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J. Biol. Chem., Vol. 262, Issue 21, 9942-9944, Jul, 1987
MR Lennartz, FS Cole, VL Shepherd, TE Wileman and PD Stahl
A receptor which recognizes glycoproteins bearing terminal mannose residues
has been isolated from human placental membranes. Washed membranes were
solubilized with buffer containing 1% Triton X-100 and applied to a
mannose-Sepharose affinity column. The column was eluted with buffer
containing 200 mM mannose and 1% cholate. The major protein eluted
exhibited a molecular weight of 175 kDa on sodium dodecyl
sulfate-polyacrylamide gel electrophoresis. The protein binds 125I- labeled
mannosylated bovine serum albumin in a saturable fashion with a
dissociation constant of 4 nM. Ligand binding is pH-dependent with maximal
binding above pH 6.5. This binding can be inhibited with EDTA, mannose,
fucose, mannan, beta-glucuronidase, and bovine serum albumin conjugated to
fucose. Polyclonal antibodies generated against the mannose binding protein
immunoprecipitate a single 175-kDa protein species from both
surface-iodinated and biosynthetically labeled human monocyte-derived
macrophages.
Isolation and characterization of a mannose-specific endocytosis receptor from human placenta
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