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Characterization of the platelet-derived growth factor beta-receptor kinase activity by use of synthetic peptides

Rönnstrand, Lars LU ; Sorokin, Andrey; Engström, Ulla and Heldin, Carl-Henrik (1990) In Biochemical and Biophysical Research Communications 167(3). p.1333-1340
Abstract
Synthetic peptides derived from the sequence surrounding tyrosine-857 in the human platelet-derived growth factor (PDGF) beta-receptor were used to elucidate the requirement for length and presence of negative and positively charged amino acids in substrates of the PDGF beta-receptor protein tyrosine kinase. The measured Km for the different peptides were all in the range 1-10 mM. A peptide of only five amino acids, lacking acidic amino acid residues, were found to be substrates for the receptor kinase. Ligand binding was found to stimulate the phosphorylation of peptides mainly by lowering the Km both for peptide and for ATP. Only minor changes in the Vmax occurred upon stimulation with PDGF. The reaction mechanism was found to be... (More)
Synthetic peptides derived from the sequence surrounding tyrosine-857 in the human platelet-derived growth factor (PDGF) beta-receptor were used to elucidate the requirement for length and presence of negative and positively charged amino acids in substrates of the PDGF beta-receptor protein tyrosine kinase. The measured Km for the different peptides were all in the range 1-10 mM. A peptide of only five amino acids, lacking acidic amino acid residues, were found to be substrates for the receptor kinase. Ligand binding was found to stimulate the phosphorylation of peptides mainly by lowering the Km both for peptide and for ATP. Only minor changes in the Vmax occurred upon stimulation with PDGF. The reaction mechanism was found to be sequential, i.e. both the peptide and ATP have to bind to the enzyme before any product is released. (Less)
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author
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published
subject
keywords
Platelet-Derived Growth Factor Recombinant Proteins/metabolism Substrate Specificity, Cell Surface/*metabolism Receptors, Amino Acid Sequence Humans Kinetics Molecular Sequence Data Oligopeptides/chemical synthesis/*metabolism/pharmacology Phosphorylation Platelet-Derived Growth Factor/metabolism Protein Kinases/*metabolism Receptors
in
Biochemical and Biophysical Research Communications
volume
167
issue
3
pages
1333 - 1340
publisher
Elsevier
ISSN
1090-2104
language
English
LU publication?
no
id
e1531d15-9a47-4cfc-883b-8082001356a5 (old id 1784225)
date added to LUP
2011-02-07 15:18:34
date last changed
2016-06-29 09:09:05
@misc{e1531d15-9a47-4cfc-883b-8082001356a5,
  abstract     = {Synthetic peptides derived from the sequence surrounding tyrosine-857 in the human platelet-derived growth factor (PDGF) beta-receptor were used to elucidate the requirement for length and presence of negative and positively charged amino acids in substrates of the PDGF beta-receptor protein tyrosine kinase. The measured Km for the different peptides were all in the range 1-10 mM. A peptide of only five amino acids, lacking acidic amino acid residues, were found to be substrates for the receptor kinase. Ligand binding was found to stimulate the phosphorylation of peptides mainly by lowering the Km both for peptide and for ATP. Only minor changes in the Vmax occurred upon stimulation with PDGF. The reaction mechanism was found to be sequential, i.e. both the peptide and ATP have to bind to the enzyme before any product is released.},
  author       = {Rönnstrand, Lars and Sorokin, Andrey and Engström, Ulla and Heldin, Carl-Henrik},
  issn         = {1090-2104},
  keyword      = {Platelet-Derived Growth Factor
Recombinant Proteins/metabolism
Substrate Specificity,Cell Surface/*metabolism
Receptors,Amino Acid Sequence
Humans
Kinetics
Molecular Sequence Data
Oligopeptides/chemical synthesis/*metabolism/pharmacology
Phosphorylation
Platelet-Derived Growth Factor/metabolism
Protein Kinases/*metabolism
Receptors},
  language     = {eng},
  number       = {3},
  pages        = {1333--1340},
  publisher    = {ARRAY(0x789a490)},
  series       = {Biochemical and Biophysical Research Communications},
  title        = {Characterization of the platelet-derived growth factor beta-receptor kinase activity by use of synthetic peptides},
  volume       = {167},
  year         = {1990},
}