Skip to main content

Lund University Publications

LUND UNIVERSITY LIBRARIES

C-CAM (cell-CAM 105) is an adhesive cell surface glycoprotein with homophilic binding properties

Tingström, Anders LU ; Blikstad, Ingrid ; Aurivillius, Magnus LU and Obrink, Björn (1990) In Journal of Cell Science 96(1). p.17-25
Abstract
C-CAM (Cell-CAM 105) is a cell surface glycoprotein that is involved in cell-cell adhesion of rat hepatocytes in vitro. To elucidate the adhesion mechanism the binding properties of purified C-CAM were investigated. Using proteins immobilized on nitrocellulose it was found that radiolabeled C-CAM bound to C-CAM but not to a variety of other proteins. Partitioning in Triton X-114 showed that C-CAM has hydrophobic properties. In accordance with this, C-CAM was effectively incorporated into phosphatidylcholine liposomes by dialysis from octylglucoside-containing solutions. The C-CAM-containing liposomes bound specifically to isolated hepatocytes. This binding was blocked by Fab fragments of anti-C-CAM antibodies. Furthermore, preincubation of... (More)
C-CAM (Cell-CAM 105) is a cell surface glycoprotein that is involved in cell-cell adhesion of rat hepatocytes in vitro. To elucidate the adhesion mechanism the binding properties of purified C-CAM were investigated. Using proteins immobilized on nitrocellulose it was found that radiolabeled C-CAM bound to C-CAM but not to a variety of other proteins. Partitioning in Triton X-114 showed that C-CAM has hydrophobic properties. In accordance with this, C-CAM was effectively incorporated into phosphatidylcholine liposomes by dialysis from octylglucoside-containing solutions. The C-CAM-containing liposomes bound specifically to isolated hepatocytes. This binding was blocked by Fab fragments of anti-C-CAM antibodies. Furthermore, preincubation of hepatocytes with anti-C-CAM antibodies followed by washing of the cells blocked binding of C-CAM-containing liposomes. At increasing C-CAM contents in the reconstituted liposomes a marked self-aggregation of the liposomes occurred. This aggregation was blocked by Fab fragments of anti-C-CAM antibodies and by alkaline pH. After neutralization a rapid reaggregation occurred. Neither C-CAM binding to C-CAM immobilized on nitrocellulose nor C-CAM-liposome aggregation required calcium ions. Liposomes reconstituted with C-CAM-depleted membrane glycoproteins did not self-aggregate or bind to hepatocytes. Thus, it is concluded that C-CAM can bind specifically to C-CAM in a homophilic binding reaction that does not require calcium. Accordingly, C-CAM has the potential of directly mediating cell-cell adhesion via C-CAM-C-CAM binding between adjacent cells. (Less)
Please use this url to cite or link to this publication:
author
; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
glycoprotein, adhesion, C-CAM
in
Journal of Cell Science
volume
96
issue
1
pages
17 - 25
publisher
The Company of Biologists Ltd
external identifiers
  • pmid:2373740
  • scopus:0025275169
ISSN
0021-9533
language
English
LU publication?
yes
id
79350f9a-521c-4ef2-9951-3c1b9f93f54b (old id 1105492)
alternative location
http://jcs.biologists.org/cgi/reprint/96/1/17
date added to LUP
2016-04-01 11:59:59
date last changed
2021-01-03 10:04:08
@article{79350f9a-521c-4ef2-9951-3c1b9f93f54b,
  abstract     = {{C-CAM (Cell-CAM 105) is a cell surface glycoprotein that is involved in cell-cell adhesion of rat hepatocytes in vitro. To elucidate the adhesion mechanism the binding properties of purified C-CAM were investigated. Using proteins immobilized on nitrocellulose it was found that radiolabeled C-CAM bound to C-CAM but not to a variety of other proteins. Partitioning in Triton X-114 showed that C-CAM has hydrophobic properties. In accordance with this, C-CAM was effectively incorporated into phosphatidylcholine liposomes by dialysis from octylglucoside-containing solutions. The C-CAM-containing liposomes bound specifically to isolated hepatocytes. This binding was blocked by Fab fragments of anti-C-CAM antibodies. Furthermore, preincubation of hepatocytes with anti-C-CAM antibodies followed by washing of the cells blocked binding of C-CAM-containing liposomes. At increasing C-CAM contents in the reconstituted liposomes a marked self-aggregation of the liposomes occurred. This aggregation was blocked by Fab fragments of anti-C-CAM antibodies and by alkaline pH. After neutralization a rapid reaggregation occurred. Neither C-CAM binding to C-CAM immobilized on nitrocellulose nor C-CAM-liposome aggregation required calcium ions. Liposomes reconstituted with C-CAM-depleted membrane glycoproteins did not self-aggregate or bind to hepatocytes. Thus, it is concluded that C-CAM can bind specifically to C-CAM in a homophilic binding reaction that does not require calcium. Accordingly, C-CAM has the potential of directly mediating cell-cell adhesion via C-CAM-C-CAM binding between adjacent cells.}},
  author       = {{Tingström, Anders and Blikstad, Ingrid and Aurivillius, Magnus and Obrink, Björn}},
  issn         = {{0021-9533}},
  keywords     = {{glycoprotein; adhesion; C-CAM}},
  language     = {{eng}},
  number       = {{1}},
  pages        = {{17--25}},
  publisher    = {{The Company of Biologists Ltd}},
  series       = {{Journal of Cell Science}},
  title        = {{C-CAM (cell-CAM 105) is an adhesive cell surface glycoprotein with homophilic binding properties}},
  url          = {{http://jcs.biologists.org/cgi/reprint/96/1/17}},
  volume       = {{96}},
  year         = {{1990}},
}