help button home button Am J Pathol Epitomics Buy 2 Antibodies Get 1 Free Special Offer
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS

This Article
Right arrow Order Full text via Infotrieve
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Brown, D.
Right arrow Articles by Mulhauser J$[corrected to Muhlhauser, J]
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Brown, D.
Right arrow Articles by Mulhauser J$[corrected to Muhlhauser, J]

American Journal of Pathology, Vol 125, 601-610, Copyright © 1986 by American Society for Investigative Pathology

REGULAR ARTICLES

Regional heterogeneity of glycoconjugate distribution in the glomerulus revealed by lectin-gold cytochemistry and SDS-PAGE [published erratum appears in Am J Pathol 1987 Aug;128(2):216]

D Brown, JD Vassalli, A Kunz, J Muhlhauser, L Orci and J] Mulhauser J$[corrected to Muhlhauser

The authors have used SDS-PAGE and lectin overlay analysis in parallel with lectin-gold cytochemistry to identify Helix pomatia lectin (HPL) binding glycoconjugates in rat kidney glomeruli. Previous work revealed HPL binding sites only beneath podocyte foot process bases, where they contact the glomerular basement membrane. It is shown here that after neuraminidase digestion of thin sections of glomeruli before incubation with HPL-gold complexes, the number of HPL binding sites is markedly increased. These new sites are mainly associated with the podocyte free surface (adjacent to the urinary space) and with capillary endothelial cells. By lectin overlays, this neuraminidase-dependent HPL binding was shown to be due to reaction of the lectin with desialylated podocalyxin. In contrast, HPL binding sites detected prior to neuraminidase digestion are associated with a novel glycoconjugate having a lower electrophoretic mobility than podocalyxin. Although any role for this glycoconjugate is at present speculative, it is strategically positioned at the site of interaction between foot process bases and the glomerular basement membrane. Its presence correlates with normal podocyte architecture, as shown by our previous studies on developmental and aminonucleoside nephrosis-associated changes in HPL binding to podocytes.




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1986 by the American Society for Investigative Pathology.