In:
Science, American Association for the Advancement of Science (AAAS), Vol. 286, No. 5437 ( 1999-10), p. 113-117
Kurzfassung:
Precursors of α-defensin peptides require activation for bactericidal activity. In mouse small intestine, matrilysin colocalized with α-defensins (cryptdins) in Paneth cell granules, and in vitro it cleaved the pro segment from cryptdin precursors. Matrilysin-deficient (MAT −/− ) mice lacked mature cryptdins and accumulated precursor molecules. Intestinal peptide preparations from MAT −/− mice had decreased antimicrobial activity. Orally administered bacteria survived in greater numbers and were more virulent in MAT −/− mice than in MAT +/+ mice. Thus, matrilysin functions in intestinal mucosal defense by regulating the activity of defensins, which may be a common role for this metalloproteinase in its numerous epithelial sites of expression.
Materialart:
Online-Ressource
ISSN:
0036-8075
,
1095-9203
DOI:
10.1126/science.286.5437.113
Sprache:
Englisch
Verlag:
American Association for the Advancement of Science (AAAS)
Publikationsdatum:
1999
ZDB Id:
128410-1
ZDB Id:
2066996-3
ZDB Id:
2060783-0
SSG:
11
