Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2007-4-26
pubmed:abstractText
Angiotensin-converting enzyme (ACE), also known as kininase II, functions not only to convert angiotensin I to angiotensin II, but also to cleave bradykinin into inactive fragments. Thus, ACE inhibition causes the tissue accumulation of bradykinin, exerting either of two opposite effects: anti- or proangiogenic. The purpose of the present study was to investigate the role of bradykinin in the development of choroidal neovascularization (CNV), with or without ACE inhibition.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Angiotensin-Converting Enzyme..., http://linkedlifedata.com/resource/pubmed/chemical/Bradykinin, http://linkedlifedata.com/resource/pubmed/chemical/Ccl2 protein, rat, http://linkedlifedata.com/resource/pubmed/chemical/Chemokine CCL2, http://linkedlifedata.com/resource/pubmed/chemical/Imidazolidines, http://linkedlifedata.com/resource/pubmed/chemical/Intercellular Adhesion Molecule-1, http://linkedlifedata.com/resource/pubmed/chemical/Peptidyl-Dipeptidase A, http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger, http://linkedlifedata.com/resource/pubmed/chemical/Receptor, Angiotensin, Type 1, http://linkedlifedata.com/resource/pubmed/chemical/Receptor, Bradykinin B2, http://linkedlifedata.com/resource/pubmed/chemical/Vascular Endothelial Growth Factor A, http://linkedlifedata.com/resource/pubmed/chemical/icatibant, http://linkedlifedata.com/resource/pubmed/chemical/imidapril, http://linkedlifedata.com/resource/pubmed/chemical/vascular endothelial growth factor...
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0146-0404
pubmed:author
pubmed:issnType
Print
pubmed:volume
48
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2321-6
pubmed:meshHeading
pubmed-meshheading:17460297-Angiotensin-Converting Enzyme Inhibitors, pubmed-meshheading:17460297-Animals, pubmed-meshheading:17460297-Bradykinin, pubmed-meshheading:17460297-Chemokine CCL2, pubmed-meshheading:17460297-Choroid, pubmed-meshheading:17460297-Choroidal Neovascularization, pubmed-meshheading:17460297-Disease Models, Animal, pubmed-meshheading:17460297-Enzyme-Linked Immunosorbent Assay, pubmed-meshheading:17460297-Imidazolidines, pubmed-meshheading:17460297-Intercellular Adhesion Molecule-1, pubmed-meshheading:17460297-Kallikrein-Kinin System, pubmed-meshheading:17460297-Laser Coagulation, pubmed-meshheading:17460297-Mice, pubmed-meshheading:17460297-Mice, Inbred C57BL, pubmed-meshheading:17460297-Microscopy, Confocal, pubmed-meshheading:17460297-Peptidyl-Dipeptidase A, pubmed-meshheading:17460297-Pigment Epithelium of Eye, pubmed-meshheading:17460297-RNA, Messenger, pubmed-meshheading:17460297-Receptor, Angiotensin, Type 1, pubmed-meshheading:17460297-Receptor, Bradykinin B2, pubmed-meshheading:17460297-Reverse Transcriptase Polymerase Chain Reaction, pubmed-meshheading:17460297-Vascular Endothelial Growth Factor A
pubmed:year
2007
pubmed:articleTitle
Suppression of choroidal neovascularization by inhibiting angiotensin-converting enzyme: minimal role of bradykinin.
pubmed:affiliation
Laboratory of Retinal Cell Biology, Keio University School of Medicine, Tokyo, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't