Increase of 30K protein in identified motoneurons by hemolymph results in inhibition of programmed cell death in silkworm, Bombyx mori (Lepidoptera, Bombycidae)

Song, Hoyoung; Kim, Mi Young; Kim, Bo Yong; Park, Sun Whan; Sung, Dong Kyoung; Kang, Pil Don; Park, Cheolin; Jeon, Soung Hoo; Lee, Bong Hee

doi:10.1016/j.jinsphys.2012.03.004

Cited by 9 publications

(5 citation statements)

References 36 publications

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“…In previous studies, 30K proteins have been shown to play a role in antiapoptosis (Kim et al ., , , ; Kim & Park, ; Choi et al ., ; Song et al ., ). At the PP stage and on PP1, genomic DNA is gradually concentrated in SG, and it is rapidly and completely degraded on PP1 according to the DNA ladder.…”

Section: Discussionmentioning

confidence: 97%

“…These results imply that the 30K proteins are involved in the degeneration of the Bombyx SG. It has been reported that the Bombyx haemolymph increases expression level of the 30Kc6 protein‐encoding gene in Bombyx motorneurones (Song et al ., ); however, the exact factors in these processes still remain unknown.…”

Section: Discussionmentioning

confidence: 99%

“…30Kc6 protein inhibits apoptosis in human and insect cells (Kim et al ., ; Kim & Park, ; Choi et al ., ). It is gradually synthesized in the Bombyx motorneurones and results in inhibition of programmed cell death in vitro by blocking ultraspiracle binding to ecdysone receptor‐B1 (EcR‐B1) through the formation of a 30K/EcR‐B1 complex (Kim et al ., ; Song et al ., ). 30Kc19 is not only an apoptosis‐inhibiting factor but also perhaps a proteinaceous factor involved in the uptake of the chymotrypsin inhibitor (CI‐8) into the midgut through the membrane (Kim et al ., ; Ueno et al ., ).…”

Section: Introductionmentioning

confidence: 97%

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Functional analysis of 30K proteins during silk gland degeneration by a caspase‐dependent pathway in Bombyx

et al. 2013

Insect Molecular Biology

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The 30K proteins are involved with important functions in the growth and development of Bombyx mori. In this study, the synthesis and regulation of 30K proteins were examined during the degeneration of Bombyx silk glands. On day 3 of the fifth instar, the protein level of 30Kc19 was low, whereas the silk proteins were rapidly synthesized. However, synthesis and accumulation of the 30Kc19 protein significantly increased at the prepupal stage and on day 1 of the pupal stage. At this stage, the silk gland cells were filled with 30Kc19 and genomic DNA. Moreover, the transcript levels of the 30K-encoding genes, including 30Kc6, 30Kc12, 30Kc19 and 30Kc23 were up-regulated during the degeneration of the Bombyx silk glands. During the time that the levels of the 30Kc19 protein were significantly up-regulated, it is notable that the transcript levels of the BmAtg8, BmAtg6 and BmDronc genes dramatically increased to regulate the programmed cell death of this gland. On day 1 of the pupal stage, intense fragmentation of genomic DNA occurred in the silk gland cells, and the putative active form of caspase was detected in the cytoplasm, showing the complete degradation of the silk glands in one day. In conclusion, the 30K proteins are synthesized in high concentrations, while proteolysis mediates silk gland degeneration in Bombyx by a caspase-dependent pathway. We propose that the 30K proteins may be nutrients and energy vectors to be absorbed by the developing tissues of pupae or moths.

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Section: Discussionmentioning

confidence: 97%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 97%

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Functional analysis of 30K proteins during silk gland degeneration by a caspase‐dependent pathway in Bombyx

et al. 2013

Insect Molecular Biology

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“…Many reports showed the apoptosis‐inhibitory activity of 30K proteins was comparable to that of whole silkworm hemolymph (Kim et al, 2001, 2004; Kim et al, 2003; Yu et al, 2013). In addition, the increase in 30K protein synthesis results in the suppression of programmed cell death (PCD) of APR6 motor neurons (Song et al, 2012; Wang et al, 2016). The in vitro expression of the Bm30K‐19G1 protein also inhibits conidial germination and hyphal growth in B. bassiana (Li et al, 2019).…”

Section: Discussionmentioning

confidence: 99%

The acetylation modification regulates the stability of Bm30K‐15 protein and its mechanism in silkworm, Bombyx mori

Liu

et al. 2021

Arch Insect Biochem Physiol

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The 30 K proteins are the major silkworm hemolymph proteins and are involved in a variety of physiological processes, such as nutrient and energy storage, embryogenesis, immune response, and inhibition of apoptosis. The Bm30K‐15 protein is one of the 30 K proteins and is abundant in the hemolymph of fifth instar silkworm larva. We previously found that the Bm30K‐15 protein can be acetylated. In the present study, we found that acetylation can improve the protein stability of Bm30K‐15. Further exploration confirmed that the increase in protein stability by acetylation was caused by competition between acetylation and ubiquitination. In summary, these findings aim to provide insight into the effect of acetylation modification on the protein level and stability of the Bm30K‐15 and the possible molecular mechanism of its existence in silkworm, Bombyx mori.

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“…Bombyx mori is an important economic and model Lepidoptera insect (Abdelli, Peng, & Keping, ; International Silkworm Genome, ). The 30K proteins are low‐density lipoproteins that are the most abundant proteins in the hemolymph of B. mori , are synthesized from silkworm fat bodies and are important nutrient storage proteins during silkworm growth and development (Song et al, ; X. F. Shi, Li, Yi, Xiao, & Zhang, ). Because these proteins have molecular weights of approximately 30 kDa, they are named 30K proteins (Tojo, Betchaku, Ziccardi, & Wyatt, ).…”

Section: Introductionmentioning

confidence: 99%

The stability and antiapoptotic activity of Bm30K‐3 can be improved by lysine acetylation in the silkworm, Bombyx mori

Liu

et al. 2019

Arch Insect Biochem Physiol

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Acetylation is an important, highly conserved, and reversible post‐translational modification of proteins. Previously, we showed by nano‐HPLC/MS/MS that many nutrient storage proteins in the silkworm are acetylated. Among these proteins, most of the known 30K proteins were shown to be acetylated, including 23 acetylated 30K proteins containing 49 acetylated sites (Kac), indicating the importance of the acetylation of 30K proteins in silkworm. In this study, Bm30K‐3, a 30K protein containing three Kac sites, was further assessed in functional studies of its acetylation. Increasing the level of Bm30K‐3 acetylation by adding the deacetylase inhibitor trichostatin A (TSA) increased the levels of this protein and further inhibited cellular apoptosis induced by H2O2. In contrast, decreasing the level of acetylation by adding the acetylase inhibitor C646 could reduce the level of Bm30K‐3 and increase H2O2‐induced apoptosis. Subsequently, BmN cells were treated with CHX and MG132, and increasing the acetylation level using TSA was shown to inhibit protein degradation and improve the stability of Bm30K‐3. Furthermore, the acetylation of Bm30K‐3 could compete with its ability to be ubiquitinated, suggesting that acetylation could inhibit the ubiquitin‐mediated proteasome degradation pathway, improving the stability and accumulation of proteins in cells. These results further indicate that acetylation might regulate nutrition storage and utilization in Bombyx mori, which requires further study.

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Increase of 30K protein in identified motoneurons by hemolymph results in inhibition of programmed cell death in silkworm, Bombyx mori (Lepidoptera, Bombycidae)

Cited by 9 publications

References 36 publications

Functional analysis of 30K proteins during silk gland degeneration by a caspase‐dependent pathway in Bombyx

Functional analysis of 30K proteins during silk gland degeneration by a caspase‐dependent pathway in Bombyx

The acetylation modification regulates the stability of Bm30K‐15 protein and its mechanism in silkworm, Bombyx mori

The stability and antiapoptotic activity of Bm30K‐3 can be improved by lysine acetylation in the silkworm, Bombyx mori

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