Laminin {alpha}1 globular domains 4-5 induce fetal development but are not vital for embryonic basement membrane assembly.

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Bibtex

@article{a01ef637b48b439ebcff18019ba716e4,
title = "Laminin {alpha}1 globular domains 4-5 induce fetal development but are not vital for embryonic basement membrane assembly.",
abstract = "basement membrane (BM) assembly, which is required for pregastrulation development. Individual domains may have other functions, not necessarily structural. The cell binding C terminus of Lm {alpha}1 chain contains five Lm globular (LG) domains. In vitro, {alpha}1LG1–3 domains bind integrins, and {alpha}1LG4 binds dystroglycan, heparin, and sulfatides. A prevailing hypothesis is that {alpha}1LG4 is crucial as a structural domain for BM assembly, whereas integrin-binding sites conduct signaling. The in vivo role of {alpha}1LG4–5 (also called E3) has not been studied. Mice lacking {alpha}1LG4–5 were therefore made. Null embryos implanted, but presumptive epiblast cells failed to polarize and did not survive past day 6.5. BM components including truncated Lm {alpha}1 were detected in Reichert's membrane. Surprisingly, embryonic BM assembly between visceral endoderm and stem cells was normal in null embryos and in embryoid bodies of {alpha}1LG4–5-null embryonic stem cells. Yet, stem cells could not develop into polarized epiblast cells. Thus, {alpha}1LG4–5 provides vital signals for the conversion of stem cells to polarized epithelium.",
keywords = "epiblast, epithelial polarity, stem cells, mouse development",
author = "Susanne Sch{\'e}ele and Mats Falk and Ahnders Franz{\'e}n and Fredrik Ellin and Maria Ferletta and Peter Lonai and Bj{\"o}rn Andersson and Rupert Timpl and Erik Forsberg and Peter Ekblom",
year = "2005",
doi = "10.1073/pnas.0405095102",
language = "English",
volume = "102",
pages = "1502--1506",
journal = "Proceedings of the National Academy of Sciences",
issn = "1091-6490",
publisher = "National Acad Sciences",
number = "5",

}