Lectin-gold labeling of glycoconjugates in normal and Brattleboro rat papilla: effect of vasopressin

Abstract

Some reports suggest that the plasma membrane glycocalyx of collecting duct epithelial cells, as well as interstitial glycoconjugates, may be involved in vasopressin action and urinary concentration. In view of this, we have used the lectin-gold technique to map and quantify Helix pomatia lectin (HPL)-binding sites in the inner medulla of kidneys from normal Long-Evans rats, vasopressin-deficient Brattleboro rats, and Brattleboro rats treated for up to 5 wk with exogenous vasopressin. The results show that the labeling of epithelial cell plasma membranes from collecting ducts and thin limbs of Henle is not different between normal and Brattleboro rats, and the labeling is not modified by chronic vasopressin treatment. In contrast, the heavy interstitial labeling seen in normal rats is virtually absent from Brattleboro rats, but it is progressively restored by chronic vasopressin treatment of Brattleboro rats. These results show that vasopressin does not modify HPL-binding glycoconjugates on epithelial cell plasma membranes, but that vasopressin treatment has a major effect on HPL-binding glycoconjugates in the medullary interstitium.

Morphology of the Loop of Henle, Distal Tubule, and Collecting Duct

“…8d; (312)]. Binding studies with various lectins have revealed distinct labeling patterns in rat and rabbit DTLs and ATLs (255,256,343,430). Structure-Function Correlations.…”

Junctional complexes and cell polarity in the urinary tubule

“…In lectin-binding studies, we have found that the lower part of the descending thin limb of Henle shows apical labeling with Helix pomatia lectin and Dolichos biflorus lectins, whereas the thin ascending limbs are unlabeled (Weyer et al, 1987). Therefore, a differential lectin binding must be added to the inventory of other differences noted among thin limb segments.…”

Lectin characterization of the gastrointestinal tract of three Nigerian passerine birds

“…In order to allow unlimited access of the lectin marker to intracellular structures, as well as cell surface components, lectin immunocytochemical studies have employed various tissue thicknesses (30 µm, 50 µm, 60 µm, 100 µm, less than 1 mm and 1 mm) in the pre-embedding procedure [27,28,29,30]. The current study made use of 1 mm initially and was subsequently adjusted to tissues of less than 1 mm thickness for pre-embedding.…”