Document Detail

PKCalpha translocation is microtubule-dependent in passaged smooth muscle cells.
MedLine Citation:
PMID:  11114946     Owner:  NLM     Status:  MEDLINE    
The translocation of protein kinase C (PKC) isozymes from their inactive cell locus to a variety of cytoskeletal, organelle, and plasmalemmal sites is thought to play an important role in their activation and substrate specificity. We have utilized confocal microscopy to compare phorbol 12, 13 dibutyrate (PDB) - stimulated translocation of PKCalpha in cultured cells derived from rat vascular smooth muscle. In enzymatically dispersed, passaged smooth muscle cells, PKCalpha was uniformly distributed throughout the unstimulated cell. PDB stimulation resulted in extensive association of the PKCalpha into filamentous strands with subsequent accumulation of the isoform in the peri-nuclear region of the cell. Dual immunostaining indicated that PKCalpha was extensively colocalized with microtubules in the interval immediately following PDB stimulation but was largely disassociated from microtubules at 10 min, at which time the translocation of PKCalpha to the peri-nucleus/nucleus was nearly complete. It was further found that the use of colchicine to disrupt the microtubules caused the loss of PKCalpha translocation to the peri-nuclear region. By comparison, cytochalasin B disruption of actin microfilaments had no significant effect on this parameter. The data suggest that PDB stimulation results in a transient association of PKCalpha with cell microtubules and that the microtubules play an important role in the translocation of PKCalpha from the cytosol in passaged cells derived from rat aortic smooth muscle.
A S Battistella-Patterson; M E Fultz; C Li; W Geng; M Norton; G L Wright
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Acta physiologica Scandinavica     Volume:  170     ISSN:  0001-6772     ISO Abbreviation:  Acta Physiol. Scand.     Publication Date:  2000 Oct 
Date Detail:
Created Date:  2000-12-21     Completed Date:  2001-01-11     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  0370362     Medline TA:  Acta Physiol Scand     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  87-97     Citation Subset:  IM    
Department of Physiology, Marshall University School of Medicine, Huntington, WV 25704, USA.
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MeSH Terms
Aorta / cytology
Biological Transport / physiology
Cells, Cultured
Colchicine / pharmacology
Cytochalasin B / pharmacology
Cytosol / metabolism
Isoenzymes / metabolism*
Microfilaments / drug effects,  metabolism
Microtubules / drug effects,  metabolism*
Muscle, Smooth, Vascular / cytology,  enzymology*
Protein Kinase C / metabolism*
Protein Kinase C-alpha
Rats, Sprague-Dawley
Reg. No./Substance:
0/Isoenzymes; 14930-96-2/Cytochalasin B; 64-86-8/Colchicine; EC Kinase C; EC Kinase C-alpha

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