Structure of the chicken neuron-glia cell adhesion molecule, Ng-CAM: origin of the polypeptides and relation to the Ig superfamily - PubMed (original) (raw)
Structure of the chicken neuron-glia cell adhesion molecule, Ng-CAM: origin of the polypeptides and relation to the Ig superfamily
M P Burgoon et al. J Cell Biol. 1991 Mar.
Abstract
The neuron-glia cell adhesion molecule (Ng-CAM) mediates both neuron-neuron and neuron-glia adhesion; it is detected on SDS-PAGE as a predominant 135-kD glycoprotein, with minor components of 80, 190, and 210 kD. We have isolated cDNA clones encoding the entire sequence of chicken Ng-CAM. The predicted extracellular region includes six immunoglobulin-like domains followed by five fibronectin-type III repeats, structural features that are characteristic of several neural CAMs of the N-CAM superfamily. The amino acid sequence of chicken Ng-CAM is most similar to that of mouse L1 but the overall identity is only 40% and Ng-CAM contains a short fibronectin-like segment with an RGD sequence that has no counterpart in L1. These findings suggest that Ng-CAM and L1 may not be equivalent molecules in chicken and mouse. The amino-terminal sequences of the 210-, 190-, and 135-kD components of Ng-CAM are all the same as the predicted amino terminus of the molecule, whereas the 80-kD component begins within the third fibronectin repeat. The cDNA sequence is continuous across the junction between the 135- and 80-kD components, and a single 170-kD Ng-CAM polypeptide was isolated from tunicamycin-treated cells. In addition, all cDNA probes hybridized on Northern blots to a 6-kb RNA, and most hybridized to single bands on Southern blots. These results indicate that the Ng-CAM components are derived from a single polypeptide encoded by a single gene, and that the 135- and 80-kD components are generated from the 210/190-kD species by proteolytic cleavage. The 135-kD component contains most of the extracellular region including all of the immunoglobulin-like domains. It has no transmembrane segment, but it is tightly associated with the membrane. The 80-kD component contains two and a half type III repeats plus the RGD-containing segment, as well as the single transmembrane and cytoplasmic domains. These structural features of Ng-CAM provide a framework for understanding its multiple functions in neuron-neuron interactions, neurite fasciculation, and neuron-glia interactions.
Similar articles
- Structure of a new nervous system glycoprotein, Nr-CAM, and its relationship to subgroups of neural cell adhesion molecules.
Grumet M, Mauro V, Burgoon MP, Edelman GM, Cunningham BA. Grumet M, et al. J Cell Biol. 1991 Jun;113(6):1399-412. doi: 10.1083/jcb.113.6.1399. J Cell Biol. 1991. PMID: 2045418 Free PMC article. - Structure of the axonal surface recognition molecule neurofascin and its relationship to a neural subgroup of the immunoglobulin superfamily.
Volkmer H, Hassel B, Wolff JM, Frank R, Rathjen FG. Volkmer H, et al. J Cell Biol. 1992 Jul;118(1):149-61. doi: 10.1083/jcb.118.1.149. J Cell Biol. 1992. PMID: 1377696 Free PMC article. - Structural features of a close homologue of L1 (CHL1) in the mouse: a new member of the L1 family of neural recognition molecules.
Holm J, Hillenbrand R, Steuber V, Bartsch U, Moos M, Lübbert H, Montag D, Schachner M. Holm J, et al. Eur J Neurosci. 1996 Aug;8(8):1613-29. doi: 10.1111/j.1460-9568.1996.tb01306.x. Eur J Neurosci. 1996. PMID: 8921253 - Tenascin-contactin/F11 interactions: a clue for a developmental role?
Vaughan L, Weber P, D'Alessandri L, Zisch AH, Winterhalter KH. Vaughan L, et al. Perspect Dev Neurobiol. 1994;2(1):43-52. Perspect Dev Neurobiol. 1994. PMID: 7530143 Review.
Cited by
- Transcytosis of NgCAM in epithelial cells reflects differential signal recognition on the endocytic and secretory pathways.
Anderson E, Maday S, Sfakianos J, Hull M, Winckler B, Sheff D, Fölsch H, Mellman I. Anderson E, et al. J Cell Biol. 2005 Aug 15;170(4):595-605. doi: 10.1083/jcb.200506051. Epub 2005 Aug 8. J Cell Biol. 2005. PMID: 16087710 Free PMC article. - Characterization of functional domains of the tenascin-R (restrictin) polypeptide: cell attachment site, binding with F11, and enhancement of F11-mediated neurite outgrowth by tenascin-R.
Nörenberg U, Hubert M, Brümmendorf T, Tárnok A, Rathjen FG. Nörenberg U, et al. J Cell Biol. 1995 Jul;130(2):473-84. doi: 10.1083/jcb.130.2.473. J Cell Biol. 1995. PMID: 7615642 Free PMC article. - Cell adhesion molecules NgCAM and axonin-1 form heterodimers in the neuronal membrane and cooperate in neurite outgrowth promotion.
Buchstaller A, Kunz S, Berger P, Kunz B, Ziegler U, Rader C, Sonderegger P. Buchstaller A, et al. J Cell Biol. 1996 Dec;135(6 Pt 1):1593-607. doi: 10.1083/jcb.135.6.1593. J Cell Biol. 1996. PMID: 8978825 Free PMC article. - Tenascin promotes cerebellar granule cell migration and neurite outgrowth by different domains in the fibronectin type III repeats.
Husmann K, Faissner A, Schachner M. Husmann K, et al. J Cell Biol. 1992 Mar;116(6):1475-86. doi: 10.1083/jcb.116.6.1475. J Cell Biol. 1992. PMID: 1371773 Free PMC article. - Neuronal cell adhesion molecule contactin/F11 binds to tenascin via its immunoglobulin-like domains.
Zisch AH, D'Alessandri L, Ranscht B, Falchetto R, Winterhalter KH, Vaughan L. Zisch AH, et al. J Cell Biol. 1992 Oct;119(1):203-13. doi: 10.1083/jcb.119.1.203. J Cell Biol. 1992. PMID: 1382076 Free PMC article.
References
- Science. 1983 Nov 18;222(4625):778-82 - PubMed
- Proc Natl Acad Sci U S A. 1983 May;80(10):3116-20 - PubMed
- J Cell Biol. 1984 May;98(5):1746-56 - PubMed
- J Neurosci. 1983 Dec;3(12):2420-30 - PubMed
- Nature. 1983 Sep 29-Oct 5;305(5933):427-30 - PubMed
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Research Materials
Miscellaneous