The cellular internalization of recombinant gamma interferon differs from that of natural interferon gamma

Autor: J. James Sedmak, Sidney E. Grossberg, Hector S. MacDonald, Vladimir M. Kushnaryov
Rok vydání: 1988
Předmět:
Zdroj: Biochemical and Biophysical Research Communications. 157:109-114
ISSN: 0006-291X
DOI: 10.1016/s0006-291x(88)80019-6
Popis: Purified natural and recombinant murine gamma interferons (MuIFN-gamma) bind at 4 degrees C to cultured L929 mouse fibroblasts with comparable receptor-binding affinity (Kd = 9 x 10(-10) M). Both 125I-labeled MuIFNs are rapidly internalized by cells at 37 degrees C, although recombinant IFN is internalized somewhat more slowly than natural IFN (t1/2 = 90 sec and 45 sec, respectively). Immunoelectronmicroscopy showed that the majority of bound recombinant MuIFN-gamma was located on the plasma membrane outside of coated areas, whereas natural interferon was found mainly in coated pits. At 37 degrees C most of the recombinant molecules entered the cytoplasm in pinocytotic vesicles, while natural interferon was internalized by the specific mechanism of receptor-mediated endocytosis [1]. However, nearly equal amounts of immunocytochemically detectable molecules of both IFNs were found in the cell nucleus within 2-3 min incubation at 37 degrees C. Thus, the process of translocation of the recombinant IFN-gamma appears to differ from that of the natural product.
Databáze: OpenAIRE