Alterations in glomerular lectin binding sites of human kidney as detected by fluorescence microscopy.
Different lectins were used to study frozen sections of kidney samples showing alterations in routine immunofluorescence studies. Arachis hypogaea agglutinin (peanut lectin, PNA), lacking binding sites in normal glomeruli, bound to the glomeruli in two of the five samples studied, giving a granular fluorescence pattern. Concomitantly with the appearance of PNA-binding, binding sites for wheat germ agglutinin (WGA) appeared to be lost at glomeruli. Furthermore, changes in the expression of glomerular binding sites for Wistaria floribunda (WFA), Helix pomatia (HPA) and Dolichos biflorus (DBA) agglutinins could be seen in the kidneys studied, whereas the binding sites for Ulex europaeus agglutin (UEA I) in vascular endothelia seemed to be unaltered. The results show that kidney specimens presenting changes in routine immunofluorescence studies may also present altered binding for certain lectins. On this basis we propose that certain lectins may aid in characterizing these changes and are thus of potential use in studying diseased kidneys.
H
H
Holthöfer
I
I
Virtanen
T
T
Törnroth
A
A
Miettinen
D005455:Fluorescent Antibody Technique; D006651:Histocytochemistry; D006801:Humans; D007678:Kidney Glomerulus / Q000378:metabolism*; D037102:Lectins / Q000378:metabolism*; D008856:Microscopy, Fluorescence; D011975:Receptors, Mitogen / Q000378:metabolism*; D013194:Staining and Labeling
D037102:Lectins; D011975:Receptors, Mitogen