Purification and structural characterization of transforming growth factor beta induced protein (TGFBIp) from porcine and human corneas
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1131059
- author
- 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
- publishing date
- 2004
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Biochemistry
- volume
- 43
- issue
- 51
- pages
- 16374 - 16384
- publisher
- The American Chemical Society (ACS)
- external identifiers
-
- pmid:15610032
- scopus:11044229726
- ISSN
- 0006-2960
- DOI
- 10.1021/bi048589s
- language
- English
- LU publication?
- no
- 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
- ee36df25-c1a3-463a-956c-f4632db5d509 (old id 1131059)
- date added to LUP
- 2016-04-01 12:26:41
- date last changed
- 2022-02-03 22:18:11
@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 (ACS)}}, 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}}, doi = {{10.1021/bi048589s}}, volume = {{43}}, year = {{2004}}, }