A critical evaluation of neoglycoprotein binding sites in vivo and in sections of mouse tissues.
Endogenous lectins are reported to play a vital role in cell to cell communication. Their distribution in tissues has been widely studied by the use of labelled neoglycoproteins. In the present study, labelled neoglycoproteins were used on fixed and unfixed tissue sections and the results were compared with those observed after i.v. application of neoglycoproteins in mice. The study indicates that neoglycoprotein binding to tissue sections is not inhibited by application of the simple monosaccharides that were used to synthesize them. Furthermore the binding of neoglycoproteins following i.v. application into mice is rather limited. It is concluded that neoglycoproteins, which are synthesized using simple monosaccharides, do not provide a sensible tool to detect endogenous lectins in animal tissue sections. This is in sharp contrast to the results of most other studies reported in the literature.
Schumacher
U
U
University of Southampton, UK.
D000818:Animals; D003337:Corpus Callosum / Q000033:anatomy & histology / Q000378:metabolism; D005260:Female; D016650:Fluorescein-5-isothiocyanate; D006023:Glycoproteins / Q000008:administration & dosage / Q000378:metabolism*; D006098:Granulocytes / Q000276:immunology / Q000378:metabolism; D006651:Histocytochemistry; D007275:Injections, Intravenous; D007728:Kupffer Cells / Q000378:metabolism; D051379:Mice; D008807:Mice, Inbred BALB C; D019038:Platelet Glycoprotein GPIb-IX Complex; D010980:Platelet Membrane Glycoproteins; D011971:Receptors, Immunologic / Q000032:analysis / Q000378:metabolism*; D016707:Tissue Fixation
D006023:Glycoproteins; D019038:Platelet Glycoprotein GPIb-IX Complex; D010980:Platelet Membrane Glycoproteins; D011971:Receptors, Immunologic; C032193:glycoprotein receptor GPIb-IX; D016650:Fluorescein-5-isothiocyanate