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Titolo:
A bacteria-induced, intracellular serpin in granular hemocytes of Manduca sexta
Autore:
Gan, H; Wang, Y; Jiang, HB; Mita, K; Kanost, MR;
Indirizzi:
Kansas State Univ, Dept Biochem, Manhattan, KS 66506 USA Kansas State Univ Manhattan KS USA 66506 Biochem, Manhattan, KS 66506 USA Natl Inst Radiol Sci, Genome Res Grp, Chiba 2638555, Japan Natl Inst Radiol Sci Chiba Japan 2638555 e Res Grp, Chiba 2638555, Japan
Titolo Testata:
INSECT BIOCHEMISTRY AND MOLECULAR BIOLOGY
fascicolo: 9, volume: 31, anno: 2001,
pagine: 887 - 898
SICI:
0965-1748(20010726)31:9<887:ABISIG>2.0.ZU;2-5
Fonte:
ISI
Lingua:
ENG
Soggetto:
SERINE PROTEINASE-INHIBITORS; HEPARIN COFACTOR-II; AMINO-ACID-SEQUENCE; BOMBYX-MORI; ELASTASE INHIBITOR; MOLECULAR-CLONING; COAGULATION INHIBITOR; HYPHANTRIA-CUNEA; OVALBUMIN FAMILY; REACTIVE CENTER;
Keywords:
insect immunity; tobacco hornworm; serine proteinase; hemolymph; granulocyte;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Life Sciences
Citazioni:
43
Recensione:
Indirizzi per estratti:
Indirizzo: Kanost, MR Kansas State Univ, Dept Biochem, Manhattan, KS 66506 USA KansasState Univ Manhattan KS USA 66506 nhattan, KS 66506 USA
Citazione:
H. Gan et al., "A bacteria-induced, intracellular serpin in granular hemocytes of Manduca sexta", INSEC BIO M, 31(9), 2001, pp. 887-898

Abstract

Serine proteinase inhibitors from the serpin superfamily have been identified as hemolymph proteins from several groups of arthropods. including horseshoe crabs, crayfish, and insects. In the tobacco hornworm, Manduca sexta,one group of serpins present in plasma is generated by alternate exon splicing from serpin gene-1. We have identified a second serpin gene from this insect, M. sexta serpin-2. A serpin-2 DNA clone was isolated from a fifth instar larval cDNA library. The full-length cDNA is 1.5 kb long and encodes a protein of 381 amino acid residues. Amino acid sequence comparisons with other invertebrate serpins reveal approximately 25-40% identity with serpin-2. An expressed sequence tag from Bombyx mori. which is very similar to M.sexta serpin-2, was identified, and the corresponding full-length cDNA sequence was determined. This silkworm homolog of serpin-2 is 57% identical toM. sexta serpin-2. Recombinant M. sexta serpin-2 was used as an antigen togenerate a rabbit polyclonal antiserum. This antiserum recognized a 43 kDaprotein present in hemocytes but absent from plasma. Western and Northern blot results revealed that serpin-2 gene expression increased dramatically after larvae were injected with bacteria. In situ hybridization showed thatthe serpin-2 mRNA is present in granular hemocytes of immune-stimulated larvae. Serpin-2 purified from hemocytes obtained 24 h after injection of larvae with bacteria lacked inhibitory activity for all proteinases rested except for human cathepsin G. The intracellular location of serpin-2 suggests a function for serpin-2 different from the plasma serpin-l proteins. (C) 2001 Elsevier Science Ltd. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 31/03/20 alle ore 22:26:22