Differential effects of the cytoplasmic domains of cell adhesion molecules on cell aggregation and sorting-out.

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  • Additional Information
    • Source:
      Publisher: National Academy of Sciences Country of Publication: United States NLM ID: 7505876 Publication Model: Print Cited Medium: Print ISSN: 0027-8424 (Print) Linking ISSN: 00278424 NLM ISO Abbreviation: Proc Natl Acad Sci U S A Subsets: MEDLINE
    • Publication Information:
      Original Publication: Washington, DC : National Academy of Sciences
    • Subject Terms:
      Cell Aggregation*/drug effects; Cell Adhesion Molecules/*physiology ; Cell Adhesion Molecules, Neuronal/*physiology; Animals ; Cell Adhesion Molecules/genetics ; Cell Adhesion Molecules, Neuronal/genetics ; Cell Line ; Cells, Cultured ; Cytochalasin D/pharmacology ; DNA/genetics ; Fluorescent Antibody Technique ; Kinetics ; L Cells/cytology ; L Cells/drug effects ; Mice ; Nocodazole/pharmacology ; Plasmids ; Restriction Mapping ; Transfection
    • Abstract:
      Cell adhesion molecules (CAMs) are cell surface glycoproteins that play important roles in morphogenesis and histogenesis, particularly in defining discrete borders between cell populations. Previous studies have suggested that the cytoplasmic domains of CAMs play a significant role in their adhesion properties. These domains may also be involved in regulating other cellular interactions, such as those involved in the sorting-out of cells to form tissues. In the present studies, we have compared the effects of replacing the cytoplasmic domain of one CAM with that of another CAM of different homophilic binding specificity on cell adhesion and cell sorting-out. The molecules studied were liver CAM (L-CAM) and the neural CAM (N-CAM) sd polypeptide. One cDNA was constructed that encodes a chimeric molecule composed of the extracellular domain of L-CAM and the cytoplasmic plus transmembrane domains of the sd polypeptide of chicken N-CAM (called L/N-CAM). Another was constructed encoding a truncated L-CAM missing the last 50 residues of the cytoplasmic domain. Permanently transfected lines of mouse L cells were obtained expressing the truncated L-CAM ("L-L-50 cells") or the chimeric L/N-CAM ("L-L/N cells") and were compared with cells expressing intact L-CAM ("L-L cells"). Immunoblotting and ELISA analyses demonstrated that these various cell lines expressed similar amounts of CAMs at the cell surface. Aggregation of L-L and L-L/N cells occurred at similar rates in short-term aggregation assays and was inhibited by antibodies to the extracellular L-CAM binding domain. In contrast, L-L-50 cells did not aggregate. Incubation of transfected cells with cytochalasin D, which disrupts microfilaments, markedly inhibited aggregation of L-L cells but had no effect on L-L/N cell aggregation. Mixed L-L and L-L/N cells co-aggregated in short-term assays; in the longer-term sorting-out assays, however, they behaved differently: L-L cells sorted out from both L-L/N and untransfected cells, whereas L-L/N cells did not sort out from untransfected cells. These studies not only suggest that interactions of cytoplasmic domains of different CAMs with the cytoskeleton can modulate cell adhesion but also suggest that specific interactions with certain cytoskeletal components are required for events such as cell sorting and cell patterning.
    • References:
      Proc Natl Acad Sci U S A. 1979 Sep;76(9):4350-4. (PMID: 388439)
      Science. 1976 Apr 16;192(4236):218-26. (PMID: 769162)
      Proc Natl Acad Sci U S A. 1989 Feb;86(3):1088-92. (PMID: 2915974)
      Crit Rev Biochem Mol Biol. 1989;24(2):119-49. (PMID: 2651008)
      EMBO J. 1989 Jun;8(6):1711-7. (PMID: 2788574)
      Proc Natl Acad Sci U S A. 1989 Sep;86(18):7043-7. (PMID: 2780560)
      Proc Natl Acad Sci U S A. 1989 Dec;86(23):9579-83. (PMID: 2687885)
      Cell Regul. 1989 Nov;1(1):37-44. (PMID: 2519616)
      Proc Natl Acad Sci U S A. 1980 Aug;77(8):4831-5. (PMID: 6933535)
      J Biol Chem. 1982 Jul 10;257(13):7720-9. (PMID: 7085646)
      Proc Natl Acad Sci U S A. 1983 Feb;80(4):1038-42. (PMID: 6573655)
      J Cell Biol. 1984 May;98(5):1746-56. (PMID: 6725397)
      EMBO J. 1984 Oct;3(10):2249-60. (PMID: 6437808)
      Cell Motil. 1985;5(3):225-37. (PMID: 3891092)
      J Cell Biol. 1986 Jan;102(1):160-78. (PMID: 2934401)
      J Cell Biol. 1986 Feb;102(2):457-68. (PMID: 3511070)
      Annu Rev Cell Biol. 1986;2:81-116. (PMID: 3548776)
      Proc Natl Acad Sci U S A. 1987 May;84(9):2808-12. (PMID: 3472238)
      Science. 1987 May 15;236(4803):799-806. (PMID: 3576199)
      Nature. 1987 Sep 24-30;329(6137):341-3. (PMID: 3498123)
      Proc Natl Acad Sci U S A. 1987 Dec;84(23):8502-6. (PMID: 3317412)
      Immunol Rev. 1987 Dec;100:11-45. (PMID: 3326819)
      Cell. 1988 Sep 23;54(7):993-1001. (PMID: 3416359)
      Development. 1988 Apr;102(4):639-55. (PMID: 3048970)
      Proc Natl Acad Sci U S A. 1988 Oct;85(19):7274-8. (PMID: 3050992)
      Annu Rev Cell Biol. 1988;4:487-525. (PMID: 3058164)
      Proc Natl Acad Sci U S A. 1988 Dec;85(24):9616-20. (PMID: 3200847)
      EMBO J. 1988 Dec 1;7(12):3679-84. (PMID: 3061804)
    • Grant Information:
      DK-04256 United States DK NIDDK NIH HHS; HD-09635 United States HD NICHD NIH HHS; HD-16550 United States HD NICHD NIH HHS
    • Accession Number:
      0 (Cell Adhesion Molecules)
      0 (Cell Adhesion Molecules, Neuronal)
      22144-77-0 (Cytochalasin D)
      9007-49-2 (DNA)
      SH1WY3R615 (Nocodazole)
    • Publication Date:
      Date Created: 19900501 Date Completed: 19900606 Latest Revision: 20191210
    • Publication Date:
      20221208
    • Accession Number:
      PMC53947
    • Accession Number:
      10.1073/pnas.87.9.3589
    • Accession Number:
      2185477