Cathepsin B from the white shrimp Litopenaeus vannamei: cDNA sequence analysis, tissues-specific expression and biological activity |
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Authors: | Stephens A Rojo L Araujo-Bernal S Garcia-Carreño F Muhlia-Almazan A |
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Institution: | a Aquatic Molecular Biology Lab. Centro de Investigacion en Alimentacion y Desarrollo (CIAD), A. C. Carretera a Ejido La Victoria Km 0.6. PO Box. 1735, Hermosillo, Sonora, 83000, Mexicob Biochemistry Lab. Centro de Investigaciones Biologicas del Noroeste (CIBNOR), Mar Bermejo 195, Col. Playa Palo de Santa Rita, P.O. Box 128, La Paz, Baja California Sur 23090, Mexico |
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Abstract: | Cathepsin B is a cystein proteinase scarcely studied in crustaceans. Its function has not been clearly described in shrimp species belonging to the sub-order Dendrobranchiata, which includes the white shrimp Litopenaeus vannamei and other species from the Penaeidae family. Studies on vertebrates suggest that these lysosomal enzymes intracellularly hydrolize protein, as other cystein proteinases. However, the expression of the gene encoding the shrimp cathepsin B in the midgut gland was affected by starvation in a similar way as other digestive proteinases which extracellularly hydrolyze food protein. In this study the white shrimp L. vannamei cathepsin B (LvCathB) cDNA was sequenced, and characterized. Its gene expression was evaluated in various shrimp tissues, and changes in the mRNA amounts were compared with those observed on other digestive proteinases from the midgut gland during starvation. By using qRT-PCR it was found that LvCathB is expressed in most shrimp tissues except in pleopods and eye stalk. Changes on LvCathB mRNA during starvation suggest that the enzyme participates during intracellular protein hydrolysis but also, after food ingestion, it participates in hydrolyzing food proteins extracellularly as confirmed by the high activity levels we found in the gastric juice and midgut gland of the white shrimp. |
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Keywords: | Cathepsin B Cystein proteinases Genes expression Shrimp Starvation |
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