Skip to main content
PMC home page
The Journal of Cell Biology logoLink to The Journal of Cell Biology
. 1987 Jun 1;104(6):1587–1595. doi: 10.1083/jcb.104.6.1587

Biochemical and functional characterization of a novel neuron-glia adhesion molecule that is involved in neuronal migration

PMCID: PMC2114497  PMID: 2438288

Abstract

Adhesion molecule on glia (AMOG) is a novel neural cell adhesion molecule that mediates neuron-astrocyte interaction in vitro. In situ AMOG is expressed in the cerebellum by glial cells at the critical developmental stages of granule neuron migration. Granule neuron migration that is guided by surface contacts between migrating neurons and astroglial processes is inhibited by monoclonal AMOG antibody, probably by disturbing neuron-glia adhesion. AMOG is an integral cell surface glycoprotein of 45-50-kD molecular weight with a carbohydrate content of at least 30%. It does not belong to the L2/HNK-1 family of neural cell adhesion molecules but expresses another carbohydrate epitope that is shared with the adhesion molecules L1 and myelin- associated glycoprotein, but is not present on N-CAM or J1.

Full Text

The Full Text of this article is available as a PDF (2.3 MB).

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Bignami A., Eng L. F., Dahl D., Uyeda C. T. Localization of the glial fibrillary acidic protein in astrocytes by immunofluorescence. Brain Res. 1972 Aug 25;43(2):429–435. doi: 10.1016/0006-8993(72)90398-8. [DOI] [PubMed] [Google Scholar]
  2. Chou K. H., Ilyas A. A., Evans J. E., Quarles R. H., Jungalwala F. B. Structure of a glycolipid reacting with monoclonal IgM in neuropathy and with HNK-1. Biochem Biophys Res Commun. 1985 Apr 16;128(1):383–388. doi: 10.1016/0006-291x(85)91690-0. [DOI] [PubMed] [Google Scholar]
  3. Edelman G. M. Cell adhesion and the molecular processes of morphogenesis. Annu Rev Biochem. 1985;54:135–169. doi: 10.1146/annurev.bi.54.070185.001031. [DOI] [PubMed] [Google Scholar]
  4. Faissner A., Kruse J., Goridis C., Bock E., Schachner M. The neural cell adhesion molecule L1 is distinct from the N-CAM related group of surface antigens BSP-2 and D2. EMBO J. 1984 Apr;3(4):733–737. doi: 10.1002/j.1460-2075.1984.tb01876.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Faissner A., Teplow D. B., Kübler D., Keilhauer G., Kinzel V., Schachner M. Biosynthesis and membrane topography of the neural cell adhesion molecule L1. EMBO J. 1985 Dec 1;4(12):3105–3113. doi: 10.1002/j.1460-2075.1985.tb04052.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Fischer G., Künemund V., Schachner M. Neurite outgrowth patterns in cerebellar microexplant cultures are affected by antibodies to the cell surface glycoprotein L1. J Neurosci. 1986 Feb;6(2):605–612. doi: 10.1523/JNEUROSCI.06-02-00605.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Friedlander D. R., Grumet M., Edelman G. M. Nerve growth factor enhances expression of neuron-glia cell adhesion molecule in PC12 cells. J Cell Biol. 1986 Feb;102(2):413–419. doi: 10.1083/jcb.102.2.413. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Fushiki S., Schachner M. Immunocytological localization of cell adhesion molecules L1 and N-CAM and the shared carbohydrate epitope L2 during development of the mouse neocortex. Brain Res. 1986 Jan;389(1-2):153–167. doi: 10.1016/0165-3806(86)90183-5. [DOI] [PubMed] [Google Scholar]
  9. Ghandour S., Langley K., Gombos G., Hirn M., Hirsch M. R., Goridis C. A surface marker for murine vascular endothelial cells defined by monoclonal antibody. J Histochem Cytochem. 1982 Feb;30(2):165–170. doi: 10.1177/30.2.7061819. [DOI] [PubMed] [Google Scholar]
  10. Goridis C., Joher M. A., Hirsch M., Schachner M. Cell surface proteins of cultured brain cells and their recognition by anti-cerebellum (anti-NS-4) antiserum. J Neurochem. 1978 Aug;31(2):531–539. doi: 10.1111/j.1471-4159.1978.tb02669.x. [DOI] [PubMed] [Google Scholar]
  11. Goridis C., Martin J., Schachner M. Characterization of an antiserum to synaptic glomeruli from rat cerebellum. Brain Res Bull. 1978 Jan-Feb;3(1):45–52. doi: 10.1016/0361-9230(78)90060-6. [DOI] [PubMed] [Google Scholar]
  12. Hawkes R., Niday E., Gordon J. A dot-immunobinding assay for monoclonal and other antibodies. Anal Biochem. 1982 Jan 1;119(1):142–147. doi: 10.1016/0003-2697(82)90677-7. [DOI] [PubMed] [Google Scholar]
  13. Heifetz A., Keenan R. W., Elbein A. D. Mechanism of action of tunicamycin on the UDP-GlcNAc:dolichyl-phosphate Glc-NAc-1-phosphate transferase. Biochemistry. 1979 May 29;18(11):2186–2192. doi: 10.1021/bi00578a008. [DOI] [PubMed] [Google Scholar]
  14. Hunkapiller M. W., Lujan E., Ostrander F., Hood L. E. Isolation of microgram quantities of proteins from polyacrylamide gels for amino acid sequence analysis. Methods Enzymol. 1983;91:227–236. doi: 10.1016/s0076-6879(83)91019-4. [DOI] [PubMed] [Google Scholar]
  15. Kearney J. F., Radbruch A., Liesegang B., Rajewsky K. A new mouse myeloma cell line that has lost immunoglobulin expression but permits the construction of antibody-secreting hybrid cell lines. J Immunol. 1979 Oct;123(4):1548–1550. [PubMed] [Google Scholar]
  16. Keilhauer G., Faissner A., Schachner M. Differential inhibition of neurone-neurone, neurone-astrocyte and astrocyte-astrocyte adhesion by L1, L2 and N-CAM antibodies. Nature. 1985 Aug 22;316(6030):728–730. doi: 10.1038/316728a0. [DOI] [PubMed] [Google Scholar]
  17. Keller R. K., Boon D. Y., Crum F. C. N-Acetylglucosamine- 1 -phosphate transferase from hen oviduct: solubilization, characterization, and inhibition by tunicamycin. Biochemistry. 1979 Sep 4;18(18):3946–3952. doi: 10.1021/bi00585a016. [DOI] [PubMed] [Google Scholar]
  18. Komitowski D., Zinser G., Stute C. Digital picture analysis as an integral part of the information system for experimental oncopathology of the German Cancer Research Center. Methods Inf Med. 1983 Apr;22(2):69–74. [PubMed] [Google Scholar]
  19. Kruse J., Keilhauer G., Faissner A., Timpl R., Schachner M. The J1 glycoprotein--a novel nervous system cell adhesion molecule of the L2/HNK-1 family. Nature. 1985 Jul 11;316(6024):146–148. doi: 10.1038/316146a0. [DOI] [PubMed] [Google Scholar]
  20. Kruse J., Mailhammer R., Wernecke H., Faissner A., Sommer I., Goridis C., Schachner M. Neural cell adhesion molecules and myelin-associated glycoprotein share a common carbohydrate moiety recognized by monoclonal antibodies L2 and HNK-1. Nature. 1984 Sep 13;311(5982):153–155. doi: 10.1038/311153a0. [DOI] [PubMed] [Google Scholar]
  21. Kücherer A., Faissner A., Schachner M. The novel carbohydrate epitope L3 is shared by some neural cell adhesion molecules. J Cell Biol. 1987 Jun;104(6):1597–1602. doi: 10.1083/jcb.104.6.1597. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  23. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  24. Lagenaur C., Sommer I., Schachner M. Subclass of astroglia in mouse cerebellum recognized by monoclonal antibody. Dev Biol. 1980 Oct;79(2):367–378. doi: 10.1016/0012-1606(80)90122-0. [DOI] [PubMed] [Google Scholar]
  25. Lander A. D., Fujii D. K., Reichardt L. F. Laminin is associated with the "neurite outgrowth-promoting factors" found in conditioned media. Proc Natl Acad Sci U S A. 1985 Apr;82(7):2183–2187. doi: 10.1073/pnas.82.7.2183. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Liabeuf A., Gorvel J. P., Goridis C. Recognition of sodium- and potassium-dependent adenosine triphosphatase on mouse lymphoid cells by means of a monoclonal antibody. Cell Tissue Res. 1984;238(2):253–261. doi: 10.1007/BF00217297. [DOI] [PubMed] [Google Scholar]
  27. Liesi P. Do neurons in the vertebrate CNS migrate on laminin? EMBO J. 1985 May;4(5):1163–1170. doi: 10.1002/j.1460-2075.1985.tb03755.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Lindner J., Guenther J., Nick H., Zinser G., Antonicek H., Schachner M., Monard D. Modulation of granule cell migration by a glia-derived protein. Proc Natl Acad Sci U S A. 1986 Jun;83(12):4568–4571. doi: 10.1073/pnas.83.12.4568. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. Lindner J., Zinser G., Werz W., Goridis C., Bizzini B., Schachner M. Experimental modification of postnatal cerebellar granule cell migration in vitro. Brain Res. 1986 Jul 9;377(2):298–304. doi: 10.1016/0006-8993(86)90872-3. [DOI] [PubMed] [Google Scholar]
  30. Martini R., Schachner M. Immunoelectron microscopic localization of neural cell adhesion molecules (L1, N-CAM, and MAG) and their shared carbohydrate epitope and myelin basic protein in developing sciatic nerve. J Cell Biol. 1986 Dec;103(6 Pt 1):2439–2448. doi: 10.1083/jcb.103.6.2439. [DOI] [PMC free article] [PubMed] [Google Scholar]
  31. Moonen G., Grau-Wagemans M. P., Selak I. Plasminogen activator-plasmin system and neuronal migration. Nature. 1982 Aug 19;298(5876):753–755. doi: 10.1038/298753a0. [DOI] [PubMed] [Google Scholar]
  32. Neuhoff V., Philipp K., Zimmer H. G., Mesecke S. A simple, versatile, sensitive and volume-independent method for quantitative protein determination which is independent of other external influences. Hoppe Seylers Z Physiol Chem. 1979 Nov;360(11):1657–1670. doi: 10.1515/bchm2.1979.360.2.1657. [DOI] [PubMed] [Google Scholar]
  33. Noronha A. B., Ilyas A., Antonicek H., Schachner M., Quarles R. H. Molecular specificity of L2 monoclonal antibodies that bind to carbohydrate determinants of neural cell adhesion molecules and their resemblance to other monoclonal antibodies recognizing the myelin-associated glycoprotein. Brain Res. 1986 Oct 22;385(2):237–244. doi: 10.1016/0006-8993(86)91069-3. [DOI] [PubMed] [Google Scholar]
  34. Oakley B. R., Kirsch D. R., Morris N. R. A simplified ultrasensitive silver stain for detecting proteins in polyacrylamide gels. Anal Biochem. 1980 Jul 1;105(2):361–363. doi: 10.1016/0003-2697(80)90470-4. [DOI] [PubMed] [Google Scholar]
  35. PORTER R. R. The hydrolysis of rabbit y-globulin and antibodies with crystalline papain. Biochem J. 1959 Sep;73:119–126. doi: 10.1042/bj0730119. [DOI] [PMC free article] [PubMed] [Google Scholar]
  36. Pollerberg G. E., Schachner M., Davoust J. Differentiation state-dependent surface mobilities of two forms of the neural cell adhesion molecule. Nature. 1986 Dec 4;324(6096):462–465. doi: 10.1038/324462a0. [DOI] [PubMed] [Google Scholar]
  37. Quarles R. H. Myelin-associated glycoprotein in development and disease. Dev Neurosci. 1983;6(6):285–303. doi: 10.1159/000112356. [DOI] [PubMed] [Google Scholar]
  38. Rathjen F. G., Rutishauser U. Comparison of two cell surface molecules involved in neural cell adhesion. EMBO J. 1984 Feb;3(2):461–465. doi: 10.1002/j.1460-2075.1984.tb01828.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  39. Rathjen F. G., Schachner M. Immunocytological and biochemical characterization of a new neuronal cell surface component (L1 antigen) which is involved in cell adhesion. EMBO J. 1984 Jan;3(1):1–10. doi: 10.1002/j.1460-2075.1984.tb01753.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  40. Rutishauser U., Gall W. E., Edelman G. M. Adhesion among neural cells of the chick embryo. IV. Role of the cell surface molecule CAM in the formation of neurite bundles in cultures of spinal ganglia. J Cell Biol. 1978 Nov;79(2 Pt 1):382–393. doi: 10.1083/jcb.79.2.382. [DOI] [PMC free article] [PubMed] [Google Scholar]
  41. Sack H. J., Stöhr M., Schachner M. Cell type-specific binding of Ricinus lectin to murine cerebellar cell surfaces in vitro. Cell Tissue Res. 1983;228(1):183–204. doi: 10.1007/BF00206276. [DOI] [PubMed] [Google Scholar]
  42. Schnitzer J., Franke W. W., Schachner M. Immunocytochemical demonstration of vimentin in astrocytes and ependymal cells of developing and adult mouse nervous system. J Cell Biol. 1981 Aug;90(2):435–447. doi: 10.1083/jcb.90.2.435. [DOI] [PMC free article] [PubMed] [Google Scholar]
  43. Schnitzer J., Schachner M. Expression of Thy-1, H-2, and NS-4 cell surface antigens and tetanus toxin receptors in early postnatal and adult mouse cerebellum. J Neuroimmunol. 1981 Dec;1(4):429–456. doi: 10.1016/0165-5728(81)90022-9. [DOI] [PubMed] [Google Scholar]
  44. Sommer I., Schachner M. Monoclonal antibodies (O1 to O4) to oligodendrocyte cell surfaces: an immunocytological study in the central nervous system. Dev Biol. 1981 Apr 30;83(2):311–327. doi: 10.1016/0012-1606(81)90477-2. [DOI] [PubMed] [Google Scholar]
  45. Stallcup W. B., Beasley L. Involvement of the nerve growth factor-inducible large external glycoprotein (NILE) in neurite fasciculation in primary cultures of rat brain. Proc Natl Acad Sci U S A. 1985 Feb;82(4):1276–1280. doi: 10.1073/pnas.82.4.1276. [DOI] [PMC free article] [PubMed] [Google Scholar]
  46. Stoeckel K., Gagnon C., Guroff G., Thoenen H. Purification of nerve growth factor antibodies by affinity chromatography. J Neurochem. 1976 Jun;26(6):1207–1211. doi: 10.1111/j.1471-4159.1976.tb07008.x. [DOI] [PubMed] [Google Scholar]
  47. Thor G., Pollerberg E. G., Schachner M. Molecular association of two neural cell adhesion molecules within the surface membrane of cultured mouse neuroblastoma cells. Neurosci Lett. 1986 May 15;66(2):121–126. doi: 10.1016/0304-3940(86)90176-x. [DOI] [PubMed] [Google Scholar]
  48. Towbin H., Staehelin T., Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci U S A. 1979 Sep;76(9):4350–4354. doi: 10.1073/pnas.76.9.4350. [DOI] [PMC free article] [PubMed] [Google Scholar]
  49. de StGroth S. F., Scheidegger D. Production of monoclonal antibodies: strategy and tactics. J Immunol Methods. 1980;35(1-2):1–21. doi: 10.1016/0022-1759(80)90146-5. [DOI] [PubMed] [Google Scholar]

Articles from The Journal of Cell Biology are provided here courtesy of The Rockefeller University Press

RESOURCES