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J. Biol. Chem., Vol. 275, Issue 43, 33969-33973, October 27, 2000
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From the Departments of Paneth cells at the base of small intestinal
crypts secrete apical granules that contain antimicrobial peptides
including
Characterization of Luminal Paneth Cell
-Defensins in
Mouse Small Intestine
ATTENUATED ANTIMICROBIAL ACTIVITIES OF PEPTIDES WITH TRUNCATED
AMINO TERMINI*
§¶,,,
, and§
Pathology and
§ Microbiology and Molecular Genetics, College of Medicine,
University of California, Irvine, California 92697-4800 and Beth
Israel Deaconess Medical Center, Boston, Massachusetts 02115
-defensins, termed cryptdins. Using an antibody specific
for mouse cryptdin-1, -2, -3, and -6, immunogold-localization studies demonstrated that cryptdins are constituents of mouse Paneth cell secretory granules. Several cryptdin peptides have been purified from
rinses of adult mouse small intestine by gel filtration and reverse-phase high performance liquid chromatography. Their primary structures were determined by peptide sequencing, and their
antimicrobial activities were compared with those of the corresponding
tissue forms. The isolated luminal cryptdins included peptides
identical to the tissue forms of cryptdin-2, -4, and -6 as well as
variants of cryptdin-1, -4, and -6 that have N termini truncated by one or two residues. In assays of antimicrobial activity against
Staphylococcus aureus, Escherichia coli, and
the defensin-sensitive Salmonella typhimurium
phoP
mutant, full-length cryptdins had the
same in vitro antibacterial activities whether isolated
from tissue or from the lumen. In contrast, the N-terminal-truncated
(des-Leu), (des-Leu-Arg)-cryptdin-6, and (des-Gly)-cryptdin-4 peptides
were markedly less active. The microbicidal activities of recombinant
cryptdin-4 and (des-Gly)-cryptdin-4 peptides against E. coli, and S. typhimurium showed that the N-terminal Gly residue or the length of the cryptdin-4 N terminus are determinants of microbicidal activity. Innate immunity in the crypt lumen may be
modulated by aminopeptidase modification of -defensins after peptide secretion.
*
Supported by National Institutes of Health Grants DK44632,
DK33506 (to A. J. O), DK 15681 (to S. J. H.), AI 22931 and Large Scale Biology, Corp. (to M. E. S). Preliminary accounts of these studies were presented at the 1996 Annual Meeting of The American Gastroenterological Association in San Francisco, CA.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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