PMID- 10066769
OWN - NLM
STAT- MEDLINE
DCOM- 19990413
LR  - 20210209
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 274
IP  - 11
DP  - 1999 Mar 12
TI  - Characterization of proteoglycans synthesized by cultured corneal fibroblasts in 
      response to transforming growth factor beta and fetal calf serum.
PG  - 7111-9
AB  - A culture system was developed to analyze the relationship between proteoglycans 
      and growth factors during corneal injury. Specifically, the effects of 
      transforming growth factor beta-1 (TGF-beta1) and fetal calf serum on 
      proteoglycan synthesis in corneal fibroblasts were examined. Glycosaminoglycan 
      synthesis and sulfation were determined using selective polysaccharidases. 
      Proteoglycan core proteins were analyzed using gel electrophoresis and Western 
      blotting. Cells cultured in 10% dialyzed fetal calf serum exhibited decreased 
      synthesis of more highly sulfated chondroitin sulfate and heparan sulfate 
      compared with cells cultured in 1% dialyzed fetal calf serum. The amount and 
      sulfation of the glycosaminoglycans was not significantly influenced by 
      TGF-beta1. The major proteoglycan species secreted into the media were decorin 
      and perlecan. Decorin was glycanated with chondroitin sulfate. Perlecan was 
      linked to either chondroitin sulfate, heparan sulfate, or both chondroitin 
      sulfate and heparan sulfate. Decorin synthesis was reduced by either TGF-beta1 or 
      serum. At early time points, both TGF-beta1 and serum induced substantial 
      increases in perlecan bearing chondroitin sulfate and/or heparan sulfate chains. 
      In contrast, after extended periods in culture, the amount of perlecan bearing 
      heparan sulfate chains was unaffected by TGF-beta1 and decreased by serum. The 
      levels of perlecan bearing chondroitin sulfate chains were elevated with 
      TGF-beta1 treatment and were decreased with serum. Because both decorin and 
      perlecan bind growth factors and are proposed to modulate their activity, changes 
      in the expression of either of these proteoglycans could substantially affect the 
      cellular response to injury.
FAU - Brown, C T
AU  - Brown CT
AD  - Department of Biochemistry, Boston University School of Medicine, Boston, 
      Massachusetts 02118, USA.
FAU - Nugent, M A
AU  - Nugent MA
FAU - Lau, F W
AU  - Lau FW
FAU - Trinkaus-Randall, V
AU  - Trinkaus-Randall V
LA  - eng
GR  - EY110004/EY/NEI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Glycosaminoglycans)
RN  - 0 (Proteoglycans)
RN  - 0 (Transforming Growth Factor beta)
SB  - IM
MH  - Animals
MH  - *Blood
MH  - Cattle
MH  - Cells, Cultured
MH  - Cornea/cytology/*drug effects/metabolism
MH  - Electrophoresis, Polyacrylamide Gel
MH  - Fibroblasts/drug effects/metabolism
MH  - Glycosaminoglycans/biosynthesis
MH  - Proteoglycans/biosynthesis/*metabolism
MH  - Rabbits
MH  - Transforming Growth Factor beta/*pharmacology
EDAT- 1999/03/06 00:00
MHDA- 1999/03/06 00:01
CRDT- 1999/03/06 00:00
PHST- 1999/03/06 00:00 [pubmed]
PHST- 1999/03/06 00:01 [medline]
PHST- 1999/03/06 00:00 [entrez]
AID - S0021-9258(18)36980-1 [pii]
AID - 10.1074/jbc.274.11.7111 [doi]
PST - ppublish
SO  - J Biol Chem. 1999 Mar 12;274(11):7111-9. doi: 10.1074/jbc.274.11.7111.