Extracellular hydrolysis of formyl peptides and subsequent uptake of liberated amino acids by alveolar macrophages.

@article{Basilion1986ExtracellularHO,
  title={Extracellular hydrolysis of formyl peptides and subsequent uptake of liberated amino acids by alveolar macrophages.},
  author={J. Basilion and D. Stickle and A. Holian},
  journal={Biochimica et biophysica acta},
  year={1986},
  volume={886 2},
  pages={
          255-66
        }
}
The mechanism of accumulation of radioactive label from fNle-Leu-[3H]Phe by guinea pig alveolar macrophages was investigated. The binding of fNle-Leu-[3H]Phe to macrophages reached equilibrium within 5 min at 4 degrees C, but equilibrium could not be achieved at temperatures where fNle-Leu-Phe stimulated superoxide anion production is observed (e.g., 21-23 degrees C). At this temperature a rapid phase of initial binding of fNle-Leu-[3H]Phe to its receptor was followed by continued accumulation… Expand
2 Citations
Identification of a human neutrophil protein of Mr 24 000 that binds N-formyl peptides: co-sedimentation with specific granules.
TLDR
The N-terminal sequence of the Mr 24 000 species was determined and it appears to be a novel protein, which will allow its relationship to the receptor, if any, to be elucidated and allow assignment of a function to this potentially important molecule. Expand
Absence of FMLP Receptors on Rat Macrophages
TLDR
In 3H‐FMLP binding studies, the lack of responsiveness of peritoneal and alveolar macrophages was associated with the lackof FMLP receptors on these cell types, in striking contrast to the presence of functional receptors on rat neutrophils. Expand

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