Alpha 2-antiplasmine

SERPINF2
Structures disponibles
PDB	Recherche d'orthologue: PDBe RCSB
Identifiants PDB
	2R9Y
Identifiants
Aliases	SERPINF2
IDs externes	OMIM: 613168 MGI: 107173 HomoloGene: 719 GeneCards: SERPINF2
Position du gène (Homme)
Chr.	Chromosome 17 humain
Fin	1,755,265 bp
Position du gène (Souris)
Chr.	Chromosome 11 (souris)
Fin	75,330,417 bp
Expression génétique
	Fortement exprimé dans
	right lobe of liver; ; left uterine tube; ; prostate; ; upper lobe of left lung; ; human kidney; ; right ovary; ; lactiferous gland; ; right testis; ; right lobe of thyroid gland; ; Myomètre;
	Fortement exprimé dans
	Vésicule vitelline; ; foie; ; right kidney; ; proximal tubule; ; left lobe of liver; ; human kidney; ; vésicule biliaire; ; fetal liver hematopoietic progenitor cell; ; paroi abdominale; ; fœtus humain;
	Plus de données d'expression de référence
	Plus de données d'expression de référence
Gene Ontology
Fonction moléculaire	peptidase inhibitor activity; protein homodimerization activity; liaison de protéase; liaison protéique; serine-type endopeptidase inhibitor activity; endopeptidase inhibitor activity;
Composant cellulaire	blood microparticle; fibrinogène; région extracellulaire; surface cellulaire; exosome; platelet alpha granule lumen; milieu extracellulaire; collagen-containing extracellular matrix;
Processus biologique	positive regulation of collagen biosynthetic process; negative regulation of peptidase activity; negative regulation of fibrinolysis; negative regulation of plasminogen activation; maintenance of blood vessel diameter homeostasis by renin-angiotensin; blood vessel morphogenesis; fibrinolyse; collagen fibril organization; platelet degranulation; positive regulation of JNK cascade; response to organic substance; acute-phase response; positive regulation of cell differentiation; positive regulation of ERK1 and ERK2 cascade; positive regulation of transforming growth factor beta production; positive regulation of stress fiber assembly; positive regulation of transcription by RNA polymerase II; positive regulation of smooth muscle cell proliferation; positive regulation of cell-cell adhesion mediated by cadherin; negative regulation of endopeptidase activity;
	Sources:Amigo / QuickGO
Orthologues
	5345
	18816
	ENSG00000167711; ENSG00000276838
	ENSMUSG00000038224
	P08697
	Q61247
	NM_000934; NM_001165920; NM_001165921
	NM_008878
	NP_000925; NP_001159392; NP_001159393
	NP_032904
	Wikidata
Voir/Editer Humain	Voir/Editer Souris

L'alpha 2-antiplasmine est une protéine inhibitrice de la plasmine, et donc de la fibrinolyse. Son gène est SERPINF2 porté par le chromosome 17 humain.

Elle a été découverte en 1976^[5].

Rôle

Formée de 464 acides aminés, elle est clivée par une protéase (APCE) en un protéine de 452 acides aminés plus actives^[6].

Il s'agit du principal inhibiteur de la plasmine^[7]. Elle se lie au facteur XIII et à la fibrine, permettant la stabilisation du thrombus^[8].

Médecine

Son taux s'élève dans le cas des maladies thromboemboliques survenant malgré une anticoagulation prophylactique^[9].

Un déficit congénital en cette protéine induit un syndrome hémorragique^[5].

Son inhibition pourrait constituer une voie thérapeutique : elle activerait la fibrinolyse sans dégrader le fibrinogène et avec un moindre risque de saignements^[10]. Cette inhibition par des anticorps monoclonaux ou par de petits peptides sont en cours de test dans le traitement des thromboses^[11].

Notes et références

↑ ^{a b et c} ENSG00000276838 GRCh38: Ensembl release 89: ENSG00000167711, ENSG00000276838 - Ensembl, May 2017
↑ ^{a b et c} GRCm38: Ensembl release 89: ENSMUSG00000038224 - Ensembl, May 2017
↑ « Publications PubMed pour l'Homme », sur National Center for Biotechnology Information, U.S. National Library of Medicine
↑ « Publications PubMed pour la Souris », sur National Center for Biotechnology Information, U.S. National Library of Medicine
↑ ^{a et b} Aoki N, Discovery of alpha2-plasmin inhibitor and its congenital deficiency, J Thromb Haemost, 2005;3:623–631
↑ Lee KN, Jackson KW, Christiansen VJ, Chung KH, McKee PA, A novel plasma proteinase potentiates alpha2-antiplasmin inhibition of fibrin digestion, Blood, 2004;103:3783–3788
↑ Leebeek FW, Kluft C, Knot EA, Los P, Cohen AF, Six AJ, Plasmin inhibitors in the prevention of systemic effects during thrombolytic therapy: specific role of the plasminogen-binding form of alpha 2-antiplasmin, J Am Coll Cardiol, 1990;15:1212–1220
↑ Mitchell JL, Lionikiene AS, Fraser SR, Whyte CS, Booth NA, Mutch NJ, Functional factor XIII-A is exposed on the stimulated platelet surface, Blood, 2014;124:3982–3990
↑ Wojcik M, Zareba L, Undas A. Prothrombotic fibrin clot properties are associated with post-discharge venous thromboembolism in acutely ill medical patients, Thromb Res, 2019;182:141–149
↑ Singh S, Houng A, Reed GL, Releasing the brakes on the fibrinolytic system in pulmonary emboli: unique effects of plasminogen activation and α2-antiplasmin inactivation, Circulation, 2017;135:1011−1020
↑ Singh S, Kumar P, Padwad YS, Jaffer FA, Reed GL, Targeting fibrinolytic inhibition for venous thromboembolism treatment: Overview of an emerging therapeutic approach, Circulation, 2024;150!884-898

[refGRCh38Ensembl-1] {a b et c} ENSG00000276838 GRCh38: Ensembl release 89: ENSG00000167711, ENSG00000276838 - Ensembl, May 2017

[refGRCm38Ensembl-2] {a b et c} GRCm38: Ensembl release 89: ENSMUSG00000038224 - Ensembl, May 2017

[3] « Publications PubMed pour l'Homme », sur National Center for Biotechnology Information, U.S. National Library of Medicine

[4] « Publications PubMed pour la Souris », sur National Center for Biotechnology Information, U.S. National Library of Medicine

[Aoki_2005-5] {a et b} Aoki N, Discovery of alpha2-plasmin inhibitor and its congenital deficiency, J Thromb Haemost, 2005;3:623–631

[Lee_2004-6] Lee KN, Jackson KW, Christiansen VJ, Chung KH, McKee PA, A novel plasma proteinase potentiates alpha2-antiplasmin inhibition of fibrin digestion, Blood, 2004;103:3783–3788

[Leebeek_1990-7] Leebeek FW, Kluft C, Knot EA, Los P, Cohen AF, Six AJ, Plasmin inhibitors in the prevention of systemic effects during thrombolytic therapy: specific role of the plasminogen-binding form of alpha 2-antiplasmin, J Am Coll Cardiol, 1990;15:1212–1220

[Mitchell_2014-8] Mitchell JL, Lionikiene AS, Fraser SR, Whyte CS, Booth NA, Mutch NJ, Functional factor XIII-A is exposed on the stimulated platelet surface, Blood, 2014;124:3982–3990

[Wojcik_2019-9] Wojcik M, Zareba L, Undas A. Prothrombotic fibrin clot properties are associated with post-discharge venous thromboembolism in acutely ill medical patients, Thromb Res, 2019;182:141–149

[Singh_2017-10] Singh S, Houng A, Reed GL, Releasing the brakes on the fibrinolytic system in pulmonary emboli: unique effects of plasminogen activation and α2-antiplasmin inactivation, Circulation, 2017;135:1011−1020

[Singh_2024-11] Singh S, Kumar P, Padwad YS, Jaffer FA, Reed GL, Targeting fibrinolytic inhibition for venous thromboembolism treatment: Overview of an emerging therapeutic approach, Circulation, 2024;150!884-898

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