Alpha 2-antiplasmin (or α2-antiplasmin or plasmin inhibitor) is a
serine protease inhibitor (serpin) responsible for inactivating
plasmin.[5] Plasmin is an important
enzyme that participates in
fibrinolysis and degradation of various other proteins. This protein is encoded by the SERPINF2 gene.[6]
Role in disease
Very few cases (<20) of A2AP deficiency have been described. As plasmin degrades blood clots, impaired inhibition of plasmin leads to a bleeding tendency, which was severe in the cases reported.
In liver
cirrhosis, there is decreased production of alpha 2-antiplasmin, leading to decreased inactivation of
plasmin and an increase in
fibrinolysis. This is associated with an increase risk of bleeding in liver disease.[7]
Interactions
Alpha 2-antiplasmin has been shown to
interact with:
Martí-Fàbregas J, Borrell M, Cocho D, Martínez-Ramírez S, Martínez-Corral M, Fontcuberta J, Martí-Vilalta JL (Jan 2008). "Change in hemostatic markers after recombinant tissue-type plasminogen activator is not associated with the chance of recanalization". Stroke: A Journal of Cerebral Circulation. 39 (1): 234–6.
doi:
10.1161/STROKEAHA.107.493767.
PMID18048863.
S2CID10052168.
Nielsen VG (Oct 2007). "Hydroxyethyl starch enhances fibrinolysis in human plasma by diminishing alpha2-antiplasmin-plasmin interactions". Blood Coagulation & Fibrinolysis. 18 (7): 647–56.
doi:
10.1097/MBC.0b013e3282a167dc.
PMID17890952.
S2CID45608070.
Magklara A, Mellati AA, Wasney GA, Little SP, Sotiropoulou G, Becker GW, Diamandis EP (Aug 2003). "Characterization of the enzymatic activity of human kallikrein 6: Autoactivation, substrate specificity, and regulation by inhibitors". Biochemical and Biophysical Research Communications. 307 (4): 948–55.
doi:
10.1016/S0006-291X(03)01271-3.
PMID12878203.
Frank PS, Douglas JT, Locher M, Llinás M, Schaller J (Feb 2003). "Structural/functional characterization of the alpha 2-plasmin inhibitor C-terminal peptide". Biochemistry. 42 (4): 1078–85.
doi:
10.1021/bi026917n.
PMID12549929.
Uszynski M, Klyszejko A, Zekanowska E (Dec 2000). "Plasminogen, alpha(2)-antiplasmin and complexes of plasmin-alpha(2)-antiplasmin (PAP) in amniotic fluid and blood plasma of parturient women". European Journal of Obstetrics, Gynecology, and Reproductive Biology. 93 (2): 167–71.
doi:
10.1016/S0301-2115(00)00283-9.
PMID11074138.
Alpha 2-antiplasmin (or α2-antiplasmin or plasmin inhibitor) is a
serine protease inhibitor (serpin) responsible for inactivating
plasmin.[5] Plasmin is an important
enzyme that participates in
fibrinolysis and degradation of various other proteins. This protein is encoded by the SERPINF2 gene.[6]
Role in disease
Very few cases (<20) of A2AP deficiency have been described. As plasmin degrades blood clots, impaired inhibition of plasmin leads to a bleeding tendency, which was severe in the cases reported.
In liver
cirrhosis, there is decreased production of alpha 2-antiplasmin, leading to decreased inactivation of
plasmin and an increase in
fibrinolysis. This is associated with an increase risk of bleeding in liver disease.[7]
Interactions
Alpha 2-antiplasmin has been shown to
interact with:
Martí-Fàbregas J, Borrell M, Cocho D, Martínez-Ramírez S, Martínez-Corral M, Fontcuberta J, Martí-Vilalta JL (Jan 2008). "Change in hemostatic markers after recombinant tissue-type plasminogen activator is not associated with the chance of recanalization". Stroke: A Journal of Cerebral Circulation. 39 (1): 234–6.
doi:
10.1161/STROKEAHA.107.493767.
PMID18048863.
S2CID10052168.
Nielsen VG (Oct 2007). "Hydroxyethyl starch enhances fibrinolysis in human plasma by diminishing alpha2-antiplasmin-plasmin interactions". Blood Coagulation & Fibrinolysis. 18 (7): 647–56.
doi:
10.1097/MBC.0b013e3282a167dc.
PMID17890952.
S2CID45608070.
Magklara A, Mellati AA, Wasney GA, Little SP, Sotiropoulou G, Becker GW, Diamandis EP (Aug 2003). "Characterization of the enzymatic activity of human kallikrein 6: Autoactivation, substrate specificity, and regulation by inhibitors". Biochemical and Biophysical Research Communications. 307 (4): 948–55.
doi:
10.1016/S0006-291X(03)01271-3.
PMID12878203.
Frank PS, Douglas JT, Locher M, Llinás M, Schaller J (Feb 2003). "Structural/functional characterization of the alpha 2-plasmin inhibitor C-terminal peptide". Biochemistry. 42 (4): 1078–85.
doi:
10.1021/bi026917n.
PMID12549929.
Uszynski M, Klyszejko A, Zekanowska E (Dec 2000). "Plasminogen, alpha(2)-antiplasmin and complexes of plasmin-alpha(2)-antiplasmin (PAP) in amniotic fluid and blood plasma of parturient women". European Journal of Obstetrics, Gynecology, and Reproductive Biology. 93 (2): 167–71.
doi:
10.1016/S0301-2115(00)00283-9.
PMID11074138.