Immunologically unique and common domains within a family of proteins related to the retina Ca2+-dependent cell adhesion molecule, NcalCAM

Rabbit polyclonal antibodies raised to gp90, a fragment of the embryonic chick neural retina Ca2+-dependent adhesive molecule, gp130, recognize gp130 and inhibit Ca2+-dependent cell-cell adhesion. When tested against a panel of 10-day embryonic tissues, one of these antisera recognizes a component with a molecular weight identical to that of gp130 in embryonic chick cerebrum, optic lobe, hind brain, spinal cord and neural retina only; the second antiserum recognizes a similar component in all of the embryonic chick tissues tested. These data imply the existence of an extended family of closely related cell surface components with immunologically distinct subgroups each of which may mediate Ca2+-dependent cell-cell adhesion. As the term CAM, or cell adhesion molecule, has become common usage we propose to refer to these molecules as calCAMs, reflecting their calcium dependence. Analysis of fragments and endoglycosidase digests of NcalCAM have allowed a comparison of its structure with similar molecules from different tissues and species that have been implicated in Ca2+-dependent cell-cell adhesion.

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Antibodies to the retina N-acetylgalactosaminylphosphotransferase modulate N-cadherin-mediated adhesion and uncouple the N-cadherin transferase complex from the actin-containing cytoskeleton.

The Journal of Cell Biology ◽

10.1083/jcb.113.2.429 ◽

1991 ◽

Vol 113 (2) ◽

pp. 429-436 ◽

Cited By ~ 26

Author(s):

J Balsamo ◽

R Thiboldeaux ◽

N Swaminathan ◽

J Lilien

Keyword(s):

Cell Adhesion ◽

Adhesion Molecule ◽

Cell Adhesion Molecule ◽

Cell Monolayer ◽

Neural Retina ◽

Embryonic Chick ◽

Intact Cells ◽

Calcium Dependent ◽

Dependent Cell ◽

A Cell

Embryonic chick neural retina cells have at their surface an N-Acetylgalactosaminylphosphotransferase (GalNAcPTase) which is associated with, and glycosylates, the calcium-dependent cell-cell adhesion molecule, N-cadherin (Balsamo, J., and J. Lilien. 1990. J. Biol. Chem. 265:2923-2928). In this manuscript, we demonstrate that antibodies directed against the GalNAcPTase, as well as anti-N-cadherin antibodies, are able to inhibit adhesion of chick neural retina cells to a cell monolayer, to immobilized N-cadherin, or to immobilized anti-N-cadherin antibody. These results indicate that anti-GalNAcPTase antibodies modulate the function of N-cadherin, interfering with the formation of N-cadherin-mediated adhesions. We also demonstrate that actin is associated with the N-cadherin/GalNAcPTase complex and that binding of anti-GalNAcPTase antibodies to intact cells results in dissociation of actin from the complex. We suggest that the GalNAcPTase modulates N-cadherin function by altering its interaction with the cytoskeleton.

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Molecular Cloning and Characterization of DdCAD-1, a Ca2+-dependent Cell-Cell Adhesion Molecule, inDictyostelium discoideum

Journal of Biological Chemistry ◽

10.1074/jbc.271.27.16399 ◽

1996 ◽

Vol 271 (27) ◽

pp. 16399-16408 ◽

Cited By ~ 49

Author(s):

Estella F. S. Wong ◽

Simuran K. Brar ◽

Hiromi Sesaki ◽

Chunzhong Yang ◽

Chi-Hung Siu

Keyword(s):

Cell Adhesion ◽

Molecular Cloning ◽

Adhesion Molecule ◽

Cell Adhesion Molecule ◽

Dependent Cell ◽

Cell Cell

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Cloning and expression of cDNA encoding a neural calcium-dependent cell adhesion molecule: its identity in the cadherin gene family.

The Journal of Cell Biology ◽

10.1083/jcb.106.3.873 ◽

1988 ◽

Vol 106 (3) ◽

pp. 873-881 ◽

Cited By ~ 230

Author(s):

K Hatta ◽

A Nose ◽

A Nagafuchi ◽

M Takeichi

Keyword(s):

Cell Adhesion ◽

Amino Acid ◽

Gene Family ◽

Adhesion Molecule ◽

Cell Adhesion Molecule ◽

Cloning And Expression ◽

Common Amino Acid ◽

Neural Tissues ◽

Dependent Cell ◽

Cell Cell

The neural cadherin (N-cadherin) is a Ca2+-dependent cell-cell adhesion molecule detected in neural tissues as well as in non-neural tissues. We report here the nucleotide sequence of the chicken N-cadherin cDNA and the deduced amino acid sequence. The sequence data suggest that N-cadherin has one transmembrane domain which divides the molecule into an extracellular and a cytoplasmic domain; the extracellular domain contains internal repeats of characteristic sequences. When the N-cadherin cDNA connected with virus promoters was transfected into L cells which have no endogenous N-cadherin, the transformants acquired the N-cadherin-mediated aggregating property, indicating that the cloned cDNA contained all information necessary for the cell-cell binding action of this molecule. We then compared the primary structure of N-cadherin with that of other molecules defined as cadherin subclasses. The results showed that these molecules contain common amino acid sequences throughout their entire length, which confirms our hypothesis that cadherins make a gene family.

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Letter to the editor: 1H, 13C and 15N resonance assignments of Ca2+-free DdCAD-1: A Ca2+-dependent cell-cell adhesion molecule

Journal of Biomolecular NMR ◽

10.1007/s10858-005-2336-5 ◽

2004 ◽

Vol 30 (3) ◽

pp. 375-376 ◽

Cited By ~ 7

Author(s):

Zhi Lin ◽

Haibo Huang ◽

Chi-Hung Siu ◽

Daiwen Yang

Keyword(s):

Cell Adhesion ◽

Adhesion Molecule ◽

Cell Adhesion Molecule ◽

Resonance Assignments ◽

Letter To The Editor ◽

Dependent Cell ◽

Cell Cell

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Identification of a Ca2(+)-dependent cell-cell adhesion molecule in endothelial cells.

The Journal of Cell Biology ◽

10.1083/jcb.110.5.1745 ◽

1990 ◽

Vol 110 (5) ◽

pp. 1745-1756 ◽

Cited By ~ 65

Author(s):

R L Heimark ◽

M Degner ◽

S M Schwartz

Keyword(s):

Monoclonal Antibody ◽

Endothelial Cells ◽

Cell Adhesion ◽

Adhesion Molecule ◽

Cell Adhesion Molecule ◽

Extracellular Calcium ◽

Cell Contact ◽

Reducing Conditions ◽

Dependent Cell ◽

Cell Cell

Confluent cultures of aortic endothelial cells contain two different cell-cell adhesion mechanisms distinguished by their requirement for calcium during trypsinization and adhesion. A hybridoma clone was isolated producing a monoclonal antibody Ec6C10, which inhibits Ca2(+)-dependent adhesion of endothelial cells. There was no inhibition of Ca2(+)-independent adhesion of endothelial cells and only a minor effect on Ca2(+)-dependent adhesion of smooth muscle cells. Immunoblotting analysis shows that the antibody Ec6C10 recognizes a protein in endothelial but not epithelial cells with an apparent molecular weight of 135,000 in reducing conditions and 130,000 in non-reducing conditions. Monoclonal antibody Ec6C10 reacts with an antigen at the cell surface as shown by indirect immunofluorescence of confluent endothelial cells in a junctional pattern outlining the cobblestone morphology of the monolayer. Removal of extracellular calcium increased the susceptibility of the antigen recognized by antibody Ec6C10 to proteolysis by trypsin. The role of the Ca2(+)-dependent cell adhesion molecule in organization of the dense peripheral microfilament band in confluent endothelial cells was examined by adjusting the level of extracellular calcium to modulate cell-cell contact. Addition of the monoclonal antibody Ec6C10 at the time of the calcium switch inhibited the extent of formation of the peripheral F-actin band. These results suggest an association between cell-cell contact and the peripheral F-actin band potentially through the Ca2(+)-dependent CAM.

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