfide bridges in Limulus α2-macroglobulin. Evidence for two forms differing primarily in their bait region sequences. J. Biol. Chem. 277 (2002) 43698-43706
    • (2002) J. Biol. Chem. , vol.277 , pp. 43698-43706
    • Husted, L.B.1    Sorensen, E.S.2    Armstrong, P.B.3    Quigley, J.P.4    Kristensen, L.5    Sottrup-Jensen, L.6
  • 23
    • 0033953792 scopus 로고    scopus 로고
    • The clip-domain family of serine proteinases in arthropods
    • Jiang H., and Kanost M.R. The clip-domain family of serine proteinases in arthropods. Insect Biochem. Mol. Biol. 30 (2000) 95-105
    • (2000) Insect Biochem. Mol. Biol. , vol.30 , pp. 95-105
    • Jiang, H.1    Kanost, M.R.2
  • 24
    • 0018873523 scopus 로고
    • Protein inhibitors of proteinases
    • Laskowski M.J., and Kato I. Protein inhibitors of proteinases. Annu. Rev. Biochem. 49 (1980) 593-626
    • (1980) Annu. Rev. Biochem. , vol.49 , pp. 593-626
    • Laskowski, M.J.1    Kato, I.2
  • 25
    • 0034694376 scopus 로고    scopus 로고
    • Environmental factors affecting immune responses in Crustacea
    • Le Moullac G., and Haffner P. Environmental factors affecting immune responses in Crustacea. Aquaculture 191 (2000) 121-131
    • (2000) Aquaculture , vol.191 , pp. 121-131
    • Le Moullac, G.1    Haffner, P.2
  • 27
    • 0035831034 scopus 로고    scopus 로고
    • Conserved role of a complement-like protein in phagocytosis revealed by dsRNA knockout in cultured cells of the mosquito, Anopheles gambiae
    • Levashina E.A., Moita L.F., Blandin S., Vriend G., Lagueux M., and Kafatos F.C. Conserved role of a complement-like protein in phagocytosis revealed by dsRNA knockout in cultured cells of the mosquito, Anopheles gambiae. Cell 104 (2001) 709-718
    • (2001) Cell , vol.104 , pp. 709-718
    • Levashina, E.A.1    Moita, L.F.2    Blandin, S.3    Vriend, G.4    Lagueux, M.5    Kafatos, F.C.6
  • 28
    • 27644472527 scopus 로고    scopus 로고
    • Purification and characterization of α2-macroglobulin from grass carp Ctenopharyngodon idellus: cloning a segment of the corresponding gene
    • Li F.L., and Lu C.P. Purification and characterization of α2-macroglobulin from grass carp Ctenopharyngodon idellus: cloning a segment of the corresponding gene. Fish Shellfish Immunol. 20 (2006) 474-481
    • (2006) Fish Shellfish Immunol. , vol.20 , pp. 474-481
    • Li, F.L.1    Lu, C.P.2
  • 30
    • 0032079041 scopus 로고    scopus 로고
    • Shrimp diseases and current diagnostic methods
    • Lightner D.V., and Redman R.M. Shrimp diseases and current diagnostic methods. Aquaculture 164 (1998) 201-220
    • (1998) Aquaculture , vol.164 , pp. 201-220
    • Lightner, D.V.1    Redman, R.M.2
  • 31
    • 0029933662 scopus 로고    scopus 로고
    • Identification of residues in α2-macroglobulins important for binding to the α2-macroglobulin receptor/low density lipoprotein receptor-related protein
    • Nielsen K.L., Holtet T.L., Etzerodt M., Moestrup S.K., Gliemann J., Sottrup-Jensen L., and Thogersen H.C. Identification of residues in α2-macroglobulins important for binding to the α2-macroglobulin receptor/low density lipoprotein receptor-related protein. J. Biol. Chem. 271 (1996) 12909-12912
    • (1996) J. Biol. Chem. , vol.271 , pp. 12909-12912
    • Nielsen, K.L.1    Holtet, T.L.2    Etzerodt, M.3    Moestrup, S.K.4    Gliemann, J.5    Sottrup-Jensen, L.6    Thogersen, H.C.7
  • 32
    • 0033956456 scopus 로고    scopus 로고
    • Origin and evolution of the complement system
    • Du Pasquier L., and Litman G.W. (Eds), Springer-Verlag, New York, USA
    • Nonaka M. Origin and evolution of the complement system. In: Du Pasquier L., and Litman G.W. (Eds). Origin and Evolution of the Vertebrate Immune System vol. 248 (2000), Springer-Verlag, New York, USA 37-50
    • (2000) Origin and Evolution of the Vertebrate Immune System , vol.248 , pp. 37-50
    • Nonaka, M.1
  • 33
    • 2442454655 scopus 로고    scopus 로고
    • Molecular cloning and expression analysis of α2-macroglobulin in the kuruma shrimp, Marsupenaeus japonicus
    • Rattanachai A., Hirono I., Ohira T., Takahashi Y., and Aoki T. Molecular cloning and expression analysis of α2-macroglobulin in the kuruma shrimp, Marsupenaeus japonicus. Fish Shellfish Immunol. 15 (2004) 599-611
    • (2004) Fish Shellfish Immunol. , vol.15 , pp. 599-611
    • Rattanachai, A.1    Hirono, I.2    Ohira, T.3    Takahashi, Y.4    Aoki, T.5
  • 35
    • 0041707780 scopus 로고    scopus 로고
    • Molecular cloning, structure and bait region splice variants of α2-macroglobulin from the soft tick Ornithodoros moubata
    • Saravanan T., Weise C., Sojka D., and Kopáek P. Molecular cloning, structure and bait region splice variants of α2-macroglobulin from the soft tick Ornithodoros moubata. Insect Biochem. Mol. Biol. 33 (2003) 841-851
    • (2003) Insect Biochem. Mol. Biol. , vol.33 , pp. 841-851
    • Saravanan, T.1    Weise, C.2    Sojka, D.3    Kopáek, P.4
  • 37
    • 0024333351 scopus 로고
    • α2-Macroglobulin structure, shape, and mechanism of proteinase complex formation
    • Sottrup-Jensen L. α2-Macroglobulin structure, shape, and mechanism of proteinase complex formation. J. Biol. Chem. 264 (1989) 11539-11542
    • (1989) J. Biol. Chem. , vol.264 , pp. 11539-11542
    • Sottrup-Jensen, L.1
  • 39
    • 0025195721 scopus 로고
    • Localization of epsilon-lysyl-gamma-glutamyl cross-links in five human alpha2-macroglobulin-proteinase complexes. Nature of the high molecular weight cross-linked products
    • Sottrup-Jensen L., Hansen H.F., Pedersen H.S., and Kristensen L. Localization of epsilon-lysyl-gamma-glutamyl cross-links in five human alpha2-macroglobulin-proteinase complexes. Nature of the high molecular weight cross-linked products. J. Biol. Chem. 265 (1990) 17727-17737
    • (1990) J. Biol. Chem. , vol.265 , pp. 17727-17737
    • Sottrup-Jensen, L.1    Hansen, H.F.2    Pedersen, H.S.3    Kristensen, L.4
  • 40
    • 0019268081 scopus 로고
    • A thiol-ester in alpha2-macroglobulin cleaved during proteinase complex formation
    • Sottrup-Jensen L., Petersen T.E., and Magnusson S. A thiol-ester in alpha2-macroglobulin cleaved during proteinase complex formation. FEBS Lett. 121 (1980) 275-279
    • (1980) FEBS Lett. , vol.121 , pp. 275-279
    • Sottrup-Jensen, L.1    Petersen, T.E.2    Magnusson, S.3
  • 41
    • 0023665215 scopus 로고
    • A functional, thioester-containing α2-macroglobulin homologue isolated from the hemolymph of the American lobster (Homarus americanus)
    • Spycher S.E., Arya S., Isenman D.E., and Painter R.H. A functional, thioester-containing α2-macroglobulin homologue isolated from the hemolymph of the American lobster (Homarus americanus). J. Biol. Chem. 262 (1987) 14606-14611
    • (1987) J. Biol. Chem. , vol.262 , pp. 14606-14611
    • Spycher, S.E.1    Arya, S.2    Isenman, D.E.3    Painter, R.H.4
  • 42
    • 0020164637 scopus 로고
    • Evolution of α2-macroglobulin. Demonstration in a variety of vertebrate species of a protein resembling human α2-macroglobulin
    • Starkey P.M., and Barrett A.J. Evolution of α2-macroglobulin. Demonstration in a variety of vertebrate species of a protein resembling human α2-macroglobulin. Biochem. J. 205 (1982) 91-95
    • (1982) Biochem. J. , vol.205 , pp. 91-95
    • Starkey, P.M.1    Barrett, A.J.2
  • 43
    • 0020164712 scopus 로고
    • Evolution of α2-macroglobulin. The purification and characterization of a protein homologous with human α2-macroglobulin from plaice (Pleuronectes platessa L.) plasma
    • Starkey P.M., Fletcher T.C., and Barrett A.J. Evolution of α2-macroglobulin. The purification and characterization of a protein homologous with human α2-macroglobulin from plaice (Pleuronectes platessa L.) plasma. Biochem. J. 205 (1982) 97-104
    • (1982) Biochem. J. , vol.205 , pp. 97-104
    • Starkey, P.M.1    Fletcher, T.C.2    Barrett, A.J.3
  • 45
    • 0032433172 scopus 로고    scopus 로고
    • Evolution and diversity of the complement system of poikilothermic vertebrates
    • Sunyer J.O., and Lambris J.D. Evolution and diversity of the complement system of poikilothermic vertebrates. Immunol. Rev. 166 (1998) 39-57
    • (1998) Immunol. Rev. , vol.166 , pp. 39-57
    • Sunyer, J.O.1    Lambris, J.D.2
  • 47
    • 0018647589 scopus 로고
    • Characterization of alkylamine-sensitive site in alpha2-macroglobulin
    • Swenson R.P., and Howard J.B. Characterization of alkylamine-sensitive site in alpha2-macroglobulin. Proc. Natl. Acad. Sci. USA 76 (1979) 4313-4316
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4313-4316
    • Swenson, R.P.1    Howard, J.B.2
  • 48
    • 0026721960 scopus 로고
    • Purification and characterization of an α2-macroglobulin proteinase inhibitor from the mollusc Octopus vulgaris
    • Thogersen I.B., Salvesen G., Brucato F.H., Pizzo S.V., and Enghild J.J. Purification and characterization of an α2-macroglobulin proteinase inhibitor from the mollusc Octopus vulgaris. Biochem. J. 285 (1992) 521-527
    • (1992) Biochem. J. , vol.285 , pp. 521-527
    • Thogersen, I.B.1    Salvesen, G.2    Brucato, F.H.3    Pizzo, S.V.4    Enghild, J.J.5
  • 49
    • 0027411971 scopus 로고
    • Complement defense mechanisms
    • Tomlinson S. Complement defense mechanisms. Curr. Opin. Immunol. 5 (1993) 83-89
    • (1993) Curr. Opin. Immunol. , vol.5 , pp. 83-89
    • Tomlinson, S.1
  • 50
    • 0020643467 scopus 로고
    • Human plasma proteinase inhibitors
    • Travis J., and Salvesen G.S. Human plasma proteinase inhibitors. Annu. Rev. Biochem. 52 (1983) 655-709
    • (1983) Annu. Rev. Biochem. , vol.52 , pp. 655-709
    • Travis, J.1    Salvesen, G.S.2
  • 51
    • 0022852274 scopus 로고
    • The epitopes of two complex-specific monoclonal antibodies, related to the receptor recognition site, map to the COOH-terminal end of human α2-macroglobulin
    • Van Leuven F., Marynen P., Cassiman J.J., and Van Den Berghe H. The epitopes of two complex-specific monoclonal antibodies, related to the receptor recognition site, map to the COOH-terminal end of human α2-macroglobulin. J. Biol. Chem. 261 (1986) 6933-6937
    • (1986) J. Biol. Chem. , vol.261 , pp. 6933-6937
    • Van Leuven, F.1    Marynen, P.2    Cassiman, J.J.3    Van Den Berghe, H.4
  • 52
    • 33748805963 scopus 로고    scopus 로고
    • Vaseeharan, B., Lin, Y.C., Ko, C.F., Chiou,T.T., Chen J.C., in press. Molecular cloning and characterisation of a thioester-containing α2-macroglobulin (α2-M) from the haemocytes of mud crab Scylla serrata. Fish Shellfish Immunol.
  • 53
    • 0035830675 scopus 로고    scopus 로고
    • Isolation and characterization of an K-macroglobulin from the gastropod mollusc Helix pomatia with tetrameric structure and preserved activity after methylamine treatment
    • Yigzaw Y., Gielens C., and Préaux G. Isolation and characterization of an K-macroglobulin from the gastropod mollusc Helix pomatia with tetrameric structure and preserved activity after methylamine treatment. Biochim. Biophys. Acta 1545 (2001) 104-113
    • (2001) Biochim. Biophys. Acta , vol.1545 , pp. 104-113
    • Yigzaw, Y.1    Gielens, C.2    Préaux, G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.