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(Received for publication, November 28, 1995; and in revised form, February 12, 1996)
Volume 271,
Number 17,
Issue of April 26, 1996 pp. 10365-10371
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

Integrins
![]()

![]()
(platelet membrane
glycoprotein IIb-IIIa) and ![]()
![]()
![]()
are
members of the ![]()
subfamily of integrin adhesion
receptors. A cyclic peptide, KYGC(s-s)HarGDWPC(s-s) (cHarGD),
originally described by Scarborough et al. (Scarborough, R.
M., Naughton, M. A., Teng, W., Rose, J. W., Phillips, D. R., Nannizzi,
L., Arsten, A., Campbell, A. M., and Charo, I. F.(1993) J. Biol.
Chem. 268, 1066-1073) has been employed as a high affinity
ligand for ![]()

![]()
to examine the
specificity of the ![]()
integrins. cHarGD interacted with
high affinity with purified ![]()

![]()
(K
= 10 nM) or with
platelets (K
= 120 nM).
While cHarGD was specific for ![]()

![]()
in
the presence of Ca
, it bound to both ![]()
integrins in the presence of Mn
. Barbourin, a
snake venom disintegrin containing a reactive KGD sequence, remained
![]()

![]()
-specific, even in the presence of
Mn
. cHarGD became cross-linked to a site in
![]()
of ![]()

![]()
, which is
distinct from that of RGD peptides. These results allow identification
of at least four classes of ![]()
ligands: Class I,
represented by RGD peptides and vitronectin, react similarly with
![]()

![]()
and
![]()
![]()
![]()
; Class II, represented by cHarGD,
-chain peptides and fibrinogen, react with both receptors in the
presence of Mn
but only with
![]()

![]()
in the presence of
Ca
; Class III, represented by barbourin, are
![]()

![]()
-specific under all cation
conditions; Class IV, represented by osteopontin, bind primarily to
![]()
![]()
![]()
.
![]()
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