A chymotrypsin-like serine protease cDNA involved in food protein digestion in the common cutworm, Spodoptera litura: Cloning, characterization, developmental and induced expression patterns, and localization

Zhang, Chun; Zhou, Daohua; Zheng, Sichun; Liu, Lin; Shu, Tao; Li, Yang; Hu, Songnian; Feng, Qili

doi:10.1016/j.jinsphys.2010.02.001

Cited by 32 publications

(38 citation statements)

References 44 publications

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“…Similar results have been also reported in A. aegypti ; 11 of A. aegypti carboxypeptidases are upregulated in response to blood meal feeding [7]. The expression profile of induced by starvation and re-feeding in our study was the same as the expression profile of a chymotrypsin-like serine protease in Spodoptera litura [41]. Here, the expression levels of BmSCP1 and BmMCP30 were higher after re-feeding compared to those during normal feeding.…”

Section: Discussionsupporting

confidence: 89%

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

Liu

et al. 2016

IJMS

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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.

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Section: Discussionsupporting

confidence: 89%

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

Liu

et al. 2016

IJMS

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“…For example, chymotrypsin-like serine proteases (SPs) are important in protein digestion in insects, but may also play roles in immune response and molting. The enzymes important for digestion can be clarified based on cDNA sequence (e.g., particular catalytic motifs), tissue localization (by fluorescent in situ hybridization of mRNA and immunohistochemistry of protein), and developmental and induced expression (e.g., during feeding vs. nonfeeding stages) (487, 488). Structure-function relationships (415) and evolutionary relationships (102) among enzyme isoforms can be discerned as well.…”

Section: Catalytic Chemical Breakdown By Intrinsic Enzymesmentioning

confidence: 99%

“…Insects provide some of the best researched examples of developmental changes in digestive biochemistry. Common cutworms ( Spodoptera litura ; Lepidoptera), a highly polyphagous pest of subtropical and tropical crops, can be used to illustrate a pattern that is probably common (488). As in many insects, chymotrypsin-like SPs are major midgut digestive enzymes.…”

Section: Matches Of Gi System To Nutritional Changes During Ontogenymentioning

confidence: 99%

“…Apparent transcription control of SP activity was also demonstrated in the scarabaeid beetle Costelytra zealandica (306). Food appears to act as a proximate signal for expression, based on up-and-down expression in cutworm larvae according to feeding regime (488) (Fig. 18B).…”

Section: Matches Of Gi System To Nutritional Changes During Ontogenymentioning

confidence: 99%

“…Bars (i.e., means) within a discrete time period (i.e., at 6, 24, 48, or 72 h) that share a common letter did not differ significantly, whereas different letters indicate significant differences at P < 0.05. Both figures based on data from reference (488). …”

Section: Figurementioning

confidence: 99%

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Comparative Digestive Physiology

Karasov

Douglas

2013

Comprehensive Physiology

261

221

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In vertebrates and invertebrates, morphological and functional features of gastrointestinal (GI) tracts generally reflect food chemistry, such as content of carbohydrates, proteins, fats, and material(s) refractory to rapid digestion (e.g., cellulose). The expression of digestive enzymes and nutrient transporters approximately matches the dietary load of their respective substrates, with relatively modest excess capacity. Mechanisms explaining differences in hydrolase activity between populations and species include gene copy number variations and single-nucleotide polymorphisms. Transcriptional and posttranscriptional adjustments mediate phenotypic changes in the expression of hydrolases and transporters in response to dietary signals. Many species respond to higher food intake by flexibly increasing digestive compartment size. Fermentative processes by symbiotic microorganisms are important for cellulose degradation but are relatively slow, so animals that rely on those processes typically possess special enlarged compartment(s) to maintain a microbiota and other GI structures that slow digesta flow. The taxon richness of the gut microbiota, usually identified by 16S rRNA gene sequencing, is typically an order of magnitude greater in vertebrates than invertebrates, and the interspecific variation in microbial composition is strongly influenced by diet. Many of the nutrient transporters are orthologous across different animal phyla, though functional details may vary (e.g., glucose and amino acid transport with K+ rather than Na+ as a counter ion). Paracellular absorption is important in many birds. Natural toxins are ubiquitous in foods and may influence key features such as digesta transit, enzymatic breakdown, microbial fermentation, and absorption

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CLONING AND CHARACTERIZATION OF A MIDGUT‐SPECIFIC FATTY ACID BINDING PROTEIN IN Spodoptera litura

Huang

Zhou

Gao

et al. 2012

Arch Insect Biochem Physiol

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A fatty acid binding protein (FABP) gene (Slfabp1) was cloned from the midgut of Spodoptera litura larvae. The gene consists of four exons and three introns and encodes a peptide of 134 amino acid residues with a predicted molecular mass of 14.7 kDa, which was confirmed by in vitro protein expression. Northern blot and Western blot analyses indicated that both of Slfabp1 mRNA and protein were highly and specifically expressed in the midgut during the fifth and sixth instar feeding larval stages. In situ hybridization and immunohistochemistry analyses confirmed the midgut-specific localization of Slfabp1 mRNA and protein. The result of Western blot showed that expression of the protein was downregulated by starvation and upregulated by refeeding in sixth instar larvae. All of the results taken together suggest that the SlFABP1 plays important role(s) in FA uptake and transport in the midgut during the larval feeding stages of the insect.

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A chymotrypsin-like serine protease cDNA involved in food protein digestion in the common cutworm, Spodoptera litura: Cloning, characterization, developmental and induced expression patterns, and localization

Cited by 32 publications

References 44 publications

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

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

Comparative Digestive Physiology

CLONING AND CHARACTERIZATION OF A MIDGUT‐SPECIFIC FATTY ACID BINDING PROTEIN IN Spodoptera litura

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