Lectin histochemistry of fallopian tube epithelial cells. Relation to ovum transport and ovum pickup

• Published in: Journal of reproductive medicine Vol. 43; no. 6; p. 535
• Main Authors: Kiss, H, Walter, I, Lehner, R, Egarter, C, Breitenecker, G, Böck, P
• Format: Journal Article
• Language: English
• Published: United States 01.06.1998
• Subjects: ABO Blood-Group System; Adult; Concanavalin A; Electrochemistry; Epithelial Cells - chemistry; Fallopian Tubes - chemistry; Fallopian Tubes - cytology; Female; Glycocalyx - chemistry; Glycoconjugates - analysis; Glycoproteins - analysis; Histocytochemistry; Humans; Lectins; Menstrual Cycle; Ovum Transport; Plant Lectins; Polylysine - pharmacology; Wheat Germ Agglutinins
• ISSN: 0024-7758

Data on histochemical and biochemical characteristics of the human oviduct are scarce. The exact mechanisms of ovum transport and pickup are not fully understood. Human fallopian tubes were obtained and prepared for histochemistry. We analyzed the distribution of negatively charged groups on the oviduct epithelium and cumulus cells and examined the distribution of glycoconjugates by means of lectin histochemistry. We tested the possible influence of poly-L-lysine and considered ABO blood group expression since these characteristics are determined by specific terminal sugar residues. A negatively charged glycocalyx exists on tubal epithelial cells and cumulus cells. Adherence by affinities similar to sugar-lectin binding forces could be disproven in case of commonly used lectins. Poly-L-lysine inhibited the cationic binding reaction but did not influence lectin binding. The blood group A glycoprotein presents terminal D-N-acetyl-galactosamine residues, which are demonstrated by HPA lectin binding. Our study indicates that it is unlikely that electrostatic interactions play a major role in ovum transport or pickup. Since poly-L-lysine has been described as inhibiting ovum transport, sugar-lectin binding affinities seem not to operate in ovum transport or pickup.