Lectin binding sites on human sperm and spermatogenic cells

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Abstract
Testes of sexually mature men were studied histochemically with 20 fluorescein isothiocyanate‐labeled lectins. Based on their pattern of reactivity with intratesticular spermatogenic cells, lectins were divided into five groups: (1) lectins reacting with all spermatogenic cells (Suc. ConA, WGA, LCA, PHA‐E, PHAL, STA, MPA, and RCA‐II); (2) lectin reacting with spermatocytes, spermatids, and spermatozoa, but not with spermatogonia (RCA‐I); (3) lectins reacting with spermatids and spermatozoa only (BPA, PNA, SBA, and VVA); (4) lectins reacting only with spermatozoa (HPA, GSA‐I, UEA‐II, and GSA‐II); and (5) lectins with no distinct staining of spermatogenic cells (DBA, LBA, and UEA‐I). All lectins from groups 1–4 were reactive with ejaculated spermatozoa. On the basis of the staining patterns of the head region of ejaculated spermatozoa, four lectin reactivity groups were defined: (1) lectins reacting with the plasma membrane of the whole head (BPA, WGA, LCA, STA, RCA‐II, PHA‐E, PHA‐L, RCA‐I, UEA‐II, and GSA‐II); (2) lectin reacting with the acrosomal cap and postacrosomal region of the plasma membrane (Suc. ConA); (3) lectin reacting with the acrosomal cap region of the plasma membrane (PNA); and (4) lectins reacting with the midregion of the sperm head in a bandlike manner (HPA, VVA, SBA, GSA‐I, and MPA). These data provide a map of lectin binding sites on human testicular spermatogenic cells and ejaculated spermatozoa and show that the distribution of glycoconjugate domains of spermatogenic cell changes during differentiation and maturation.

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