Genome-Wide Identification and Characterization of Carboxypeptidase Genes in Silkworm (Bombyx mori)

Abstract

The silkworm (Bombyx mori) is an economically-important insect that can secrete silk. Carboxypeptidases have been found in various metazoan species and play important roles in physiological and biochemical reactions. Here, we analyzed the silkworm genome database and characterized 48 carboxypeptidases, including 34 metal carboxypeptidases (BmMCP1–BmMCP34) and 14 serine carboxypeptidases (BmSCP1–BmSCP14), to better understand their diverse functions. Compared to other insects, our results indicated that carboxypeptidases from silkworm have more family members. These silkworm carboxypeptidases could be divided into four families: Peptidase_M2 carboxypeptidases, Peptidase_M14 carboxypeptidases, Peptidase_S10 carboxypeptidases and Peptidase_S28 carboxypeptidases. Microarray analysis showed that the carboxypeptidases had distinct expression patterns, whereas quantitative real-time PCR demonstrated that the expression level of 13 carboxypeptidases significantly decreased after starvation and restored after re-feeding. Overall, our study provides new insights into the functional and evolutionary features of silkworm carboxypeptidases.

Cytotoxicity of AuCu–Cu2S Nanocomposites: Implications for Biological Evaluation of the Nanocomposite Effect on Bombyx mori Silkworms and Cell Lines

“…Previous studies have shown that carboxypeptidases found in the midgut are involved in the release of free amino acids from food proteins. The study also demonstrated that midgut-specific carboxypeptidases were downregulated after starvation and restored after the refeeding of the larvae . There is a massive increase in feed intake in the fifth instar of the silkworm larvae as they prepare to spin silk and metamorphose into other stages, and as such, the upregulation of MSTRG.5590 in this study is not surprising.…”

iTRAQ-Based Quantitative Proteomic Analysis of Digestive Juice across the First 48 Hours of the Fifth Instar in Silkworm Larvae

“…The exopeptidases are further divided into carboxypeptidases (cleaving at the carboxylic terminus) and aminopeptidases (cleaving at the amino terminus). A total of 48 genes encoding carboxypeptidases have been identified in silkworm and midgut-specific carboxypeptidases were significantly downregulated after starvation and restored after re-feeding [49]. A total of 9 carboxypeptidases were successfully identified in silkworm digestive juice; among them, BGIBMGA004830, BGIBMGA009486, and BGIBMGA004797 were upregulated in DJ48/24h.…”

Hemocyte Clusters Defined by scRNA-Seq in Bombyx mori: In Silico Analysis of Predicted Marker Genes and Implications for Potential Functional Roles

“…Carboxypeptidase B-like can be tracked to the gene BmMCP18 that encodes a metallocarboxypeptidase with Peptidase_M14 domain and a divalent metal (zinc) cation in its active site (206). In mammals, carboxypeptidase B can modulate the coagulation cascade in the plasma (207) but in insects it remains unknown whether a protease cascade is involved in the clotting process (208).…”