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Proteomic analysis during larval development and metamorphosis of the spionid polychaete Pseudopolydora vexillosa
BACKGROUND: While the larval-juvenile transition (metamorphosis) in the spionid polychaete Pseudopolydora vexillosa involves gradual morphological changes and does not require substantial development of juvenile organs, the opposite occurs in the barnacle Balanus amphitrite. We hypothesized that the...
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Formato: | Texto |
Lenguaje: | English |
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BioMed Central
2009
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2803448/ https://www.ncbi.nlm.nih.gov/pubmed/20003395 http://dx.doi.org/10.1186/1477-5956-7-44 |
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author | Mok, Flora SY Thiyagarajan, Vengatesen Qian, Pei-Yuan |
author_facet | Mok, Flora SY Thiyagarajan, Vengatesen Qian, Pei-Yuan |
author_sort | Mok, Flora SY |
collection | PubMed |
description | BACKGROUND: While the larval-juvenile transition (metamorphosis) in the spionid polychaete Pseudopolydora vexillosa involves gradual morphological changes and does not require substantial development of juvenile organs, the opposite occurs in the barnacle Balanus amphitrite. We hypothesized that the proteome changes during metamorphosis in the spionids are less drastic than that in the barnacles. To test this, proteomes of pre-competent larvae, competent larvae (ready to metamorphose), and juveniles of P. vexillosa were compared using 2-dimensional gel electrophoresis (2-DE), and they were then compared to those of the barnacle. RESULTS: Unlike the significant changes found during barnacle metamorphosis, proteomes of competent P. vexillosa larvae were more similar to those of their juveniles. Pre-competent larvae had significantly fewer protein spots (384 spots), while both competent larvae and juveniles expressed about 660 protein spots each. Proteins up-regulated during competence identified by MALDI-TOF/TOF analysis included a molecular chaperon (calreticulin), a signal transduction regulator (tyrosin activation protein), and a tissue-remodeling enzyme (metallopeptidase). CONCLUSIONS: This was the first time to study the protein expression patterns during the metamorphosis of a marine polychaete and to compare the proteomes of marine invertebrates that have different levels of morphological changes during metamorphosis. The findings provide promising initial steps towards the development of a proteome database for marine invertebrate metamorphosis, thus deciphering the possible mechanisms underlying larval metamorphosis in non-model marine organisms. |
format | Text |
id | pubmed-2803448 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2009 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-28034482010-01-09 Proteomic analysis during larval development and metamorphosis of the spionid polychaete Pseudopolydora vexillosa Mok, Flora SY Thiyagarajan, Vengatesen Qian, Pei-Yuan Proteome Sci Research BACKGROUND: While the larval-juvenile transition (metamorphosis) in the spionid polychaete Pseudopolydora vexillosa involves gradual morphological changes and does not require substantial development of juvenile organs, the opposite occurs in the barnacle Balanus amphitrite. We hypothesized that the proteome changes during metamorphosis in the spionids are less drastic than that in the barnacles. To test this, proteomes of pre-competent larvae, competent larvae (ready to metamorphose), and juveniles of P. vexillosa were compared using 2-dimensional gel electrophoresis (2-DE), and they were then compared to those of the barnacle. RESULTS: Unlike the significant changes found during barnacle metamorphosis, proteomes of competent P. vexillosa larvae were more similar to those of their juveniles. Pre-competent larvae had significantly fewer protein spots (384 spots), while both competent larvae and juveniles expressed about 660 protein spots each. Proteins up-regulated during competence identified by MALDI-TOF/TOF analysis included a molecular chaperon (calreticulin), a signal transduction regulator (tyrosin activation protein), and a tissue-remodeling enzyme (metallopeptidase). CONCLUSIONS: This was the first time to study the protein expression patterns during the metamorphosis of a marine polychaete and to compare the proteomes of marine invertebrates that have different levels of morphological changes during metamorphosis. The findings provide promising initial steps towards the development of a proteome database for marine invertebrate metamorphosis, thus deciphering the possible mechanisms underlying larval metamorphosis in non-model marine organisms. BioMed Central 2009-12-14 /pmc/articles/PMC2803448/ /pubmed/20003395 http://dx.doi.org/10.1186/1477-5956-7-44 Text en Copyright ©2009 Mok et al; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Mok, Flora SY Thiyagarajan, Vengatesen Qian, Pei-Yuan Proteomic analysis during larval development and metamorphosis of the spionid polychaete Pseudopolydora vexillosa |
title | Proteomic analysis during larval development and metamorphosis of the spionid polychaete Pseudopolydora vexillosa |
title_full | Proteomic analysis during larval development and metamorphosis of the spionid polychaete Pseudopolydora vexillosa |
title_fullStr | Proteomic analysis during larval development and metamorphosis of the spionid polychaete Pseudopolydora vexillosa |
title_full_unstemmed | Proteomic analysis during larval development and metamorphosis of the spionid polychaete Pseudopolydora vexillosa |
title_short | Proteomic analysis during larval development and metamorphosis of the spionid polychaete Pseudopolydora vexillosa |
title_sort | proteomic analysis during larval development and metamorphosis of the spionid polychaete pseudopolydora vexillosa |
topic | Research |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2803448/ https://www.ncbi.nlm.nih.gov/pubmed/20003395 http://dx.doi.org/10.1186/1477-5956-7-44 |
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