JBC American Association for Cancer Research Centennial

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Jiang, H.
Right arrow Articles by Kanost, M. R.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Jiang, H.
Right arrow Articles by Kanost, M. R.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Volume 272, Number 2, Issue of January 10, 1997 pp. 1082-1087
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

Characterization and Functional Analysis of 12 Naturally Occurring Reactive Site Variants of Serpin-1 from Manduca sexta

(Received for publication, September 25, 1996, and in revised form, October 28, 1996)

Haobo Jiang and Michael R. Kanost

From the Department of Biochemistry, Kansas State University, Manhattan, Kansas 66506

Serpin gene-1 from the tobacco hornworm, Manduca sexta, encodes, through alternative exon usage, 12 reactive site variants (Jiang, H., Wang, Y. and Kanost, M. R., (1994) J. Biol. Chem. 269, 55-58; Jiang, H., Wang, Y., Huang, Y., Mulnix, A. B., Kadel, J., Cole, K., and Kanost, M. R. (1996) J. Biol. Chem. 271, 28017-28023). These 43-kDa proteins differ from each other only in their COOH-terminal 39-46 residues, which include the reactive site. To test the hypothesis that these proteins are proteinase inhibitors of diverse selectivities and to begin to elucidate their physiological functions, we expressed the 12 serpin-1 variants in Escherichia coli. Seven of the variants inhibited mammalian serine proteinases, with association rate constants comparable with those of human serpins. Serpin-1A, with a P1 Arg residue, inhibited both trypsin and plasmin. Serpin-1B (P1 Ala) and serpin-1F (P1 Val) inhibited porcine pancreatic elastase and human neutrophil elastase. Serpin-1H, -1K, and -1Z, all with a Tyr residue at the P1 position, inhibited chymotrypsin and cathepsin G. Serpin-1I (P1 Leu) inhibited both elastase and chymotrypsin. Nine of the serpin variants were active as inhibitors of microbial serine proteinases, including subtilisin Carlsberg, proteinase K, and two proteinases secreted by an entomopathogenic fungus, Metarhizium anisopliae. In addition, one of the serpin variants, serpin-1J, strongly inhibited activation of M. sexta hemolymph phenoloxidase, a pathway involving a serine proteinase cascade. This pathway is a component of the defensive response of insects to microbial infection. These results suggest that the products of M. sexta serpin gene-1 may be important in regulating both exogenous and endogenous serine proteinases in hemolymph.


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
 J. Biol. Chem.Home page
Y. Wang and H. Jiang
Interaction of beta-1,3-Glucan with Its Recognition Protein Activates Hemolymph Proteinase 14, an Initiation Enzyme of the Prophenoloxidase Activation System in Manduca sexta
J. Biol. Chem., April 7, 2006; 281(14): 9271 - 9278.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
Y. Tong and M. R. Kanost
Manduca sexta Serpin-4 and Serpin-5 Inhibit the Prophenol Oxidase Activation Pathway: cDNA CLONING, PROTEIN EXPRESSION, AND CHARACTERIZATION
J. Biol. Chem., April 15, 2005; 280(15): 14923 - 14931.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
Y. Tong, H. Jiang, and M. R. Kanost
Identification of Plasma Proteases Inhibited by Manduca sexta Serpin-4 and Serpin-5 and Their Association with Components of the Prophenol Oxidase Activation Pathway
J. Biol. Chem., April 15, 2005; 280(15): 14932 - 14942.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
Z. Zou and H. Jiang
Manduca sexta Serpin-6 Regulates Immune Serine Proteinases PAP-3 and HP8: cDNA CLONING, PROTEIN EXPRESSION, INHIBITION KINETICS, AND FUNCTION ELUCIDATION
J. Biol. Chem., April 8, 2005; 280(14): 14341 - 14348.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
Y. Zhu, Y. Wang, M. J. Gorman, H. Jiang, and M. R. Kanost
Manduca sexta Serpin-3 Regulates Prophenoloxidase Activation in Response to Infection by Inhibiting Prophenoloxidase-activating Proteinases
J. Biol. Chem., November 21, 2003; 278(47): 46556 - 46564.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
A. Danielli, F. C. Kafatos, and T. G. Loukeris
Cloning and Characterization of Four Anopheles gambiae Serpin Isoforms, Differentially Induced in the Midgut by Plasmodium berghei Invasion
J. Biol. Chem., January 31, 2003; 278(6): 4184 - 4193.
[Abstract] [Full Text] [PDF]

Home page
 Mol Biol EvolHome page
K. W. Barbour, R. L. Goodwin, F. Guillonneau, Y. Wang, H. Baumann, and F. G. Berger
Functional Diversification During Evolution of the Murine {alpha}1-Proteinase Inhibitor Family: Role of the Hypervariable Reactive Center Loop
Mol. Biol. Evol., May 1, 2002; 19(5): 718 - 727.
[Abstract] [Full Text] [PDF]

Home page
 BloodHome page
X. Zang, M. Yazdanbakhsh, H. Jiang, M. R. Kanost, and R. M. Maizels
A Novel Serpin Expressed by Blood-Borne Microfilariae of the Parasitic Nematode Brugia malayi Inhibits Human Neutrophil Serine Proteinases
Blood, August 15, 1999; 94(4): 1418 - 1428.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
H. Jiang, Y. Wang, and M. R. Kanost
Pro-phenol oxidase activating proteinase from an insect, Manduca sexta: A bacteria-inducible protein similar to Drosophila easter
PNAS, October 13, 1998; 95(21): 12220 - 12225.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
H. Ostergaard, S. K. Rasmussen, T. H. Roberts, and J. Hejgaard
Inhibitory Serpins from Wheat Grain with Reactive Centers Resembling Glutamine-rich Repeats of Prolamin Storage Proteins. CLONING AND CHARACTERIZATION OF FIVE MAJOR MOLECULAR FORMS
J. Biol. Chem., October 20, 2000; 275(43): 33272 - 33279.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
B.-C. Yoo, K. Aoki, Y. Xiang, L. R. Campbell, R. J. Hull, B. Xoconostle-Cazares, J. Monzer, J.-Y. Lee, D. E. Ullman, and W. J. Lucas
Characterization of Cucurbita maxima Phloem Serpin-1 (CmPS-1). A DEVELOPMENTALLY REGULATED ELASTASE INHIBITOR
J. Biol. Chem., November 3, 2000; 275(45): 35122 - 35128.
[Abstract] [Full Text] [PDF]

Home page
 Genome Res.Home page
J. A. Irving, R. N. Pike, A. M. Lesk, and J. C. Whisstock
Phylogeny of the Serpin Superfamily: Implications of Patterns of Amino Acid Conservation for Structure and Function
Genome Res., December 1, 2000; 10(12): 1845 - 1864.
[Abstract] [Full Text]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 1997 by the American Society for Biochemistry and Molecular Biology.