Wang Y et al. (2020), Investigation of structural proteins in sea cuc...

ECB-ART-49518

Sci Rep 2020 Oct 30;101:18744. doi: 10.1038/s41598-020-75580-x.

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Investigation of structural proteins in sea cucumber (Apostichopus japonicus) body wall.

Wang Y , Tian M , Chang Y , Xue C , Li Z .

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Structural proteins play critical roles in the food quality, especially texture properties, of sea cucumbers and their products. Most of the previous studies on sea cucumbers focused on few individual proteins, which limited our understanding of how structural proteins influenced the quality of sea cucumbers. Inspired by the clarification of sea cucumber (Apostichopus japonicus) genome, we established an integrated data of structural proteins in the sea cucumber body wall. A portfolio of 2018 structural proteins was screened out from the sea cucumber annotated proteome by bioinformatics analysis. The portfolio was divided into three divisions, including extracellular matrix proteins, muscle proteins, and proteases, and further classified into 18 categories. The presence of 472 proteins in the sea cucumber body wall was confirmed by using a proteomics approach. Moreover, comparative proteomics analysis revealed the spatial distribution heterogeneity of structural proteins in the sea cucumber body wall at a molecular scale. This study suggested that future researches on sea cucumbers could be performed from an integrated perspective, which would reshape the component map of sea cucumber and provide novel insights into the understanding of how the food quality of sea cucumber was determined on a molecular level.

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References [+] :

Ackermann, Myosin binding protein-C: a regulator of actomyosin interaction in striated muscle. 2011, Pubmed

	Figure 1. Experimental coverage of in silico identified structural proteins.
	Figure 2. List of collagens and proteoglycans in the sea cucumber body wall detected by using iTRAQ-based mass spectrometry.
	Figure 3. List of major extracellular matrix glycoproteins in the sea cucumber body wall detected by using iTRAQ-based mass spectrometry.
	Figure 4. List of muscle proteins with signficantly different abundances (fold change ≥ 1.5 or ≤ 0.67) among samples from different spatial locations of sea cucumber body wall detected by using iTRAQ-based mass spectrometry.
	Figure 5. List of proteases with signficantly different abundances (fold change ≥ 1.5 or ≤ 0.67) among samples from different spatial locations of sea cucumber body wall detected by using iTRAQ-based mass spectrometry.