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Phosphorylation of MARCKS by endothelin in rat cerebral cortex slices

✍ Scribed by María J. Pérez-Alvarez; M. Carmen Calcerrada; R. Edgardo Catalán; Ana M. Martínez

Publisher
John Wiley and Sons
Year
1999
Tongue
English
Weight
778 KB
Volume
24
Category
Article
ISSN
0893-6609

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✦ Synopsis

The action of endothelin-1 (ET-l) on protein phosphorylation was studied in rat cerebral cortex. The peptide caused an increase in 32P incorporation into a 87 kDa protein, identified as myristoilated alanine-rich protein kinase C substrate (MARCKS). This effect was dose-and time-dependent, and was mimicked by ET-3, sarafotoxin 6c and 12-0tetradecanoylphorbol-13-acetate (TPA). However, it disappeared in the presence of Ro-3 l-8220, a protein kinase C (PKC) inhibitor. These findings indicate that ET-1 may have a functional role in protein phosphorylation processes in brain.

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