Linked Life Data

7513122

Source:http://linkedlifedata.com/resource/pubmed/id/7513122

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3 Pt 1
pubmed:dateCreated
1994-5-20
pubmed:abstractText
We have previously shown that fibroblasts from patients with cystic fibrosis (CF) display a higher response to 4 beta-phorbol 12-myristate 13-acetate (PMA) than control fibroblasts for stimulation of both protein kinase C (PKC) cytosol-to-membrane translocation and glycoconjugate secretion. In this study we took advantage of these cells with differential responsiveness to PMA to investigate the endogenous substrate(s) involved in PKC stimulation of glycoconjugate secretion after verification of cystic fibrosis transmembrane conductance regulator gene expression in control and CF fibroblasts. We show that a 57-kDa protein that was associated with cytoskeleton and was identified as vimentin by immunoblotting emerged as a good candidate for mediating PKC stimulation of glycoconjugate secretion. 1) Its phosphorylation by PMA was abolished by PKC inhibition or depletion. 2) In both control and CF fibroblasts, the PMA-induced increase in its phosphorylation preceded the phorbol ester stimulation of glycoconjugate secretion. 3) For both processes, the concentration-response curves were superimposable, with higher maximal levels for CF fibroblasts relative to controls. 4) PMA-stimulated 57-kDa protein phosphorylation, like PMA-stimulated glycoconjugate secretion, was significantly increased by Ca2+. 5) Increased PMA phosphorylation of the 57-kDa protein as a result of okadaic acid inhibition of intracellular phosphatases was reflected in increased PMA stimulation of glycoconjugate secretion. In conclusion, 1) PMA phosphorylation of a cytoskeletal 57-kDa protein, identified as vimentin, appears to be an intermediate step in PKC stimulation of constitutive glycoconjugate secretion in human skin fibroblasts; and 2) this process is impaired in CF disease.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0002-9513
pubmed:author
pubmed:issnType
Print
pubmed:volume
266
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
C611-21
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed-meshheading:7513122-Base Sequence, pubmed-meshheading:7513122-Cells, Cultured, pubmed-meshheading:7513122-Cystic Fibrosis, pubmed-meshheading:7513122-Cystic Fibrosis Transmembrane Conductance Regulator, pubmed-meshheading:7513122-Fibroblasts, pubmed-meshheading:7513122-Glycoconjugates, pubmed-meshheading:7513122-Humans, pubmed-meshheading:7513122-Membrane Proteins, pubmed-meshheading:7513122-Molecular Probes, pubmed-meshheading:7513122-Molecular Sequence Data, pubmed-meshheading:7513122-Phosphorylation, pubmed-meshheading:7513122-Polymerase Chain Reaction, pubmed-meshheading:7513122-Protein Kinase C, pubmed-meshheading:7513122-RNA, Messenger, pubmed-meshheading:7513122-Reference Values, pubmed-meshheading:7513122-Skin, pubmed-meshheading:7513122-Tetradecanoylphorbol Acetate, pubmed-meshheading:7513122-Transcription, Genetic, pubmed-meshheading:7513122-Vimentin
pubmed:year
1994
pubmed:articleTitle
Phosphorylation of vimentin is an intermediate step in protein kinase C-mediated glycoconjugate secretion.
pubmed:affiliation
Laboratoire de Biochimie-Biologie Cellulaire, Institut National de la Santé et de la Recherche Médicale Unité 402, Faculté de Médecine Saint-Antoine, Paris, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't