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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1121325
- author
- Lorenzo, Pilar
LU
; Aspberg, Anders
LU
; Önnerfjord, Patrik
LU
; Bayliss, Michael T.
; Neame, Peter J.
and Heinegård, Dick
LU
- organization
- publishing date
- 2001
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Journal of Biological Chemistry
- volume
- 276
- issue
- 15
- pages
- 12201 - 12211
- publisher
- American Society for Biochemistry and Molecular Biology
- external identifiers
-
- pmid:11152692
- scopus:0035853783
- ISSN
- 1083-351X
- DOI
- 10.1074/jbc.M010932200
- language
- English
- LU publication?
- yes
- additional info
- The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Connective Tissue Biology (013230151)
- id
- 2dccf46b-ab6b-4e5f-bcae-bbb732dd82a3 (old id 1121325)
- date added to LUP
- 2016-04-01 11:46:51
- date last changed
- 2022-04-05 04:55:38
@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 = {{American Society for Biochemistry and Molecular Biology}},
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}},
doi = {{10.1074/jbc.M010932200}},
volume = {{276}},
year = {{2001}},
}