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A START-domain-containing protein is a novel marker of nervous system components of the sea cucumber Holothuria glaberrima.
- 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
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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.)
- Subjects :
- Amino Acid Sequence
Animals
Antibodies chemistry
Binding Sites
Biomarkers metabolism
Cloning, Molecular
Escherichia coli genetics
Escherichia coli metabolism
Gene Expression
Holothuria classification
Holothuria metabolism
Nerve Tissue Proteins metabolism
Nervous System cytology
Neurons cytology
Organ Specificity
Phosphoproteins metabolism
Phylogeny
Protein Binding
Protein Interaction Domains and Motifs
Recombinant Proteins genetics
Recombinant Proteins metabolism
Sequence Alignment
Sequence Homology, Amino Acid
Holothuria genetics
Nerve Tissue Proteins genetics
Nervous System metabolism
Neurons metabolism
Phosphoproteins genetics
Subjects
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