Linked Life Data

11158975

Source:http://linkedlifedata.com/resource/pubmed/id/11158975

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2001-2-22
pubmed:abstractText
Using adenovirus (Adv)-mediated overexpression of constitutively active (ca) and dominant-negative (dn) mutants, we examined whether protein kinase C (PKC)-epsilon, the major novel PKC isoenzyme expressed in the adult heart, was necessary and/or sufficient to induce specific aspects of the hypertrophic phenotype in low-density, neonatal rat ventricular myocytes (NRVM) in serum-free culture. Adv-caPKC-epsilon did not increase cell surface area or the total protein-to-DNA ratio. However, cell shape was markedly affected, as evidenced by a 67% increase in the cell length-to-width ratio and a 17% increase in the perimeter-to-area ratio. Adv-caPKC-epsilon also increased atrial natriuretic factor (ANF) and beta-myosin heavy chain (MHC) mRNA levels 2.5 +/- 0.3- and 2.1 +/- 0.2-fold, respectively, compared with NRVM infected with an empty, parent vector (P < 0.05 for both). Conversely, Adv-dnPKC-epsilon did not block endothelin-induced increases in cell surface area, the total protein-to-DNA ratio, or upregulation of beta-MHC and ANF gene expression. However, the dominant-negative inhibitor markedly suppressed endothelin-induced extracellular signal-regulated kinase (ERK) 1/2 activation. Taken together, these results indicate that caPKC-epsilon overexpression alters cell geometry, producing cellular elongation and remodeling without a significant, overall increase in cell surface area or total protein accumulation. Furthermore, PKC-epsilon activation and downstream signaling via the ERK cascade may not be necessary for cell growth, protein accumulation, and gene expression changes induced by endothelin.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0363-6135
pubmed:author
pubmed:issnType
Print
pubmed:volume
280
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
H756-66
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:11158975-Adenoviridae, pubmed-meshheading:11158975-Amino Acid Sequence, pubmed-meshheading:11158975-Animals, pubmed-meshheading:11158975-Atrial Natriuretic Factor, pubmed-meshheading:11158975-Cardiomegaly, pubmed-meshheading:11158975-Cell Size, pubmed-meshheading:11158975-Cells, Cultured, pubmed-meshheading:11158975-Endothelin-1, pubmed-meshheading:11158975-Gene Expression Regulation, Enzymologic, pubmed-meshheading:11158975-Heart Ventricles, pubmed-meshheading:11158975-Isoenzymes, pubmed-meshheading:11158975-MAP Kinase Signaling System, pubmed-meshheading:11158975-Mitogen-Activated Protein Kinases, pubmed-meshheading:11158975-Molecular Sequence Data, pubmed-meshheading:11158975-Muscle Fibers, Skeletal, pubmed-meshheading:11158975-Mutagenesis, pubmed-meshheading:11158975-Myocardium, pubmed-meshheading:11158975-Myosin Heavy Chains, pubmed-meshheading:11158975-Protein Kinase C, pubmed-meshheading:11158975-Protein Kinase C-epsilon, pubmed-meshheading:11158975-RNA, Messenger, pubmed-meshheading:11158975-Rats, pubmed-meshheading:11158975-Rats, Sprague-Dawley
pubmed:year
2001
pubmed:articleTitle
Role of protein kinase C-epsilon in hypertrophy of cultured neonatal rat ventricular myocytes.
pubmed:affiliation
Department of Physiology, Loyola University Chicago Stritch School of Medicine, Maywood, Illinois 60153, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't