Presenilin-dependent intramembrane proteolysis of CD44 leads to the liberation of its intracellular domain and the secretion of an Abeta-like peptide.

Lammich, Sven

Presenilin-dependent intramembrane proteolysis of CD44 leads to the liberation of its intracellular domain and the secretion of an Abeta-like peptide. [electronic resource] - The Journal of biological chemistry Nov 2002 - 44754-9 p. digital

Publication Type: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.

0021-9258

10.1074/jbc.M206872200 doi


Alzheimer Disease--metabolism
Amino Acid Sequence
Amyloid Precursor Protein Secretases
Amyloid beta-Peptides--metabolism
Amyloid beta-Protein Precursor--genetics
Animals
Aspartic Acid Endopeptidases--metabolism
Carbamates--pharmacology
Cell Line
Cell Membrane--metabolism
Dipeptides--pharmacology
Endopeptidases--metabolism
Enzyme Inhibitors--pharmacology
Fibroblasts--cytology
Humans
Hyaluronan Receptors--genetics
Membrane Proteins--genetics
Mice
Mice, Knockout
Molecular Sequence Data
Peptides--genetics
Presenilin-1
Presenilin-2
Protein Structure, Tertiary
Sequence Alignment
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Triglycerides--pharmacology
gamma-Aminobutyric Acid--analogs & derivatives