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Related Experiment Videos

Intracellular calcium requirements for beta1 integrin activation

M E Rowin1, R E Whatley, T Yednock

  • 1Department of Pediatrics, University of Utah School of Medicine, Salt Lake City 84132, USA.

Journal of Cellular Physiology
|April 3, 1998
PubMed
Summary

Intracellular calcium ([Ca++]i) and protein kinase C (PKC) synergistically activate beta1 integrins in human white blood cells. Lowering calcium levels impairs integrin activation, highlighting calcium's crucial role in this process.

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Area of Science:

  • Cellular Biology
  • Immunology
  • Molecular Biology

Background:

  • Human polymorphonuclear leukocytes (PMNs) utilize beta1 integrins for adhesion to extracellular matrix proteins.
  • This adhesion is triggered by agonists that elevate intracellular calcium ([Ca++]i).
  • Dimethyl sulfoxide (DMSO)-differentiated granulocytic HL60 cells serve as a model for human PMNs.

Purpose of the Study:

  • To investigate the contribution of intracellular calcium ([Ca++]i) alterations to the inside-out activation of beta1 integrins.
  • To elucidate the synergistic roles of intracellular calcium and protein kinase C (PKC) in beta1 integrin activation.

Main Methods:

  • Beta1 integrin activation was assessed by measuring the expression of an activation-dependent epitope using monoclonal antibody (mAb) 15/7.

Related Experiment Videos

  • Experiments involved exposing granulocytic HL60 cells to ionomycin (calcium ionophore), dioctanoylglycerol (PKC activator), or both.
  • Intracellular calcium levels were manipulated using chelators (Quin-2, EGTA) and replenished with ionomycin; phorbol myristate acetate (PMA) was used to stimulate PKC.

    • Main Results:

    • Neither ionomycin nor di-C8 alone increased mAb 15/7 binding or adhesion to fibronectin.
    • Simultaneous application of di-C8 and ionomycin significantly enhanced beta1 integrin activation and cell adhesion, indicating synergy.
    • Calcium chelation reduced basal and PMA-stimulated beta1 integrin activation, effects reversible by calcium repletion or higher PMA concentrations.

    Conclusions:

    • Intracellular calcium ([Ca++]i) plays a significant role in the inside-out activation of beta1 integrins.
    • A synergistic interaction between elevated [Ca++]i and protein kinase C (PKC) activation is crucial for optimal beta1 integrin activation.
    • These findings provide insights into the regulatory mechanisms of integrin function in human leukocytes.