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Blood, Vol. 92 No. 8 (October 15), 1998:
pp. 2650-2656
RAPID COMMUNICATION
Integrins Involved in the Adhesion of Megakaryocytes to Fibronectin
and Fibrinogen
P.K. Schick,
C.M. Wojenski,
X. He,
J. Walker,
C. Marcinkiewicz, and
S. Niewiarowski
From the Cardeza Foundation for Hematologic Research, the Department
of Medicine, and the Department of Biochemistry and Molecular
Pharmacology, Thomas Jefferson Medical College, Philadelphia, PA; and
the Department of Physiology, Temple University Medical School,
Philadelphia, PA.
We studied integrins involved in the adhesion of resting and
activated megakaryocytes (MK) to fibronectin (FN) and fibrinogen (FGN).
Guinea pig MK were isolated and in some experiments were activated by
thrombin. MK adhering to FN or FGN coated on coverslips were
quantitated by a computerized image analysis program. The binding of
soluble human FN to MK was detected by Western blotting. Anti-integrin
antibodies, disintegrins, and cyclic RGD peptides were used to identify
integrins involved in the adhesion of MK to FN or FGN. Resting MK
adhered to coverslips with immobilized FN. The adhesion of MK to FN was
primarily inhibited by an anti- 5 antibody and EMF-10, a distintegrin
highly specific for 5 1. However, the adhesion of MK to FN was not
blocked by agents that inhibit IIb3, v3 or 41. A
1 activating antibody increased the number of MK bound to FN due to
the activation of 51. The binding of soluble FN was also
primarily inhibited by agents that block 51. Resting MK did not
adhere to FGN. However, MK activated by thrombin did adhere to FGN.
This binding was mediated by IIb3, because binding was
inhibited by bitistatin, a disintegrin, and a cyclic RGD peptide that
are known to block this integrin. The binding of thrombin-activated MK
to FN was mediated by both 51 and IIb3 based on the
additive effect of agents that inhibit these integrins. The study
indicates that resting MK bind to FN but not to FGN and that 51
is the major integrin involved in the binding of MK to FN. Activated MK
bind to FGN primarily by IIb3. However, the binding of activated
MK to FN is due to both 51 and IIb3. The demonstration that
51 and that IIb3 are involved in MK adhesion indicates that
these integrins may have a role in MK maturation and platelet
production.
© 1998 by The American Society of Hematology.
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