Thromb Haemost 1994; 72(02): 302-308
DOI: 10.1055/s-0038-1648857
Original Article
Schattauer GmbH Stuttgart

Platelet Activation Induced by lnterleukin-6: Evidence for a Mechanism Involving Arachidonic Acid Metabolism

Leslie Oleksowicz
1   The Department of Oncology, Montefiore Medical Center Hospital, Albert Einstein College of Medicine, Bronx, New York, USA
,
Zbignelw Mrowlec
1   The Department of Oncology, Montefiore Medical Center Hospital, Albert Einstein College of Medicine, Bronx, New York, USA
,
Dina Zuckerman
1   The Department of Oncology, Montefiore Medical Center Hospital, Albert Einstein College of Medicine, Bronx, New York, USA
,
Randi Isaacs
2   The Cytokine Development Unit, Sandoz Pharmaceuticals Corporation, East Hanover, New Jersey, USA
,
Janice Dutcher
1   The Department of Oncology, Montefiore Medical Center Hospital, Albert Einstein College of Medicine, Bronx, New York, USA
,
Elena Puszkin
3   The Department of Pathology, Montefiore Medical Center Hospital, Albert Einstein College of Medicine, Bronx, New York, USA
› Author Affiliations
Further Information

Publication History

Received: 15 November 1993

Accepted after resubmission07 April 1994

Publication Date:
24 July 2018 (online)

Summary

The effect of IL-6 on in vitro platelet function was investigated. Platelet-rich plasma (PRP) incubated with IL-6 showed a dose dependent enhancement of agonist induced maximum aggregation (AIMA) and secretion of thromboxane B2 (TXB2) as measured by RIA, in short term incubations. Dazoxiben (0.2 to 160 (µM) pretreated PRP incubated with IL-6 and aggregated with ionophore A23187, showed a dose dependent inhibition of TXB2 secretion concomitant with a dose dependent abrogation of IL-6’s enhancement of AIMA. A similar abrogation of AIMA was observed when these experiments were repeated using indomethacin. Further, PRP incubated with IL-6 showed a dose dependent increase in TXB2 and BTG secretion as measured by RIA and an increased incorporation of actin binding protein, talin, and myosin into the cytoskeletal core (triton insoluble residue) as shown by SDS-PAGE. The integrin glycoprotein Ilia (GPIIIa) was also observed to be retained into the cytoskeleton by immunoblot. These results suggest that IL-6 activates platelets in vitro and enhances AIMA via a mechanism involving arachidonic acid metabolism.

 
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