Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1997-12-23
pubmed:abstractText
In order to explore candidates for proteins required in exocytosis, we used two anti-allergic drugs, amlexanox and cromolyn, which inhibit IgE mediated degranulation of mast cells and basophils, as molecular probes in affinity chromatography. These two drugs chiefly bound to the same kinds of calcium binding proteins in bovine lung. These proteins were as follows: bovine calgranulin C homolog, an 8-kDa unknown protein, S-100L, calgranulin B, calcyphosine, and annexins I-V. The homologous affinity of the two drugs to these proteins is in accord with the similar anti-allergic property of both drugs. From these findings it is presumed that these drugs interact with these proteins and affect pharmacologically the degranulation.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Aminopyridines, http://linkedlifedata.com/resource/pubmed/chemical/Annexins, http://linkedlifedata.com/resource/pubmed/chemical/Anti-Allergic Agents, http://linkedlifedata.com/resource/pubmed/chemical/CAPS protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Calgranulin B, http://linkedlifedata.com/resource/pubmed/chemical/Calmodulin, http://linkedlifedata.com/resource/pubmed/chemical/Cromolyn Sodium, http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments, http://linkedlifedata.com/resource/pubmed/chemical/S100 Proteins, http://linkedlifedata.com/resource/pubmed/chemical/S100A12 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/amlexanox
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
17
pubmed:volume
240
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
341-7
pubmed:dateRevised
2004-8-18
pubmed:meshHeading
pubmed-meshheading:9388479-Amino Acid Sequence, pubmed-meshheading:9388479-Aminopyridines, pubmed-meshheading:9388479-Animals, pubmed-meshheading:9388479-Annexins, pubmed-meshheading:9388479-Anti-Allergic Agents, pubmed-meshheading:9388479-Binding Sites, pubmed-meshheading:9388479-Calcium-Binding Proteins, pubmed-meshheading:9388479-Calgranulin B, pubmed-meshheading:9388479-Calmodulin, pubmed-meshheading:9388479-Cattle, pubmed-meshheading:9388479-Chromatography, Affinity, pubmed-meshheading:9388479-Chromatography, High Pressure Liquid, pubmed-meshheading:9388479-Cromolyn Sodium, pubmed-meshheading:9388479-Lung, pubmed-meshheading:9388479-Molecular Sequence Data, pubmed-meshheading:9388479-Molecular Weight, pubmed-meshheading:9388479-Peptide Fragments, pubmed-meshheading:9388479-S100 Proteins, pubmed-meshheading:9388479-Sequence Alignment, pubmed-meshheading:9388479-Sequence Homology, Amino Acid
pubmed:year
1997
pubmed:articleTitle
Two distinct anti-allergic drugs, amlexanox and cromolyn, bind to the same kinds of calcium binding proteins, except calmodulin, in bovine lung extract.
pubmed:affiliation
Department of Chemistry, Kagawa Medical University, Japan.
pubmed:publicationType
Journal Article