Lisinopril-Induced Angioedema in a Patient with Plasma Prekallikrein Deficiency

Swapan K. Dasgupta; Stefanie Rivera; Perumal Thiagarajan

doi:10.1055/s-0040-1701238

TH Open, Inhaltsverzeichnis

CC BY 4.0 · TH Open 2020; 04(01): e33-e35
DOI: 10.1055/s-0040-1701238

Case Report

Georg Thieme Verlag KG Stuttgart · New York

Lisinopril-Induced Angioedema in a Patient with Plasma Prekallikrein Deficiency

Swapan K. Dasgupta

¹Department of Pathology, Baylor College of Medicine, Houston, Texas, United States

,

Stefanie Rivera

¹Department of Pathology, Baylor College of Medicine, Houston, Texas, United States

,

Perumal Thiagarajan

¹Department of Pathology, Baylor College of Medicine, Houston, Texas, United States

²Department of Medicine, Baylor College of Medicine, Houston, Texas, United States

³Center for Translational Research on Inflammatory Diseases (CTRID), Michael E. DeBakey Veterans Affairs Medical Center, Houston, Texas, United States

› Institutsangaben

Abstract

Angiotensin-converting enzyme (ACE) inhibitors are extensively prescribed to treat patients with hypertension, congestive heart failure, and diabetic nephropathy. A small fraction of these patients (approximately 0.7%) develop angioedema, manifested by swelling of the lips and oropharynx. Angioedema of oropharynx is a medical emergency that can lead to asphyxiation and death. The angioedema is due to bradykinin generated from high molecular weight kininogen by kallikrein, which is derived from plasma prekallikrein by action of the factor XIIa, factor Xia, or prolylcarboxypeptidase. Bradykinin induces vasodilation and increased vascular permeability. ACE is the major degrading enzyme of bradykinin in the intravascular department. ACE inhibitors inhibit the proteolytic inactivation of bradykinin. We report a patient with oropharyngeal angioedema associated with an ACE inhibitor with complete absence of plasma prekallikrein due to homozygous mutation (Ser97PhefsTer173).

Keywords

bradykinin - prekallikrein - kininogen

Volltext

Referenzen

References
1 Katsuda I, Maruyama F, Ezaki K, Sawamura T, Ichihara Y. A new type of plasma prekallikrein deficiency associated with homozygosity for Gly104Arg and Asn124Ser in apple domain 2 of the heavy-chain region. Eur J Haematol 2007; 79 (01) 59-68
2 Bezalel S, Mahlab-Guri K, Asher I, Werner B, Sthoeger ZM. Angiotensin-converting enzyme inhibitor-induced angioedema. Am J Med 2015; 128 (02) 120-125
3 Schmaier AH. The contact activation and kallikrein/kinin systems: pathophysiologic and physiologic activities. J Thromb Haemost 2016; 14 (01) 28-39
4 Cugno M, Nussberger J, Cicardi M, Agostoni A. Bradykinin and the pathophysiology of angioedema. Int Immunopharmacol 2003; 3 (03) 311-317
5 Bafunno V, Firinu D, D'Apolito M. , et al. Mutation of the angiopoietin-1 gene (ANGPT1) associates with a new type of hereditary angioedema. J Allergy Clin Immunol 2018; 141 (03) 1009-1017
6 Pathak M, Wong SS, Dreveny I, Emsley J. Structure of plasma and tissue kallikreins. Thromb Haemost 2013; 110 (03) 423-433
7 Alving BM, Hojima Y, Pisano JJ. , et al. Hypotension associated with prekallikrein activator (Hageman-factor fragments) in plasma protein fraction. N Engl J Med 1978; 299 (02) 66-70
8 Colman RW, Edelman R, Scott CF, Gilman RH. Plasma kallikrein activation and inhibition during typhoid fever. J Clin Invest 1978; 61 (02) 287-296