Antiapoptotic activity of 30 kDa lipoproteins family from fat body tissue of silkworm, <i>Bombyx mori</i>

Pakkianathan, Britto Cathrin; Singh, Nitin Kumar; König, Simone; Krishnan, Muthukalingan

doi:10.1111/1744-7917.12119

Cited by 10 publications

(7 citation statements)

References 52 publications

(72 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…This result was an update from a previous analysis based on the newly identified 30K proteins in the UniProt database, as in previous analysis, we only identified 11 acetylated 30K proteins containing 23 Kac sites (Nie et al, ). As members of the lipoprotein family, 30K proteins mainly perform the lipid loading (J. P. Yang et al, ) and antiapoptosis functions (E. J. Kim et al, ; E. J. Kim, Rhee, & Park, ; M. Y. Kim et al, ; Pakkianathan et al, ; Yu et al, ). The widespread acetylation of B. mori 30K proteins might suggest important roles of acetylation with respect to the function of 30K proteins in silkworms, which requires additional studies.…”

Section: Resultsmentioning

confidence: 99%

“…J. Kim, Rhee, & Park, 2001; M. Y. Kim et al, 2012;Pakkianathan et al, 2015;Yu et al, 2013). The widespread acetylation of B. mori 30K proteins might suggest important roles of acetylation with respect to the function of 30K proteins in silkworms, which requires additional studies.…”

Section: Acetylation Profiles Of 30k Proteins In B Morimentioning

confidence: 99%

“…Because these proteins have molecular weights of approximately 30 kDa, they are named 30K proteins (Tojo, Betchaku, Ziccardi, & Wyatt, ). Previous studies have shown that the 30K proteins not only have the function of lipid loading (J. P. Yang et al, ) but also have a significant suppressive effect on mammalian and insect cell apoptosis (E. J. Kim, Park, & Park, ; M. Y. Kim et al, ; Pakkianathan, Singh, Konig, & Krishnan, ; Yu, Li, Yao, Quan, & Zhang, ). In addition, 30K proteins also perform other important functions, such as anti‐fungus (Li et al, ; Ujita et al, ), protein delivery (Park et al, ), and production and sialylation of recombinant proteins (Koo, Park, Park, & Park, ; Z. Wang, Park, Park, Tan, & Park, ).…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

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

View full text Add to dashboard Cite

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.

show abstract

Section: Resultsmentioning

confidence: 99%

Section: Acetylation Profiles Of 30k Proteins In B Morimentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

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

View full text Add to dashboard Cite

show abstract

“…Silkworm eggs were obtained from the Bursa Kozabirlik Company, Turkey, and reared in the laboratory at 26 ± 1°C and 75 ± 5 % relative humidity on fresh mulberry leaves (Li et al 2012;Pakkianathan et al 2015). Stages of insects were selected as 3rd (the youngest sample) and 5th (young) larval instar, motionless prepupa (the oldest sample) and 13 dayold pupa (adult development).…”

Section: Methodsmentioning

confidence: 99%

Monosaccharide profiling of silkworm (Bombyx mori L.) nervous system during development and aging

2016

View full text Add to dashboard Cite

Glycoconjugates have various functions in differentiation, development, aging and in all aspects of normal functioning of organisms. The reason for increased research on this topic is that glycoconjugates locate mostly on the cell surface and play crucial biological roles in the nervous system including brain development, synaptic plasticity, learning, and memory. Considering their roles in the nervous system, information about their existence in the insect nervous system is rather sparse. Therefore, in order to detect monosaccharide content of N- and O-glycans, we carried out capLC-ESI-MS/MS analysis to determine the concentration changes of glucose, mannose, galactose, N-acetylglucosamine (GlcNAc), N-acetylgalactosamine (GalNAc), fucose, xylose, arabinose, and ribose monosaccharides in the nervous system of Bombyx mori during development and aging processes. In addition to LC-MS, lectin blotting was done to detect quantitative changes in N- and O-glycans. Developmental stages were selected as 3rd (the youngest sample), 5th (young) larval instar, motionless prepupa (the oldest sample), and pupa (adult development). Derivatization of monosaccharides was performed with a solution of PMP agent and analyzed with capLC-ESI-MS/MS. For lectin blotting, determination of glycan types was carried out with Galanthus nivalis agglutinin and Peanut agglutinin lectins. In all stages, the most abundant monosaccharide was glucose. Although all monosaccharides were present most abundantly in the youngest stage (3rd instar), they are generally reduced gradually during the aging process. It was observed that amounts of monosaccharides increased again in the pupa stage. According to lectin blotting, N- and O-linked glycoproteins expressions were different and there were some specific glycoprotein expression differences between stages. These findings suggest that the glycosylation state of proteins in the nervous system changes during development and aging in insects in a similar fashion to that reported for vertebrates.

show abstract

“…Studies with Bombyx mori hemolymph demonstrated beneficial effects on lepidopteran cells and various rodent and human cell lines (Rhee and Park, 2000;Rhee et al, 2002;Park et al, 2003;Kim et al, 2004;Yu et al, 2013). A group of approximately 30 proteins (named 30K protein family due to their molecular sizes around 30 kDa) was identified to promote cell survival, with individual proteins contributing some portion of the protective effects (Kim et al, 2001(Kim et al, , 2003(Kim et al, , 2004Rhee et al, 2002;Park et al, 2003;Zhong et al, 2005;Yu et al, 2013;Pakkianathan et al, 2015). Protective effects of these 30K proteins seem to be mediated (at least to a large extent) by adhesion to cellular membranes rather than by activation of a particular receptor.…”

Section: Introductionmentioning

confidence: 99%

Locust Hemolymph Conveys Erythropoietin-Like Cytoprotection via Activation of the Cytokine Receptor CRLF3

et al. 2021

View full text Add to dashboard Cite

The cytokine receptor-like factor 3 (CRLF3) is an evolutionary conserved class 1 cytokine receptor present in all major eumetazoan groups. Endogenous CRLF3 ligands have not been identified and the physiological responses mediated by mammalian CRLF3 are poorly characterized. Insect CRLF3 is activated by erythropoietin (Epo) and several related molecules that protect mammalian neurons from stress-induced apoptosis. However, insects neither express Epo nor “classical” Epo receptor. Cell-protective effects of insect hemolymph have been described for several species. In this study, we explored the possibility that the endogenous CRLF3 ligand is contained in locust hemolymph. PCR analyses confirmed expression of crfl3-transcripts in neurons and hemocytes of Locusta migratoria and Tribolium castaneum. Survival of locust hemocytes in primary cultures was significantly increased by supplementation of culture medium with locust hemolymph serum. Locust primary neuron cultures were also protected by locust hemolymph, though preceding exposure to fetal bovine serum changed the hemolymph dose-dependency of neuroprotection. Direct comparison of 10% hemolymph serum with recombinant human Epo in its optimal neuroprotective concentration revealed equivalent anti-apoptotic effects on hypoxia-exposed locust neurons. The same concentration of locust hemolymph serum also protected hypoxia-exposed T. castaneum neurons. This indicates that the neuroprotective factor in locust hemolymph is sufficiently conserved in insects to allow activation of neuroprotective receptors in different species. Locust hemolymph-induced neuroprotection in both L. migratoria and T. castaneum was abolished after RNAi-mediated suppression of crlf3-expression. In summary, we report the presence of a conserved endogenous cytokine in locust hemolymph that activates CRLF3 and connected anti-apoptotic processes in hemocytes and neurons. Identification and characterization of the CRLF3 ligand will promote knowledge about cytokine evolution and may unravel cell-protective agents with potential clinical application.

show abstract

Antiapoptotic activity of 30 kDa lipoproteins family from fat body tissue of silkworm, Bombyx mori

Cited by 10 publications

References 52 publications

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

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

Monosaccharide profiling of silkworm (Bombyx mori L.) nervous system during development and aging

Locust Hemolymph Conveys Erythropoietin-Like Cytoprotection via Activation of the Cytokine Receptor CRLF3

Contact Info

Product

Resources

About