PUBLICATION

Cloning of the calpain regulatory subunit cDNA from fish reveals a divergent domain-V

Authors
Salem, M., Nath, J., and Killefer, J.
ID
ZDB-PUB-061226-9
Date
2004
Source
Animal biotechnology   15(2): 145-157 (Journal)
Registered Authors
Keywords
none
MeSH Terms
  • Calcium/metabolism
  • Phylogeny
  • Gene Expression Regulation
  • Peptide Fragments/genetics
  • Animals
  • Base Sequence
  • Amino Acid Sequence
  • Fishes/genetics*
  • DNA, Complementary/analysis*
  • Calpain/chemistry
  • Calpain/genetics*
  • Gene Library
  • Sequence Alignment
  • Evolution, Molecular
  • Molecular Sequence Data
(all 15)
PubMed
15595700 Full text @ Anim. Biotech.
Abstract
Calpains are Ca2+-dependent intracellular cysteine proteases, including the ubiquitously expressed micro- and m-calpains. Both are heterodimers, consisting of a distinct catalytic subunit and a common regulatory subunit. We describe cloning and sequencing of the calpain small (regulatory) subunit (cpns) cDNA from rainbow trout. This represents the first fish and lower vertebrate full cDNA of cpns. The rainbow trout cpns cDNA was used to retrieve the zebra fish and Japanese flounder homologues. We present evidence that fish cpns, unlike the conventional mammalian predominant isoform, cpnsl, is lacking the glycine-rich region of domain V. Because the glycine-rich region is known to play a role in membrane targeting, this divergent cpns suggests potentially different functional and activation mechanisms of the fish calpain system. A phylogenetic tree for the cpns gene superfamily has been constructed and the evolution of cpns considered.
Genes / Markers
Figures
No images available
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Antibodies
Orthology
Engineered Foreign Genes
Mapping
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Citation
Salem, M., Nath, J., and Killefer, J. (2004) Cloning of the calpain regulatory subunit cDNA from fish reveals a divergent domain-V. Animal biotechnology. 15(2):145-157.