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Molecular Biology Reports

, Volume 39, Issue 8, pp 8447–8456 | Cite as

Comparative proteomic and phosphoproteomic analysis of the silkworm (Bombyx mori) posterior silk gland under high temperature treatment

  • Jisheng Li
  • Lupeng Ye
  • Tianyun Lan
  • Meilan Yu
  • Jianshe Liang
  • Boxiong Zhong
Article

Abstract

The proteins from the posterior silk gland of silkworm hybrids and their parents reared under high temperatures were studied by using comparative proteomic and phosphoproteomic analysis. A total of 82.07, 6.17 and 11.76 % protein spots showed additivity, overdominance and underdominance patterns, respectively. Fifteen differentially expressed protein spots were identified by peptide mass fingerprinting. Among these, four spots, including sHSPs and prohibitin protein that were directly relevant to heat response, were identified. Eleven protein spots were found to play an important role in silk synthesis, and nine protein spots expressed phosphorylation states. According to Gene ontology and KEGG pathway analysis, these nine spots played an important role in stress-induced signal transduction. Expression of most silk synthesis-related proteins was reduced, whereas stress-responsive proteins increased with heat exposure time in three breeds. Furthermore, most proteins showed under- or overdominance in the hybrids compared to the parents. The results suggested that high temperature could alter the expression of proteins related to silk synthesis and heat response in silkworm. Moreover, differentially expressed proteins occurring in the hybrid and its parents may be the main explanation of the observed heterosis.

Keywords

Bombyx mori Posterior silk gland Phosphoproteomic 2D electrophoresis MALDI-TOF/TOF MS 

Abbreviations

2-DE

Two-dimensional gel electrophoresis

MS

Mass spectrum

QB

Qiufeng × Baiyu

Q

Qiufeng

B

Baiyu

ADK

Adenosine kinase

EF

Elongation factor

GO

Gene ontology

Notes

Acknowledgments

This work was supported by the National Basic Research Program of China (Grant No. 2012CB114601) and the National Nature Science Foundation of China (Grant No. 30972142).

Supplementary material

11033_2012_1698_MOESM1_ESM.doc (4.5 mb)
Supplementary material 1 (DOC 4634 kb)

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Copyright information

© Springer Science+Business Media B.V. 2012

Authors and Affiliations

  • Jisheng Li
    • 1
    • 4
  • Lupeng Ye
    • 1
  • Tianyun Lan
    • 1
  • Meilan Yu
    • 2
  • Jianshe Liang
    • 3
  • Boxiong Zhong
    • 1
  1. 1.College of Animal SciencesZhejiang UniversityHangzhouPeople’s Republic of China
  2. 2.College of Life SciencesZhejiang University of Science and TechnologyHangzhouPeople’s Republic of China
  3. 3.College of Environmental and Resource SciencesZhejiang UniversityHangzhouPeople’s Republic of China
  4. 4.Institute of SericultureChengde Medical UniversityChengdePeople’s Republic of China

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