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These results suggest that alpha2AP negatively affects osteoblast differentiation and function by inhibiting the Wnt/beta-catenin pathway.
alpha2AP has a profibrotic effect probably not by the action as a plasmin inhibitor, and the blocking of alpha2AP exerts an antifibrotic effect in humans and mice with systemic sclerosis
A2AP is not significantly affected by the Pla protease during pneumonic plague, and although A2AP participates in immune modulation in the lungs, it has limited impact on the course or ultimate outcome of the infection.
a2AP deficiency enhanced thrombus dissolution, increased cerebral blood flow, reduced brain infarction, and decreased brain swelling.
our findings suggest that alpha2AP is a crucial mediator of motor function, cognitive function, anxiety-like behavior and depression-like behavior, providing new insights into the role of alpha2AP in the brain functions.
Alpha 2 antiplasmin is involved in the recruitment of lymphocytes in the peripheral tissues.Alpha 2 antiplasmin contributes to the maintenance of immunological functions that are related to IgE.
alpha2AP is associated with the progression of fibrosis.
Plasmin/alpha(2)-AP system played an important role in hepatic repair via clearance from the injury area.
PgtE mediated degradation of the antiprotease alpha(2)-antiplasmin leads to functional inactivation of the antiprotease in infected macrophages
alpha2-antiplasmin induction inhibits E-cadherin processing mediated by the plasminogen activator/plasmin system, leading to suppression of progression of oral squamous cell carcinoma via upregulation of cell-cell adhesion
The lack of alpha2AP attenuated TGF-beta(1) synthesis, thereby resulting in attenuated fibrosis
2.65A X-ray crystal structure of an N-terminal truncated murine alpha(2)-antiplasmin.
Results show that alpha2-antiplasmin is a critical regulator for vascular remodeling by inhibiting p53/p21 pathway.
findings suggest that the alpha2AP Arg407Lys polymorphism could be involved in the pathogenesis of cerebral ischemia and its outcomes
Data suggest that protein aggregates interact with tissue-type plasminogen activator and plasminogen to efficiently generate plasmin; this aggregate-bound plasmin is shielded from inhibition by alpha-2-antiplasmin and degrades protein aggregates to release smaller, soluble but relatively hydrophobic peptide fragments; these fragments bind to and are cytotoxic to microglia (by not vascular endothelial cells).
Higher plasma concentrations of a-2-AP and PAI-1 in patients with OSA indicated that these patients had increased prothrombotic activity. OSA increases the risk of cardiovascular complications as it enhances prothrombotic activity.
This review presents recent findings regarding the main aspects of the natural heterogeneity of A2AP with particular focus on the functional and possible clinical implications. [review]
Possession of the alpha2AP 407Lys allele was negatively associated with AAA, and thus changes in alpha2AP may affect aneurysm growth and development.
Changes in plasma A2AP are associated with cardiovascular disease event presentation.
A significant correlation was found between soluble fibroblast activation protein levels and alpha2-antiplasmin cleavage in coronary thrombosis.
increased N-terminal cleavage of alpha2AP may have a role in liver cirrhosis
FXIII-A has a functional role through exposure on the activated platelet membrane where it exerts antifibrinolytic function by cross-linking alpha2AP to fibrin
Two differentially expressed proteins, alpha-1-antitrypsin (SERPINA1) and alpha-2 antiplasmin (SERPINF2) are associated with purpura fulminans.
Data suggest serum A2AP (SERPINF2) level can serve as biomarker for diabetic retinopathy; levels of A2AP (but not fibrinogen, plasminogen, or plasminogen activator inhibitor 1) are up-regulated in hyperglycemic type 1 diabetes with retinopathy.
protective mediator during gram-negative (pneumo)sepsis, limiting bacterial growth, inflammation, tissue injury, and coagulation
Study revealed that plasmin was present in tumor tissue, and that it was responsible for processing progalanin to galanin(1-20) in the extracellular environment.
Data suggest that decreased amounts of alpha2-plasmin inhibitor in plasma vs serum ex vivo may reflect reduced factor XIII (FXIII) in vivo; thus, plasma vs serum alpha2-plasmin inhibitor may be useful diagnostic marker for severe FXIII deficiency.
When the C terminus of alpha(2)-antiplasmin was removed, the binding affinity for active site-blocked plasmin remained high, suggesting additional exosite interactions between the serpin core and plasmin.
fibrinolysis is enhanced by inhibiting enzymatic cleavage of precursor alpha2-antiplasmin
Truncation of monocyte chemoattractant protein 1 by plasmin promotes blood-brain barrier disruption.
Levels of free full-length alpha2AP were decreased in myocardial infarction (MI); the percentage of C-terminally cleaved alpha2AP was unaltered, and Arg407Lys did not influence alpha2AP levels or MI risk.
the antifibrinolytic function of FXIII is independent of fibrin-fibrin cross-linking and is expressed exclusively through alphaAP.
The highly conserved nature of rabbit alpha(2)AP reinforces its role as a vital antifibrinolytic protein and supports fibrinolytic investigations in models employing this small animal.
This gene encodes a member of the serpin family of serine protease inhibitors. The protein is a major inhibitor of plasmin, which degrades fibrin and various other proteins. Consequently, the proper function of this gene has a major role in regulating the blood clotting pathway. Mutations in this gene result in alpha-2-plasmin inhibitor deficiency, which is characterized by severe hemorrhagic diathesis. Multiple transcript variants encoding different isoforms have been found for this gene.
alpha 2 antiplasmin
, alpha-2-plasmin inhibitor
, pigment epithelium derived factor
, plasmin inhibitor alpha 2
, serine (or cysteine) proteinase inhibitor, clade F, member 2
, serpin F2
, serine (or cysteine) peptidase inhibitor, clade F, member 2
, serpin peptidase inhibitor, clade F , member 2, like
, serine (or cysteine) proteinase inhibitor, clade F (alpha-2 antiplasmin, pigment epithelium derived factor), member 2
, alpha-2-PI serine protease inhibitor