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Posttranslational processing and targeting of transgenic human defensin in
murine granulocyte, macrophage, fibroblast, and pituitary adenoma cell
lines
T Ganz, L Liu, EV Valore and A Oren
Will Rogers Institute Pulmonary Research Laboratory, UCLA School of
Medicine.
Human defensins are 29 to 30 amino acid (aa) antimicrobial peptides that
are among the principal constituents of the neutrophil's azurophil
granules. To determine the tissue specificity of posttranslational
processing and subcellular targeting of defensins, the cDNA for a 94 aa
human preprodefensin was transduced into murine cell lines (NIH 3T3
embryonic fibroblasts, AtT-20 pituitary adenoma, J774.1 and RAW 264.7
macrophages, and 32D and 32D cl3 granulocytes) using retroviral vectors.
All transduced cell types expressed and to a variable extent constitutively
secreted a 75 aa prodefensin formed by the removal of the amino terminal
signal sequence. In AtT-20 cells, the 75 aa form accumulated
intracellularly in granules and was releasable by secretagogues.
Proteolytic processing to mature defensins was seen only in myeloid cells
(J774.1, RAW 264.7, 32D, and 32D cl3). Newly formed mature defensin was
rapidly degraded in J774.1 and RAW 264.7 macrophages, but accumulated
stably in multivesicular bodies in 32D cells and in cytoplasmic granules of
32D cl3 cells. Our data suggest that the enzymatic and transport machinery
required to process preprodefensin to mature defensin and to store it in
cytoplasmic granules is a specialized feature of cells of granulocytic
lineage.
Volume 82,
Issue 2,
pp. 641-650,
07/15/1993
Copyright © 1993 by The American Society of Hematology
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