TNF-alpha suppresses the PDGF beta-receptor kinase
Molander, Catrin ; Kallin, Anders ; Izumi, H ; Rönnstrand, Lars LU
and Funa, Keiko
(2000)
In Experimental Cell Research
258(1).
p.65-71
- Abstract
- PDGF and TNF-alpha are both known to play important roles in inflammation, albeit frequently by opposing actions. Typically, TNF-alpha can attenuate PDGF beta-receptor signaling. Pretreatment of mouse 3T3 L1 fibroblasts with TNF-alpha greatly diminished their proliferative response to PDGF. However, TNF-alpha affected neither the binding of PDGF-BB to cell surface receptors nor the total amount of PDGF beta-receptor in the cells, but decreased the PDGF-induced in vitro kinase activity of the receptor. The phosphatase inhibitor ortho-vanadate did not prevent this effect. Ortho-phosphate labeling of cells prior to TNF-alpha treatment and PDGF-BB stimulation confirmed a decrease of in vivo phosphorylation of the PDGF beta-receptor.... (More)
- PDGF and TNF-alpha are both known to play important roles in inflammation, albeit frequently by opposing actions. Typically, TNF-alpha can attenuate PDGF beta-receptor signaling. Pretreatment of mouse 3T3 L1 fibroblasts with TNF-alpha greatly diminished their proliferative response to PDGF. However, TNF-alpha affected neither the binding of PDGF-BB to cell surface receptors nor the total amount of PDGF beta-receptor in the cells, but decreased the PDGF-induced in vitro kinase activity of the receptor. The phosphatase inhibitor ortho-vanadate did not prevent this effect. Ortho-phosphate labeling of cells prior to TNF-alpha treatment and PDGF-BB stimulation confirmed a decrease of in vivo phosphorylation of the PDGF beta-receptor. Two-dimensional mapping after tryptic cleavage as well as phosphoamino acid analysis demonstrated a general decrease in phosphorylation of all known tyrosine residues in the PDGF beta-receptor. The exact mechanism for this suppression remains to be clarified (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1782600
- author
- Molander, Catrin
; Kallin, Anders
; Izumi, H
; Rönnstrand, Lars
LU
and Funa, Keiko
- publishing date
- 2000
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- 3T3 Cells Animals Cell Division/drug effects Kinetics Mice Platelet-Derived Growth Factor/pharmacokinetics/*pharmacology Receptor Protein-Tyrosine Kinases/*antagonists & inhibitors Receptor, Platelet-Derived Growth Factor beta/drug effects/*physiology Signal Transduction/drug effects Transforming Growth Factor beta/*pharmacology Vanadates/pharmacology
- in
- Experimental Cell Research
- volume
- 258
- issue
- 1
- pages
- 65 - 71
- publisher
- Academic Press
- external identifiers
-
- scopus:0034631829
- ISSN
- 1090-2422
- DOI
- 10.1006/excr.2000.4917
- 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
- e08300d1-ec60-4d49-9b7e-91c4c00b11cf (old id 1782600)
- date added to LUP
- 2016-04-04 08:43:20
- date last changed
- 2022-01-29 03:53:44
@article{e08300d1-ec60-4d49-9b7e-91c4c00b11cf,
abstract = {{PDGF and TNF-alpha are both known to play important roles in inflammation, albeit frequently by opposing actions. Typically, TNF-alpha can attenuate PDGF beta-receptor signaling. Pretreatment of mouse 3T3 L1 fibroblasts with TNF-alpha greatly diminished their proliferative response to PDGF. However, TNF-alpha affected neither the binding of PDGF-BB to cell surface receptors nor the total amount of PDGF beta-receptor in the cells, but decreased the PDGF-induced in vitro kinase activity of the receptor. The phosphatase inhibitor ortho-vanadate did not prevent this effect. Ortho-phosphate labeling of cells prior to TNF-alpha treatment and PDGF-BB stimulation confirmed a decrease of in vivo phosphorylation of the PDGF beta-receptor. Two-dimensional mapping after tryptic cleavage as well as phosphoamino acid analysis demonstrated a general decrease in phosphorylation of all known tyrosine residues in the PDGF beta-receptor. The exact mechanism for this suppression remains to be clarified}},
author = {{Molander, Catrin and Kallin, Anders and Izumi, H and Rönnstrand, Lars and Funa, Keiko}},
issn = {{1090-2422}},
keywords = {{3T3 Cells
Animals
Cell Division/drug effects
Kinetics
Mice
Platelet-Derived Growth Factor/pharmacokinetics/*pharmacology
Receptor Protein-Tyrosine Kinases/*antagonists & inhibitors
Receptor; Platelet-Derived Growth Factor beta/drug effects/*physiology
Signal Transduction/drug effects
Transforming Growth Factor beta/*pharmacology
Vanadates/pharmacology}},
language = {{eng}},
number = {{1}},
pages = {{65--71}},
publisher = {{Academic Press}},
series = {{Experimental Cell Research}},
title = {{TNF-alpha suppresses the PDGF beta-receptor kinase}},
url = {{http://dx.doi.org/10.1006/excr.2000.4917}},
doi = {{10.1006/excr.2000.4917}},
volume = {{258}},
year = {{2000}},
}