Thromb Haemost 1998; 79(02): 395-399
DOI: 10.1055/s-0037-1614998
Letters to the Editor
Schattauer GmbH

Nickel Enhances Collagen-induced Platelet Activation Acting by Increasing the Organization of the Cytoskeleton

Fabio M. Pulcinelli
1   From the Dept. of Experimental Medicine and Pathology, University La Sapienza, Rome, Italy; Pharmacology Dept. and Sol Sherry Thrombosis Center, Temple University, Philadelphia, PA, USA
,
Silvia Sebastiani
1   From the Dept. of Experimental Medicine and Pathology, University La Sapienza, Rome, Italy; Pharmacology Dept. and Sol Sherry Thrombosis Center, Temple University, Philadelphia, PA, USA
,
Marzia Pesciotti
1   From the Dept. of Experimental Medicine and Pathology, University La Sapienza, Rome, Italy; Pharmacology Dept. and Sol Sherry Thrombosis Center, Temple University, Philadelphia, PA, USA
,
Pasquale Pignatelli
1   From the Dept. of Experimental Medicine and Pathology, University La Sapienza, Rome, Italy; Pharmacology Dept. and Sol Sherry Thrombosis Center, Temple University, Philadelphia, PA, USA
,
Pier Paolo Gazzaniga
1   From the Dept. of Experimental Medicine and Pathology, University La Sapienza, Rome, Italy; Pharmacology Dept. and Sol Sherry Thrombosis Center, Temple University, Philadelphia, PA, USA
,
James L. Daniel
1   From the Dept. of Experimental Medicine and Pathology, University La Sapienza, Rome, Italy; Pharmacology Dept. and Sol Sherry Thrombosis Center, Temple University, Philadelphia, PA, USA
› Author Affiliations
Further Information

Publication History

Received 10 March 1997

Accepted after resubmission 23 September 1997

Publication Date:
08 December 2017 (online)

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Summary

In keratinocytes, osteoclasts and enterocytes, Ni2+ acts as an agonist working through selective activation of the polyvalent cation-sensing receptor.

We report here that while Ni2+ alone had no direct ability to induce platelet aggregation or secretion, Ni2+ pretreatment produced these responses when platelets were stimulated with subthreshold concentrations of collagen. In addition, pretreatment with Ni2+ significantly enhanced collagen-induced phospholipase C activation and calcium mobilization. Platelet adhesion to collagen was increased and the inhibition of collagen-induced adhesion normally seen after cytochalasin D treatment was significantly diminished.

When Ni2+ was added to platelets alone, tyrosine phosphorylation of p60src was increased. Moreover, Ni2+ enhanced the amount of protein, especially actin, found in the low-speed Triton X-100 insoluble cyto-skeleton. Our results indicate that nickel, possibly acting via a platelet cation sensing receptor analogous to that which has been described in other cell types, may cause a rapid tyrosine kinase-dependent cyto-skeleton reorganization leading to enhanced adhesion of platelets to collagen and increasing collagen-dependent responses.