Title : Phorbol ester- and retinoic acid-induced regulation of the protein kinase C substrate MARCKS in immortalized hippocampal cells.

Pub. Date : 1994 Nov

PMID : 7931322






6 Functional Relationships(s)
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1 Phorbol ester- and retinoic acid-induced regulation of the protein kinase C substrate MARCKS in immortalized hippocampal cells. Tretinoin myristoylated alanine rich protein kinase C substrate Homo sapiens
2 The expression of MARCKS, a major protein kinase C (PKC) substrate, was examined in the immortalized hippocampal cell line HN33, following differentiation using phorbol esters or retinoic acid. Tretinoin myristoylated alanine rich protein kinase C substrate Homo sapiens
3 MARCKS protein expression was also down-regulated in a dose-dependent manner on exposure of HN33 cells to retinoic acid. Tretinoin myristoylated alanine rich protein kinase C substrate Homo sapiens
4 In cells exposed to 10 microM retinoic acid, the MARCKS protein level was reduced in the membrane fraction within 4 h. Reduction of MARCKS protein levels was maximal (> 90%) by 12 h with no evidence for any alteration in PKC activity. Tretinoin myristoylated alanine rich protein kinase C substrate Homo sapiens
5 In cells exposed to 10 microM retinoic acid, the MARCKS protein level was reduced in the membrane fraction within 4 h. Reduction of MARCKS protein levels was maximal (> 90%) by 12 h with no evidence for any alteration in PKC activity. Tretinoin myristoylated alanine rich protein kinase C substrate Homo sapiens
6 Reduced levels of MARCKS protein were also observed in the soluble fraction of retinoic acid-exposed cells, but to a significantly lesser extent. Tretinoin myristoylated alanine rich protein kinase C substrate Homo sapiens