Failure to detect IL-3-binding sites on human mast cells.
J Immunol
; 145(10): 3432-7, 1990 Nov 15.
Article
em En
| MEDLINE
| ID: mdl-2230127
ABSTRACT
IL-3, a pleiotropic lymphokine, has been termed mast cell growth factor because it promotes growth and differentiation of murine mast cells. Murine mast cells, in turn, express cell surface receptors for IL-3. Human rIL-3 has been shown to induce proliferation and differentiation of human basophils and to activate basophils via high affinity binding sites. To investigate whether human mast cells express IL-3R, binding studies with 125I-radiolabeled human rIL-3 were performed on HMC-1, a novel human mast cell line, and on pure populations (i.e., 93 to 99% purity) of human tissue mast cells obtained with mAb and C from dispersed lung (n = 2). Unexpectedly, neither enriched human lung mast cells nor HMC-1 cells bound radiolabeled human rIL-3 specifically. Moreover, human rIL-3 failed to promote uptake of [3H]thymidine, synthesis of histamine, histamine releasability, or changes in expression of mast cell differentiation Ag (YB5B8, CD54/ICAM-1, CD9/p24, CD33/gp67) on either human lung mast cells or HMC-1 cells. It is hypothesized that the fundamental difference in the biologic response to IL-3 between human and murine mast cells is due to a loss during evolution of mast cell high affinity IL-3 binding sites.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Receptores de Interleucina-3
/
Interleucina-3
/
Mastócitos
Limite:
Humans
Idioma:
En
Revista:
J Immunol
Ano de publicação:
1990
Tipo de documento:
Article
País de afiliação:
Áustria