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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)
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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
ASBMB
ISSN
1083-351X
language
English
LU publication?
no
id
6ff842d7-3190-46db-9371-84af7c161c5d (old id 1784220)
date added to LUP
2011-02-07 15:21:13
date last changed
2016-06-29 09:14:26
@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},
  keyword      = {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    = {ASBMB},
  series       = {Journal of Biological Chemistry},
  title        = {Purification of the transforming growth factor-beta (TGF-beta) binding proteoglycan betaglycan},
  volume       = {266},
  year         = {1991},
}