PUBLICATION

Molecular and Functional Analyses of Aspolin, a Fish-Specific Protein Extremely Rich in Aspartic Acid

Authors
Kinoshita, S., Katsumi, E., Yamamoto, H., Takeuchi, K., and Watabe, S.
ID
ZDB-PUB-101011-19
Date
2011
Source
Marine biotechnology (New York, N.Y.)   13(3): 517-526 (Journal)
Registered Authors
Kinoshita, Shigeharu, Watabe, Shugo
Keywords
Aspolin, Molecular evolution, Histidine-rich calcium binding protein (HRC), Sarcoplasmic reticulum, Muscle, Fish
MeSH Terms
  • Animals
  • Physical Chromosome Mapping
  • Base Sequence
  • In Situ Hybridization
  • Cluster Analysis
  • Sequence Analysis, DNA
  • DNA Primers/genetics
  • Cloning, Molecular
  • Muscle, Skeletal/metabolism
  • Gene Knockdown Techniques
  • Muscle Proteins/genetics*
  • Muscle Proteins/metabolism*
  • Amino Acid Sequence
  • Immunohistochemistry
  • Gene Components
  • Blotting, Western
  • Molecular Sequence Data
  • Reverse Transcriptase Polymerase Chain Reaction
  • Zebrafish*
  • Phylogeny*
  • DNA, Complementary/genetics
  • Calcium-Binding Proteins/genetics*
  • Calcium-Binding Proteins/metabolism*
(all 23)
PubMed
20878432 Full text @ Mar. Biotechnol.
Abstract
Aspolin is a muscular protein having unique structural characteristics where the most part of its primary structure is occupied by aspartic acid. Aspolin has been found exceptionally in fish muscle, suggesting its specific role in this tissue. However, biological functions of aspolin have remained unknown. In the present study, we cloned full-length cDNAs encoding zebrafish Danio rerio aspolins 1 and 2, revealed their genomic organization, and examined in vivo function using knockdown techniques. Genomic analysis clearly showed that aspolin is a paralog of the histidine-rich calcium binding protein gene, which encodes a calcium binding protein in sarcoplasmic reticulum (SR). Expression analysis showed that the transcripts and their translated products, aspolins 1 and 2, are distributed in myotomal skeletal muscle, but not in cardiac muscle. Injection of antisense morpholino oligo targeting both aspolins 1 and 2 increased the mRNA levels of calsequestrin 1, another calcium binding protein in SR. These lines of evidence suggest that aspolins regulate calcium concentrations in SR.
Genes / Markers
Figures
No images available
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Expression
Phenotype
No data available
Mutations / Transgenics
No data available
Human Disease / Model
No data available
Sequence Targeting Reagents
Target Reagent Reagent Type
aspolinMO1-aspolinMRPHLNO
1 - 1 of 1
Show
Fish
Fish
WT
WT + MO1-aspolin
1 - 2 of 2
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Antibodies
Orthology
No data available
Engineered Foreign Genes
No data available
Mapping
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Citation
Kinoshita, S., Katsumi, E., Yamamoto, H., Takeuchi, K., and Watabe, S. (2011) Molecular and Functional Analyses of Aspolin, a Fish-Specific Protein Extremely Rich in Aspartic Acid. Marine biotechnology (New York, N.Y.). 13(3):517-526.