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ANNA2

ANNA2 generally refers to annexin A2, a member of the annexin family of calcium-dependent phospholipid-binding proteins. In humans the canonical gene symbol is ANXA2, and ANNA2 is an alternative name used in some databases and literature to denote the same gene product. The annexin A2 protein is about 36 kilodaltons and is broadly expressed across tissues, with roles in membrane dynamics and cytoskeletal organization.

Function and mechanism

Annexin A2 binds to phospholipid membranes in a calcium-dependent manner and participates in a range of cellular

Clinical and biological significance

Annexin A2 has been studied in various physiological and pathological contexts. It is implicated in inflammatory

Notes

While ANXA2 is the standard gene symbol, ANNA2 may appear in some sources; readers should verify with

processes
including
vesicle
trafficking,
membrane
organization,
endocytosis,
and
exocytosis.
It
forms
a
functional
heterotetrameric
complex
with
S100A10
(p11),
known
as
the
A2t
complex,
which
promotes
plasminogen
activation
on
the
cell
surface.
Through
these
interactions,
annexin
A2
participates
in
regulating
fibrinolysis,
cell
surface
receptor
activity,
and
extracellular
matrix
remodeling.
The
protein
also
associates
with
actin
and
other
cytoskeletal
elements,
influencing
cell
migration
and
adhesion.
Phosphorylation,
notably
by
Src-family
kinases
at
specific
tyrosine
residues,
modulates
its
localization
and
activity,
including
translocation
to
the
cell
surface.
responses,
wound
healing,
and
angiogenesis.
In
oncology,
altered
ANXA2
expression
is
linked
with
tumor
progression
and
metastasis
in
several
cancers,
and
the
A2t
complex
can
affect
cancer
cell
invasiveness.
Autoimmune
conditions
may
feature
autoantibodies
against
annexin
A2,
reflecting
a
role
in
immune-related
processes.
due
to
its
surface
localization
and
involvement
in
plasmin
generation,
annexin
A2
is
also
explored
as
a
potential
biomarker
and
therapeutic
target
in
certain
diseases.
current
gene
and
protein
databases
for
precise
nomenclature
and
isoforms.