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LAMININ‐2/4 FROM HUMAN PLACENTA IS A BETTER ADHESION AGENT FOR PRIMARY KERATINOCYTES THAN LAMININ‐1 FROM EHS SARCOMA
Author(s) -
Gorelik J. V.,
Cherepanova O. A.,
Voronkina I. V.,
Diakonov I. A.,
Blinova M. I.,
Pinaev G. P.
Publication year - 2001
Publication title -
cell biology international
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.932
H-Index - 77
eISSN - 1095-8355
pISSN - 1065-6995
DOI - 10.1006/cbir.2000.0642
Subject(s) - laminin , fibronectin , adhesion , cell adhesion , microbiology and biotechnology , involucrin , chemistry , keratinocyte , in vitro , biology , extracellular matrix , biochemistry , organic chemistry
A comparison of the adhesion of human primary keratinocytes to laminin‐1 from murine EHS sarcoma and laminin‐2/4 from human placenta was carried out using two methods, cell adhesion to substrates covered with the laminin isoforms, and interaction of keratinocytes from suspension with latex beads coated with the proteins. Laminin‐2/4 was considerably more potent as a promoter of attachment of primary human keratinocytes than laminin‐1 (and fibronectin), with increased attachment of cells correlating well with the number of latex bead binding sites. Only small cells of diameter of less than 20μm bound more than 5 beads. Staining of keratinocytes with involucrin antibodies confirmed the existence of an inverse relationship between laminin‐2/4‐coated bead binding and differentiation.