Neurotensin alters phosphorylation of neostriatal proteins

S. T. Cain, Charles Nemeroff

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

Our finding that NT influences the phosphorylation of synaptosomal proteins demonstrates that protein phosphorylation-dephosphorylation must now be considered as a candidate mechanism for the transduction of the NT signal. As the current experiments did not include a protease inhibitor to prevent degradation of NT, we are currently refining the dose-response and time course of the NT-induced phosphorylation changes using such inhibitors. Work is also in progress to identify individual NT-sensitive phosphoprotein substrates and the second messenger systems (cAMP, cGMP, Ca2+-calmodulin, diacylglycerol) that mediate the NT message.

Original languageEnglish
Pages (from-to)98-100
Number of pages3
JournalAnnals of the New York Academy of Sciences
Volume494
StatePublished - Dec 1 1987
Externally publishedYes

Fingerprint

Neurotensin
Phosphorylation
Proteins
Phosphoproteins
Diglycerides
Second Messenger Systems
Calmodulin
Protease Inhibitors
Refining
Reaction Time
Signal Transduction
Degradation
Substrates
Protein
Experiments
Time Course
Substrate
Protease
Transduction
Dose

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

Cite this

Neurotensin alters phosphorylation of neostriatal proteins. / Cain, S. T.; Nemeroff, Charles.

In: Annals of the New York Academy of Sciences, Vol. 494, 01.12.1987, p. 98-100.

Research output: Contribution to journalArticle

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