Purification of the transforming growth factor-beta (TGF-beta) binding proteoglycan betaglycan
Andres, Janet L. ; Rönnstrand, Lars LU
; Cheifetz, Sela
and Massagué, Joan
(1991)
In Journal of Biological Chemistry
266(34).
p.23282-23287
- Abstract
- We report the purification of betaglycan, a low-abundance membrane proteoglycan with high affinity for transforming growth factor-beta (TGF-beta). Betaglycan solubilized from rat embryo membrane preparations was purified to near-homogeneity by sequential chromatography through DEAE-Trisacryl, wheat germ lectin-Sepharose, and TGF-beta 1-agarose. Purified betaglycan has properties similar to betaglycan affinity-labeled in intact cells: it binds TGF-beta 1 and TGF-beta 2 with KD approximately 0.2 nM, contains heparan sulfate and chondroitin sulfate glycosaminoglycan (GAG) chains and N-linked glycans attached to a 110-kDa core protein, and can spontaneously associate with phosphatidylcholine liposomes. The betaglycan core obtained by enzymatic... (More)
- We report the purification of betaglycan, a low-abundance membrane proteoglycan with high affinity for transforming growth factor-beta (TGF-beta). Betaglycan solubilized from rat embryo membrane preparations was purified to near-homogeneity by sequential chromatography through DEAE-Trisacryl, wheat germ lectin-Sepharose, and TGF-beta 1-agarose. Purified betaglycan has properties similar to betaglycan affinity-labeled in intact cells: it binds TGF-beta 1 and TGF-beta 2 with KD approximately 0.2 nM, contains heparan sulfate and chondroitin sulfate glycosaminoglycan (GAG) chains and N-linked glycans attached to a 110-kDa core protein, and can spontaneously associate with phosphatidylcholine liposomes. The betaglycan core obtained by enzymatic removal of the GAG chains has high affinity for TGF-beta and associates with artificial liposomes, indicating that the core protein binds TGF-beta and anchors to membranes independently of the GAG chains present on the native protein or of any ancillary protein. (Less)
Please use this url to cite or link to this publication:
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- author
- Andres, Janet L.
; Rönnstrand, Lars
LU
; Cheifetz, Sela
and Massagué, Joan
- publishing date
- 1991
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- Animals Binding, Affinity Chromatography, Ion Exchange Humans Liposomes/metabolism Membrane Proteins/*isolation & purification/metabolism Proteoglycans/*isolation & purification/metabolism Rats *Receptors, Competitive Cattle Chromatography, Transforming Growth Factor beta Transforming Growth Factor beta/*metabolism
- in
- Journal of Biological Chemistry
- volume
- 266
- issue
- 34
- pages
- 23282 - 23287
- publisher
- American Society for Biochemistry and Molecular Biology
- ISSN
- 1083-351X
- 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: Experimental Clinical Chemistry (013016010)
- id
- 6ff842d7-3190-46db-9371-84af7c161c5d (old id 1784220)
- date added to LUP
- 2016-04-04 07:07:40
- date last changed
- 2019-05-22 02:18:20
@article{6ff842d7-3190-46db-9371-84af7c161c5d,
abstract = {{We report the purification of betaglycan, a low-abundance membrane proteoglycan with high affinity for transforming growth factor-beta (TGF-beta). Betaglycan solubilized from rat embryo membrane preparations was purified to near-homogeneity by sequential chromatography through DEAE-Trisacryl, wheat germ lectin-Sepharose, and TGF-beta 1-agarose. Purified betaglycan has properties similar to betaglycan affinity-labeled in intact cells: it binds TGF-beta 1 and TGF-beta 2 with KD approximately 0.2 nM, contains heparan sulfate and chondroitin sulfate glycosaminoglycan (GAG) chains and N-linked glycans attached to a 110-kDa core protein, and can spontaneously associate with phosphatidylcholine liposomes. The betaglycan core obtained by enzymatic removal of the GAG chains has high affinity for TGF-beta and associates with artificial liposomes, indicating that the core protein binds TGF-beta and anchors to membranes independently of the GAG chains present on the native protein or of any ancillary protein.}},
author = {{Andres, Janet L. and Rönnstrand, Lars and Cheifetz, Sela and Massagué, Joan}},
issn = {{1083-351X}},
keywords = {{Animals
Binding; Affinity
Chromatography; Ion Exchange
Humans
Liposomes/metabolism
Membrane Proteins/*isolation & purification/metabolism
Proteoglycans/*isolation & purification/metabolism
Rats
*Receptors; Competitive
Cattle
Chromatography; Transforming Growth Factor beta
Transforming Growth Factor beta/*metabolism}},
language = {{eng}},
number = {{34}},
pages = {{23282--23287}},
publisher = {{American Society for Biochemistry and Molecular Biology}},
series = {{Journal of Biological Chemistry}},
title = {{Purification of the transforming growth factor-beta (TGF-beta) binding proteoglycan betaglycan}},
volume = {{266}},
year = {{1991}},
}