These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Regulation of PDGF-beta receptor-operated Ca2+ channels by phospholipase C-gamma 1 in glomerular mesangial cells.
    Author: Ma H, Matsunaga H, Li B, Marrero MB, Ling BN.
    Journal: Am J Physiol; 1996 Nov; 271(5 Pt 2):F994-1003. PubMed ID: 8945993.
    Abstract:
    Platelet-derived growth factor (PDGF)-induced Ca2+ signaling mechanisms were examined in cultured rat glomerular mesangial cells. PDGF-BB stimulated the tyrosine phosphorylation of phospholipase C (PLC)-gamma 1, the formation of a PLC-gamma 1/PDGF-beta receptor membrane complex, and the generation of intracellular inositol 1,4,5-trisphosphate (IP3). Preincubation with a tyrosine kinase inhibitor (genistein) abolished these PDGF-induced responses. Activation of 1-pS Ca2+ channels in cell-attached patches by intrapipette PDGF-BB was also abolished by tyrosine kinase inhibition. In the absence of PDGF-BB, channels were activated in cell-attached patches exposed to intrapipette thapsigargin (IP3-independent releaser of intracellular Ca2+ stores) and in excised inside-out patches exposed to increasing "cytoplasmic" Ca2+ (10(-8) to 10(-6) M). In cell-attached patches, channel activation by PDGF-BB was abolished when extracellular Ca2+ was < 1 mM. In glomerular mesangial cells 1) PDGF-BB stimulates tyrosine phosphorylation of PLC-gamma 1, PDGF-beta receptor/PLC-gamma 1 membrane complex formation, IP3 production, and 1-pS Ca2+ channel activity; 2) all four PDGF-induced responses are abolished by tyrosine kinase inhibition; 3) PDGF receptor-operated Ca2+ channels are sensitive to both intra- and extracellular Ca2+.
    [Abstract] [Full Text] [Related] [New Search]