Primary digestive cathepsins L of Tribolium castaneum larvae: Proteomic identification, properties, comparison with human lysosomal cathepsin L

Dvoryakova, E.A.; Vinokurov, K.S.; Tereshchenkova, V.F.; Dunaevsky, Y.E.; Belozersky, M.A.; Oppert, B.; Filippova, I.Y.; Elpidina, E.N.

Статья опубликована в высокорейтинговом журнале

Информация о цитировании статьи получена из Web of Science
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 12 января 2022 г.

Авторы: Dvoryakova E.A., Vinokurov K.S., Tereshchenkova V.F., Dunaevsky Y.E., Belozersky M.A., Oppert B., Filippova I.Y., Elpidina E.N.
Журнал: Insect Biochemistry and Molecular Biology
Том: 140
Год издания: 2022
Издательство: Pergamon Press Ltd.
Местоположение издательства: United Kingdom
Номер статьи: 103679
DOI: 10.1016/j.ibmb.2021.103679
Аннотация: We previously described the most highly expressed enzymes from the gut of the red flour beetle, Tribolium castaneum, as cathepsins L. In the present study, two C1 family-specific cysteine cathepsin L enzymes from the larval midgut were isolated and identified using MALDI-TOF MS analysis. The isolated T. castaneum cathepsins were characterized according to their specificity against chromogenic and fluorogenic peptide substrates, and the most efficiently hydrolyzed substrate was Z-FR-pNA with Arg in the P1 subsite. The specificity of insect digestive cathepsins was compared with human lysosomal cathepsin L, the well-studied peptidase of the C1 family cathepsins. T. castaneum digestive cathepsins efficiently hydrolyzed substrates with small and uncharged amino acid residues at P1 (Ala, Gln) more than human cathepsin L. In particular, these insect digestive cathepsins cleaved with higher efficiency the analogs of immunogenic peptides of gliadins, which contribute to autoimmune celiac disease in susceptible people, and thus insect enzymes may be useful in enzymatic treatments for this disease. A bioinformatic study supported by the proteomic analysis of the primary structures of the isolated cathepsins was used to compare tertiary models. The phylogenetic analysis of coleopteran and human cathepsins from the L subfamily indicated that insect digestive cathepsins grouped separately from lysosomal cathepsins. This work was supported by the Russian Foundation for Basic Research, grant N◦ 20-54-56044 Iran_t.
Добавил в систему: Терещенкова Валерия Феликсовна

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Primary digestive cathepsins L of Tribolium castaneum larvae: Proteomic identification, properties, comparison with human lysosomal cathepsin Lстатья Исследовательская статья

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