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Identification and characterization of asporin. a novel member of the leucine-rich repeat protein family closely related to decorin and biglycan

Lorenzo, Pilar LU ; Aspberg, Anders LU ; Önnerfjord, Patrik LU ; Bayliss, Michael T.; Neame, Peter J. and Heinegård, Dick LU (2001) In Journal of Biological Chemistry 276(15). p.12201-12211
Abstract
Asporin, a novel member of the leucine-rich repeat family of proteins, was partially purified from human articular cartilage and meniscus. Cloning of human and mouse asporin cDNAs revealed that the protein is closely related to decorin and biglycan. It contains a putative propeptide, 4 amino-terminal cysteines, 10 leucine-rich repeats, and 2 C-terminal cysteines. In contrast to decorin and biglycan, asporin is not a proteoglycan. Instead, asporin contains a unique stretch of aspartic acid residues in its amino-terminal region. A polymorphism was identified in that the number of consecutive aspartate residues varied from 11 to 15. The 8 exons of the human asporin gene span 26 kilobases on chromosome 9q31.1-32, and the putative promoter... (More)
Asporin, a novel member of the leucine-rich repeat family of proteins, was partially purified from human articular cartilage and meniscus. Cloning of human and mouse asporin cDNAs revealed that the protein is closely related to decorin and biglycan. It contains a putative propeptide, 4 amino-terminal cysteines, 10 leucine-rich repeats, and 2 C-terminal cysteines. In contrast to decorin and biglycan, asporin is not a proteoglycan. Instead, asporin contains a unique stretch of aspartic acid residues in its amino-terminal region. A polymorphism was identified in that the number of consecutive aspartate residues varied from 11 to 15. The 8 exons of the human asporin gene span 26 kilobases on chromosome 9q31.1-32, and the putative promoter region lacks TATA consensus sequences. The asporin mRNA is expressed in a variety of human tissues with higher levels in osteoarthritic articular cartilage, aorta, uterus, heart, and liver. The deduced amino acid sequence of asporin was confirmed by mass spectrometry of the isolated protein resulting in 84% sequence coverage. The protein contains an N-glycosylation site at Asn(281) with a heterogeneous oligosaccharide structure and a potential O-glycosylation site at Ser(54). The name asporin reflects the aspartate-rich amino terminus and the overall similarity to decorin. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Journal of Biological Chemistry
volume
276
issue
15
pages
12201 - 12211
publisher
ASBMB
external identifiers
  • pmid:11152692
  • scopus:0035853783
ISSN
1083-351X
DOI
10.1074/jbc.M010932200
language
English
LU publication?
yes
id
2dccf46b-ab6b-4e5f-bcae-bbb732dd82a3 (old id 1121325)
date added to LUP
2008-07-04 11:49:21
date last changed
2018-02-11 03:24:03
@article{2dccf46b-ab6b-4e5f-bcae-bbb732dd82a3,
  abstract     = {Asporin, a novel member of the leucine-rich repeat family of proteins, was partially purified from human articular cartilage and meniscus. Cloning of human and mouse asporin cDNAs revealed that the protein is closely related to decorin and biglycan. It contains a putative propeptide, 4 amino-terminal cysteines, 10 leucine-rich repeats, and 2 C-terminal cysteines. In contrast to decorin and biglycan, asporin is not a proteoglycan. Instead, asporin contains a unique stretch of aspartic acid residues in its amino-terminal region. A polymorphism was identified in that the number of consecutive aspartate residues varied from 11 to 15. The 8 exons of the human asporin gene span 26 kilobases on chromosome 9q31.1-32, and the putative promoter region lacks TATA consensus sequences. The asporin mRNA is expressed in a variety of human tissues with higher levels in osteoarthritic articular cartilage, aorta, uterus, heart, and liver. The deduced amino acid sequence of asporin was confirmed by mass spectrometry of the isolated protein resulting in 84% sequence coverage. The protein contains an N-glycosylation site at Asn(281) with a heterogeneous oligosaccharide structure and a potential O-glycosylation site at Ser(54). The name asporin reflects the aspartate-rich amino terminus and the overall similarity to decorin.},
  author       = {Lorenzo, Pilar and Aspberg, Anders and Önnerfjord, Patrik and Bayliss, Michael T. and Neame, Peter J. and Heinegård, Dick},
  issn         = {1083-351X},
  language     = {eng},
  number       = {15},
  pages        = {12201--12211},
  publisher    = {ASBMB},
  series       = {Journal of Biological Chemistry},
  title        = {Identification and characterization of asporin. a novel member of the leucine-rich repeat protein family closely related to decorin and biglycan},
  url          = {http://dx.doi.org/10.1074/jbc.M010932200},
  volume       = {276},
  year         = {2001},
}