Binding of histamine-albumin conjugates to human lymphocytes: evidence for labelling of histamine H-1 but not H-2 receptors.
Acta Pathol Microbiol Immunol Scand C
; 95(5): 199-205, 1987 Oct.
Article
em En
| MEDLINE
| ID: mdl-3425322
ABSTRACT
Histamine conjugated to human serum albumin (HSA) bound to a major proportion of human peripheral blood lymphocytes in a rosetting assay. In contrast, red cells coated with the control conjugates pentylamine-HSA and ethanolamine-HSA were unreactive. Amine conjugation by the carbodiimide method imposed a positive charge on the albumin molecule. However, the percentage histamine-HSA-binding lymphocytes was related to the amount of histamine coupled to the albumin molecule and not to differences in isoelectric point (pI) of the modified protein carriers. Four different histamine-albumin conjugates and one pentylamine-HSA conjugate inhibited lymphocyte binding of histamine-HSA, whereas ethanolamine-albumin, carbodiimide-reacted HSA and native albumin were not inhibitory. The histamine H-2 receptor antagonists cimetidine, ranitidine, metiamide, and burimamide lacked inhibitory effects. The histamine H-1 receptor antagonists clemastine, mepyramine, and diphenhydramine efficiently inhibited lymphocyte binding of the histamine-albumin conjugate with IC50 values of 0.2, 1, and 40 mM, respectively, indicating interactions with low affinity H-1 receptors.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Albumina Sérica
/
Receptores Histamínicos
/
Receptores Histamínicos H1
/
Receptores Histamínicos H2
/
Linfócitos
/
Histamina
Limite:
Humans
Idioma:
En
Revista:
Acta Pathol Microbiol Immunol Scand C
Ano de publicação:
1987
Tipo de documento:
Article
País de afiliação:
Suécia