Alpha 2-antiplasmin

From Wikipedia, the free encyclopedia

Serpin peptidase inhibitor, clade F (alpha-2 antiplasmin, pigment epithelium derived factor), member 2

Identifiers

SERPINF2; A2AP; AAP; ALPHA-2-PI; API; PLI

External IDs

OMIM: 262850 MGI: 107173 HomoloGene: 719

Gene ontology
Molecular Function:	• serine-type endopeptidase inhibitor activity • protein binding
Cellular Component:	• extracellular region • Golgi apparatus
Biological Process:	• acute-phase response

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_000934 (mRNA)
NP_000925 (protein)

NM_008878 (mRNA)
NP_032904 (protein)

Location

Chr 17: 1.59 - 1.61 Mb

Chr 11: 75.25 - 75.26 Mb

Pubmed search

[1]

[2]

Alpha 2-antiplasmin (or α₂-antiplasmin or plasmin inhibitor) is a serine protease inhibitor (serpin) responsible for inactivating plasmin, an important enzyme that participates in fibrinolysis and degradation of various other proteins. This protein is encoded by the SERPINF2 gene.^[1]

Fibrinolysis (simplified). Blue arrows denote stimulation, and red arrows inhibition.

1 Role in disease
2 See also
3 References
4 Further reading
5 External links

[edit] 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.

[edit] See also

Serpin

[edit] References

^ Entrez Gene: SERPINF2 serpin peptidase inhibitor, clade F (alpha-2 antiplasmin, pigment epithelium derived factor), member 2.

[edit] Further reading

Martí-Fàbregas J, Borrell M, Cocho D, et al. (2008). "Change in hemostatic markers after recombinant tissue-type plasminogen activator is not associated with the chance of recanalization.". Stroke 39 (1): 234-6. doi:10.1161/STROKEAHA.107.493767. PMID 18048863.
Nielsen VG (2007). "Hydroxyethyl starch enhances fibrinolysis in human plasma by diminishing alpha2-antiplasmin-plasmin interactions.". Blood Coagul. Fibrinolysis 18 (7): 647-56. doi:10.1097/MBC.0b013e3282a167dc. PMID 17890952.
Sazonova IY, Thomas BM, Gladysheva IP, et al. (2007). "Fibrinolysis is amplified by converting alpha-antiplasmin from a plasmin inhibitor to a substrate.". J. Thromb. Haemost. 5 (10): 2087-94. doi:10.1111/j.1538-7836.2007.02652.x. PMID 17883703.
Mutch NJ, Thomas L, Moore NR, et al. (2007). "TAFIa, PAI-1 and alpha-antiplasmin: complementary roles in regulating lysis of thrombi and plasma clots.". J. Thromb. Haemost. 5 (4): 812-7. doi:10.1111/j.1538-7836.2007.02430.x. PMID 17388801.
Christiansen VJ, Jackson KW, Lee KN, McKee PA (2007). "The effect of a single nucleotide polymorphism on human alpha 2-antiplasmin activity.". Blood 109 (12): 5286-92. doi:10.1182/blood-2007-01-065185. PMID 17317851.
Hayashido Y, Hamana T, Ishida Y, et al. (2007). "Induction of alpha2-antiplasmin 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.". Oncol. Rep. 17 (2): 417-23. PMID 17203182.
Shibata N, Kawarai T, Meng Y, et al. (2007). "Association studies between the plasmin genes and late-onset Alzheimer's disease.". Neurobiol. Aging 28 (7): 1041-3. doi:10.1016/j.neurobiolaging.2006.05.028. PMID 16828203.
Liu T, Qian WJ, Gritsenko MA, et al. (2006). "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry.". J. Proteome Res. 4 (6): 2070-80. doi:10.1021/pr0502065. PMID 16335952.
Lee KN, Jackson KW, Christiansen VJ, et al. (2004). "A novel plasma proteinase potentiates alpha2-antiplasmin inhibition of fibrin digestion.". Blood 103 (10): 3783-8. doi:10.1182/blood-2003-12-4240. PMID 14751930.
Anderson NL, Polanski M, Pieper R, et al. (2004). "The human plasma proteome: a nonredundant list developed by combination of four separate sources.". Mol. Cell Proteomics 3 (4): 311-26. doi:10.1074/mcp.M300127-MCP200. PMID 14718574.
Kapadia C, Yousef GM, Mellati AA, et al. (2004). "Complex formation between human kallikrein 13 and serum protease inhibitors.". Clin. Chim. Acta 339 (1-2): 157-67. doi:10.1016/j.cccn.2003.10.009. PMID 14687906.
Matsuno H, Okada K, Ueshima S, et al. (2004). "Alpha2-antiplasmin plays a significant role in acute pulmonary embolism.". J. Thromb. Haemost. 1 (8): 1734-9. doi:10.1046/j.1538-7836.2003.00252.x. PMID 12911586.
Magklara A, Mellati AA, Wasney GA, et al. (2003). "Characterization of the enzymatic activity of human kallikrein 6: Autoactivation, substrate specificity, and regulation by inhibitors.". Biochem. Biophys. Res. Commun. 307 (4): 948-55. doi:10.1016/S0006-291X(03)01271-3. PMID 12878203.
Cardoso C, Leventer RJ, Ward HL, et al. (2003). "Refinement of a 400-kb critical region allows genotypic differentiation between isolated lissencephaly, Miller-Dieker syndrome, and other phenotypes secondary to deletions of 17p13.3.". Am. J. Hum. Genet. 72 (4): 918-30. doi:10.1086/374320. PMID 12621583.
Frank PS, Douglas JT, Locher M, et al. (2003). "Structural/functional characterization of the alpha 2-plasmin inhibitor C-terminal peptide.". Biochemistry 42 (4): 1078-85. doi:10.1021/bi026917n. PMID 12549929.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899-903. doi:10.1073/pnas.242603899. PMID 12477932.
Turner RB, Liu L, Sazonova IY, Reed GL (2002). "Structural elements that govern the substrate specificity of the clot-dissolving enzyme plasmin.". J. Biol. Chem. 277 (36): 33068-74. doi:10.1074/jbc.M203782200. PMID 12080056.
Askew YS, Pak SC, Luke CJ, et al. (2002). "SERPINB12 is a novel member of the human ov-serpin family that is widely expressed and inhibits trypsin-like serine proteinases.". J. Biol. Chem. 276 (52): 49320-30. doi:10.1074/jbc.M108879200. PMID 11604408.
Uszynski M, Klyszejko A, Zekanowska E (2001). "Plasminogen, alpha(2)-antiplasmin and complexes of plasmin-alpha(2)-antiplasmin (PAP) in amniotic fluid and blood plasma of parturient women.". Eur. J. Obstet. Gynecol. Reprod. Biol. 93 (2): 167-71. doi:10.1016/S0301-2115(00)00283-9. PMID 11074138.
Hevessy Z, Patthy A, Kárpáti L, Muszbek L (2000). "alpha(2)-plasmin inhibitor is a substrate for tissue transglutaminase: an in vitro study.". Thromb. Res. 99 (4): 399-406. doi:10.1016/S0049-3848(00)00261-9. PMID 10963790.

[edit] External links

v • d • e Proteins: coagulation

Coagulation factors	primary hemostasis: vWF intrinsic pathway: HMWK/Bradykinin - Kallikrein - Hageman / FXII - FXI - FIX - FVIII extrinsic pathway: Tissue factor / FIII - FVII common pathway: FX - FV - (Pro)thrombin / FII, Fibrin / FI - FXIII

Inhibitors	Antithrombin (inhibits II, IX, X, XI, XII) - Protein C (inhibits V, VIII)/Protein S (cofactor for protein C) - Protein Z (inhibits X) - ZPI (inhibits X, XI) - TFPI (inhibits III)

Fibrinolysis	Plasmin - tPA/urokinase - PAI-1/2 - α2-AP - α2-macroglobulin - TAFI

v • d • e Serpins

inhibitory	Alpha 1-antichymotrypsin · Alpha 1-antitrypsin · Alpha 2-antiplasmin · Antithrombin · C1-inhibitor · Heparin cofactor II · Protein C inhibitor · Plasminogen activator inhibitor-1 · Plasminogen activator inhibitor-2 · Protein Z-related protease inhibitor · SERPINA4 · SERPINA6 · SERPINB1 · SERPINB3 · SERPINB4 · SERPINB6 · SERPINB7 · SERPINB8 · SERPINB9 · SERPINB13 · SERPINE2 · SERPINF2

Cross class inhibitory	MENT · SCCA-1 · crmA

noninhibitory	Heat shock protein 47 · Maspin · Ovalbumin · SERPINF1 · Thyroxine-binding globulin · Transcortin · SERPINF1

v • d • e Globulins: alpha globulins

Alpha 1-antichymotrypsin - Alpha 1-antitrypsin - Alpha 2-macroglobulin - Alpha 2-antiplasmin - Antithrombin - Ceruloplasmin - Haptoglobin - Heparin cofactor II - Orosomucoid - Retinol binding protein - Transcortin