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Digestive physiology and characterization of digestive cathepsin L-like proteinase from the sugarcane weevil Sphenophorus levis.
J Insect Physiol. 2011 Apr; 57(4):462-8.JI

Abstract

Sugarcane is an important crop that has recently become subject to attacks from the weevil Sphenophorus levis, which is not efficiently controlled with chemical insecticides. This demands the development of new control devices for which digestive physiology data are needed. In the present study, ion-exchange chromatography of S. levis whole midgut homogenates, together with enzyme assays with natural and synthetic substrates and specific inhibitors, demonstrated that a cysteine proteinase is a major proteinase, trypsin is a minor one and chymotrypsin is probably negligible. Amylase, maltase and the cysteine proteinase occur in the gut contents and decrease throughout the midgut; trypsin is constant in the entire midgut, whereas a membrane-bound aminopeptidase predominates in the posterior midgut. The cysteine proteinase was purified to homogeneity through ion-exchange chromatography. The purified enzyme had a mass of 37 kDa and was able to hydrolyze Z-Phe-Arg-MCA and Z-Leu-Arg-MCA with k(cat)/K(m) values of 20.0±1.1 μM(-1)s(-1) and 30.0±0.5 μM(-1)s(-1), respectively, but not Z-Arg-Arg-MCA. The combined results suggest that protein digestion starts in the anterior midgut under the action of a cathepsin L-like proteinase and ends on the surface of posterior midgut cells. All starch digestion takes place in anterior midgut. These data will be instrumental to developing S. levis-resistant sugarcane.

Links

Publisher Full Text
linkinghub.elsevier.com
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Authors+Show Affiliations

Soares-Costa A
Laboratory of Molecular Biology, Department of Genetics and Evolution, Federal University of São Carlos, Rodovia Washington Luis Km 235, São Carlos, 13565-905 São Paulo, Brazil.
Dias AB
No affiliation info available
Dellamano M
No affiliation info available
de Paula FF
No affiliation info available
Carmona AK
No affiliation info available
Terra WR
No affiliation info available
Henrique-Silva F
No affiliation info available

MeSH

AnimalsCathepsin LDigestive SystemDigestive System Physiological PhenomenaInsect ProteinsKineticsSaccharumWeevils

Pub Type(s)

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

Language

eng

PubMed ID

21256130

Citation

Soares-Costa, Andrea, et al. "Digestive Physiology and Characterization of Digestive Cathepsin L-like Proteinase From the Sugarcane Weevil Sphenophorus Levis." Journal of Insect Physiology, vol. 57, no. 4, 2011, pp. 462-8.
Soares-Costa A, Dias AB, Dellamano M, et al. Digestive physiology and characterization of digestive cathepsin L-like proteinase from the sugarcane weevil Sphenophorus levis. J Insect Physiol. 2011;57(4):462-8.
Soares-Costa, A., Dias, A. B., Dellamano, M., de Paula, F. F., Carmona, A. K., Terra, W. R., & Henrique-Silva, F. (2011). Digestive physiology and characterization of digestive cathepsin L-like proteinase from the sugarcane weevil Sphenophorus levis. Journal of Insect Physiology, 57(4), 462-8. https://doi.org/10.1016/j.jinsphys.2011.01.006
Soares-Costa A, et al. Digestive Physiology and Characterization of Digestive Cathepsin L-like Proteinase From the Sugarcane Weevil Sphenophorus Levis. J Insect Physiol. 2011;57(4):462-8. PubMed PMID: 21256130.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Digestive physiology and characterization of digestive cathepsin L-like proteinase from the sugarcane weevil Sphenophorus levis. AU - Soares-Costa,Andrea, AU - Dias,Alcides B, AU - Dellamano,Márcia, AU - de Paula,Fernando Fonseca Pereira, AU - Carmona,Adriana K, AU - Terra,Walter R, AU - Henrique-Silva,Flávio, Y1 - 2011/01/20/ PY - 2010/10/27/received PY - 2011/01/13/revised PY - 2011/01/14/accepted PY - 2011/1/25/entrez PY - 2011/1/25/pubmed PY - 2011/6/15/medline SP - 462 EP - 8 JF - Journal of insect physiology JO - J Insect Physiol VL - 57 IS - 4 N2 - Sugarcane is an important crop that has recently become subject to attacks from the weevil Sphenophorus levis, which is not efficiently controlled with chemical insecticides. This demands the development of new control devices for which digestive physiology data are needed. In the present study, ion-exchange chromatography of S. levis whole midgut homogenates, together with enzyme assays with natural and synthetic substrates and specific inhibitors, demonstrated that a cysteine proteinase is a major proteinase, trypsin is a minor one and chymotrypsin is probably negligible. Amylase, maltase and the cysteine proteinase occur in the gut contents and decrease throughout the midgut; trypsin is constant in the entire midgut, whereas a membrane-bound aminopeptidase predominates in the posterior midgut. The cysteine proteinase was purified to homogeneity through ion-exchange chromatography. The purified enzyme had a mass of 37 kDa and was able to hydrolyze Z-Phe-Arg-MCA and Z-Leu-Arg-MCA with k(cat)/K(m) values of 20.0±1.1 μM(-1)s(-1) and 30.0±0.5 μM(-1)s(-1), respectively, but not Z-Arg-Arg-MCA. The combined results suggest that protein digestion starts in the anterior midgut under the action of a cathepsin L-like proteinase and ends on the surface of posterior midgut cells. All starch digestion takes place in anterior midgut. These data will be instrumental to developing S. levis-resistant sugarcane. SN - 1879-1611 UR - https://www.unboundmedicine.com/medline/citation/21256130/Digestive_physiology_and_characterization_of_digestive_cathepsin_L_like_proteinase_from_the_sugarcane_weevil_Sphenophorus_levis_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0022-1910(11)00018-7 DB - PRIME DP - Unbound Medicine ER -