Molecular cloning and sequence analysis of cDNA encoding the macrophage lectin specific for galactose and N-acetylgalactosamine

The primary structure of the macrophage lectin specific for galactose and N-acetylgalactosamine (macrophage asialoglycoprotein-binding protein, M-ASGP-BP) has been deduced from its cDNA sequence. The M-ASGP-BP cDNA encoded a protein consisting of 306 amino acid residues with a molecular mass of 34,2...

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Bibliographic Details
Published in:The Journal of biological chemistry 1990-07, Vol.265 (19), p.11295-11298
Main Authors: II, M, KURATA, H, ITOH, N, YAMASHINA, I, KAWASAKI, T
Format: Article
Language:English
Subjects:
Acetylgalactosamine - metabolism
Amino Acid Sequence
Analytical, structural and metabolic biochemistry
Animals
Asialoglycoprotein Receptor
asialoglycoprotein-binding protein
Asialoglycoproteins
Base Sequence
Biological and medical sciences
Carrier Proteins - genetics
Cloning, Molecular
Codon
DNA - genetics
DNA - isolation & purification
Fundamental and applied biological sciences. Psychology
Galactosamine - analogs & derivatives
Galactose - metabolism
Glycoproteins
Glycosylation
lectins
Lectins - genetics
Lectins, C-Type
macrophages
Macrophages - analysis
Membrane Proteins
Mice
Molecular Sequence Data
Molecular Weight
Proteins
Rats
Receptors, Cell Surface
Receptors, Immunologic
Sequence Homology, Nucleic Acid
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Summary:The primary structure of the macrophage lectin specific for galactose and N-acetylgalactosamine (macrophage asialoglycoprotein-binding protein, M-ASGP-BP) has been deduced from its cDNA sequence. The M-ASGP-BP cDNA encoded a protein consisting of 306 amino acid residues with a molecular mass of 34,242 daltons. The sequence was highly homologous with that of the rat liver asialoglycoprotein receptor (rat hepatic lectin, RHL), particularly that of RHL-1 (the major form of RHL), throughout its whole length, and especially so in its putative membrane-spanning region and carbohydrate recognition domain. There were two N-glycosylation sites in M-ASGP-BP, the location of which were identical to those in RHL-1. However, M-ASGP-BP was characteristic in having a shorter cytoplasmic tail, and an inserted segment of 24 amino acids containing an Arg-Gly-Asp sequence between the membrane-spanning region and carbohydrate recognition domain.
ISSN:0021-9258
1083-351X
DOI:10.1016/s0021-9258(19)38590-4