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Lysplasminogen

Lysplasminogen, commonly written Lys-plasminogen, is a proteolytic zymogen variant of plasminogen. It differs from the canonical Glu-plasminogen in that its N-terminal residue is a lysine, which confers enhanced affinity for lysine-binding sites in plasminogen kringle domains and for lysine-containing targets such as fibrin.

Lys-plasminogen can be formed by proteolytic processing that exposes an N-terminal lysine; this form retains the

On fibrin surfaces, Lys-plasminogen binds with higher affinity and is readily activated by tissue-type plasminogen activator

In clinical contexts, plasminogen disorders can cause mucosal lesions such as ligneous conjunctivitis; Lys-plasminogen is a

overall
structure
of
plasminogen
with
its
kringle
domains
and
the
catalytic
region
and
shows
altered
interactions
with
activators
and
inhibitors.
The
lysine-terminus
influences
how
the
molecule
engages
with
binding
sites
on
fibrin
and
other
surfaces.
(tPA)
or
urokinase-type
plasminogen
activator
(uPA),
generating
plasmin
and
promoting
fibrinolysis.
The
lysine-binding
property
also
facilitates
recruitment
of
plasminogen
to
sites
of
clot
formation,
supporting
localized
breakdown
of
fibrin.
component
of
the
broader
plasminogen
system
and
is
not
by
itself
a
separate
disease
entity.
Researchers
study
its
role
in
clot
resolution,
its
interactions
with
receptors
and
inhibitors,
and
its
contribution
to
the
regulation
of
fibrinolysis.