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PMID: 8674415 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Amphiregulin in lung branching morphogenesis: interaction with heparan sulfate proteoglycan modulates cell proliferation.

Development (Cambridge, England) ·Vol. 122 ·No. 6 ·1996-06-00 ·Pages 1759-67

Schuger L, Johnson GR, Gilbride K, Plowman GD, Mandel R

Abstract

Epithelial and mesenchymal cells isolated from mouse embryonic lungs synthesized and responded to amphiregulin (AR) in a different fashion. Mesenchymal cells produced and deposited 3- to 4-fold more AR than epithelial cells, proliferated in the presence of exogenous AR, and their spontaneous growth was blocked by up to 85% by anti-AR antibodies. In contrast, epithelial cells exhibited a broad response to this growth regulator factor depending on whether they were supplemented with extracellular matrix (ECM) and whether this ECM was of epithelial or mesenchymal origin. AR-treated epithelial cells proliferated by up to 3-fold in the presence of mesenchymal-deposited ECM, remained unchanged in the presence of epithelial-deposited ECM, and decreased in their proliferation rate below controls in the absence of ECM supplementation. This effect was abolished by treatment with the glycosaminoglycan-degrading enzymes heparinase and heparitinase suggesting the specific involvement of heparan sulfate proteoglycan (HSPG) in AR-mediated cell proliferation. In whole lung explants, branching morphogenesis was inhibited by antibodies against the AR heparan sulfate binding site and stimulated by exogenous AR. Since during development, epithelial cells are in contact with mesenchymal ECM at the tips of the growing buds and alongside the basement membrane, focal variations in the proportion of epithelial and mesenchymal HSPG will focally affect epithelial proliferation rates. Therefore, AR-HSPG interaction may underlie the process of branching morphogenesis by inducing differential cell proliferation.

MeSH Terms
Amphiregulin Animals Cell Division/physiology Cells, Cultured EGF Family of Proteins Epithelial Cells Extracellular Matrix/metabolism Female Glycoproteins/metabolism,physiology Growth Substances/metabolism,physiology Heparan Sulfate Proteoglycans Heparin Lyase Heparitin Sulfate/metabolism,physiology Humans Intercellular Signaling Peptides and Proteins Lung/embryology,metabolism Male Mesoderm/cytology Mice Morphogenesis/physiology Polysaccharide-Lyases/metabolism Proteoglycans/metabolism,physiology
Chemicals
AREG protein, human Amphiregulin Areg protein, mouse EGF Family of Proteins Glycoproteins Growth Substances Heparan Sulfate Proteoglycans Intercellular Signaling Peptides and Proteins Proteoglycans Heparitin Sulfate Polysaccharide-Lyases Heparin Lyase heparitinsulfate lyase
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Schuger L
Department of Pathology and Laboratory Medicine, Wayne State University School of Medicine, Detroit, MI 48201, USA.
Johnson G R
Gilbride K
Plowman G D
Mandel R
Article Info
Journal
Development (Cambridge, England)
Abbr.
Development
ISSN
0950-1991
Published
1996-06-00
Pages
1759-67
Language
English
Region
England
NLM ID
8701744
Subset
IM
Grants
NHLBI NIH HHS · HL 48730-01 · United States
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