Proteolysis of liver plectin by mu-calpain.
Rat liver plectin was found to be mainly associated with plasma membrane fractions enriched in junctional complexes. The membrane-associated plectin has been partially isolated. Plectin co-purifies with a 200 kDa polypeptide which, on the basis of sequence homology, has been identified as a myosin like-protein. The interaction of mu-calpain with liver plectin has been investigated. Plectin is very sensitive to mu-calpain and is digested to give a fragment of 240 kDa.
Laboratory of Biochemistry III, Swiss Federal Institute of Technology (ETH), Zurich, CH-8092, Switzerland.
M
M
Muenchbach
M
M
Dell'Ambrogio
P
P
Gazzotti
D000595:Amino Acid Sequence; D000818:Animals; D002154:Calpain / Q000378:metabolism*; D002462:Cell Membrane / Q000737:chemistry; D003488:Cyanogen Bromide; D005260:Female; D007381:Intermediate Filament Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D008099:Liver / Q000737:chemistry*; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry / Q000378:metabolism; D051190:Plectin; D051381:Rats
D007381:Intermediate Filament Proteins; D010446:Peptide Fragments; C495334:Plec protein, rat; D051190:Plectin; D002154:Calpain; D003488:Cyanogen Bromide