Endothelin Stimulates Protein Phosphorylation in Blood–Brain Barrier

The vasoactive neuropeptide endothelin stimulated phosphorylation of specific proteins in rat brain microvessels. Major effects were observed with endothelin-1. These effects were dose- and time-dependent. Among substrates for kinase actions, the 17.5 KDa and 80 KDa proteins were mainly affected by...

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Veröffentlicht in:	Biochemical and biophysical research communications 1996-02, Vol.219 (2), p.366-369
Hauptverfasser:	Catalán, R.E., Martı́nez, A.M., Aragonés, M.D., Hernández, F., Dı́az, G.
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Blood-Brain Barrier Brain - blood supply Cerebrovascular Circulation Electrophoresis, Polyacrylamide Gel Endothelins - pharmacology Intracellular Signaling Peptides and Proteins Male Membrane Proteins Microcirculation - metabolism Molecular Weight Myristoylated Alanine-Rich C Kinase Substrate Phosphates - metabolism Phosphoproteins - isolation & purification Phosphoproteins - metabolism Phosphorus Radioisotopes Phosphorylation Protein Kinase C - metabolism Proteins - isolation & purification Proteins - metabolism Rats Rats, Wistar Substrate Specificity
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Beschreibung
Zusammenfassung:	The vasoactive neuropeptide endothelin stimulated phosphorylation of specific proteins in rat brain microvessels. Major effects were observed with endothelin-1. These effects were dose- and time-dependent. Among substrates for kinase actions, the 17.5 KDa and 80 KDa proteins were mainly affected by endothelin-1. It was demonstrated that the 80 KDa protein affected corresponds to MARCKS (myristoylated alanine-rich C kinase substrate), a specific substrate for protein kinase C action.
ISSN:	0006-291X 1090-2104
DOI:	10.1006/bbrc.1996.0239