TY - JOUR
T1 - Differential expression of proteins and phosphoproteins during larval metamorphosis of the polychaete Capitella sp. I
AU - Chandramouli, Kondethimmanahalli
AU - Soo, Lisa
AU - Qian, Pei-Yuan
N1 - KAUST Repository Item: Exported on 2020-10-01
Acknowledged KAUST grant number(s): SA-C0040, UK-C0016
Acknowledgements: The authors thank Mr. Y Zhang for his technical help in generating the 2-DE gels and Mr. Yue Him Wong for help with RT-PCR. We are also thankful to Dr. On On Lee for critically reviewing the manuscript and Cherry Kwan for proof-reading the manuscript. This study was supported by an award from the King Abdullah University of Science and Technology (SA-C0040/UK-C0016) and a grant from the Research Grants Council of the Hong Kong Special Administrative Region (AoE/P-04/04-II) to P.-Y. Qian.
This publication acknowledges KAUST support, but has no KAUST affiliated authors.
PY - 2011/9/3
Y1 - 2011/9/3
N2 - Background: The spontaneous metamorphosis of the polychaete Capitella sp. I larvae into juveniles requires minor morphological changes, including segment formation, body elongation, and loss of cilia. In this study, we investigated changes in the expression patterns of both proteins and phosphoproteins during the transition from larvae to juveniles in this species. We used two-dimensional gel electrophoresis (2-DE) followed by multiplex fluorescent staining and MALDI-TOF mass spectrometry analysis to identify the differentially expressed proteins as well as the protein and phosphoprotein profiles of both competent larvae and juveniles.Results: Twenty-three differentially expressed proteins were identified in the two developmental stages. Expression patterns of two of those proteins were examined at the protein level by Western blot analysis while seven were further studied at the mRNA level by real-time PCR. Results showed that proteins related to cell division, cell migration, energy storage and oxidative stress were plentifully expressed in the competent larvae; in contrast, proteins involved in oxidative metabolism and transcriptional regulation were abundantly expressed in the juveniles.Conclusion: It is likely that these differentially expressed proteins are involved in regulating the larval metamorphosis process and can be used as protein markers for studying molecular mechanisms associated with larval metamorphosis in polychaetes. © 2011 Chandramouli et al; licensee BioMed Central Ltd.
AB - Background: The spontaneous metamorphosis of the polychaete Capitella sp. I larvae into juveniles requires minor morphological changes, including segment formation, body elongation, and loss of cilia. In this study, we investigated changes in the expression patterns of both proteins and phosphoproteins during the transition from larvae to juveniles in this species. We used two-dimensional gel electrophoresis (2-DE) followed by multiplex fluorescent staining and MALDI-TOF mass spectrometry analysis to identify the differentially expressed proteins as well as the protein and phosphoprotein profiles of both competent larvae and juveniles.Results: Twenty-three differentially expressed proteins were identified in the two developmental stages. Expression patterns of two of those proteins were examined at the protein level by Western blot analysis while seven were further studied at the mRNA level by real-time PCR. Results showed that proteins related to cell division, cell migration, energy storage and oxidative stress were plentifully expressed in the competent larvae; in contrast, proteins involved in oxidative metabolism and transcriptional regulation were abundantly expressed in the juveniles.Conclusion: It is likely that these differentially expressed proteins are involved in regulating the larval metamorphosis process and can be used as protein markers for studying molecular mechanisms associated with larval metamorphosis in polychaetes. © 2011 Chandramouli et al; licensee BioMed Central Ltd.
UR - http://hdl.handle.net/10754/334584
UR - http://proteomesci.biomedcentral.com/articles/10.1186/1477-5956-9-51
UR - http://www.scopus.com/inward/record.url?scp=80052215711&partnerID=8YFLogxK
U2 - 10.1186/1477-5956-9-51
DO - 10.1186/1477-5956-9-51
M3 - Article
C2 - 21888661
SN - 1477-5956
VL - 9
SP - 51
JO - Proteome Science
JF - Proteome Science
IS - 1
ER -