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A START-domain-containing protein is a novel marker of nervous system components of the sea cucumber Holothuria glaberrima.

Authors :
Rosado-Olivieri EA
Ramos-Ortiz GA
Hernández-Pasos J
Díaz-Balzac CA
Vázquez-Rosa E
Valentín-Tirado G
Vega IE
García-Arrarás JE
Source :
Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology [Comp Biochem Physiol B Biochem Mol Biol] 2017 Dec; Vol. 214, pp. 57-65. Date of Electronic Publication: 2017 Aug 31.
Publication Year :
2017

Abstract

One of the main challenges faced by investigators studying the nervous system of members of the phylum Echinodermata is the lack of markers to identify nerve cells and plexi. Previous studies have utilized an antibody, RN1, that labels most of the nervous system structures of the sea cucumber Holothuria glaberrima and other echinoderms. However, the antigen recognized by RN1 remained unknown. In the present work, the antigen has been characterized by immunoprecipitation, tandem mass spectrometry, and cDNA cloning. The RN1 antigen contains a START lipid-binding domain found in Steroidogenic Acute Regulatory (StAR) proteins and other lipid-binding proteins. Phylogenetic tree assembly showed that the START domain is highly conserved among echinoderms. We have named this antigen HgSTARD10 for its high sequence similarity to the vertebrate orthologs. Gene and protein expression analyses revealed an abundance of HgSTARD10 in most H. glaberrima tissues including radial nerve, intestine, muscle, esophagus, mesentery, hemal system, gonads and respiratory tree. Molecular cloning of HgSTARD10, consequent protein expression and polyclonal antibody production revealed the STARD10 ortholog as the antigen recognized by the RN1 antibody. Further characterization into this START domain-containing protein will provide important insights for the biochemistry, physiology and evolution of deuterostomes.<br /> (Copyright © 2017 Elsevier Inc. All rights reserved.)

Details

Language :
English
ISSN :
1879-1107
Volume :
214
Database :
MEDLINE
Journal :
Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology
Publication Type :
Academic Journal
Accession number :
28864221
Full Text :
https://doi.org/10.1016/j.cbpb.2017.08.004