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alpha2AP has a profibrotic effect probably not by the action as a plasmin (show PLG Proteins) inhibitor, and the blocking of alpha2AP exerts an antifibrotic effect in humans and mice with systemic sclerosis
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.
Plasmin (show PLG Proteins)/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 (show Alpha2 Antiplasmin Proteins) leads to functional inactivation of the antiprotease in infected macrophages
alpha2-antiplasmin induction inhibits E-cadherin (show CDH1 Proteins) processing mediated by the plasminogen (show PLG Proteins) activator/plasmin (show PLG Proteins) 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 (show TGFB1 Proteins)) synthesis, thereby resulting in attenuated fibrosis
2.65A X-ray crystal structure of an N-terminal truncated murine alpha(2)-antiplasmin (show Alpha2 Antiplasmin Proteins).
Results show that alpha2-antiplasmin is a critical regulator for vascular remodeling by inhibiting p53 (show TP53 Proteins)/p21 pathway.
Data suggest that protein aggregates interact with tissue-type plasminogen activator (show PLAT Proteins) and plasminogen (show PLG Proteins) to efficiently generate plasmin (show PLG Proteins); this aggregate-bound plasmin (show PLG Proteins) is shielded from inhibition by alpha-2-antiplasmin (show Alpha2 Antiplasmin Proteins) 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 (show SERPINE1 Proteins) in patients with OSA indicated that these patients had increased prothrombotic activity. OSA increases the risk of cardiovascular complications as it enhances prothrombotic activity.
Possession of the alpha2AP 407Lys allele was negatively associated with AAA (show APP Proteins), and thus changes in alpha2AP may affect aneurysm growth and development.
Two differentially expressed proteins, alpha-1-antitrypsin (SERPINA1 (show SERPINA1 Proteins)) and alpha-2 antiplasmin (SERPINF2 (show Alpha2 Antiplasmin Proteins)) 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 (show PLG Proteins), or plasminogen activator inhibitor 1 (show SERPINE1 Proteins)) are up-regulated in hyperglycemic type 1 diabetes with retinopathy.
Study revealed that plasmin (show PLG Proteins) was present in tumor tissue, and that it was responsible for processing progalanin to galanin (show GAL Proteins)(1-20) in the extracellular environment.
Data suggest that decreased amounts of alpha2-plasmin (show PLG Proteins) inhibitor in plasma vs serum ex vivo may reflect reduced factor XIII (show UGDH Proteins) (FXIII) in vivo; thus, plasma vs serum alpha2-plasmin (show PLG Proteins) inhibitor may be useful diagnostic marker for severe FXIII deficiency.
When the C terminus of alpha(2)-antiplasmin (show Alpha2 Antiplasmin Proteins) was removed, the binding affinity for active site-blocked plasmin (show PLG Proteins) remained high, suggesting additional exosite interactions between the serpin core and plasmin (show PLG Proteins).
Truncation of monocyte chemoattractant protein 1 (show CCL2 Proteins) by plasmin (show PLG Proteins) promotes blood-brain barrier disruption.
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