Annexins
247
to be determined, a number of biotech-
nological and medical applications are
under development. Most of these appli-
cations relate to the signature ability of
annexins to bind to acidic phospholipids
in the presence of calcium. Members of
this protein family have potential utility
as anticoagulants because they can pre-
vent the association of clotting factors with
acidic lipids on the surface of activated
platelets and endothelial cells. Annexins
may also function as immunosuppressive
agents by shielding phospholipids from at-
tack by phospholipase A
2
,thuspreventing
the release of arachidonic acid, which is
the precursor for a number of inflamma-
tory lipid mediators. Annexins are a staple
of any research laboratory studying apop-
tosis
in vitro
since one hallmark of the cell
death pathway is the exposure of phos-
phatidylserine on the cell surface, which
can be marked by the binding of a fluores-
cent annexin. Labeled annexins have also
been tested in whole animals for the ability
to localize occult thromboses or apoptotic
cells in whole-body imaging techniques,
and annexins fused to clot-dissolving en-
zymes have been tested for the ability to
direct these enzymes to thromboses.
See
also
Bioorganic
Chemistry;
Bioinorganic Chemistry; Calcium
Biochemistry; Phospholipids.
Bibliography
Books and Reviews
Creutz, C.E. (1992) The annexins and exocytosis,
Science
258
, 924–931.
Creutz, C.E. (2003) Reflections on twenty-Fve
years of annexin research, in: Bandorowicz-
Pikula, J. (Ed.)
Annexins: Biological Importance
and
Annexin-Related
Pathologies
,L
i
n
d
e
s
Bioscience, Georgetown, Texas, pp. 1–20.
Crumpton, M.J., Dedman, J.R. (1990) Protein
terminology tangle,
Nature
345
, 212.
Dedman, J.R.,
Smith, V.L.
(Eds.)
(1990)
Stimulus–Response
Coupling:
The
Role
of
Intracellular Calcium-Binding Proteins
,C
RC
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Gerke, V., Moss, S.E. (2002) Annexins: from
structure
to
function,
Physiol.
Rev.
82
,
331–371.
Moss, S.E. (Ed.) (1992)
The Annexins
,Po
r
t
land
Press, London.
Seaton, B.A. (Ed.) (1996)
Annexins: Molecular
Structure to Cellular Function
, RG Landes Co.,
Austin.
Primary Literature
Avila-Sakar, A.J., Kretsinger, R.H., Creutz, C.E.
(2000) Membrane-bound 3D structures reveal
the intrinsic flexibility of annexin VI,
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Biol.
130
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Berendes, R.,
Voges, D.,
Demange, P.,
Hu-
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Science
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medullary
protein
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causes
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J.
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Creutz, C.E.,
Sterner, D.C.
(1983)
Calcium
dependence
of
the
binding
of
synexin
to isolated chromafFn granules,
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Biophys. Res. Commun.
114
, 355–364.
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