Shotgun proteomic analysis on the embryos of silkworm Bombyx mori at the end of organogenesis

Li, Jianying; Moghaddam, Seyed Hossein Hosseini; Chen, Jine; Chen, Ming; Zhong, Boxiong

doi:10.1016/j.ibmb.2010.01.008

Cited by 18 publications

(16 citation statements)

References 38 publications

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“…The relative concentration of a protein identified by MS in a biological sample is directly related to the number of identified peptides, neglecting possible effects such as the enzymatic digestion constraint, the detection mass range of the mass spectrometer and differential post-translational modifications. Therefore the number of identified unique peptides assembled into a protein may reflect the protein’s relative abundance [25], [41]. So according to the amount of identified unique peptides, vitellogenin precursor, egg-specific protein, low molecular lipoprotein 30 K precursor, and some predicted proteins such as BGIBMGA013342-PA, BGIBMGA004585-PA and BGIBMGA004399-PA are highly represented in the samples.…”

Section: Resultsmentioning

confidence: 99%

“…Database search was carried out against the in-house database [34], with the protein sequences downloaded from NCBInr protein database (http://www.ncbi.nlm.nih.gov/) including the domesticated silkworm ( B.mori ,2224 entries), the wild silkworm ( B. mandarina ,13 entries) and the fruit fly ( D. melanogaster , 27777 entries), along with predicted B. mori protein sequence data (14,623 entries) [35]. _The four raw datasets of ND and D samples were searched against the in-house database on a local server using Turbo SEQUEST software (Bioworks version 3.2, Thermo Finnigan).…”

Section: Methodsmentioning

confidence: 99%

“…Another relevant approach in proteomics for large-scale characterization of proteome profiles is shotgun proteomics, which is based on in-gel or gel free digestion of protein mixtures followed by liquid chromatography tandem mass spectrometry (LC-MS/MS) separation, MS detection and database searching, and provides an extremely sensitive and high-throughput approach to determine the proteome components in a complex biological sample. This approach has been widely used in many organisms, such as Bombyx mori [23], [24], [25], Homo sapiens [26], [27] and Orientia tsutsugamushi [28], [29].…”

Section: Introductionmentioning

confidence: 99%

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Shotgun Proteomic Analysis on the Diapause and Non-Diapause Eggs of Domesticated Silkworm Bombyx mori

et al. 2013

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To clarify the molecular mechanisms of silkworm diapause, it is necessary to investigate the molecular basis at protein level. Here, the spectra of peptides digested from silkworm diapause and non-diapause eggs were obtained from liquid chromatography tandem mass spectrometry (LC-MS/MS) and were analyzed by bioinformatics methods. A total of 501 and 562 proteins were identified from the diapause and non-diapause eggs respectively, of which 309 proteins were shared commonly. Among these common-expressed proteins, three main storage proteins (vitellogenin precursor, egg-specific protein and low molecular lipoprotein 30 K precursor), nine heat shock proteins (HSP19.9, 20.1, 20.4, 20.8, 21.4, 23.7, 70, 90-kDa heat shock protein and heat shock cognate protein), 37 metabolic enzymes, 22 ribosomal proteins were identified. There were 192 and 253 unique proteins identified in the diapause and non-diapause eggs respectively, of which 24 and 48 had functional annotations, these unique proteins indicated that the metabolism, translation of the mRNA and synthesis of proteins were potentially more highly represented in the non-dipause eggs than that in the diapause eggs. The relative mRNA levels of four identified proteins in the two kinds of eggs were also compared using quantitative reverse transcription PCR (qRT-PCR) and showed some inconsistencies with protein expression. GO signatures of 486 out of the 502 and 545 out of the 562 proteins identified in the diapause and non-diapause eggs respectively were available. In addition, Kyoto Encyclopedia of Genes and Genomes (KEGG) pathway analysis showed the Metabolism, Translation and Transcription pathway were potentially more active in the non-dipause eggs at this stage.

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Section: Resultsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Shotgun Proteomic Analysis on the Diapause and Non-Diapause Eggs of Domesticated Silkworm Bombyx mori

et al. 2013

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“…However, information on carboxypeptidases is still limited. The carboxypeptidase gene MF-CPA from silkworm molting fluid has been previously cloned, characterized [18] and identified in the embryos at the end of the organogenesis [19]. Since silkworm genome sequencing is completed, it is possible to identify the carboxypeptidases family members in the whole genome of silkworm, B. mori [20,21,22].…”

Section: Introductionmentioning

confidence: 99%

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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“…In recent years, the shotgun proteome technology becomes powerful in large-scale proteomic analyses. Various proteome profiles of silkworm tissues have been established covering head [16], integument [17], midgut [18], fat baby [19], embryos [20], peritrophic membrane [21], as well as some endocrine Organs [22]. In this study, Shotgun and 2-DE followed by MALDI-TOF MS were attempted to analyze the proteome profile of silkworm MTs from Day-5 fifth instar larvae.…”

Section: Introductionmentioning

confidence: 99%

Proteomic-Based Insight into Malpighian Tubules of Silkworm Bombyx mori

et al. 2013

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Malpighian tubules (MTs) are highly specific organs of arthropods (Insecta, Myriapoda and Arachnida) for excretion and osmoregulation. In order to highlight the important genes and pathways involved in multi-functions of MTs, we performed a systematic proteomic analysis of silkworm MTs in the present work. Totally, 1,367 proteins were identified by one-dimensional gel electrophoresis coupled with liquid chromatography-tandem mass spectrometry, and as well as by Trans Proteomic Pipeline (TPP) and Absolute protein expression (APEX) analyses. Forty-one proteins were further identified by two-dimensional gel electrophoresis. Some proteins were revealed to be significantly associated with various metabolic processes, organic solute transport, detoxification and innate immunity. Our results might lay a good foundation for future functional studies of MTs in silkworm and other lepidoptera.

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Shotgun proteomic analysis on the embryos of silkworm Bombyx mori at the end of organogenesis

Cited by 18 publications

References 38 publications

Shotgun Proteomic Analysis on the Diapause and Non-Diapause Eggs of Domesticated Silkworm Bombyx mori

Shotgun Proteomic Analysis on the Diapause and Non-Diapause Eggs of Domesticated Silkworm Bombyx mori

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

Proteomic-Based Insight into Malpighian Tubules of Silkworm Bombyx mori

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