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Differential osmosensing signalling pathways and G-protein involvement in human cervical cells with different tumour

M R Shen1, C Y Chou, M L Wu

  • 1Department of Obstetrics and Gynecology, National Cheng Kung University Medical College, Tainan, Taiwan.

Cellular Signalling
|March 3, 1998
PubMed

Insights

Cell volume regulation in cervical cells differs by tumor potential. Phospholipase C (PLC) and protein kinase C (PKC) pathways are key in cancer cells, while other PKC isoforms regulate normal and HPV-immortalized cells.

Area of Science:

  • Cell biology
  • Molecular signaling
  • Cancer research

Background:

  • Regulatory volume decrease (RVD) mechanisms vary across human cervical cells with differing tumor potential.
  • The specific ion channels and intracellular signaling events governing RVD remain incompletely understood.

Purpose of the Study:

  • To investigate the intracellular mechanisms and second messengers involved in cell volume regulation in human cervical cells.
  • To differentiate the signaling pathways mediating RVD in normal, HPV-immortalized, and cancerous cervical cells.

Main Methods:

  • Screening of intracellular mechanisms including phospholipase C (PLC), phospholipase A2 (PLA2), tyrosine kinase (TK), protein kinase C (PKC), protein kinase A (PKA), and cAMP.
  • Assessment of G-protein involvement using GTP-gamma S and pertussis toxin.

Main Results:

  • Phospholipase C (PLC) signaling, leading to protein kinase C (PKC) activation, is implicated in the RVD of cervical cancer cells.
  • Distinct PKC isoforms, independent of upstream PLC, mediate RVD in human papillomavirus (HPV)-immortalized and normal cervical epithelia.
  • G-protein involvement was observed in cervical cancer cells (facilitated by GTP-gamma S, inhibited by pertussis toxin) but not in normal or HPV-immortalized cells.

Conclusions:

  • Cell volume regulation in cervical cancer cells involves PLC-dependent PKC signaling and G-protein pathways.
  • RVD in normal and HPV-immortalized cervical cells is regulated by alternative PKC isoforms, independent of PLC and G-protein signaling pathways examined.

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