Intracellular processing of epidermal growth factor. I. Acidification of 125I-epidermal growth factor in intracellular organelles

L. M. Matrisian, S. R. Planck, B. E. Magun

Research output: Contribution to journalArticlepeer-review

38 Scopus citations

Abstract

We previously reported that 125I-labeled epidermal growth factor is processed intracellularly to acidic macromolecules in Rat-1 fibroblasts. The present study defines the precursor-product relationship and localization of the processing steps to subcellular organelles by the use of a single isoelectric species of 125I-epidermal growth factor and Percoll gradient fractionation. The native pI 4.55 125I-epidermal growth factor was rapidly processed to a pI 4.2 species on or near the cell surface and in organelles corresponding to clathrin-coated vesicles, Golgi, and endoplasmic reticulum. This species was then processed to a pI 4.35 species in similar organelles. The pI 4.2 and 4.35 species were converted to a pI 4.0 species in dense, lysosome-like organelles. This species was ultimately degraded and exocytosed from the cell as low molecular weight products.

Original languageEnglish (US)
Pages (from-to)3047-3052
Number of pages6
JournalJournal of Biological Chemistry
Volume259
Issue number5
StatePublished - 1984

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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