Alpha 2 antiplasmin. Medical search

A member of the serpin superfamily found in plasma that inhibits the lysis of fibrin clots which are induced by plasminogen activator. It is a glycoprotein, molecular weight approximately 70,000 that migrates in the alpha 2 region in immunoelectrophoresis. It is the principal plasmin inactivator in blood, rapidly forming a very stable complex with plasmin.

A product of the lysis of plasminogen (profibrinolysin) by PLASMINOGEN activators. It is composed of two polypeptide chains, light (B) and heavy (A), with a molecular weight of 75,000. It is the major proteolytic enzyme involved in blood clot retraction or the lysis of fibrin and quickly inactivated by antiplasmins.

The natural enzymatic dissolution of FIBRIN.

Precursor of plasmin (FIBRINOLYSIN). It is a single-chain beta-globulin of molecular weight 80-90,000 found mostly in association with fibrinogen in plasma; plasminogen activators change it to fibrinolysin. It is used in wound debriding and has been investigated as a thrombolytic agent.

Spontaneous or near spontaneous bleeding caused by a defect in clotting mechanisms (BLOOD COAGULATION DISORDERS) or another abnormality causing a structural flaw in the blood vessels (HEMOSTATIC DISORDERS).

Agents that prevent fibrinolysis or lysis of a blood clot or thrombus. Several endogenous antiplasmins are known. The drugs are used to control massive hemorrhage and in other coagulation disorders.

A protein derived from FIBRINOGEN in the presence of THROMBIN, which forms part of the blood clot.

Activated form of FACTOR XIII, a transglutaminase, which stabilizes the formation of the fibrin polymer (clot) culminating the blood coagulation cascade.

Glycoproteins with a molecular weight of approximately 620,000 to 680,000. Precipitation by electrophoresis is in the alpha region. They include alpha 1-macroglobulins and alpha 2-macroglobulins. These proteins exhibit trypsin-, chymotrypsin-, thrombin-, and plasmin-binding activity and function as hormonal transporters.

A proteolytic enzyme in the serine protease family found in many tissues which converts PLASMINOGEN to FIBRINOLYSIN. It has fibrin-binding activity and is immunologically different from UROKINASE-TYPE PLASMINOGEN ACTIVATOR. The primary sequence, composed of 527 amino acids, is identical in both the naturally occurring and synthetic proteases.

The process of the interaction of BLOOD COAGULATION FACTORS that results in an insoluble FIBRIN clot.

A heterogeneous group of proteolytic enzymes that convert PLASMINOGEN to FIBRINOLYSIN. They are concentrated in the lysosomes of most cells and in the vascular endothelium, particularly in the vessels of the microcirculation.

A metallocarboxypeptidase that removes C-terminal lysine and arginine from biologically active peptides and proteins thereby regulating their activity. It is a zinc enzyme with no preference shown for lysine over arginine. Pro-carboxypeptidase U in human plasma is activated by thrombin or plasmin during clotting to form the unstable carboxypeptidase U.

Plasma glycoprotein clotted by thrombin, composed of a dimer of three non-identical pairs of polypeptide chains (alpha, beta, gamma) held together by disulfide bonds. Fibrinogen clotting is a sol-gel change involving complex molecular arrangements: whereas fibrinogen is cleaved by thrombin to form polypeptides A and B, the proteolytic action of other enzymes yields different fibrinogen degradation products.

The process which spontaneously arrests the flow of BLOOD from vessels carrying blood under pressure. It is accomplished by contraction of the vessels, adhesion and aggregation of formed blood elements (eg. ERYTHROCYTE AGGREGATION), and the process of BLOOD COAGULATION.

Streptococcal fibrinolysin . An enzyme produced by hemolytic streptococci. It hydrolyzes amide linkages and serves as an activator of plasminogen. It is used in thrombolytic therapy and is used also in mixtures with streptodornase (STREPTODORNASE AND STREPTOKINASE). EC 3.4.-.

A proteolytic enzyme that converts PLASMINOGEN to FIBRINOLYSIN where the preferential cleavage is between ARGININE and VALINE. It was isolated originally from human URINE, but is found in most tissues of most VERTEBRATES.

Serum proteins that inhibit, antagonize, or inactivate COMPLEMENT C1 or its subunits.

Soluble protein fragments formed by the proteolytic action of plasmin on fibrin or fibrinogen. FDP and their complexes profoundly impair the hemostatic process and are a major cause of hemorrhage in intravascular coagulation and fibrinolysis.

An antifibrinolytic agent that acts by inhibiting plasminogen activators which have fibrinolytic properties.

Important modulators of the activity of plasminogen activators. The inhibitors belong to the serpin family of proteins and inhibit both the tissue-type and urokinase-type plasminogen activators.

Plasma glycoprotein member of the serpin superfamily which inhibits TRYPSIN; NEUTROPHIL ELASTASE; and other PROTEOLYTIC ENZYMES.

A single-chain polypeptide derived from bovine tissues consisting of 58 amino-acid residues. It is an inhibitor of proteolytic enzymes including CHYMOTRYPSIN; KALLIKREIN; PLASMIN; and TRYPSIN. It is used in the treatment of HEMORRHAGE associated with raised plasma concentrations of plasmin. It is also used to reduce blood loss and transfusion requirements in patients at high risk of major blood loss during and following open heart surgery with EXTRACORPOREAL CIRCULATION. (Reynolds JEF(Ed): Martindale: The Extra Pharmacopoeia (electronic version). Micromedex, Inc, Englewood, CO, 1995)

A plasma alpha 2 glycoprotein that accounts for the major antithrombin activity of normal plasma and also inhibits several other enzymes. It is a member of the serpin superfamily.

A fibrin-stabilizing plasma enzyme (TRANSGLUTAMINASES) that is activated by THROMBIN and CALCIUM to form FACTOR XIIIA. It is important for stabilizing the formation of the fibrin polymer (clot) which culminates the coagulation cascade.

Immunoelectrophoresis in which a second electrophoretic transport is performed on the initially separated antigen fragments into an antibody-containing medium in a direction perpendicular to the first electrophoresis.

A puncture or hole through the CORNEAL STROMA resulting from various diseases or trauma.

Triple-looped protein domains linked by disulfide bonds. These common structural domains, so-named for their resemblance to Danish pastries known as kringlers, play a role in binding membranes, proteins, and phospholipids as well as in regulating proteolysis. Kringles are also present in coagulation-related and fibrinolytic proteins and other plasma proteinases.

A member of the serpin family of proteins. It inhibits both the tissue-type and urokinase-type plasminogen activators.

The rate dynamics in chemical or physical systems.

Exogenous or endogenous compounds which inhibit SERINE ENDOPEPTIDASES.

Stable blood coagulation factor activated by contact with the subendothelial surface of an injured vessel. Along with prekallikrein, it serves as the contact factor that initiates the intrinsic pathway of blood coagulation. Kallikrein activates factor XII to XIIa. Deficiency of factor XII, also called the Hageman trait, leads to increased incidence of thromboembolic disease. Mutations in the gene for factor XII that appear to increase factor XII amidolytic activity are associated with HEREDITARY ANGIOEDEMA TYPE III.

One of the two major pharmacological subdivisions of adrenergic receptors that were originally defined by the relative potencies of various adrenergic compounds. The alpha receptors were initially described as excitatory receptors that post-junctionally stimulate SMOOTH MUSCLE contraction. However, further analysis has revealed a more complex picture involving several alpha receptor subtypes and their involvement in feedback regulation.

Endogenous substances, usually proteins, that are involved in the blood coagulation process.

Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.

Proteins prepared by recombinant DNA technology.

Hypoxia-inducible factor 1, alpha subunit is a basic helix-loop-helix transcription factor that is regulated by OXYGEN availability and is targeted for degradation by VHL TUMOR SUPPRESSOR PROTEIN.

The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.

Fibrinolysin or agents that convert plasminogen to FIBRINOLYSIN.

Laboratory tests for evaluating the individual's clotting mechanism.

Hemorrhagic and thrombotic disorders resulting from abnormalities or deficiencies of coagulation proteins.

Hemorrhagic and thrombotic disorders that occur as a consequence of abnormalities in blood coagulation due to a variety of factors such as COAGULATION PROTEIN DISORDERS; BLOOD PLATELET DISORDERS; BLOOD PROTEIN DISORDERS or nutritional conditions.

The time required for the appearance of FIBRIN strands following the mixing of PLASMA with phospholipid platelet substitute (e.g., crude cephalins, soybean phosphatides). It is a test of the intrinsic pathway (factors VIII, IX, XI, and XII) and the common pathway (fibrinogen, prothrombin, factors V and X) of BLOOD COAGULATION. It is used as a screening test and to monitor HEPARIN therapy.

Blood-coagulation factor VIII. Antihemophilic factor that is part of the factor VIII/von Willebrand factor complex. Factor VIII is produced in the liver and acts in the intrinsic pathway of blood coagulation. It serves as a cofactor in factor X activation and this action is markedly enhanced by small amounts of thrombin.

Storage-stable blood coagulation factor acting in the intrinsic pathway. Its activated form, IXa, forms a complex with factor VIII and calcium on platelet factor 3 to activate factor X to Xa. Deficiency of factor IX results in HEMOPHILIA B (Christmas Disease).

The classic hemophilia resulting from a deficiency of factor VIII. It is an inherited disorder of blood coagulation characterized by a permanent tendency to hemorrhage.

A deficiency of blood coagulation factor IX inherited as an X-linked disorder. (Also known as Christmas Disease, after the first patient studied in detail, not the holy day.) Historical and clinical features resemble those in classic hemophilia (HEMOPHILIA A), but patients present with fewer symptoms. Severity of bleeding is usually similar in members of a single family. Many patients are asymptomatic until the hemostatic system is stressed by surgery or trauma. Treatment is similar to that for hemophilia A. (From Cecil Textbook of Medicine, 19th ed, p1008)

Relationship of plasmin generation to cardiovascular disease risk factors in elderly men and women. (1/266)

Plasmin-alpha2-antiplasmin complex (PAP) marks plasmin generation and fibrinolytic balance. We recently observed that elevated levels of PAP predict acute myocardial infarction in the elderly, yet little is known about the correlates of PAP. We measured PAP in 800 elderly subjects who were free of clinical cardiovascular disease in 2 cohort studies: the Cardiovascular Health Study and the Honolulu Heart Program. Median PAP levels did not differ between the Cardiovascular Health Study (6.05+/-1.46 nmol/L) and the Honolulu Heart Program (6.11+/-1.44 nmol/L), and correlates of PAP were similar in both cohorts. In CHS, PAP levels increased with age (r=0. 30), procoagulant factors (eg, factor VIIc, r=0.15), thrombin activity (prothrombin fragment F1+2, r=0.29), and inflammation-sensitive proteins (eg, fibrinogen, r=0.44; factor VIIIc, r=0.37). PAP was associated with increased atherosclerosis as measured by the ankle-arm index (AAI) (P for trend, +info)

Alpha2-antiplasmin gene deficiency in mice is associated with enhanced fibrinolytic potential without overt bleeding. (2/266)

alpha2-antiplasmin (alpha2-AP) is the main physiologic plasmin inhibitor in mammalian plasma. Inactivation of the murine alpha2-AP gene was achieved by replacing, through homologous recombination in embryonic stem cells, a 7-kb genomic sequence encoding the entire murine protein (exon 2 through part of exon 10, including the stop codon) with the neomycin resistance expression cassette. Germline transmission of the mutated allele was confirmed by Southern blot analysis. Mendelian inheritance of the inactivated alpha2-AP allele was observed, and homozygous deficient (alpha2-AP-/-) mice displayed normal fertility, viability, and development. Reverse transcription-polymerase chain reaction confirmed the absence of alpha2-AP mRNA in kidney and liver from alpha2-AP-/- mice, in contrast to wild-type (alpha2-AP+/+) mice. Immunologic and functional alpha2-AP levels were undetectable in plasma of alpha2-AP-/- mice, and were about half of wild-type in heterozygous littermates (alpha2-AP+/-). Other hemostasis parameters, including plasminogen activator inhibitor-1, plasminogen, fibrinogen, hemoglobin, hematocrit, and blood cell counts were comparable for alpha2-AP+/+, alpha2-AP+/-, and alpha2-AP-/- mice. After amputation of tail or toe tips, bleeding stopped spontaneously in alpha2-AP+/+, as well as in alpha2-AP+/- and alpha2-AP-/- mice. Spontaneous lysis after 4 hours of intravenously injected 125I-fibrin-labeled plasma clots was significantly higher in alpha2-AP-/- than in alpha2-AP+/+ mice when injecting clots prepared from alpha2-AP+/+ plasma (78% +/- 5% v 46% +/- 9%; mean +/- SEM, n = 6 to 7; P =.02) or from alpha2-AP-/- plasma (81% +/- 5% v 46% +/- 5%; mean +/- SEM, n = 5; P =.008). Four to 8 hours after endotoxin injection, fibrin deposition in the kidneys was significantly reduced in alpha2-AP-/- mice, as compared with alpha2-AP+/+ mice (P +info)

Angiostatin inhibits endothelial and melanoma cellular invasion by blocking matrix-enhanced plasminogen activation. (3/266)

Angiostatin, a kringle-containing fragment of plasminogen, is a potent inhibitor of angiogenesis. The mechanism(s) responsible for the anti-angiogenic properties of angiostatin are unknown. We now report that human angiostatin blocks plasmin(ogen)-enhanced in vitro invasion of tissue plasminogen activator (t-PA)-producing endothelial and melanoma cells. Kinetic analyses demonstrated that angiostatin functions as a non-competitive inhibitor of extracellular-matrix (ECM)-enhanced, t-PA-catalysed plasminogen activation, with a Ki of 0.9+/-0.03 microM. This mechanism suggests that t-PA has a binding site for the inhibitor angiostatin, as well as for its substrate plasminogen that, when occupied, prevents ternary complex formation between t-PA, plasminogen and matrix protein. Direct binding experiments confirmed that angiostatin bound to t-PA with an apparent Kd [Kd(app)] of 6.7+/-0.7 nM, but did not bind with high affinity to ECM proteins. Together, these data suggest that angiostatin in the cellular micro-environment can inhibit matrix-enhanced plasminogen activation, resulting in reduced invasive activity, and suggest a biochemical mechanism whereby angiostatin-mediated regulation of plasmin formation could influence cellular migration and invasion. (+info)

Role of plasminogen system components in focal cerebral ischemic infarction: a gene targeting and gene transfer study in mice. (4/266)

BACKGROUND: The role of plasminogen system components in focal cerebral ischemic infarction (FCI) was studied in mice deficient in plasminogen (Plg-/-), in tissue or urokinase plasminogen activator (tPA-/- or uPA-/-), or in plasminogen activator inhibitor-1 or alpha2-antiplasmin (PAI-1(-/-) or alpha2-AP-/-). METHODS AND RESULTS: FCI was produced by ligation of the left middle cerebral artery and measured after 24 hours by planimetry of stained brain slices. In control (wild-type) mice, infarct size was 7.6+/-1.1 mm3 (mean+/-SEM), uPA-/- mice had similar infarcts (7.8+/-1.0 mm3, P=NS), tPA-/- mice smaller (2.6+/-0.80 mm3, P<0.0001), PAI-1(-/-) mice larger (16+/-0.52 mm3, P<0.0001), and Plg-/- mice larger (12+/-1.2 mm3, P=0.037) infarcts. alpha2-AP-/- mice had smaller infarcts (2. 2+/-1.1 mm3, P<0.0001 versus wild-type), which increased to 13+/-2.5 mm3 (P<0.005 versus alpha2-AP-/-) after intravenous injection of human alpha2-AP. Injection into alpha2-AP-/- mice of Fab fragments of affinospecific rabbit IgG against human alpha2-AP, after injection of 200 microg human alpha2-AP, reduced FCI from 11+/-1.5 to 5.1+/-1.1 mm3 (P=0.004). CONCLUSIONS: Plg system components affect FCI at 2 different levels: (1) reduction of tPA activity (tPA gene inactivation) reduces whereas its augmentation (PAI-1 gene inactivation) increases infarct size, and (2) reduction of Plg activity (Plg gene inactivation or alpha2-AP injection) increases whereas its augmentation (alpha2-AP gene inactivation or alpha2-AP neutralization) reduces infarct size. Inhibition of alpha2-AP may constitute a potential avenue to treatment of FCI. (+info)

Characterization of wild-type and mutant alpha2-antiplasmins: fibrinolysis enhancement by reactive site mutant. (5/266)

During human blood clotting, alpha2-antiplasmin (alpha2AP) becomes covalently linked to fibrin when activated blood clotting factor XIII (FXIIIa) catalyzes the formation of an isopeptide bond between glutamine at position two in alpha2AP and a specific epsilon-lysyl group in each of the alpha-chains of fibrin. This causes fibrin to become resistant to plasmin-mediated lysis. We found that chemically Arg-modified alpha2AP, which lacked plasmin-inhibitory activity, competed effectively with native alpha2AP for becoming cross-linked to fibrin and as a consequence, enhanced fibrinolysis. Recombinant alpha2AP reported to date by other groups either lacked or possessed a low level of FXIIIa substrate activity. As a first step in the development of an engineered protein that might have potential as a localized fibrin-specific fibrinolytic enhancer, we expressed recombinant alpha2AP in Pichia pastoris yeast. Two forms of nonglycosylated recombinant alpha2AP were expressed, isolated and characterized: (1) wild-type, which was analogous to native alpha2AP, and (2) a mutant form, which had Ala substituted for the reactive-site Arg364. Both the wild-type and mutant forms of alpha2AP functioned as FXIIIa substrates with affinities and kinetic efficiencies comparable to those of native alpha2AP, despite each having an additional acetylated Met blocking group at their respective amino-termini. Wild-type recombinant alpha2AP displayed full plasmin inhibitory activity, while mutant alpha2AP had none. Neither the absence of glycosylation nor blockage of the amino-terminus affected plasmin-inhibitory or FXIIIa substrate activities of wild-type alpha2AP. When our mutant alpha2AP, which lacked plasmin-inhibitory function, was added to human plasma or whole blood clots, urokinase (UK)-induced clot lysis was enhanced in a dose-dependent manner, indicating that mutant alpha2AP augmented lysis by competing with native alpha2AP for FXIIIa-catalyzed incorporation into fibrin. (+info)

Hepatitis C virus NS3 serine protease interacts with the serpin C1 inhibitor. (6/266)

Both NS3 protein (1007-1657) and its protease moiety (NS3p, 1027-1207) were able to interact in vitro with C1 Inhibitor (C1Inh) to give a 95-kDa Mr C1Inh cleavage product similar to that obtained upon proteolysis by complement protease C1s. High-Mr reaction products were also detected after incubation of C1Inh with NS3 but not with NS3p; they correspond to ester-bonded complexes from their hydroxylamine lability. Similar reactivity of NS3 was observed upon incubation with alpha2-antiplasmin. Serpin cleavage was prevented by treatment of NS3 with synthetic serine protease inhibitors. This interaction between viral NS3 and host serpins suggests that NS3 is likely to be controlled by infected cell protease inhibitors. (+info)

Solvent/detergent-treated plasma has decreased antitrypsin activity and absent antiplasmin activity. (7/266)

Solvent/detergent (S/D)-treated plasma is currently marketed by the American Red Cross as a virally inactivated alternative to fresh-frozen plasma (FFP). The serpin-type serine proteinase inhibitors have a flexible reactive site loop (RSL) that can convert from the active conformation to the inactive latent or polymerized conformations when exposed to heat and/or detergents. We have compared the conformational stability and inhibitory activity of 3 plasma serpins-antithrombin, antitrypsin, and antiplasmin-in S/D plasma and FFP. In S/D plasma, virtually 100% of the antiplasmin and approximately 50% of the antitrypsin are in either the latent or polymerized conformation and lack inhibitory activity, while in FFP only the active conformation is present. Interestingly, antithrombin is not affected by S/D treatment and remains fully active. These data demonstrate that S/D plasma is not simply a virally inactivated equivalent of FFP. The lack of antiplasmin activity and decreased antitrypsin activity in S/D plasma suggest that it may not be as effective as FFP for the treatment of bleeding in patients with systemic activation of proteolytic cascades, such as disseminated intravascular coagulation and sepsis, acquired fibrinolytic states, and large-volume transfusion. Although there has been extensive use of S/D plasma in several European countries with no reports of adverse effects, clinical studies directly comparing the efficacy of these 2 plasma products are needed to directly evaluate the relative therapeutic efficacy of FFP and S/D plasma for the treatment of these diseases. (+info)

Comparative effects of tissue plasminogen activator, streptokinase, and staphylokinase on cerebral ischemic infarction and pulmonary clot lysis in hamster models. (8/266)

BACKGROUND: The effects of alteplase (rtPA), streptokinase, and staphylokinase (rSak) on focal cerebral ischemia (FCI) and on pulmonary clot lysis (PCL) were studied in hamsters. METHODS AND RESULTS: ++FCI was produced by ligation of the left middle cerebral artery (MCA) and common carotid artery (CCA) and a 10-minute occlusion of the right CCA. FCI was measured after 24 hours by 2,3, 5-triphenyltetrazolium chloride staining. (125)I-fibrin-labeled plasma clots were injected via the jugular vein, and clot lysis was determined from residual radioactivity at 90 minutes. Study drugs were given intravenously over 60 minutes. FCI increased from 1.2 (0. 27 to 2.3) mm(3) (median and 17th to 83rd percentile range, n=24) in controls to 19 to 27 mm(3) with thrombolytic agent, with maximal rates at 0.13+/-0.05 mg/kg rtPA, 0.23+/-0.09 mg/kg streptokinase, and 0.037+/-0.025 mg/kg rSak. PCL increased from 18+/-2% (mean+/-SEM, n=27) in controls to approximately 85% with thrombolytics, with maximal rates at 0.12+/-0.03 mg/kg rtPA, 0.17+/-0.05 mg/kg streptokinase, and 0.018+/-0.002 mg/kg rSak. All agents caused maximal FCI and PCL rates at similar doses without alpha(2)-antiplasmin and fibrinogen depletion. Injection of 6 mg/kg human plasminogen combined with streptokinase caused a "systemic fibrinolytic state" with fibrinogen depletion. Maximal rates of FCI were obtained with 0.097+/-0.077 mg/kg streptokinase (P=0.26 versus streptokinase alone) and of PCL with 0.010+/-0.002 mg/kg (P=0.006 versus streptokinase alone). CONCLUSIONS: Thrombolytic agents cause similar dose-related extension of FCI after MCA ligation and PCL, irrespective of the agent or systemic plasmin generation. (+info)

... (or α2-antiplasmin or plasmin inhibitor) is a serine protease inhibitor (serpin) responsible for ...

https://en.wikipedia.org/wiki/Alpha_2-antiplasmin

Shieh BH, Travis J (1987). "The reactive site of human alpha 2-antiplasmin". J. Biol. Chem. 262 (13): 6055-9. doi:10.1016/S0021 ... 1997). "Assignment of a single disulphide bridge in human alpha2-antiplasmin: implications for the structural and functional ... 3.0.CO;2-P. PMID 9633818. S2CID 45885044. Chen JM, Ferec C (2000). "Molecular basis of hereditary pancreatitis". Eur. J. Hum. ... 41 (2-3): 305-10. doi:10.1016/0378-1119(86)90111-3. PMID 3011602. Honey NK, Sakaguchi AY, Quinto C, et al. (1984). "Chromosomal ...

https://en.wikipedia.org/wiki/Trypsin_1

Wiman B, Collen D (September 1979). "On the mechanism of the reaction between human alpha 2-antiplasmin and plasmin". J. Biol. ... Plasmin is inactivated by proteins such as α2-macroglobulin and α2-antiplasmin. The mechanism of plasmin inactivation involves ... Shieh BH, Travis J (May 1987). "The reactive site of human alpha 2-antiplasmin". J. Biol. Chem. 262 (13): 6055-9. doi:10.1016/ ... Plasmin has been shown to interact with Thrombospondin 1, Alpha 2-antiplasmin and IGFBP3. Moreover, plasmin induces the ...

https://en.wikipedia.org/wiki/Plasmin

Shieh BH, Travis J (May 1987). "The reactive site of human alpha 2-antiplasmin". J. Biol. Chem. 262 (13): 6055-9. doi:10.1016/ ... Brower MS, Harpel PC (August 1982). "Proteolytic cleavage and inactivation of alpha 2-plasmin inhibitor and C1 inactivator by ... Neutrophil elastase has been shown to interact with Alpha 2-antiplasmin, which belongs to the Serpin family of proteins. ... Humans have six elastase genes that encode the structurally similar proteins elastase 1, 2, 2A, 2B, 3A, and 3B. Neutrophil ...

https://en.wikipedia.org/wiki/Neutrophil_elastase

Carpenter SL, Mathew P (2008). "Alpha-2-antiplasmin and its deficiency: fibrinolysis out of balance". Haemophilia. 14 (6): 1250 ... Among the congenital conditions for hyperfibrinolysis, deficiency of alpha-2-antiplasmin (alpha-2-plasmin inhibitor) or ... complexes of plasmin and alpha-2-antiplasmin (PAP). However, the sensitivity and specificity of these methods is limited ...

https://en.wikipedia.org/wiki/Hyperfibrinolysis

Gogstad, GO; Stormorken, H; Solum, NO (15 July 1983). "Platelet alpha 2-antiplasmin is located in the platelet alpha-granules ... Stormorken, H; Gogstad, GO; Brosstad, F (August 1983). "Hereditary α2-antiplasmin deficiency". Thrombosis Research. 31 (4): 647 ... 5 (2): 129-37. doi:10.1111/j.1600-0609.1968.tb01727.x. PMID 5673825. Holmsen, H; Day, HJ; Stormorken, H (1969). "The blood ... 34 (2): 587-8. PMID 1105879. Dale, J; Myhre, E; Storstein, O; Stormorken, H; Efskind, L (July 1977). "Prevention of arterial ...

https://en.wikipedia.org/wiki/Helge_Stormorken

The disorder alpha-1 antitrypsin deficiency is one of the most common hereditary diseases. Since the stressed serpin fold is ... Lijnen HR, Okada K, Matsuo O, Collen D, Dewerchin M (April 1999). "Alpha2-antiplasmin gene deficiency in mice is associated ... alpha 1-antitrypsin Pittsburgh (358 Met leads to Arg), a fatal bleeding disorder". The New England Journal of Medicine. 309 (12 ... "Alpha-1-antitrypsin: molecular abnormality of S variant". British Medical Journal. 1 (6002): 130-131. January 1976. doi:10.1136 ...

https://en.wikipedia.org/wiki/Serpin

The PEDF structure includes 3 beta sheets and 10 alpha helices. This discovery demonstrated that PEDF has an asymmetrical ... "Entrez Gene: SERPINF1 serpin peptidase inhibitor, clade F (alpha-2 antiplasmin, pigment epithelium derived factor), member 1". ... 76 (2): 213-23. doi:10.1016/j.cardiores.2007.06.032. PMID 17651710. Guan M, Pang CP, Yam HF, Cheung KF, Liu WW, Lu Y (May 2004 ... 113 (2): 294-301. doi:10.1016/j.ophtha.2005.10.030. PMID 16406543. Becker J, Semler O, Gilissen C, Li Y, Bolz HJ, Giunta C, ...

https://en.wikipedia.org/wiki/PEDF

α1-antitrypsin Alpha 1-antichymotrypsin Orosomucoid (acid glycoprotein) Serum amyloid A Alpha 1-lipoprotein Haptoglobin Alpha- ... The alpha globulins typically have molecular weights of around 93 kDa. Alpha globulins include certain hormones, proteins that ... Alpha globulins are a group of globular proteins in plasma that are highly mobile in alkaline or electrically charged solutions ... 2u globulin α2-macroglobulin Ceruloplasmin Thyroxine-binding globulin Alpha 2-antiplasmin Protein C Alpha 2-lipoprotein ...

https://en.wikipedia.org/wiki/Alpha_globulin

... such as alpha 1-antichymotrypsin, alpha 2-antiplasmin and Heparin cofactor II. The physiological target proteases of ... Turk B, Brieditis I, Bock SC, Olson ST, Björk I (1997). "The oligosaccharide side chain on Asn-135 of alpha-antithrombin, ... alpha 1-antichymotrypsin and MENT. The conformational change most relevant for Factor IXa and Xa inhibition involves the P14 ... J. 314 (2): 647-653. doi:10.1042/bj3140647. PMC 1217096. PMID 8670081. Bedsted T, Swanson R, Chuang YJ, Bock PE, Björk I, Olson ...

https://en.wikipedia.org/wiki/Antithrombin

α2 - haptoglobin, α2-macroglobulin, α2-antiplasmin, ceruloplasmin. The beta (β) band - transferrin, LDL, complement The gamma ( ... The alpha (α) band consists of two parts, 1 and 2: α1 - α1-antitrypsin, α1-acid glycoprotein. ... 2, Method and application to human serum proteins". Ann. N. Y. Acad. Sci. 121 (2): 404-427. Bibcode:1964NYASA.121..404D. doi: ... 199 (2): 223-231. doi:10.1016/0003-2697(91)90094-A. PMID 1812789. Wittig, I.; Braun, H.P.; Schägger, H. (2006). "Blue native ...

https://en.wikipedia.org/wiki/Gel_electrophoresis_of_proteins

... alpha 1-antitrypsin MeSH D12.776.377.715.085.100 - alpha-macroglobulins MeSH D12.776.377.715.085.118 - antiplasmin MeSH D12.776 ... alpha-crystallin a chain MeSH D12.776.306.366.100.300 - alpha-crystallin b chain MeSH D12.776.306.366.300.100 - beta-crystallin ... steroid 12-alpha-hydroxylase MeSH D12.776.422.220.453.915.737 - steroid 16-alpha-hydroxylase MeSH D12.776.422.220.453.915.748 ... Retinoid X receptor alpha MeSH D12.776.826.701.500.625 - Retinoid X receptor beta MeSH D12.776.826.701.500.750 - Retinoid X ...

https://en.wikipedia.org/wiki/List_of_MeSH_codes_(D12.776)

... alpha 1-antitrypsin MeSH D12.776.124.790.106.100 - alpha-macroglobulins MeSH D12.776.124.790.106.118 - antiplasmin MeSH D12.776 ... alpha-macroglobulins MeSH D12.776.124.790.720.100.500 - pregnancy-associated alpha 2-macroglobulins The list continues at List ... immunoglobulin alpha-chains MeSH D12.776.124.486.485.114.619.251 - immunoglobulin d MeSH D12.776.124.486.485.114.619.251.500 - ... immunoglobulin alpha-chains MeSH D12.776.124.790.651.114.619.251 - immunoglobulin d MeSH D12.776.124.790.651.114.619.251.500 - ...

https://en.wikipedia.org/wiki/List_of_MeSH_codes_(D12.776.124)

... human alpha2 antiplasmin and denatured collagen I and III. NPY, FGF-21 and alpha2 antiplasmin are considered to be ... Fibroblast activation protein alpha (FAP-alpha) also known as prolyl endopeptidase FAP is an enzyme that in humans is encoded ... Bae S, Park CW, Son HK, Ju HK, Paik D, Jeon CJ, Koh GY, Kim J, Kim H (September 2008). "Fibroblast activation protein alpha ... Lee KN, Jackson KW, Christiansen VJ, Lee CS, Chun JG, McKee PA (February 2006). "Antiplasmin-cleaving enzyme is a soluble form ...

https://en.wikipedia.org/wiki/Fibroblast_activation_protein,_alpha

Alpha-ketoglutarate dehydrogenase deficiency Alpha-L-iduronidase deficiency Alpha-mannosidosis Alpha-sarcoglycanopathy Alpha- ... drugs antenatal infection Antinolo-Nieto-Borrego syndrome Antiphospholipid syndrome Anti-plasmin deficiency Anti-plasmin ... thalassemia Alpha thalassemia abnormal morphogenesis Alpha-thalassemia mental retardation syndrome Alport syndrome Alport ... totalis Alopecia universalis Alopecia universalis onychodystrophy vitiligo Alpers disease Alpha 1-antitrypsin deficiency Alpha- ...

https://en.wikipedia.org/wiki/List_of_diseases_(A)

Alpha-2 Antiplasmin deficiency. *. *. *. *. *. *. *. *. *. *. 13. *. Bernard Soulier syndrome. 19. 20. 21. 31. 31. 25. 28. 29. ... 2 "Multi-year patients" is the total number of individual patients who were reported by the HTCs in more than one calendar year ...

https://www.cdc.gov/ncbddd/hemophilia/communitycounts/data-reports/2021-03/table-1-patient-characteristics-by-calendar.html

Alpha-2 Antiplasmin Deficiency. PAI-1 Deficiency. #. (%). #,. (%). #. (%). #. (%). #. (%). #. (%). #. (%). #. (%). #. (%). #. ...

https://www.cdc.gov/ncbddd/hemophilia/communitycounts/data-reports/2019-3/table-4-rare-factors.html

... antiplasmin.". What is the importance of alpha(2)-antiplasmin?. Alpha(2)-antiplasmin is a molecule that prevents the breakdown ... But, with high levels of alpha(2)-antiplasmin in the blood of Long COVID patients - the bodys ability to break down the clots ... So normally, the bodys plasmin-antiplasmin system balances between clotting blood at wound sites and preventing internal blood ... Some of the trapped molecules contain clotting proteins such as fibrinogen, as well as alpha(2)- ...

https://www.openaccessgovernment.org/blood-clots-long-covid/121511/

Robert A Schwartz, MD, MPH is a member of the following medical societies: Alpha Omega Alpha, American Academy of Dermatology, ... Pere Gascon, MD, PhD is a member of the following medical societies: Alpha Omega Alpha, American College of Physicians, New ... and the pro-polypeptide of von Willebrand factor are all ligands for the integrins alpha 9beta 1 and alpha 4beta 1. J Biol Chem ... Jenner L, Husted L, Thirup S, Sottrup-Jensen L, Nyborg J. Crystal structure of the receptor-binding domain of alpha 2- ...

https://www.medscape.com/answers/209179-172608/what-is-the-role-of-fxiii-replacement-in-factor-xiii-fxiii-deficiency

Alpha-Globulins [D12.776.124.790.106] * alpha 1-Antichymotrypsin [D12.776.124.790.106.050] * alpha 1-Antitrypsin [D12.776. ... 2010; see ANTIPLASMIN 1980-2009. History Note. 2010(1980). Date Established. 1980/01/01. Date of Entry. 1979/05/23. Revision ... Alpha-Globulins [D12.776.377.715.085] * alpha 1-Antichymotrypsin [D12.776.377.715.085.050] * alpha 1-Antitrypsin [D12.776. ... alpha-2-Antiplasmin Preferred Term Term UI T358821. Date11/08/1999. LexicalTag NON. ThesaurusID NLM (2000). ...

https://meshb.nlm.nih.gov/record/ui?ui=D000979

Unfortunately, the quick action of alpha 2-antiplasmin is sometimes too fast, leaving clots in the body to do their damage. " ... A protein inhibitor called alpha 2-antiplasmin in blood stops the clot-busting effects of plasmin. ...

https://news.harvard.edu/gazette/story/2002/08/medical-student-engineers-protein-to-dissolve-blood-clots/

The other protein was identified as SerpinF2 (alpha 2-antiplasmin), the main inhibitor of plasmin and fibrinolytic activity. ...

https://asu.pure.elsevier.com/en/projects/fy15-arizona-alzheimers-consortium-15

... antiplasmin is intimately involved in thrombus stability and in the generation of fibrin-rich vessel wall lesions. Finally, it ... PLATELET ALPHA-GRANULES, FAST-ACTING INHIBITOR, VENOUS THROMBOSIS, T-PA, ENDOTHELIAL-CELLS, ANGINA-PECTORIS", ... antiplasmin is intimately involved in thrombus stability and in the generation of fibrin-rich vessel wall lesions. Finally, it ... antiplasmin is intimately involved in thrombus stability and in the generation of fibrin-rich vessel wall lesions. Finally, it ...

https://abdn.pure.elsevier.com/en/publications/fibrinolysis-and-thrombosis

C10.228.518.625.312 alpha-2-Antiplasmin D12.776.124.790.106.118 D12.776.124.790.106.90 D12.776.377.715.85.118 D12.776.377.715. ... D8.811.682.47.820.125 3-alpha-Hydroxysteroid Dehydrogenase (B-Specific) D8.811.682.47.820.186 3-Hydroxyacyl CoA Dehydrogenases ... D12.776.476.24.406 20-alpha-Hydroxysteroid Dehydrogenase D8.811.682.47.436.400.74 D8.811.682.47.820.125.74 20-Hydroxysteroid ... D8.811.641.752 Cyclooxygenase 2 Inhibitors D27.505.954.329.30.500.500 Cyclooxygenase Inhibitors D27.505.954.329.30.500 D- ...

https://decs.bvs.br/P/mnchg2014.txt

Soluble IL-2R alpha (CD25). < 24 hours (7 days a week). No. serum. ... 2013;38(2):235-240.. Beattie DT. Et al. An in vitro investigation of the cardiovascular effects of the 5-HT4 receptor selective ... 2017;9(2):7053.. Jensen G. et al. Consumption of nattokinase is associated with reduced blood pressure and von Willebrand ... 2007 Apr;12(2):137-45.. Fareed D. et al. Nitric oxide levels are upregulated in patients with malignancy-associated ...

https://www.machaondiagnostics.com/general/heparin-turns-100/

Sakata Y, Aoki N. Cross-linking of alpha 2-plasmin inhibitor to fibrin by fibrin-stabilizing factor. J Clin Invest. 1980;65(2): ... antiplasmin cross-linking. Blood. 2011;117(23):6371-4.. Article PubMed PubMed Central Google Scholar ... The antifibrinolytic function of factor XIII is exclusively expressed through alpha(2)- ... Alpha 2-antiplasmin (α2AP) is also cross-linked to fibrin via FXIII-A to stabilise the clot against premature degradation by ...

https://ccforum.biomedcentral.com/articles/10.1186/s13054-022-04167-x

DNA topoisomerase II alpha). ENSG00000131747. The enzyme, DNA topoisomerase II alpha is required to chromosome condensation, ... RECQL5 cooperates with Topoisomerase II alpha in DNA decatenation and cell cycle progression. Nucleic Acids Res. 2012;40:1621- ... Dual Effects of Alpha-Hydroxy Acids on the Skin. Molecules. 2018 23 ... alpha-2 antiplasmin, pigment epithelium derived factor), member 1) and SERPING 1 (serpin peptidase inhibitor, clade G (C1 ...

https://medsci.org/v18p1519.htm

Patients with intracerebral haemorrhage had higher D-dimer and plasmin-alpha-2-antiplasmin complex levels compared to healthy ... TICH-2) trial.. Two systematic reviews explore available evidence on efficacy and safety of tranexamic acid and other ... a range of plasma biomarkers involved in fibrinolysis and haemostasis were examined in a single-centre substudy of the TICH-2 ... lower baseline plasminogen and elevated day 2 matrix metalloproteinase-9 levels were associated with haematoma progression. ...

http://eprints.nottingham.ac.uk/58990/

Alpha-2-antiplasmin Active Synonym false false 75469019 Antiplasmin Active Synonym false false ... Antiplasmin (substance). Code System Preferred Concept Name. Antiplasmin (substance). Concept Status. Published. ...

https://phinvads.cdc.gov/vads/ViewCodeSystemConcept.action?oid=2.16.840.1.113883.6.96&code=45266004