Age-Related Changes in the Expression of Cadherin-11, the Mesenchyme Specific Calcium-Dependent Cell Adhesion Molecule

1998 ◽  
Vol 62 (6) ◽  
pp. 532-537 ◽  
Author(s):  
R. S. Goomer ◽  
T. Maris ◽  
D. Amiel
Keyword(s):  
Cell Adhesion ◽  
Adhesion Molecule ◽  
Cell Adhesion Molecule ◽  
Calcium Dependent ◽  
Age Related ◽  
Dependent Cell ◽  
Age Related Changes

Age-related changes in neural cell adhesion molecule (NCAM) isoforms in the mouse telencephalon

1993 ◽  
Vol 628 (1-2) ◽  
pp. 286-292 ◽  
Author(s):  
Ben A. Bahr ◽  
Annette C. Godshall ◽  
Ben A. Murray ◽  
Gary Lynch
Keyword(s):  
Cell Adhesion ◽  
Adhesion Molecule ◽  
Cell Adhesion Molecule ◽  
Neural Cell Adhesion Molecule ◽  
Neural Cell ◽  
Age Related ◽  
Neural Cell Adhesion ◽  
Age Related Changes

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

1991 ◽  
Vol 113 (2) ◽  
pp. 429-436 ◽  
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.

scholarly journals Affinity and Kinetic Analysis of L-selectin (CD62L) Binding to Glycosylation-dependent Cell-adhesion Molecule-1

1998 ◽  
Vol 273 (2) ◽  
pp. 763-770 ◽  
Author(s):  
Martin W. Nicholson ◽  
A. Neil Barclay ◽  
Mark S. Singer ◽  
Steven D. Rosen ◽  
P. Anton van der Merwe
Keyword(s):  
Cell Adhesion ◽  
Kinetic Analysis ◽  
Adhesion Molecule ◽  
Cell Adhesion Molecule ◽  
Dependent Cell ◽  
Cell Adhesion Molecule 1

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

Development ◽  
1987 ◽  
Vol 101 (4) ◽  
pp. 729-740
Author(s):  
S.L. Crittenden ◽  
R.S. Pratt ◽  
J.H. Cook ◽  
J. Balsamo ◽  
J. Lilien
Keyword(s):  
Cell Adhesion ◽  
Adhesion Molecule ◽  
Cell Adhesion Molecule ◽  
Extended Family ◽  
Polyclonal Antibodies ◽  
Neural Retina ◽  
Embryonic Chick ◽  
Adhesive Molecule ◽  
Dependent Cell ◽  
Cell Cell

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.

scholarly journals Identification of the promoter and a transcriptional enhancer of the gene encoding L-CAM, a calcium-dependent cell adhesion molecule

1993 ◽  
Vol 90 (23) ◽  
pp. 11356-11360 ◽  
Author(s):  
B C Sorkin ◽  
F S Jones ◽  
B A Cunningham ◽  
G M Edelman
Keyword(s):  
Cell Adhesion ◽  
Cell Adhesion Molecule ◽  
Simian Virus 40 ◽  
Simian Virus ◽  
Cell Type ◽  
Cis Acting ◽  
Calcium Dependent ◽  
Dependent Cell ◽  
Cell Type Specific ◽  
Lmh Cells

L-CAM is a calcium-dependent cell adhesion molecule that is expressed in a characteristic place-dependent pattern during development. Previous studies of ectopic expression of the chicken L-CAM gene under the control of heterologous promoters in transgenic mice suggested that cis-acting sequences controlling the spatiotemporal expression patterns of L-CAM were present within the gene itself. We have now examined the L-CAM gene for sequences that control its expression and have found an enhancer within the second intron of the gene. A 2.5-kb Kpn I-EcoRI fragment from the intron acted as an enhancer of a simian virus 40 minimal promoter driving a chloramphenicol acetyltransferase (CAT) reporter gene and produced 14.0-fold induction of CAT activity in MDCK cells. To narrow down the region responsible for enhancer activity and to determine whether the enhancer could function in a cell type-specific manner, a number of smaller restriction fragments from the intron were tested for activity in two chicken cell lines, the LMH hepatoma line, which produces high levels of L-CAM, and the SL-29 fibroblast line, which produces little, if any, L-CAM. Four L-CAM enhancer plasmids containing shorter segments derived from the intron showed enhanced CAT activity levels (between 9.4- and 16.5-fold) in extracts from transfected LMH cells but not from SL-29 cells. DNA sequence analysis of the L-CAM enhancer region revealed putative binding sites for the transcription factors SP1, E2A, and AP-2. In addition, LE-9, the smallest L-CAM enhancer segment (310 bp), contained a consensus binding site for the liver-enriched POU-homeodomain transcription factor, HNF-1. Tests of upstream sequences showed that a 630-bp fragment, corresponding to nearly the entire intergenic region between L-CAM and its neighboring CAM gene, K-CAM, could function as a promoter. In combination with the L-CAM enhancer, this fragment directed cell type-specific expression of the CAT reporter gene in LMH cells at a level comparable to that observed with enhancer constructs using the simian virus 40 minimal promoter. These combined observations define a promoter and an enhancer for the chicken L-CAM gene. They raise the possibility that these cis-acting regulatory sequences may be instrumental in directing specific place-dependent expression of the L-CAM gene in the chicken.

Sign in / Sign up

Export Citation Format

Share Document