Nephritogenoside,the receptor glycoprotein for concanavalin a in rat glomerular basement membrane: Demonstration of α-glucopyranosyl unit at the non-reducing terminus

Rat glomerular basement membrane was extracted for 3 h with trypsin, pH 8.0. The supernatant solution was treated with trichloroacetic acid and the supernatant thus obtained was applied to Bio-Gel P200. The first of the two glycoprotein peaks was applied onto Sepharose derivatives of concanavalin A (Con A.).Examination of the material retained by the unsolubilized Con A and subsquently eluted with methyl α-d-mannopyranoside reveals that the principal high affinity receptor for Con A is the renal glycoprotein, having antigenic activity that induces nephrotoxic antibody. This glycoprotein has also nephritogenicity (the activity capable of inducing glomerulonephritis in homologous animals by a single foot pad injection with Freund's incomplete adjuvant). Evidence is given to show that this binding is specific.The remainder of the renal glycoprotein is unretarded and is revealed to contain none of the activities described above.When fluorescein isothiocyanate-labelled Con A is, conversely, injected into rats through the renal artery, the specific binding of Con A to the glomerular capillary loop is proved.The results demonstrated here appear to, indicate that the receptor for Con A present in normal rat glomerular basement membrane can be identified as the well-established chemical substance, the nephritogenoside, having the α-d-glucopyranosyl unit at the non-reducing terminus which is facing the endothelial aspects of the glomerular capillary loop.