Shotgun proteomic analysis of the <i>Bombyx mori</i>
 anterior silk gland: An insight into the biosynthetic fiber spinning process

Yi, Qiying; Zhao, Ping; Wang, Xin; Zou, Yong; Zhong, Xiaowu; Wang, Chen; Zhang, Xiang; Xia, Qingyou

doi:10.1002/pmic.201200443

Cited by 34 publications

(36 citation statements)

References 25 publications

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“…Previous studies have shown that chitin‐binding proteins were involved in the formation of shear force in the anterior silk gland . The chitin and chitin‐binding cuticular proteins inside the anterior silk gland lumen form a extracellular matrix layer to protect the gland cells from being damaged by high mechanical shear of spinning, whereas shear force is important to induce the self‐assembly of silk proteins into fibrils …”

Section: Discussionmentioning

confidence: 99%

“…In the silk gland, the chitin layer is present only in the anterior part, but not in the middle and posterior parts, and is localized between the cell layer and the sericin layer . Recent studies indicated that dozens of cuticular proteins are important components of the chitin layer in the silk gland of the fifth instar.…”

Section: Introductionmentioning

confidence: 99%

“…Yi et al. (2013) identified 33 cuticular proteins in the anterior silk gland, including CPRs (RR‐motif proteins) and hypothetical cuticular proteins (CPHs) . Chang et al.…”

Section: Introductionmentioning

confidence: 99%

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Comparative Proteome Analysis Reveals that Cuticular Proteins Analogous to Peritrophin‐Motif Proteins are Involved in the Regeneration of Chitin Layer in the Silk Gland of Bombyx mori at the Molting Stage

et al. 2018

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The silk gland of silkworm produces silk proteins during larval development. Many studies have long focused on the silk gland of the fifth instar larvae, but few have investigated this gland at other larval stages. In the present study, the silk gland proteomes of the fourth instar and fourth molt are analyzed using liquid chromatography-tandem mass spectrometry. In total, 2654 proteins are identified from the silk gland. A high abundance of ribosomal proteins and RR-motif chitin-binding proteins is identified during day 2 of the fourth instar (IV-2) larval developmental stage, and the expression of cuticular proteins analogous to peritrophin (CPAP)-motif chitin-binding proteins is higher during the fourth molt (IV-M). In all, nine enzymes are found to be involved in the chitin regeneration pathway in the silk gland. Among them, two chitinase and two chitin deacetylases are identified as CPAP-motif proteins. Furthermore, the expression of CPAP3-G, the most abundant CPAP-motif cuticular protein in the silk gland during the IV-M stage, is investigated using western blot and immunofluorescence analyses; CPAP3-G shows a reverse changing trend with chitin in the silk gland. The findings of this study suggest that CPAP-motif chitin-binding proteins are involved in the degradation of the chitin layer in the silk gland. The data have been deposited to the ProteomeXchange with identifier PXD008677.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Comparative Proteome Analysis Reveals that Cuticular Proteins Analogous to Peritrophin‐Motif Proteins are Involved in the Regeneration of Chitin Layer in the Silk Gland of Bombyx mori at the Molting Stage

et al. 2018

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“…The anterior silk gland is the key site for the conformational changes in silk fibroin. Studies have shown that V‐ATPase is highly expressed in the anterior silk gland and spinning duct to maintain a low pH environment, which is beneficial to silk ﬁbrillogenesis (Azuma & Ohta, ; X. Wang et al, ; Yi et al, ). In this study, we found that Baf‐A1 can efficiently inhibit the activity of V‐ATPase.…”

Section: Discussionmentioning

confidence: 99%

“…Silkworm is a model of Lepidoptera . Using the proteomic approach, V‐ATPase has been identified with a high expression level in the spinnerets and anterior silk gland in silkworm by Wang and Yi, respectively (X. Wang, Li, Liu, Xia, & Zhao, ; Yi et al, ). Azuma confirmed that V‐ATPase is a key factor in controlling the acidification in these tissues (Azuma & Ohta, ).…”

Section: Introductionmentioning

confidence: 99%

Inhibition of silkworm vacuolar‐type ATPase activity by its inhibitor Bafilomycin A1 induces caspase‐dependent apoptosis in an embryonic cell line of silkworm

Tan

Wang

Liu

et al. 2018

Arch Insect Biochem Physiol

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Vacuolar‐type ATPase (V‐ATPase) is a type of hydrogen ion transporter located in the vesicular membrane‐like system, which mediates active transport and intracellular acidification in various compartments. In mammals, V‐ATPase has been reported to play a key role in cell proliferation and apoptosis. The studies of V‐ATPase in silkworm mainly focus on the acidification regulation of midgut and silk gland and immune resistance. However, there are few reports about the function of silkworm V‐ATPase on cell proliferation, autophagy, and apoptosis. Thus, the function of V‐ATPase in a cell line of Bombyx mori (BmE) was investigated by treating the cell line with bafilomycin A1, a specific inhibitor of V‐ATPase. Cell counting kit 8 (CCK8) and flow cytometry analysis showed that bafilomycin A1 treatment decreased the cell proliferation activity, affected the cell cycle progression and induced cell apoptosis. LysoTracker Red staining showed that the target of bafilomycin A1 is lysosome. The expression of all autophagy‐related genes ( BmATG5, BmATG6, and BmATG8) decreased, indicating that cell autophagy was inhibited. The analysis of the apoptosis pathway demonstrated that inhibiting the activity of V‐ATPase of BmE cells could promote mitochondria to release cytochrome C, inhibit the expression of BmIAP, and activate the caspase cascade to induce apoptosis. All these findings systematically illustrate the effects of V‐ATPase on the proliferation, autophagy, and apoptosis in BmE cells, and provide new ideas and a theoretical basis for further study on the function of V‐ATPase in BmE.

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Proteome profile of spinneret from the silkworm, Bombyx mori

Wang

Liu

et al. 2017

Proteomics

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The silkworm spinneret is an important tissue for silk fibrillogenesis and spinning. All biochemical processes during silk fibrillogenesis are correlated with silk properties. Understanding the role of spinneret in silk fibrillogenesis may help to reveal the mechanism of silk fibrillogenesis as well as improve silk quality for commercial purposes. Thus, we profiled the proteome of silkworm spinneret. A total of 1572 proteins and 232 differential abundance proteins were identified. Silk fibrillogenesis-related proteins, such as cuticle proteins, ion-transporting proteins, muscular proteins, and energy metabolic proteins, were abundant in spinneret. Metabolic pathway and GO enrichment analyses revealed that the identified proteins were involved in energy metabolism, chitin binding, and cuticle construction. Active energy metabolism may provide abundant energy for the muscle contraction as well as ion and water exchange. The chitin binding and cuticle construction process may provide sufficient shear forces for silk formation. Our data suggest that silkworm spinneret provides a suitable physiological and biochemical environment for silk fibrillogenesis. These proteins are potential targets for improving silk quality in the silk industry. Data are available via ProteomeXchange with identifier PXD004455.

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Shotgun proteomic analysis of the Bombyx mori anterior silk gland: An insight into the biosynthetic fiber spinning process

Cited by 34 publications

References 25 publications

Comparative Proteome Analysis Reveals that Cuticular Proteins Analogous to Peritrophin‐Motif Proteins are Involved in the Regeneration of Chitin Layer in the Silk Gland of Bombyx mori at the Molting Stage

Comparative Proteome Analysis Reveals that Cuticular Proteins Analogous to Peritrophin‐Motif Proteins are Involved in the Regeneration of Chitin Layer in the Silk Gland of Bombyx mori at the Molting Stage

Inhibition of silkworm vacuolar‐type ATPase activity by its inhibitor Bafilomycin A1 induces caspase‐dependent apoptosis in an embryonic cell line of silkworm

Proteome profile of spinneret from the silkworm, Bombyx mori

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