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Pulmonary macrophages were preincubated for 1 or 20 h with L-[U-14C]phenylalanine and the degradation of labeled proteins studied by reincubating these cells in the presence of 4 mM L-phenylalanine and measuring rates of [14C]phenylalanine released from the cells into the medium. We found that proteins prelabeled in 1 or 20 h were degraded 8.0 and 3.0%.h-1, respectively. Decreases in cell viability reduced the rate of protein degradation. Lack of exogenous glucose slowed the rate of degradation of proteins labeled in 1 h, but not of those labeled in 20 h. Varying amino acids in the medium from normal to 5 times normal rabbit plasma levels had no effect on the degradation of either group of proteins. Rates of degradation of both fast and slowly turning over proteins were inhibited during phagocytosis of polystyrene latex particles by about 62 and 33%, respectively. The time course of the changes in protein degradation suggests they are related to intracellular events in the phagocytic process, rather than particle attachment or uptake.
K H Woodside, and
D Massaro
July 1981,
The American review of respiratory disease,
K H Woodside, and
D Massaro
July 1979,
The Journal of laboratory and clinical medicine,
K H Woodside, and
D Massaro
November 1982,
Biochemistry,
K H Woodside, and
D Massaro
December 1977,
Life sciences,
K H Woodside, and
D Massaro
June 1988,
Journal of applied physiology (Bethesda, Md. : 1985),
K H Woodside, and
D Massaro
January 1998,
The American journal of physiology,
K H Woodside, and
D Massaro
October 1993,
The Biochemical journal,
K H Woodside, and
D Massaro
July 1981,
The Biochemical journal,
K H Woodside, and
D Massaro
January 1980,
Archives of environmental health,
K H Woodside, and
D Massaro
March 1976,
Biochemical and biophysical research communications,
