Crustacean neuroparsins-a mini-review

Gene. 2020 Mar 30:732:144361. doi: 10.1016/j.gene.2020.144361. Epub 2020 Jan 11.

Abstract

Crustacean neuroparsins are poly-cysteine rich neuropeptides that share some similarities with the ovary ecdysteroidogenesis hormone (OEH) of mosquitoes, the N-terminal end of the growth factor binding protein region of the vertebrate and mollusk insulin-like growth factor binding protein and single insulin binding domain protein. Neuroparsins can promote reproduction and neurite outgrowth in various insects. Though many studies have been made in insects, the amount of work reported in crustaceans is still limited. This review emphasizes the neuroparsins found in decapod crustaceans with references to the neuroparsin first discovered in insects. To be more complete in identifying all the neuroparsin members and to understand the structure/function relationship within a single species, we have collected all neuroparsins from the GenBank and our transcriptome datasets. Then, we employed a comparative approach to study the sequence homology, tissue expression patterns, making predictions of their function and the evolutionary relationship particularly in decapod crustaceans. Results from alignment and phylogenetic studies indicated that crustacean neuroparsins consist of unique feature that can be used as criteria for their classification. These features include the presence of 12 cysteine residues in the mature peptide, the strict spacing between these cysteine residues and the size of the mature peptide. Because of the limited data on the expression information, the functions of most neuroparsin are unknown. The review will focus on the site of synthesis, expression, functions, the sequence homology and the evolutionary relationship of this group of neurohormones.

Keywords: Crustaceans; Cysteine-rich neuropeptides; Insects; Neuroparsins.

Publication types

  • Review

MeSH terms

  • Animals
  • Binding Sites
  • Decapoda / classification
  • Decapoda / metabolism*
  • Neuropeptides / chemistry
  • Neuropeptides / genetics*
  • Neuropeptides / metabolism*
  • Phylogeny
  • Protein Binding
  • Sequence Homology, Amino Acid
  • Tissue Distribution

Substances

  • Neuropeptides