Advanced

Inhibitory effects of PG-H/aggrecan and PG-M/versican on avian neural crest cell migration

Perris, Roberto; Perissinotto, Daniela; Pettway, Zoe; Bronner-Fraser, Marianne; Mörgelin, Matthias LU and Kimata, Koji (1996) In FASEB Journal 10(2). p.293-301
Abstract
Aggrecans and PG-M/versicans represent two newly defined families of hyaluronan-binding proteoglycans for which the function is still poorly understood. Using the avian neural crest as a model system, we have examined the molecular mechanisms entailed in the cell-proteoglycan interaction during embryonic cell motility. Both the primary cartilage aggrecan of the avian embryo (PG-H/aggrecan) and the largest variant of the avian mesenchymal versican (PG-M/versican VO) failed to support neural crest cell adhesion and migration when topographically immobilized onto the substrate. Conversely, solely the PG-H/aggrecan, and similar aggrecans from other species, counteracted the migration-promoting effect of a number of matrix molecules lacking... (More)
Aggrecans and PG-M/versicans represent two newly defined families of hyaluronan-binding proteoglycans for which the function is still poorly understood. Using the avian neural crest as a model system, we have examined the molecular mechanisms entailed in the cell-proteoglycan interaction during embryonic cell motility. Both the primary cartilage aggrecan of the avian embryo (PG-H/aggrecan) and the largest variant of the avian mesenchymal versican (PG-M/versican VO) failed to support neural crest cell adhesion and migration when topographically immobilized onto the substrate. Conversely, solely the PG-H/aggrecan, and similar aggrecans from other species, counteracted the migration-promoting effect of a number of matrix molecules lacking proteoglycan affinity. This inhibitory effect was not reproduced by the isolated glycosaminoglycan chains, the isolated core protein, the reduced and alkylated macromolecule, or the aggrecan in which the G1 hyaluronan-binding domain had been inactivated with hyaluronan fragments or antibodies. Limited depolymerization of the side chains and preincubation of the PG-H/aggrecan with anti-glycosaminoglycan antibodies differentially reduced the inhibitory activity of the proteoglycan on cell motility. The results demonstrate a diverse inhibitory effect of aggrecans and PG-M/versicans on embryonic cell movement and show that the inhibitory action of aggrecans is independent of substrate binding, is dependent on a G1 domain-mediated association of the intact proteoglycan with cell surface-bound hyaluronan, and is differentially mediated by its glycosaminoglycan side chains. (Less)
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
FASEB Journal
volume
10
issue
2
pages
293 - 301
publisher
The Federation of American Societies for Experimental Biology
external identifiers
  • pmid:8641562
  • scopus:0029873884
ISSN
1530-6860
language
English
LU publication?
yes
id
d76fcdd4-1794-4fb7-8c43-e210259dc1c1 (old id 1110702)
alternative location
http://www.fasebj.org/cgi/content/abstract/10/2/293
date added to LUP
2008-07-29 09:02:44
date last changed
2017-10-22 04:31:44
@article{d76fcdd4-1794-4fb7-8c43-e210259dc1c1,
  abstract     = {Aggrecans and PG-M/versicans represent two newly defined families of hyaluronan-binding proteoglycans for which the function is still poorly understood. Using the avian neural crest as a model system, we have examined the molecular mechanisms entailed in the cell-proteoglycan interaction during embryonic cell motility. Both the primary cartilage aggrecan of the avian embryo (PG-H/aggrecan) and the largest variant of the avian mesenchymal versican (PG-M/versican VO) failed to support neural crest cell adhesion and migration when topographically immobilized onto the substrate. Conversely, solely the PG-H/aggrecan, and similar aggrecans from other species, counteracted the migration-promoting effect of a number of matrix molecules lacking proteoglycan affinity. This inhibitory effect was not reproduced by the isolated glycosaminoglycan chains, the isolated core protein, the reduced and alkylated macromolecule, or the aggrecan in which the G1 hyaluronan-binding domain had been inactivated with hyaluronan fragments or antibodies. Limited depolymerization of the side chains and preincubation of the PG-H/aggrecan with anti-glycosaminoglycan antibodies differentially reduced the inhibitory activity of the proteoglycan on cell motility. The results demonstrate a diverse inhibitory effect of aggrecans and PG-M/versicans on embryonic cell movement and show that the inhibitory action of aggrecans is independent of substrate binding, is dependent on a G1 domain-mediated association of the intact proteoglycan with cell surface-bound hyaluronan, and is differentially mediated by its glycosaminoglycan side chains.},
  author       = {Perris, Roberto and Perissinotto, Daniela and Pettway, Zoe and Bronner-Fraser, Marianne and Mörgelin, Matthias and Kimata, Koji},
  issn         = {1530-6860},
  language     = {eng},
  number       = {2},
  pages        = {293--301},
  publisher    = {The Federation of American Societies for Experimental Biology},
  series       = {FASEB Journal},
  title        = {Inhibitory effects of PG-H/aggrecan and PG-M/versican on avian neural crest cell migration},
  volume       = {10},
  year         = {1996},
}