LAMP-1 in cho cells is a primary carrier of poly-N-acetyllactosamine chains and is bound preferentially by a mammalian S-type lectin

• Published in: Biochemical and biophysical research communications Vol. 173; no. 3; pp. 1123 - 1128
• Main Authors: Do, Ki-Young, Smith, David F., Cummings, Richard D.
• Format: Journal Article
• Language: English
• Published: San Diego, CA Elsevier Inc 31.12.1990; Elsevier
• Subjects: Analytical, structural and metabolic biochemistry; Animals; Antigens, CD; Biological and medical sciences; Carbohydrate Sequence; Cell Line; Chromatography, Affinity; Cricetinae; Cricetulus; Fundamental and applied biological sciences. Psychology; Glycoproteins; Lectins - metabolism; Lysosomal Membrane Proteins; Membrane Glycoproteins - chemistry; Membrane Glycoproteins - metabolism; Molecular Sequence Data; Molecular Weight; Polysaccharides - chemistry; Proteins; PBS; LAMP; PL; L14; Lectin; Vertebrata; Immunoprecipitation reaction; Mammalia; Affinity chromatography; Rodentia; Lysosome; Glycoproteins; Hamster; CHO cell line; Biological receptor
• ISSN: 0006-291X; 1090-2104
• DOI: 10.1016/S0006-291X(05)80902-7

Recent studies indicate that some mammalian S-type lectins bind preferentially to oligosaccharides containing the repeating disaccharide [3Galβ1,4GlcNAcβ1] n or poly-N-acetyllactosamine (PL) sequence. We report here our investigation on the distribution of these sequences in glycoproteins in Chinese hamster ovary (CHO) cells and the interaction of glycoproteins containing PL chains with an immobilized S-type lectin (L14) from calf heart tissue. Our results demonstrate that PL chains are carried by a few high molecular weight glycoproteins which are bound by tomato-lectin Sepharose and one of these was precipitated by antibody to LAMP-1 (a lysosomal-associated membrane glycoprotein). More importantly, these high molecular weight glycoproteins, including LAMP-1, were bound with high affinity by L14. These results indicate that mammalian S-type lectins are highly specific in their interactions with glycoproteins and that LAMPs carry important recognition sequences for these lectins.