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

Dvoryakova, Elena A.; Vinokurov, Konstantin S.; Tereshchenkova, Valeriia F.; Dunaevsky, Yakov E.; Belozersky, M. A.; Oppert, Brenda; Filippova, I. Yu.; Elpidina, Elena N.

doi:10.1016/j.ibmb.2021.103679

Cited by 10 publications

(17 citation statements)

References 46 publications

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Section: Mass-spectrometry Analysis Of Rptccathl1 and Rtccathl1supporting

confidence: 67%

“…The results of the MS analysis of mature rTcCathL1 after trypsinolysis showed the presence of several peptides at the putative N-terminus of the enzyme differing by several amino acids SGKPAAAEVDWR GKPAAAEVDWR KPAAAEVDWR AAEVDWR Apparently, several forms of the mature enzyme are present in the final preparation of the mature rTcCathL1. The shortest peptide coincides with the found N-terminus of the native cathepsin L T. castaneum [11]. The results of the MS analysis of mature rTcCathL1 after trypsinolysis showed the presence of several peptides at the putative N-terminus of the enzyme differing by several amino acids SGKPAAAEVDWR GKPAAAEVDWR KPAAAEVDWR AAEVDWR Apparently, several forms of the mature enzyme are present in the final preparation of the mature rTcCathL1.…”

Section: Mass-spectrometry Analysis Of Rptccathl1 and Rtccathl1mentioning

confidence: 76%

“…Of particular interest are studies on insect cysteine cathepsins and the identification of a digestive function in these peptidases. Cysteine digestive peptidases are found in limited groups of insects such as infraorder Cucuiformia of the Coleoptera order [4][5][6][7][8][9][10][11] and Hemiptera order [12,13]. The digestive cysteine peptidases of stored product beetles from the family Tenebrionidae have been studied in the most detail-in particular, Tribolium castaneum.…”

Section: Introductionmentioning

confidence: 99%

“…According to the transcriptomic data [14,15], together with biochemical [7] and proteomic [16] studies, the most highly expressed T. castaneum C1 endopeptidase is cathepsin L, whose gene transcripts account for 72% of the total expression level of cysteine peptidase genes in the insect larvae gut. Cathepsin L (NCBI ID NP_001164001) (TcCathL1) appears to be the main cysteine digestive peptidase in T. castaneum and plays an important role in the initial steps of food protein digestion [11].…”

Section: Introductionmentioning

confidence: 99%

“…Recent studies attempt to identify the enzymes that can effectively hydrolyze immunogenic prolamin peptides so that they can be used for the enzymatic therapy of celiac disease [19][20][21][22][23][24][25][26][27][28]. In our laboratory, the main T. castaneum digestive cathepsins L NP_001164001 (TcCathL1) and NP_001164314 (TcCathL2) were isolated, and their ability to cleave the fluorogenic analogues of immunogenic prolamin peptides was shown [11], which allows them to be considered as potential candidates for the treatment of celiac disease. However, the isolation of native cathepsin L from T. castaneum larvae is difficult due to its low stability and the complex multienzyme composition of the initial mixture.…”

Section: Introductionmentioning

confidence: 99%

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Recombinant Cathepsin L of Tribolium castaneum and Its Potential in the Hydrolysis of Immunogenic Gliadin Peptides

Dvoryakova

Klimova

Simonyan

et al. 2022

IJMS

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Wheat gliadins contain a large amount of glutamine- and proline-rich peptides which are not hydrolyzed by human digestive peptidases and can cause autoimmune celiac disease and other forms of gluten intolerance in predisposed people. Peptidases that efficiently cleave such immunogenic peptides can be used in enzyme therapy. The stored product insect pest Tribolium castaneum efficiently hydrolyzes gliadins. The main digestive peptidase of T. castaneum is cathepsin L, which is from the papain C1 family with post-glutamine cleavage activity. We describe the isolation and characterization of T. castaneum recombinant procathepsin L (rpTcCathL1, NP_001164001), which was expressed in Pichia pastoris cells. The activation of the proenzyme was conducted by autocatalytic processing. The effects of pH and proenzyme concentration in the reaction mixture on the processing were studied. The mature enzyme retained high activity in the pH range from 5.0 to 9.0 and displayed high pH-stability from 4.0 to 8.0 at 20 °C. The enzyme was characterized according to electrophoretic mobility under native conditions, activity and stability at various pH values, a sensitivity to various inhibitors, and substrate specificity, and its hydrolytic effect on 8-, 10-, 26-, and 33-mer immunogenic gliadins peptides was demonstrated. Our results show that rTcCathL1 is an effective peptidase that can be used to develop a drug for the enzyme therapy of various types of gluten intolerance.

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Section: Mass-spectrometry Analysis Of Rptccathl1 and Rtccathl1supporting

confidence: 67%

Section: Mass-spectrometry Analysis Of Rptccathl1 and Rtccathl1mentioning

confidence: 76%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Recombinant Cathepsin L of Tribolium castaneum and Its Potential in the Hydrolysis of Immunogenic Gliadin Peptides

Dvoryakova

Klimova

Simonyan

et al. 2022

IJMS

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Effect of gluten on the digestive tract and fat body of Telodeinopus aoutii (Diplopoda)

Błaszczyk

Sosinka

Wilczek

et al. 2022

Journal of Morphology

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Adult specimens or larvae of invertebrates used as food for vertebrates are often maintained close to gluten so they might become vectors for cereal proteins.However, the tissues and internal organs can respond differently in animals with different feeding habits. The midgut epithelium might be a first and sufficient barrier preventing uptake and effects of gluten on the whole body, while the fat body is the main organ that accumulates different xenobiotics. Good models for such research are animals that do not feed on gluten-rich products in their natural environment. The project's goal was to investigate alterations in the midgut epithelium and fat body of the herbivorous millipede Telodeinopus aoutii (Diplopoda) and analyze cell death processes activated by gluten. It enabled us to determine whether changes were intensified or reversed by adaptive mechanisms. Adult specimens were divided into control and experimental animals fed with mushrooms supplemented with gluten and analyzed using transmission electron microscopy, flow cytometry, and confocal microscopy. Two organs were isolated for the qualitative and quantitative analysis: the midgut and the fat body. Our study of the herbivorous T. aoutii which does not naturally feed on gluten containing diet showed that continuous and prolonged gluten feeding activates repair processes that inhibit the processes of cell death (apoptosis and necrosis) and induce an increase in cell viability.

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Development of the Fundamentals of a Technology for the Production of Tribolium castaneum Recombinant Cathepsin L in Komagataella kurtzmanii Yeast

Serkina,

Gubaidullin,

Akentiev

et al. 2023

Appl Biochem Microbiol

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

Cited by 10 publications

References 46 publications

Recombinant Cathepsin L of Tribolium castaneum and Its Potential in the Hydrolysis of Immunogenic Gliadin Peptides

Recombinant Cathepsin L of Tribolium castaneum and Its Potential in the Hydrolysis of Immunogenic Gliadin Peptides

Effect of gluten on the digestive tract and fat body of Telodeinopus aoutii (Diplopoda)

Development of the Fundamentals of a Technology for the Production of Tribolium castaneum Recombinant Cathepsin L in Komagataella kurtzmanii Yeast

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