TY - JOUR
T1 - Expression of Lamp-1 and Lamp-2 and their interactions with galectin-3 in human tumor cells
AU - Sarafian, Victoria
AU - Jadot, Michel
AU - Foidart, Jean Michel
AU - Letesson, Jean-Jacques
AU - Van den Brule, Frédéric
AU - Castrunovo, Vincent
AU - Wattiaux, Robert
AU - Wattiaux-De Coninck, Simone
PY - 1998/1/5
Y1 - 1998/1/5
N2 - Lysosomal-membrane-associated glycoproteins (Lamps) 1 and 2 are rarely found on the plasma membranes of normal cells. There is evidence suggesting an increase in their cell-surface expression in tumor cells, with some data indicating that the adhesion of some cancer cells to the extracellular matrix is partly mediated by interactions between Lamps and E-selectin and between Lamps and galectins (endogenous-galactoside-binding lectins). The present study examined the expression of Lamp-1 and Lamp-2 and their interactions with galectin-3 in different human tumor cell lines. Indirect immunofluorescence staining revealed accumulation of Lamp molecules at the edges of A2058 human metastasizing melanoma cells suggesting that these glycoproteins could participate in cell adhesion. Flow cytometry showed the presence of cell-surface Lamps in A2058, HT1080 (human fibrosarcoma) and CaCo-2 (human colon-adenocarcinoma) cells. Treatment with 2 mM sodium butyrate for 24 and 48 hr resulted in a significant increase in Lamps surface expression. A strong binding of A2058 to recombinant galectin-3 was detected by FACS. The application of 2 and 5 mM butyrate for the same incubation period enhanced galectin-3 binding to Lamps-expressing cells. Our results support the idea that Lamps may be considered a new family of adhesive glycoproteins participating in the complex process of tumor invasion and metastasis.
AB - Lysosomal-membrane-associated glycoproteins (Lamps) 1 and 2 are rarely found on the plasma membranes of normal cells. There is evidence suggesting an increase in their cell-surface expression in tumor cells, with some data indicating that the adhesion of some cancer cells to the extracellular matrix is partly mediated by interactions between Lamps and E-selectin and between Lamps and galectins (endogenous-galactoside-binding lectins). The present study examined the expression of Lamp-1 and Lamp-2 and their interactions with galectin-3 in different human tumor cell lines. Indirect immunofluorescence staining revealed accumulation of Lamp molecules at the edges of A2058 human metastasizing melanoma cells suggesting that these glycoproteins could participate in cell adhesion. Flow cytometry showed the presence of cell-surface Lamps in A2058, HT1080 (human fibrosarcoma) and CaCo-2 (human colon-adenocarcinoma) cells. Treatment with 2 mM sodium butyrate for 24 and 48 hr resulted in a significant increase in Lamps surface expression. A strong binding of A2058 to recombinant galectin-3 was detected by FACS. The application of 2 and 5 mM butyrate for the same incubation period enhanced galectin-3 binding to Lamps-expressing cells. Our results support the idea that Lamps may be considered a new family of adhesive glycoproteins participating in the complex process of tumor invasion and metastasis.
UR - http://www.scopus.com/inward/record.url?scp=0032484530&partnerID=8YFLogxK
U2 - 10.1002/(SICI)1097-0215(19980105)75:1<105::AID-IJC16>3.0.CO;2-F
DO - 10.1002/(SICI)1097-0215(19980105)75:1<105::AID-IJC16>3.0.CO;2-F
M3 - Article
C2 - 9426697
AN - SCOPUS:0032484530
SN - 0020-7136
VL - 75
SP - 105
EP - 111
JO - International Journal of Cancer
JF - International Journal of Cancer
IS - 1
ER -