TY - JOUR
T1 - Soluble form of Lamp II in purified rat liver lysosomes
AU - Jadot, Michel
AU - Wattiaux, Robert
AU - Mainferme, Francis
AU - Dubois, Franz
AU - Claessens, Anick
AU - Wattiaux-De Coninck, Simone
PY - 1996/6/14
Y1 - 1996/6/14
N2 - Lamp II (for lysosomal associated membrane protein II) is an integral type I glycoprotein. It consists of a very large and heavily glycosylated luminal domain, a single transmembrane segment, and a short cytoplasmic tail. We show that in highly purified lysosomes from rat liver, Lamp II, immunodetected with a monoclonal antibody on Western blots, is surprisingly distributed between a membrane bound form and a 'soluble' form. The partition of the protein between the membrane and the content of lysosomes is strongly pH dependent. The soluble Lamp II population is sensitive to pH dependent aggregation as it is for many lysosomal content enzymes.
AB - Lamp II (for lysosomal associated membrane protein II) is an integral type I glycoprotein. It consists of a very large and heavily glycosylated luminal domain, a single transmembrane segment, and a short cytoplasmic tail. We show that in highly purified lysosomes from rat liver, Lamp II, immunodetected with a monoclonal antibody on Western blots, is surprisingly distributed between a membrane bound form and a 'soluble' form. The partition of the protein between the membrane and the content of lysosomes is strongly pH dependent. The soluble Lamp II population is sensitive to pH dependent aggregation as it is for many lysosomal content enzymes.
UR - http://www.scopus.com/inward/record.url?scp=0030583155&partnerID=8YFLogxK
U2 - 10.1006/bbrc.1996.0898
DO - 10.1006/bbrc.1996.0898
M3 - Article
C2 - 8670286
AN - SCOPUS:0030583155
SN - 0006-291X
VL - 223
SP - 353
EP - 359
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 2
ER -