PUBLICATION
Identification of Proteoglycan from Salmon Nasal Cartilage
- Authors
- Kakizaki, I., Tatara, Y., Majima, M., Kato, Y., and Endo, M.
- ID
- ZDB-PUB-101115-6
- Date
- 2011
- Source
- Archives of biochemistry and biophysics 506(1): 58-65 (Journal)
- Registered Authors
- Keywords
- Proteoglycan, Aggrecan, Core protein, Amino acid, Glycosaminoglycan
- MeSH Terms
-
- Aggrecans/chemistry
- Aggrecans/genetics
- Amino Acid Sequence
- Amino Acids/analysis
- Animals
- Base Sequence
- Cattle
- DNA Primers/genetics
- DNA, Complementary/genetics
- Fish Proteins/chemistry*
- Fish Proteins/genetics
- Humans
- Molecular Sequence Data
- Nasal Cartilages/chemistry*
- Oncorhynchus keta/genetics
- Oncorhynchus keta/metabolism*
- Protein Structure, Tertiary
- Proteoglycans/chemistry*
- Proteoglycans/genetics
- Sequence Homology, Amino Acid
- Species Specificity
- PubMed
- 21056541 Full text @ Arch. Biochem. Biophys.
Citation
Kakizaki, I., Tatara, Y., Majima, M., Kato, Y., and Endo, M. (2011) Identification of Proteoglycan from Salmon Nasal Cartilage. Archives of biochemistry and biophysics. 506(1):58-65.
Abstract
There has been no structural information about the core protein of salmon nasal cartilage proteoglycan although its physiological activities have been investigated. Internal amino acid sequencing using nano-LC/MS/MS revealed that the salmon proteoglycan was aggrecan. Primer walk sequencing based on the amino acid information determined that the salmon aggrecan cDNA is comprised of 4207 bp nucleotides predicted to encode 1324 amino acids with a molecular mass of 143,276. It exhibited significant similarities to predicted pufferfish aggrecan, zebrafish similar to aggrecan, zebrafish aggrecan, bovine aggrecan and human aggrecan isoform 2 precursor; whose amino acid identities were 56, 55, 49, 31 and 30% respectively. Salmon cartilage aggrecan had globular domains G1, G2 and G3 as in mammalian aggrecans. Neither the putative keratan sulphate attachment domain enriched with serine, glutamic acid and proline, nor the putative chondroitin sulphate attachment domain with repeating amino acid sequence containing serine-glycine, found in mammalian aggrecans were observed in salmon, however, random serine-glycine (or glycine-serine) sequences predicted to the sugar chain attachment sites were observed. Based on cDNA analysis and amino acid analysis after β-elimination, the ratio of serine attached to sugar chains was calculated to be approximately 37.7% of total serine, that is, 46 of 123 serine residues.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping