Variation in the binding of /sup 125/I-labeled interferon-beta ser to cellular receptors during growth of human renal and bladder carcinoma cells in vitro

Journal Article · Tue Sep 01 04:00:00 EDT 1987 · Cancer Res.; (United States)

OSTI ID:5905494

Ruzicka, F J; Schmid, S M; Groveman, D S; Cummings, K B; Borden, E C

Studies of various established human bladder and renal carcinoma cell lines cultured in vitro demonstrated the presence of specific, saturable, high affinity binding sites for /sup 125/I-labeled human interferon Beta ser IFN-beta ser). This recombinant produced interferon labeled with approximately one atom of /sup 125/I/molecule of IFN expressed minimal or no loss of antiviral activity. A single class of binding sites (1000-2000/cell) with an affinity constant of 10(10)-10(11) L/M was measured at 4 degrees C for cells exhibiting widely different sensitivity to the antiproliferative effect of IFN-beta ser. Major fluctuations in the binding of /sup 125/I-labeled IFN-beta ser to cellular receptors were observed during in vitro proliferation of four of five cell lines examined. A significant decrease (P less than 0.001) in specific binding was observed 48 h after cultures were established. Cell cycle analysis suggested that within the first 24 h and in the very late log and stationary phase of growth of ACHN (human renal carcinoma) cells, variations in the binding of /sup 125/I-labeled IFN-beta ser were partially attributable to binding fluctuations during the mitotic cycle. The 2- to 3-fold decline 24 h following plating of ACHN cells corresponded to a 70% decrease in the number of cells in G0-G1. T24 (human transitional cell carcinoma) and ACHN cells, synchronized by serum starvation, demonstrated increased binding of /sup 125/I-labeled IFN-beta ser 4-16 h following serum replenishment. This increase in receptor binding occurred prior to the onset of DNA and protein synthesis and was followed by a decline immediately prior to cell division. Binding site analysis indicated that the increased binding prior to DNA synthesis was due to a 5- to 6-fold increase in receptor affinity for the radiolabeled ligand.

• Research Organization: Univ. of Wisconsin Clinical Cancer Center, Madison
• OSTI ID: 5905494
• Journal Information: Cancer Res.; (United States), Journal Name: Cancer Res.; (United States) Vol. 47:17; ISSN CNREA
• Country of Publication: United States
• Language: English

Related Subjects

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59 BASIC BIOLOGICAL SCIENCES
AFFINITY
ANIMAL CELLS
BETA DECAY RADIOISOTOPES
BIOCHEMICAL REACTION KINETICS
BLADDER
BODY
CARCINOMAS
CELL CYCLE
CELL PROLIFERATION
DAYS LIVING RADIOISOTOPES
DISEASES
DNA REPLICATION
ELECTRON CAPTURE RADIOISOTOPES
GROWTH
GROWTH FACTORS
IN VITRO
INTERFERON
INTERMEDIATE MASS NUCLEI
IODINE 125
IODINE ISOTOPES
ISOTOPE APPLICATIONS
ISOTOPES
KINETICS
LYMPHOKINES
MEMBRANE PROTEINS
MITOGENS
NEOPLASMS
NUCLEI
NUCLEIC ACID REPLICATION
ODD-EVEN NUCLEI
ORGANIC COMPOUNDS
ORGANS
PROTEINS
RADIOISOTOPES
REACTION KINETICS
RECEPTORS
TRACER TECHNIQUES
TUMOR CELLS
URINARY TRACT