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Purification and structural characterization of transforming growth factor beta induced protein (TGFBIp) from porcine and human corneas

Andersen, Rolf B; Karring, Henrik LU ; Moller-Pedersen, Torben; Valnickova, Zuzana; Thogersen, Ida B; Hedegaard, Chris J; Kristensen, Torsten; Klintworth, Gordon K and Enghild, Jan J (2004) In Biochemistry 43(51). p.16374-16384
Abstract
Mutations in the TGFBI (BIGH3) gene that encodes for transforming growth factor beta induced protein (TGFBIp) are the cause of several phenotypically different corneal dystrophies. While the genetics of these protein misfolding diseases are well documented, relatively little is known about this extracellular matrix protein itself. In this study, we have purified TGFBIp from normal human and porcine corneas using nondenaturing conditions and standard chromatography techniques. The two homologues were shown to be monomers, and we did not find evidence for posttranslational additions. The C-terminal of both human and porcine TGFBIp is truncated predominantly after the integrin binding sequence Arg(642)-Gly(643)-Asp(644) (RGD). However, using... (More)
Mutations in the TGFBI (BIGH3) gene that encodes for transforming growth factor beta induced protein (TGFBIp) are the cause of several phenotypically different corneal dystrophies. While the genetics of these protein misfolding diseases are well documented, relatively little is known about this extracellular matrix protein itself. In this study, we have purified TGFBIp from normal human and porcine corneas using nondenaturing conditions and standard chromatography techniques. The two homologues were shown to be monomers, and we did not find evidence for posttranslational additions. The C-terminal of both human and porcine TGFBIp is truncated predominantly after the integrin binding sequence Arg(642)-Gly(643)-Asp(644) (RGD). However, using an antibody against the C-terminal fragment (residues 648-683), we also detected a small amount of full-length TGFBIp in corneal extracts. Approximately 60% of TGFBIp was covalently associated with insoluble components of the extracellular matrix in both human and porcine corneas through a disulfide bridge. (Less)
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author
publishing date
type
Contribution to journal
publication status
published
subject
in
Biochemistry
volume
43
issue
51
pages
16374 - 16384
publisher
The American Chemical Society
external identifiers
  • pmid:15610032
  • scopus:11044229726
ISSN
0006-2960
DOI
10.1021/bi048589s
language
English
LU publication?
no
id
ee36df25-c1a3-463a-956c-f4632db5d509 (old id 1131059)
date added to LUP
2008-06-12 12:18:17
date last changed
2017-11-19 03:37:47
@article{ee36df25-c1a3-463a-956c-f4632db5d509,
  abstract     = {Mutations in the TGFBI (BIGH3) gene that encodes for transforming growth factor beta induced protein (TGFBIp) are the cause of several phenotypically different corneal dystrophies. While the genetics of these protein misfolding diseases are well documented, relatively little is known about this extracellular matrix protein itself. In this study, we have purified TGFBIp from normal human and porcine corneas using nondenaturing conditions and standard chromatography techniques. The two homologues were shown to be monomers, and we did not find evidence for posttranslational additions. The C-terminal of both human and porcine TGFBIp is truncated predominantly after the integrin binding sequence Arg(642)-Gly(643)-Asp(644) (RGD). However, using an antibody against the C-terminal fragment (residues 648-683), we also detected a small amount of full-length TGFBIp in corneal extracts. Approximately 60% of TGFBIp was covalently associated with insoluble components of the extracellular matrix in both human and porcine corneas through a disulfide bridge.},
  author       = {Andersen, Rolf B and Karring, Henrik and Moller-Pedersen, Torben and Valnickova, Zuzana and Thogersen, Ida B and Hedegaard, Chris J and Kristensen, Torsten and Klintworth, Gordon K and Enghild, Jan J},
  issn         = {0006-2960},
  language     = {eng},
  number       = {51},
  pages        = {16374--16384},
  publisher    = {The American Chemical Society},
  series       = {Biochemistry},
  title        = {Purification and structural characterization of transforming growth factor beta induced protein (TGFBIp) from porcine and human corneas},
  url          = {http://dx.doi.org/10.1021/bi048589s},
  volume       = {43},
  year         = {2004},
}