Dipeptidyl peptidase IV in angiotensin-converting enzyme inhibitor-associated angioedema
dc.contributor.author | Byrd, JB | |
dc.contributor.author | Harris, S | |
dc.contributor.author | Gainer, JV | |
dc.contributor.author | Yu, C | |
dc.contributor.author | Shreevatsa, A | |
dc.contributor.author | Putlur, P | |
dc.contributor.author | Nadeau, J | |
dc.contributor.author | Touzin, K | |
dc.contributor.author | Summar, M | |
dc.contributor.author | Adam, A | |
dc.contributor.author | Brown, NJ | |
dc.coverage.spatial | San Antonio | |
dc.date.accessioned | 2024-03-12T14:58:38Z | |
dc.date.available | 2024-03-12T14:58:38Z | |
dc.date.issued | 2008-01-01 | |
dc.identifier.issn | 0194-911X | |
dc.identifier.issn | 1524-4563 | |
dc.identifier.uri | https://www.ncbi.nlm.nih.gov/pubmed/18025295 | |
dc.identifier.uri | https://hdl.handle.net/2027.42/192635 | en |
dc.description.abstract | Angioedema is a potentially life-threatening adverse effect of angiotensin-converting enzyme inhibitors. Bradykinin and substance P, substrates of angiotensin-converting enzyme, increase vascular permeability and cause tissue edema in animals. Studies indicate that amino-terminal degradation of these peptides, by aminopeptidase P and dipeptidyl peptidase IV, may be impaired in individuals with angiotensin-converting enzyme inhibitor-associated angioedema. This case-control study tested the hypothesis that dipeptidyl peptidase IV activity and antigen are decreased in sera of patients with a history of angiotensin-converting enzyme inhibitor-associated angioedema. Fifty subjects with a history of angiotensin-converting enzyme inhibitor-associated angioedema and 176 angiotensin-converting enzyme inhibitor-exposed control subjects were ascertained. Sera were assayed for angiotensin-converting enzyme activity, aminopeptidase P activity, aminopeptidase N activity, dipeptidyl peptidase IV activity, and antigen and the ex vivo degradation half-lives of bradykinin, des-Arg-bradykinin, and substance P in a subset. The prevalence of smoking was increased and of diabetes decreased in case versus control subjects. Overall, dipeptidyl peptidase IV activity (26.6±7.8 versus 29.6±7.3 nmol/mL per minute; P=0.026) and antigen (465.8±260.8 versus 563.1±208.6 ng/mL; P=0.017) were decreased in sera from individuals with angiotensin-converting enzyme inhibitor-associated angioedema compared with angiotensin-converting enzyme inhibitor-exposed control subjects without angioedema. Dipeptidyl peptidase IV activity (21.5±4.9 versus 29.8±6.7 nmol/mL per minute; P=0.001) and antigen (354.4±124.7 versus 559.8±163.2 ng/mL; P=0.003) were decreased in sera from cases collected during angiotensin-converting enzyme inhibition but not in the absence of angiotensin-converting enzyme inhibition. The degradation half-life of substance P correlated inversely with dipeptidyl peptidase IV antigen during angiotensin-converting enzyme inhibition. Environmental or genetic factors that reduce dipeptidyl peptidase IV activity may predispose individuals to angioedema. © 2008 American Heart Association, Inc. | |
dc.format.medium | Print-Electronic | |
dc.language | eng | |
dc.publisher | Wolters Kluwer | |
dc.subject | Adult | |
dc.subject | Aged | |
dc.subject | Angioedema | |
dc.subject | Angiotensin-Converting Enzyme Inhibitors | |
dc.subject | Antigens | |
dc.subject | Bradykinin | |
dc.subject | Case-Control Studies | |
dc.subject | Dipeptidyl Peptidase 4 | |
dc.subject | Female | |
dc.subject | Genetic Predisposition to Disease | |
dc.subject | Humans | |
dc.subject | Hypertension | |
dc.subject | Male | |
dc.subject | Middle Aged | |
dc.subject | Peptidyl-Dipeptidase A | |
dc.subject | Substance P | |
dc.title | Dipeptidyl peptidase IV in angiotensin-converting enzyme inhibitor-associated angioedema | |
dc.type | Article | |
dc.identifier.pmid | 18025295 | |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/192635/2/Dipeptidyl peptidase IV in angiotensin-converting enzyme inhibitor associated angioedema.pdf | |
dc.identifier.doi | 10.1161/HYPERTENSIONAHA.107.096552 | |
dc.identifier.doi | https://dx.doi.org/10.7302/22451 | |
dc.identifier.source | Hypertension | |
dc.description.version | Published version | |
dc.date.updated | 2024-03-12T14:58:36Z | |
dc.identifier.volume | 51 | |
dc.identifier.issue | 1 | |
dc.identifier.startpage | 141 | |
dc.identifier.endpage | 147 | |
dc.identifier.name-orcid | Byrd, JB | |
dc.identifier.name-orcid | Harris, S | |
dc.identifier.name-orcid | Gainer, JV | |
dc.identifier.name-orcid | Yu, C | |
dc.identifier.name-orcid | Shreevatsa, A | |
dc.identifier.name-orcid | Putlur, P | |
dc.identifier.name-orcid | Nadeau, J | |
dc.identifier.name-orcid | Touzin, K | |
dc.identifier.name-orcid | Summar, M | |
dc.identifier.name-orcid | Adam, A | |
dc.identifier.name-orcid | Brown, NJ | |
dc.working.doi | 10.7302/22451 | en |
dc.owningcollname | Internal Medicine, Department of |
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