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Cysteine and serine protease-mediated proteolysis in body homogenate of a zooplankter, Moina macrocopa, is inhibited by the toxic cyanobacterium, Microcystis aeruginosa PCC7806.
Comp Biochem Physiol B Biochem Mol Biol. 2005 May; 141(1):33-41.CB

Abstract

The paper describes the characterization of proteases in the whole body homogenate of Moina macrocopa, which can possibly be inhibited by the extracts of Microcystis aeruginosa PCC7806. With the use of oligopeptide substrates and specific inhibitors, we detected the activities of trypsin, chymotrypsin, elastase and cysteine protease. Cysteine protease, the predominant enzyme behind proteolysis of a natural substrate, casein, was partially purified by gel filtration. The substrate SDS-polyacrylamide gel electrophoresis of body homogenate revealed the presence of nine bands of proteases (17-72 kDa). The apparent molecular mass of an exclusive cysteine protease was 60 kDa, whereas of trypsin, it was 17-24 kDa. An extract of M. aeruginosa PCC7806 significantly inhibited the activities of trypsin, chymotrypsin and cysteine protease in M. macrocopa body homogenate at estimated IC(50) of 6- to 79-microg dry mass mL(-1). Upon fractionation by C-18 solid-phase extraction, 60% methanolic elute contained all the protease inhibitors, and these metabolites could be further separated by reverse-phase liquid chromatography. The metabolites inhibitory to M. macrocopa proteases also inhibited the corresponding class of proteases of mammalian/plant origin. The study suggests that protease inhibition may contribute to chemical interaction of cyanobacteria and crustacean zooplankton.

Authors+Show Affiliations

Agrawal MK
Department of Biological Sciences, Rani Durgavati University, Jabalpur 482001, India.
Bagchi D
No affiliation info available
Bagchi SN
No affiliation info available

MeSH

AnimalsBenzoylarginine NitroanilideCaseinsChymotrypsinCladoceraCysteine EndopeptidasesCysteine Proteinase InhibitorsInhibitory Concentration 50MicrocystisMolecular WeightPancreatic ElastaseProteinsSerine EndopeptidasesSubstrate SpecificityTrypsinZooplankton

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

15820132

Citation

Agrawal, Manish Kumar, et al. "Cysteine and Serine Protease-mediated Proteolysis in Body Homogenate of a Zooplankter, Moina Macrocopa, Is Inhibited By the Toxic Cyanobacterium, Microcystis Aeruginosa PCC7806." Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology, vol. 141, no. 1, 2005, pp. 33-41.
Agrawal MK, Bagchi D, Bagchi SN. Cysteine and serine protease-mediated proteolysis in body homogenate of a zooplankter, Moina macrocopa, is inhibited by the toxic cyanobacterium, Microcystis aeruginosa PCC7806. Comp Biochem Physiol B Biochem Mol Biol. 2005;141(1):33-41.
Agrawal, M. K., Bagchi, D., & Bagchi, S. N. (2005). Cysteine and serine protease-mediated proteolysis in body homogenate of a zooplankter, Moina macrocopa, is inhibited by the toxic cyanobacterium, Microcystis aeruginosa PCC7806. Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology, 141(1), 33-41.
Agrawal MK, Bagchi D, Bagchi SN. Cysteine and Serine Protease-mediated Proteolysis in Body Homogenate of a Zooplankter, Moina Macrocopa, Is Inhibited By the Toxic Cyanobacterium, Microcystis Aeruginosa PCC7806. Comp Biochem Physiol B Biochem Mol Biol. 2005;141(1):33-41. PubMed PMID: 15820132.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Cysteine and serine protease-mediated proteolysis in body homogenate of a zooplankter, Moina macrocopa, is inhibited by the toxic cyanobacterium, Microcystis aeruginosa PCC7806. AU - Agrawal,Manish Kumar, AU - Bagchi,Divya, AU - Bagchi,Suvendra Nath, PY - 2004/08/30/received PY - 2004/12/17/revised PY - 2005/01/03/accepted PY - 2005/4/12/pubmed PY - 2005/7/30/medline PY - 2005/4/12/entrez SP - 33 EP - 41 JF - Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology JO - Comp Biochem Physiol B Biochem Mol Biol VL - 141 IS - 1 N2 - The paper describes the characterization of proteases in the whole body homogenate of Moina macrocopa, which can possibly be inhibited by the extracts of Microcystis aeruginosa PCC7806. With the use of oligopeptide substrates and specific inhibitors, we detected the activities of trypsin, chymotrypsin, elastase and cysteine protease. Cysteine protease, the predominant enzyme behind proteolysis of a natural substrate, casein, was partially purified by gel filtration. The substrate SDS-polyacrylamide gel electrophoresis of body homogenate revealed the presence of nine bands of proteases (17-72 kDa). The apparent molecular mass of an exclusive cysteine protease was 60 kDa, whereas of trypsin, it was 17-24 kDa. An extract of M. aeruginosa PCC7806 significantly inhibited the activities of trypsin, chymotrypsin and cysteine protease in M. macrocopa body homogenate at estimated IC(50) of 6- to 79-microg dry mass mL(-1). Upon fractionation by C-18 solid-phase extraction, 60% methanolic elute contained all the protease inhibitors, and these metabolites could be further separated by reverse-phase liquid chromatography. The metabolites inhibitory to M. macrocopa proteases also inhibited the corresponding class of proteases of mammalian/plant origin. The study suggests that protease inhibition may contribute to chemical interaction of cyanobacteria and crustacean zooplankton. SN - 1096-4959 UR - https://www.unboundmedicine.com/medline/citation/15820132/Cysteine_and_serine_protease_mediated_proteolysis_in_body_homogenate_of_a_zooplankter_Moina_macrocopa_is_inhibited_by_the_toxic_cyanobacterium_Microcystis_aeruginosa_PCC7806_ DB - PRIME DP - Unbound Medicine ER -