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Physiological Reviews, Vol. 82, No. 2, April 2002, pp. 331-371; 10.1152/physrev.00030.2001.
Copyright ©2002 by the American Physiological Society
Institute for Medical Biochemistry, Center for Molecular Biology of Inflammation, University of Münster, Münster, Germany; and Department of Cell Biology, Institute of Ophthalmology, University College London, London, United Kingdom
Gerke, Volker and
Stephen E. Moss.
Annexins: From Structure to Function. Physiol. Rev. 82: 331-371, 2002.
Annexins are Ca2+ and
phospholipid binding proteins forming an evolutionary conserved
multigene family with members of the family being expressed throughout
animal and plant kingdoms. Structurally, annexins are characterized by
a highly
-helical and tightly packed protein core domain considered
to represent a Ca2+-regulated membrane binding module. Many
of the annexin cores have been crystallized, and their molecular
structures reveal interesting features that include the architecture of
the annexin-type Ca2+ binding sites and a central
hydrophilic pore proposed to function as a Ca2+ channel. In
addition to the conserved core, all annexins contain a second principal
domain. This domain, which NH2-terminally precedes the
core, is unique for a given member of the family and most likely
specifies individual annexin properties in vivo. Cellular and animal
knock-out models as well as dominant-negative mutants have
recently been established for a number of annexins, and the effects of
such manipulations are strikingly different for different members of
the family. At least for some annexins, it appears that they
participate in the regulation of membrane organization and membrane
traffic and the regulation of ion (Ca2+) currents across
membranes or Ca2+ concentrations within cells. Although
annexins lack signal sequences for secretion, some members of the
family have also been identified extracellularly where they can act as
receptors for serum proteases on the endothelium as well as inhibitors
of neutrophil migration and blood coagulation. Finally, deregulations
in annexin expression and activity have been correlated with human
diseases, e.g., in acute promyelocytic leukemia and the
antiphospholipid antibody syndrome, and the term
annexinopathies has been coined.
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