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PMID: 8601594 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Human amnion contains a novel laminin variant, laminin 7, which like laminin 6, covalently associates with laminin 5 to promote stable epithelial-stromal attachment.

The Journal of cell biology ·Vol. 132 ·No. 6 ·1996-03-00 ·Pages 1189-98

Champliaud MF, Lunstrum GP, Rousselle P, Nishiyama T, Keene DR, Burgeson RE

Abstract

Stable attachment of external epithelia to the basement membrane and underlying stroma is mediated by transmembrane proteins such as the integrin alpha6beta4 and bullous pemphigoid antigen 2 within the hemidesmosomes along the basolateral surface of the epithelial cell and their ligands that include a specialized subfamily of laminins. The laminin 5 molecule (previously termed kalinin/nicein/epiligrin) is a member of this epithelial-specific subfamily. Laminin 5 chains are not only considerably truncated within domains III-VI, but are also extensively proteolytically processed in vitro and in vivo. As a result, the domains expected to be required for the association of laminins with other basement membrane components are lacking in the mature laminin 5 molecule. Therefore, the tight binding of laminin 5 to the basement membrane may occur by a unique mechanism. To examine laminin 5 in tissue, we chose human amnion as the source, because of its availability and the similarity of the amniotic epithelial basement membrane with that of skin. We isolated the laminin 5 contained within the basement membrane of human amnion. In addition to monomeric laminin 5, we find that much of the laminin 5 isolated is covalently adducted with laminin 6 (alpha3beta1gamma1) and a novel laminin isotype we have termed laminin 7 (alpha3beta2gamma1). We propose that the association between laminin 5 and laminins 6 and 7 is a mechanism used in amnion to allow stable association of laminin 5 with the basement membrane. The beta2 chain is seen at the human amniotic epithelial-stromal interface and at the dermal-epidermal junction of fetal and adult bovine skin by immunofluorescence, but is not present, or only weakly present, in neonatal human skin.

MeSH Terms
Adult Amino Acid Sequence Amnion/cytology,metabolism Animals Cattle Cell Adhesion/physiology Cell Adhesion Molecules/metabolism Connective Tissue/metabolism Connective Tissue Cells Epithelial Cells Epithelium/metabolism Humans Infant, Newborn Laminin/chemistry,isolation & purification,metabolism Molecular Sequence Data Molecular Weight Protein Structure, Tertiary Sequence Alignment Sequence Homology, Amino Acid
Chemicals
Cell Adhesion Molecules Laminin kalinin laminin 7
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Champliaud M F
Cutaneous Biology Research Center, Massachusetts General Hospital, Charlestown 02129, USA.
Lunstrum G P
Rousselle P
Nishiyama T
Keene D R
Burgeson R E
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Article Info
Journal
The Journal of cell biology
Abbr.
J Cell Biol
ISSN
0021-9525
DOI
10.1083/jcb.132.6.1189
Published
1996-03-00
Pages
1189-98
Language
English
Region
United States
NLM ID
0375356
PMCID
PMC2120759
Subset
IM
Grants
NIAMS NIH HHS · AR35689 · United States
External Links
PubMed source DOI: 10.1083/jcb.132.6.1189 PMC Full Text View journal details
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