Purification and primary structure of murine cryptdin-1, a Paneth cell defensin.
We have purified and determined the amino acid sequence of cryptdin-1, a murine Paneth cell defensin. The peptide corresponds to a previously characterized mRNA that accumulates to high abundance during postnatal ontogeny of the small bowel. Acid-extracted intestinal protein was fractionated by cation-exchange chromatography and fractions were assayed for antimicrobial activity. One peak of anti-Salmonella activity contained a putative defensin, based on its predicted electrophoretic migration in acid-urea PAGE. The peptide was purified to homogeneity by RP-HPLC and sequenced. These studies demonstrate defensin expression in non-myeloid tissue. The N-terminal extension of cryptdin-1 is a unique structural feature of this novel epithelial defensin.
Ouellette
A J
AJ
Cell Biology Unit, Shriners Burns Institute, Cambridge, MA 02142.
Miller
S I
SI
Henschen
A H
AH
Selsted
M E
ME
D000595:Amino Acid Sequence; D000818:Animals; D016384:Consensus Sequence; D007082:Ileum / Q000737:chemistry*; D007413:Intestinal Mucosa / Q000737:chemistry*; D007583:Jejunum / Q000737:chemistry*; D008297:Male; D051379:Mice; D008969:Molecular Sequence Data; D011498:Protein Precursors / Q000737:chemistry* / Q000302:isolation & purification; D011506:Proteins / Q000737:chemistry* / Q000302:isolation & purification; D012689:Sequence Homology, Nucleic Acid
D011498:Protein Precursors; D011506:Proteins; C059569:cryptdin