Identification of tyrosine sulfation in extracellular leucine-rich-repeat proteins using mass spectrometry.
Önnerfjord, Patrik LU
; Heathfield, Terrence
LU
and Heinegård, Dick
LU
(2004)
In Journal of Biological Chemistry
279(1).
p.26-33
- Abstract
- Multiple and variable tyrosine sulfation in extracellular class II leucine-rich repeat proteins/proteoglycans were characterized by mass spectrometry. The sulfogroup on tyrosine is labile and is released from peptides under normal mass spectrometric conditions. Thus, special approaches must be considered in order to identify this modification. By using a combination of mass spectrometry studies operating in negative and positive ion mode, tyrosine sulfation could be identified. In positive mode, the peptides normally appeared non-sulfated, whereas in negative mode a mixture of sulfated and non-sulfated species was observed. A combination of peptides released by different proteinases was used to obtain details on the locations of sulfate... (More)
- Multiple and variable tyrosine sulfation in extracellular class II leucine-rich repeat proteins/proteoglycans were characterized by mass spectrometry. The sulfogroup on tyrosine is labile and is released from peptides under normal mass spectrometric conditions. Thus, special approaches must be considered in order to identify this modification. By using a combination of mass spectrometry studies operating in negative and positive ion mode, tyrosine sulfation could be identified. In positive mode, the peptides normally appeared non-sulfated, whereas in negative mode a mixture of sulfated and non-sulfated species was observed. A combination of peptides released by different proteinases was used to obtain details on the locations of sulfate groups. Multiple tyrosine sulfates were observed in the N-terminal region of fibromodulin ( up to 9 sites), osteoadherin ( up to 6 sites), and lumican ( 2 sites). Osteoadherin contains two additional sulfated tyrosine residues close to its C terminus. We also identified an error in the published sequence of bovine fibromodulin, resulting in the replacement of Thr(37) by Tyr(37)-Gly(38), thus increasing its homology with its human counterpart. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/118302
- author
- Önnerfjord, Patrik
LU
; Heathfield, Terrence
LU
and Heinegård, Dick
LU
- organization
- publishing date
- 2004
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Journal of Biological Chemistry
- volume
- 279
- issue
- 1
- pages
- 26 - 33
- publisher
- American Society for Biochemistry and Molecular Biology
- external identifiers
-
- pmid:14551184
- wos:000187555300004
- scopus:0347683486
- ISSN
- 1083-351X
- DOI
- 10.1074/jbc.M308689200
- 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), Faculty of Medicine (000022000)
- id
- c0c2e46e-06fc-40d7-b517-aa3cba34e49f (old id 118302)
- alternative location
- http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=14551184&dopt=Abstract
- date added to LUP
- 2016-04-01 11:42:23
- date last changed
- 2022-03-28 01:53:17
@article{c0c2e46e-06fc-40d7-b517-aa3cba34e49f,
abstract = {{Multiple and variable tyrosine sulfation in extracellular class II leucine-rich repeat proteins/proteoglycans were characterized by mass spectrometry. The sulfogroup on tyrosine is labile and is released from peptides under normal mass spectrometric conditions. Thus, special approaches must be considered in order to identify this modification. By using a combination of mass spectrometry studies operating in negative and positive ion mode, tyrosine sulfation could be identified. In positive mode, the peptides normally appeared non-sulfated, whereas in negative mode a mixture of sulfated and non-sulfated species was observed. A combination of peptides released by different proteinases was used to obtain details on the locations of sulfate groups. Multiple tyrosine sulfates were observed in the N-terminal region of fibromodulin ( up to 9 sites), osteoadherin ( up to 6 sites), and lumican ( 2 sites). Osteoadherin contains two additional sulfated tyrosine residues close to its C terminus. We also identified an error in the published sequence of bovine fibromodulin, resulting in the replacement of Thr(37) by Tyr(37)-Gly(38), thus increasing its homology with its human counterpart.}},
author = {{Önnerfjord, Patrik and Heathfield, Terrence and Heinegård, Dick}},
issn = {{1083-351X}},
language = {{eng}},
number = {{1}},
pages = {{26--33}},
publisher = {{American Society for Biochemistry and Molecular Biology}},
series = {{Journal of Biological Chemistry}},
title = {{Identification of tyrosine sulfation in extracellular leucine-rich-repeat proteins using mass spectrometry.}},
url = {{http://dx.doi.org/10.1074/jbc.M308689200}},
doi = {{10.1074/jbc.M308689200}},
volume = {{279}},
year = {{2004}},
}