Welcome to the new version of CaltechAUTHORS. Login is currently restricted to library staff. If you notice any issues, please email coda@library.caltech.edu
Published February 1996 | public
Journal Article

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

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.

Additional Information

© 1996 The Federation of American Societies for Experimental Biology. Received for publication August 7, 1995. Accepted for publication October 17, 1995. We are indebted to Mats Paulsson and Michael Sorrell for the various purified matrix molecules and antibodies. The work was supported by grants from Associazione Italians Ricerca sul Cancro, National Institute of Health grant USPHS HD 15527, the M. E. Muller Foundation, the Swedish Medical Research Council, the Swedish Natural Research Council, and the Roche Research Foundation.

Additional details

Created:
August 20, 2023
Modified:
October 18, 2023