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Calmodulin Antagonist W‐7 Inhibits Lysosomal Sphingomyelinase Activity in C6 Glioma Cells
Author(s) -
Masson Martial,
Albouz Samia,
Boutry JeanneMarie,
Spezzatti Bettina,
Castagna Monique,
Baumann Nicole
Publication year - 1989
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1989.tb09221.x
Subject(s) - calmodulin , antagonist , kinase , biochemistry , protein kinase a , acid sphingomyelinase , enzyme , biology , sphingomyelin , chemistry , microbiology and biotechnology , receptor , membrane
N ‐(6‐Aminohexyl)‐5‐chloro‐1‐naphthalenesulfonamide (W‐7) is known to be a potent calmodulin antagonist and inhibitor of calmodulin‐dependent protein kinases. W‐7 and 1‐(5‐isoquinolinyl‐sulfonyl)‐2‐methylpiperazine (H‐7) are inhibitors of protein kinase C and cyclic nucleotide‐dependent protein kinases. In C6 glioma cells, W‐7 and not H‐7 inhibited dose‐dependently acid sphingomyelinase, a result indicating the modulation of this lysosomal enzyme by a calmodulin‐dependent system. Other lysosomal enzymes, such as β‐glucosidase, α‐galactosidase, and arylsulfatase A, were unaffected by W‐7 and H‐7, a finding indicating a selective effect of W‐7 on sphingomyelinase.