Lectins as Probes of the Spermatozoon Surface

References

• Acott T S, Hoskins D D. Bovine sperm forward motility protein. Partial purification and characterization. J Biol Chem 1978; 23: 6744–6750
   Google Scholar
• Agrawal B BL, Goldstein I J. Protein-carbohydrate interaction. VI. Isolation of concanavalin A by specific adsorption on cross-linked dextran gels. Biochim Biophys Acta 1967; 147: 262–271
   PubMed Web of Science ®Google Scholar
• Ahkong Q F, Fisher D, Tampion W, Lucy J A. Mechanisms of cell fusion. Nature (London) 1975; 253: 194–195
   PubMed Web of Science ®Google Scholar
• Allen A K, Neuberger A. The purification and properties of the lectin from potatoe tubers, a hydroxyproline containing glycoprotein. Biochem J 1973; 135: 307–314
   PubMed Web of Science ®Google Scholar
• Austin C R. The capacitation of mammalian sperm. Nature (London) 1952; 170: 326
   PubMed Web of Science ®Google Scholar
• Badel P, Brilliantine L. Agglutination of spermatozoa of clams and of human A, B and O blood groups by phytagglutinins. Proc Cos Expl Biol Med 1969; 130: 621–623
   Google Scholar
• Becker J W, Reeke G N, Edelman G M. Location of the saccharide binding sites of concanavalin A. J Biol Chem 1971; 246: 6123–6125
   PubMed Web of Science ®Google Scholar
• Bedford J M. Changes in fine structure of the rabbit sperm head during passage through the epididymis. J Anat 1965; 99: 891–906
   Google Scholar
• Bedford J M. Development of the fertilizing ability of spermatozoa in the epididymis of the rabbit. J Exp Zooi 1966; 163: 319–329
   Google Scholar
• Bedford J M. Changes in the electropho-retic properties of rabbit spermatozoa during passage through the epididymis. Nature (London) 1963; 200: 1178–1180
   PubMedGoogle Scholar
• Bedford J M. Sperm capacitation and fertilization in mammals. Biol Reprod SuppI 1970; 2: 128–158
   PubMedGoogle Scholar
• Bedford J M, Cooper G W. Membrane fusion events in the fertilization of vertebrate eggs. Cell Surface Reviews, Membrane Fusion, G Poste, G L Nicolson. Elsevier North Holland, New York 1978; 65–125
   Google Scholar
• Bracken B G, Oliphant G. Capacitation of rabbit spermatozoa in vitro. Biol Reprod 1975; 12: 260–274
   Google Scholar
• Calvin H I, Bedford J M. Formation of disulfide bonds in the nucleus and accessory structures of mammalian spermatozoa during maturation in the epididymis. J Reprod Fertil SuppI 1971; 13: 65–75
   PubMedGoogle Scholar
• Chang M C. The fertilizing capacity of spermatozoa deposited into the Fallopian tubes. Nature (London) 1951; 168: 697–698
   PubMed Web of Science ®Google Scholar
• Cooper G W, Bedford J M. Acquisition of surface charge by the plasma membrane of mammalian spermatozoa during epididymal maturation. Anat Rec 1971; 169: 300–301
   Google Scholar
• Edelman G M, Millette C F. Molecular probes of spermatozoon structures. Proc Natl Acad Sci USA 1971; 68: 2436–2440
   PubMed Web of Science ®Google Scholar
• Eng L A., Oliphant G. Rabbit sperm reversible decapacitation by membrane stabilization with a highly purified glycoprotein from seminal plasma. Biol Reprod 1978; 19: 1083–1094
   PubMed Web of Science ®Google Scholar
• Fournier-Delpech S, Banzo B J, Orgebin-Crist M C. Extraction of concanavalin A affinity material from rat testicular and epididymal spermatozoa. Ann Biol Anim Biochem Biophys 1977; 17: 207–213
   Google Scholar
• Friend D S, Rudolf I. Acrosomal disruption in sperm: freeze fracture of altered membranes. J Cell Biol 1974; 63: 466–479
   Google Scholar
• Friend D S, Orci L, Perrelet A, Yanagimachi R. Membrane particle changes attending the acrosome reaction in guinea pig spermatozoa. J Cell Biol 1977; 74: 561–577
   Google Scholar
• Gall W E, Millette C R, Edelman G M. Chemical and structural analysis of mammalian spermatozoa. Physiology and Genetics of Reproduction, E M Continno, F Fuchs. Plenum Press, New York 1974; 241–257, Part A
   Google Scholar
• Gordon M, Dandekar P V, Bartoszewicz W. Ultrastructural localization of surface receptors for concanavalin A on rabbit spermatozoa. J Reprod Fertil 1974; 36: 211–214
   PubMedGoogle Scholar
• Gordon M, Dandekar P V, Bartoszewicz W. The surface coat of epididymal, ejaculated and capacitated sperm. J Ultrastruct Res 1975; 50: 199–207
   PubMedGoogle Scholar
• Hardman K D, Ainsworth C F. Myoinositol binding site of concanavalin A. Nature (London) New Biology 1972; 237: 54–55
   Google Scholar
• Kashiwabara T, Tanaka R, Matsumoto T. Tail to tail agglomeration of bull spermatozoa by phytoagglutinins present in soy beans. Nature 1965; 207: 831–832
   Google Scholar
• Kinsey W H, Koehler J K. Fine structural localization of Concanavalin A binding sites on hamster spermatozoa. J Supramol Struct 1976; 5: 185–189
   Google Scholar
• Kinsey W H., Koehler J K. Cell surface changes associated with in vitro capacitation of hamster sperm. J Ultrastruct Res 1978; 64: 1–13
   PubMedGoogle Scholar
• Koehler J K. Changes in antigenic site distribution on rabbit spermatozoa after incubation in capacitating media. Biol Reprod 1976; 15: 444–456
   Google Scholar
• Koehler J K. The mammalian sperm surface: studies with specific labeling techniques. Int Rev Cytol 1978; 54: 73–108
   PubMedGoogle Scholar
• Koehler J K, Gaddum-Rosse P. Media induced alterations of membrane associated particles of the guinea pig sperm tail. J Ultrastruct Res 1975; 51: 106–118
   Google Scholar
• Koehler J K, Sato K. Changes in lectin labeling pattern of mouse spermatozoa accompanying capacitation and the acrosome reaction. J Cell Biol 1978; 79: 165a
   Google Scholar
• Kopecny V. Acrosome labeling in mammalian spermatozoa. Ann Biol Anim Biochem Biophys 1979; 19: 695–701
   Google Scholar
• Lewin L M, Weissenberg R, Sobel J S, Marcus Z, Nebel L. Differences in Con A-FITC binding to rat spermatozoa during epididymal maturation and capacitation. Arch Androl 1979; 2: 279–281
   PubMed Web of Science ®Google Scholar
• Millette C F. Chemical dissection and surface mapping of spermatozoa. The Rockefeller University, New York 1975, Doctoral thesis
   Google Scholar
• Millette C F. Distribution and mobility of lectin binding sites on mammalian spermatozoa. Immunobiology of Gametes, M Edidin, M H Johnson. Cambridge University Press, Cambridge 1977; 51–71
   Google Scholar
• Nicolson G L. The interactions of lectins with animal cell surfaces. Int Rev Cytol 1974; 39: 89–190
   PubMed Web of Science ®Google Scholar
• Nicolson G L. Ultrastructural localization of lectin receptors. Advanced Techniques in Biological Electron Microscopy, J K Koehler. Springer Verlag, Heidelberg 1978; Vol II: 1–38
   Google Scholar
• Nicolson G L, Lacorbiere M, Yanagimachi R. Quantitative determination of plant agglutinin membrane sites on mammalian spermatozoa. Proc Soc Exp Biol Med 1972; 141: 661–663
   Google Scholar
• Nicolson G L, Yanagimachi R. Terminal saccharides on sperm plasma membranes. Identification by specific agglutinins. Science 1972; 177: 276–279
   PubMed Web of Science ®Google Scholar
• Nicolson G L, Yanagimachi R. Mobility and the restriction of mobility of plasma membrane lectin-binding components. Science 1974; 184: 1294–1296
   Google Scholar
• Nicolson G L, Poste G. Cell shape changes and transmembrane receptor uncoupling induced by tertiary amine local anesthetics. J Supramol Struct 1976; 5: 65–72
   Google Scholar
• Nicolson G L, Poste G, Ji T H. The dynamics of cell membrane organization. Dynamic Aspects of Cell Surface Organization, G Poste, G L Nicolson. North Holland Publishing Co., Amsterdam 1977; 1–73
   Google Scholar
• Nicolson G L, Usui N, Yanagimachi R, Yanagimachi H, Smith J R. Lectin binding sites on the plasma membrane of rabbit spermatozoa. J Cell Biol 1977; 74: 950–962
   PubMed Web of Science ®Google Scholar
• Oikawa T, Nicolson G L, Yanagimachi R. Inhibition of hamster fertilization by phyto-agglutinins. Exp Cell Res 1974; 83: 239–246
   PubMed Web of Science ®Google Scholar
• Orgebin-Crist M C. Maturation of spermatozoa in the rabbit epididymis: Fertilizing ability and embryonic mortality in does inseminated with epididymal spermatozoa. Ann Biol Anim Biochem Biophys 1967; 7: 373–389
   Google Scholar
• Papahadjopoulos D, Kimelberg H K. Phospholipid vesicles (liposomes) as models for biological membranes: Their properties and interactions with cholesterol and proteins. Progress in Surface Science, S G Davidson. Pergamon Press, Oxford 1973; Vol 3: 141–232
   Google Scholar
• Papahadjopoulos D W, Vail J W, Pangborn W A, Poste G. Studies on membrane fusion. II. Induction of fusion in pure phospholipid membranes by calcium ions and other divalent metals. Biochim Biophys Acta 1976; 448: 265–283
   PubMed Web of Science ®Google Scholar
• Presant C A, Kornfeld S. Characterization of the cell surface receptor for the Agaricus bisporus agglutinin. J Biol Chem 1972; 247: 6937–6945
   PubMed Web of Science ®Google Scholar
• Schwarz M A, Koehler J K. Alterations in lectin binding to guinea pig spermatozoa accompanying in vitro capacitation and the acrosome reaction. Biol Reprod 1979; 21: 1295–1307
   Google Scholar
• Sharon N, Lis H. Use of lectin for the study of membranes. Methods in Membrane Biology, E D Korn. Academic Press, New York, New York 1974; Vol 3: 147–199
   Google Scholar
• Talbot P, Franklin L E. Surface modification of guinea pig sperm during in vitro capacitation: An assessment using lectin-induced agglutination of living sperm. J Exp Zool 1978; 203: 1–14
   Google Scholar
• Talbot P, Franklin L E. Trypsinization increases lectin-induced agglutinability of un-capacitated guinea pig sperm. J Exp Zool 1978; 204: 291–297
   Google Scholar
• Talbot P, Chacon R. A new technique for rapidly scoring acrosome reactions in human sperm. J Cell Biol 1979; 83: 208a
   Google Scholar
• Uhlenbruck G, Herrmann W P. Agglutination of normal, coated and enzyme treated human spermatozoa with heterophide agglutinins. Vox Sang 1972; 23: 444–451
   Google Scholar
• Yanagimachi R, Noda Y D, Fujimoto M, Nicolson G L. The distribution of negative surface charges on mammalian spermatozoa. Am J Anat 1972; 135: 497–520
   PubMedGoogle Scholar
• Yanagimachi R, Usui N. Calcium dependent of the acrosome reaction and activation of guinea pig spermatozoa. Exp Cell Res 1974; 89: 161–174
   PubMed Web of Science ®Google Scholar
• Young W C. A study of the function of the epididymis III. Functional changes undergone by sperm during their passage through the epididymis and vas deferens in the guinea pig. J Exp Biol 1931; 8: 151–175
   Google Scholar