Studies of hybrid hematopoietic growth factor receptors.
To gain further insight into the mechanisms by which both granulocyte-macrophage-colony stimulating factor (GM-CSF) and erythropoietin receptors function, we have utilized a GM-CSF erythropoietin hybrid receptor with GM-CSF as the external domain and erythropoietin as the intracellular domain. Results show that the beta common GM-CSF receptor both enhances the affinity binding of GM-CSF to the receptor and plays an important role in signaling through the receptor. A truncated form of the beta common receptor actually acts as a dominant negative regulatory factor.
Nathan
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Division of Hematology/Oncology, Children's Hospital, Boston, Massachusetts.
D000818:Animals; D000911:Antibodies, Monoclonal / Q000096:biosynthesis; D001665:Binding Sites; D002460:Cell Line; D015870:Gene Expression; D006801:Humans; D051379:Mice; D011233:Precipitin Tests; D017467:Receptors, Erythropoietin / Q000737:chemistry / Q000235:genetics / Q000502:physiology*; D016187:Receptors, Granulocyte-Macrophage Colony-Stimulating Factor / Q000737:chemistry / Q000235:genetics / Q000502:physiology*; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000235:genetics / Q000502:physiology; D013329:Structure-Activity Relationship; D014162:Transfection
D000911:Antibodies, Monoclonal; D017467:Receptors, Erythropoietin; D016187:Receptors, Granulocyte-Macrophage Colony-Stimulating Factor; D011993:Recombinant Fusion Proteins