Immobilized amines as mimetic heparin-binding domains for cell surface proteoglycan-mediated cell adhesion

S. P. Massia; J. A. Hubbell

Immobilized amines as mimetic heparin-binding domains for cell surface proteoglycan-mediated cell adhesion

S. P. Massia, J. A. Hubbell

Chemical and Biomolecular Engineering

Research output: Contribution to conference › Paper › peer-review

Abstract

In this study, we investigate the nature of human foreskin fibroblast (HFF) adhesion in the absence of serum proteins to glass substrates containing covalently linked amines. Based on this study, it can be concluded that cell adhesion to diamine derivatized substrates, which are positively charged at neutral pH, is chondroitin sulfate proteoglycan-mediated in the HFF. The immobilized N, N-dimethyl ED provided a good functional mimic of the so-called heparin-binding domain of cell adhesion proteins for this cell type.

Original language	English (US)
Pages	240
Number of pages	1
State	Published - 1991
Event	17th Annual Meeting of the Society for Biomaterials in conjunction with the 23rd International Biomaterials Symposium - Scottsdale, AZ, USA Duration: May 1 1991 → May 5 1991

Other

Other	17th Annual Meeting of the Society for Biomaterials in conjunction with the 23rd International Biomaterials Symposium
City	Scottsdale, AZ, USA
Period	5/1/91 → 5/5/91

ASJC Scopus subject areas

General Materials Science

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Immobilized amines as mimetic heparin-binding domains for cell surface proteoglycan-mediated cell adhesion. / Massia, S. P.; Hubbell, J. A.
1991. 240 Paper presented at 17th Annual Meeting of the Society for Biomaterials in conjunction with the 23rd International Biomaterials Symposium, Scottsdale, AZ, USA.

Research output: Contribution to conference › Paper › peer-review

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abstract = "In this study, we investigate the nature of human foreskin fibroblast (HFF) adhesion in the absence of serum proteins to glass substrates containing covalently linked amines. Based on this study, it can be concluded that cell adhesion to diamine derivatized substrates, which are positively charged at neutral pH, is chondroitin sulfate proteoglycan-mediated in the HFF. The immobilized N, N-dimethyl ED provided a good functional mimic of the so-called heparin-binding domain of cell adhesion proteins for this cell type.",

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AU - Massia, S. P.

AU - Hubbell, J. A.

PY - 1991

Y1 - 1991

N2 - In this study, we investigate the nature of human foreskin fibroblast (HFF) adhesion in the absence of serum proteins to glass substrates containing covalently linked amines. Based on this study, it can be concluded that cell adhesion to diamine derivatized substrates, which are positively charged at neutral pH, is chondroitin sulfate proteoglycan-mediated in the HFF. The immobilized N, N-dimethyl ED provided a good functional mimic of the so-called heparin-binding domain of cell adhesion proteins for this cell type.

AB - In this study, we investigate the nature of human foreskin fibroblast (HFF) adhesion in the absence of serum proteins to glass substrates containing covalently linked amines. Based on this study, it can be concluded that cell adhesion to diamine derivatized substrates, which are positively charged at neutral pH, is chondroitin sulfate proteoglycan-mediated in the HFF. The immobilized N, N-dimethyl ED provided a good functional mimic of the so-called heparin-binding domain of cell adhesion proteins for this cell type.

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T2 - 17th Annual Meeting of the Society for Biomaterials in conjunction with the 23rd International Biomaterials Symposium

Y2 - 1 May 1991 through 5 May 1991

ER -

Immobilized amines as mimetic heparin-binding domains for cell surface proteoglycan-mediated cell adhesion

Abstract

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ASJC Scopus subject areas

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