Mammalian brain microtubules are sensitive to cyclic AMP in Vitro

Manso-Martínez, Rafael; Palomares, Rosario; Pariente, F.

doi:10.1016/0003-9861(84)90268-6

Cited by 8 publications

(3 citation statements)

References 32 publications

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“…On the other hand, 2008/C13*5.25 cells were hypersensitive to taxol (Fig. 10 B) (27) 12.5,M (25). In addition, DDP has been shown to alter microtubule assembly by direct tubulin modification (29) and to induce changes in the cytoskeletal pattern of tumor cells (30).…”

Section: Microsequence Analysismentioning

confidence: 94%

In vitro modulation of cisplatin accumulation in human ovarian carcinoma cells by pharmacologic alteration of microtubules.

Christen

Jekunen²,

Jones³

et al. 1993

J. Clin. Invest.

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Section: Microsequence Analysismentioning

confidence: 94%

In vitro modulation of cisplatin accumulation in human ovarian carcinoma cells by pharmacologic alteration of microtubules.

Christen

Jekunen²,

Jones³

et al. 1993

J. Clin. Invest.

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“…Previously, we had immunolocalized the C-subunit also in keratin filaments of parotid gland duct cells, another type of intermediate filaments [16]. Experiments performed in vitro with vimentin [18], desmin [I91 and neurofilaments f20] as well as with nerve cell microtubules [21] suggest that the CAMP-dependent protein kinases are involved in filament assembly. The consequences of such phosphorylations for behavioral functions are yet unknown.…”

Section: Discussionmentioning

confidence: 99%

Immunoelectron microscopical localization of the catalytic subunit of cAMP‐dependent protein kinases in brain microtubules and neurofilaments

Trinczek¹,

Schwoch²

1990

FEBS Letters

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The catalytic subunit of CAMP-dependent protein kinases was localized in microtubules and neurotilaments by immunogold electron microscopy. In microtubules, the label was similarly distributed as an immunolabel for the microtubule associated protein MAP 2. The neurofilaments showed no reaction with the MAP 2-antiserum. Our results support the suggestion of an in vivo role of CAMP-dependent protein kinases in the regulation of microtubules. In addition, this is the first demonstration that CAMP-dependent protein kinase is associated with neurofilaments.Neurofilament; Microtubule; CAMP-dependent protein kinase; Immunogold electron microscopy; Rat brain

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“…In mammalian brain a major part of protein kinase A seems to be harbored by microtubules, through binding to microtubule-associated protein-2 (MAP-2) (Vallee et al, 1981;Theurkauf and Vallee, 1982). MAP-2 is a good substrate for protein kinase A capable of incorporation of about 10 to 20 phosphate groups per molecule [molecular mass = 270 kilodaltons (kD)] under the effect of cyclic AMP (Theurkauf and Vallee, 1983;Selden and Pollard, 1983;Manso-Martinez et al, 1984;Goldenring et al, 1985). In vitro, the phosphorylation of MAPs increases the propensity of microtubules for depolymerization (Margolis and Wilson, 1979;Jameson et al, 1980;Jameson and Caplow, 1981;Lindwall and Cole, 1984) and weakens interactions with other cytoskeletal elements (Selden and Pollard, 1983).…”

mentioning

confidence: 99%

Microtubule‐Associated Cyclic AMP‐Dependent Protein Kinase in Drosophila melanogaster

Ádám

Friedrich

1988

Journal of Neurochemistry

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Microtubules were prepared from head extracts of the adult fruit fly, Drosophila melanogaster, by one-step, taxol-assisted polymerization. The microtubular fraction displayed cyclic AMP-dependent protein kinase (protein kinase A) activity, as witnessed by endogenous protein phosphorylation and by protein kinase assay. Microtubule-bound protein kinase A amounts to 4-5% of total soluble kinase activity, which is almost an order of magnitude less than in mammals. The high-molecular-weight microtubule-associated protein-2 (MAP-2), the main binding species for protein kinase A in mammalian brain microtubules, is not detectable in the fly system by protein staining and immunoblotting with anti-pig MAP-2 serum, as well as by hybridization of fly DNA with a cDNA probe for human MAP-2. Cyclic AMP removes a major part of the regulatory (R) subunit of the enzyme from Drosophila microtubules, as demonstrated by enzyme assay, autophosphorylation of R subunit, and quantitating cyclic AMP binding sites. It is proposed that permanently elevated cyclic AMP levels may elute protein kinase A from crucial intracellular binding sites, thereby interfering with signal transduction.

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Mammalian brain microtubules are sensitive to cyclic AMP in Vitro

Cited by 8 publications

References 32 publications

In vitro modulation of cisplatin accumulation in human ovarian carcinoma cells by pharmacologic alteration of microtubules.

In vitro modulation of cisplatin accumulation in human ovarian carcinoma cells by pharmacologic alteration of microtubules.

Immunoelectron microscopical localization of the catalytic subunit of cAMP‐dependent protein kinases in brain microtubules and neurofilaments

Microtubule‐Associated Cyclic AMP‐Dependent Protein Kinase in Drosophila melanogaster

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