Inhibitory effects of PG-H/aggrecan and PG-M/versican on avian neural crest cell migration
(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:
https://lup.lub.lu.se/record/1110702
- author
- Perris, Roberto ; Perissinotto, Daniela ; Pettway, Zoe ; Bronner-Fraser, Marianne ; Mörgelin, Matthias LU and Kimata, Koji
- organization
- publishing date
- 1996
- type
- Contribution to journal
- publication status
- published
- subject
- in
- FASEB Journal
- volume
- 10
- issue
- 2
- pages
- 293 - 301
- publisher
- Wiley
- 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
- 2016-04-01 15:35:52
- date last changed
- 2023-09-04 03:58:49
@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 = {{Wiley}},
series = {{FASEB Journal}},
title = {{Inhibitory effects of PG-H/aggrecan and PG-M/versican on avian neural crest cell migration}},
url = {{http://www.fasebj.org/cgi/content/abstract/10/2/293}},
volume = {{10}},
year = {{1996}},
}