Biomaterial Database

Evidence for a low-affinity interleukin-3 receptor. 1990

J Schreurs, and K Arai, and A Miyajima

Department of Molecular Biology, DNAX Research Institute of Molecular and Cellular Biology, Palo Alto, CA 94304-1104.

Interleukin-3 (IL-3) regulates the proliferation of myeloid, erythroid, and lymphoid cells. Previous reports showed IL-3 binding restricted to a single high-affinity (Kd = 50-200 pM) site. Here, we demonstrate by equilibrium studies an additional binding site for IL-3 with lower apparent affinity (Kd = 5-20 nM). Furthermore, kinetic analysis shows that two binding sites for IL-3 exist: IL-3 dissociates slowly from the first site (T1/2 = 4 hr; k-1 = 2.7 x 10(-3) min-1), whereas it dissociates rapidly (T1/2 = 4.0 min; k-1 = 0.116 min-1) from the second site. Cross-linking showed that [125I]IL-3 binding to the 115- and 140-kD proteins was not saturable at concentrations commensurate with high-affinity binding and IL-3 dissociated rapidly from these same molecules. Thus, the low affinity IL-3 receptor is a molecule(s) of 115- to 140-kD.

UI	MeSH Term	Description	Entries
D007377	Interleukin-3	A multilineage cell growth factor secreted by LYMPHOCYTES; EPITHELIAL CELLS; and ASTROCYTES which stimulates clonal proliferation and differentiation of various types of blood and tissue cells.	Burst-Promoting Factor, Erythrocyte,Colony-Stimulating Factor 2 Alpha,Colony-Stimulating Factor, Mast-Cell,Colony-Stimulating Factor, Multipotential,Erythrocyte Burst-Promoting Factor,IL-3,Mast-Cell Colony-Stimulating Factor,Multipotential Colony-Stimulating Factor,P-Cell Stimulating Factor,Eosinophil-Mast Cell Growth-Factor,Hematopoietin-2,Burst Promoting Factor, Erythrocyte,Colony Stimulating Factor, Mast Cell,Colony Stimulating Factor, Multipotential,Eosinophil Mast Cell Growth Factor,Erythrocyte Burst Promoting Factor,Hematopoietin 2,Interleukin 3,Multipotential Colony Stimulating Factor,P Cell Stimulating Factor
D007700	Kinetics	The rate dynamics in chemical or physical systems.
D008970	Molecular Weight	The sum of the weight of all the atoms in a molecule.	Molecular Weights,Weight, Molecular,Weights, Molecular
D011971	Receptors, Immunologic	Cell surface molecules on cells of the immune system that specifically bind surface molecules or messenger molecules and trigger changes in the behavior of cells. Although these receptors were first identified in the immune system, many have important functions elsewhere.	Immunologic Receptors,Immunologic Receptor,Immunological Receptors,Receptor, Immunologic,Receptors, Immunological
D002460	Cell Line	Established cell cultures that have the potential to propagate indefinitely.	Cell Lines,Line, Cell,Lines, Cell
D003432	Cross-Linking Reagents	Reagents with two reactive groups, usually at opposite ends of the molecule, that are capable of reacting with and thereby forming bridges between side chains of amino acids in proteins; the locations of naturally reactive areas within proteins can thereby be identified; may also be used for other macromolecules, like glycoproteins, nucleic acids, or other.	Bifunctional Reagent,Bifunctional Reagents,Cross Linking Reagent,Crosslinking Reagent,Cross Linking Reagents,Crosslinking Reagents,Linking Reagent, Cross,Linking Reagents, Cross,Reagent, Bifunctional,Reagent, Cross Linking,Reagent, Crosslinking,Reagents, Bifunctional,Reagents, Cross Linking,Reagents, Cross-Linking,Reagents, Crosslinking
D000818	Animals	Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA.	Animal,Metazoa,Animalia
D001665	Binding Sites	The parts of a macromolecule that directly participate in its specific combination with another molecule.	Combining Site,Binding Site,Combining Sites,Site, Binding,Site, Combining,Sites, Binding,Sites, Combining
D001667	Binding, Competitive	The interaction of two or more substrates or ligands with the same binding site. The displacement of one by the other is used in quantitative and selective affinity measurements.	Competitive Binding
D016185	Receptors, Interleukin-3	High affinity receptors for INTERLEUKIN-3. They are found on early HEMATOPOIETIC PROGENITOR CELLS; progenitors of MYELOID CELLS; EOSINOPHILS; and BASOPHILS. Interleukin-3 receptors are formed by the dimerization of the INTERLEUKIN-3 RECEPTOR ALPHA SUBUNIT and the CYTOKINE RECEPTOR COMMON BETA SUBUNIT.	IL-3 Receptors,Interleukin-3 Receptors,Receptors, IL-3,IL-3 Receptor,IL3 Receptor,IL3 Receptors,Interleukin-3 Receptor,IL 3 Receptor,IL 3 Receptors,Interleukin 3 Receptor,Interleukin 3 Receptors,Receptor, IL-3,Receptor, IL3,Receptor, Interleukin-3,Receptors, IL 3,Receptors, IL3,Receptors, Interleukin 3