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J Biol Chem, Vol. 273, Issue 44, 28633-28641, October 30, 1998
From the Craniofacial Developmental Biology and Regeneration
Branch, NIDR, National Institutes of Health,
Bethesda, Maryland 20892-4370
The culture of human submandibular gland (HSG)
cells on laminin-1 induces acinar differentiation. We identified a site
on laminin involved in acinar differentiation using synthetic peptides derived from the C-terminal G-domain of the laminin 
1 and 2 chains. The 1 chain peptide AG73 (RKRLQVQLSIRT) decreases the size
of acini formed on laminin-1. Cells cultured with either AG73 or the
homologous 2 chain peptide MG73 (KNRLTIELEVRT) form structures that
appear acinar-like, but the cell nuclei are not polarized to the basal
surface and no lumen formation occurs, indicating that additional sites
on laminin are required for complete differentiation. The G-domain of
laminin-1 contains both integrin and heparin binding sites, and
anti-
1-integrin antibodies disrupt acinar
formation. Cell adhesion to the peptides and to E3, an elastase digest
fragment of laminin-1 containing AG73, is specific, since other laminin
peptides or EDTA do not compete the binding. Heparin and heparan
sulfate decrease cell adhesion to AG73 and MG73 but
anti-1-integrin antibodies have no effect. Treating the
cell surface with heparitinase inhibits adhesion to both AG73 and MG73.
We isolated cell surface ligands using both peptide affinity
chromatography and laminin-1 affinity chromatography. Treating the
material bound to the affinity columns with heparitinase and
chondroitinase enriches for a core protein identified as syndecan-1 by
Western blot analysis, thus identifying a syndecan-1 binding site in
the globular domain of laminin-1 and laminin-2. In summary, multiple
interactions between laminin and HSG cells contribute to acinar
differentiation, involving both 1-integrins and
syndecan-1.
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