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Proteomic and bioinformatic analysis on endocrine organs of domesticated silkworm, Bombyx mori L. for a comprehensive understanding of their roles and relations.
- Source :
-
Journal of proteome research [J Proteome Res] 2009 Jun; Vol. 8 (6), pp. 2620-32. - Publication Year :
- 2009
-
Abstract
- Three organs of silkworm larva endocrine system, including brain (Br), subesophageal ganglion (SG) and prothoracic glands (PG), were studied employing shotgun LC-MS/MS combined with bioinformatic analysis to comprehensively understand their roles and relations. Totally, 3430, 2683, and 3395 proteins were identified including 1885 common and 652, 253, and 790 organ-specific ones in Br, SG, and PG, respectively. Identified common-expressed proteins indicated the existence of intrinsic complex interactions among these parts of endocrine system. Most of the reputed organs-specific proteins were identified by this approach. KEGG pathway analysis showed 162 same pathways among the 169, 164, and 171 relating Br, SG, and PG. This analysis revealed functional similarities with exceptional resemblance in their metabolism and signaling pathways of the three organs. On the other hand, 70, 57, and 114 organ-specific enzymes related pathways were detected for Br, SG, and PG confirming their functional differences. These results reveal a cooperative mechanism among the three endocrine organs in regulating various physiological and developmental events, and also suggest that the organ-specific proteins might be the fundamental factors responsible for the functional differentiation of these organs.
- Subjects :
- Animals
Bombyx genetics
Bombyx physiology
Chromatography, Liquid
Computational Biology
Endocrine Glands chemistry
Endocrine Glands metabolism
Gene Expression
Insect Proteins genetics
Insulin metabolism
Metamorphosis, Biological
Models, Biological
Proteomics
Reproducibility of Results
Signal Transduction
Tandem Mass Spectrometry
Bombyx metabolism
Insect Proteins metabolism
Proteome metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1535-3893
- Volume :
- 8
- Issue :
- 6
- Database :
- MEDLINE
- Journal :
- Journal of proteome research
- Publication Type :
- Academic Journal
- Accession number :
- 19382758
- Full Text :
- https://doi.org/10.1021/pr8006123