Advanced

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:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Journal of Biological Chemistry
volume
279
issue
1
pages
26 - 33
publisher
ASBMB
external identifiers
  • pmid:14551184
  • wos:000187555300004
  • scopus:0347683486
ISSN
1083-351X
DOI
10.1074/jbc.M308689200
language
English
LU publication?
yes
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
2007-07-18 14:47:13
date last changed
2017-06-11 03:27:39
@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    = {ASBMB},
  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},
  volume       = {279},
  year         = {2004},
}