Mystery solved
Open Access
- 23 July 2001
- journal article
- editorial
- Published by Rockefeller University Press in The Journal of cell biology
- Vol. 154 (2) , 257-260
- https://doi.org/10.1083/jcb.200106124
Abstract
Mutant mice lacking the integrin α8 subunit exhibit variable defects in kidney development with most mutants missing both kidneys. Several lines of evidence indicate that the known extracellular matrix ligands for integrin α8β1 are either dispensable for or not involved in α8β1 signaling during kidney development. This suggests the presence of an unknown ligand. A novel α8β1 ligand, nephronectin, has now been identified. Nephronectin is a new extracellular matrix protein associated with the Wolffian duct and the ureteric bud, epithelial structures with well-defined roles in kidney development.Keywords
This publication has 20 references indexed in Scilit:
- Identification and characterization of a novel extracellular matrix protein nephronectin that is associated with integrin α8β1 in the embryonic kidneyThe Journal of cell biology, 2001
- Stereocilia defects in the sensory hair cells of the inner ear in mice deficient in integrin α8β1Nature Genetics, 2000
- Kidney morphogenesis: cellular and molecular regulationMechanisms of Development, 2000
- Defective Glomerulogenesis in the Absence of Laminin α5 Demonstrates a Developmental Role for the Kidney Glomerular Basement MembraneDevelopmental Biology, 2000
- Identification of Osteopontin as a Novel Ligand for the Integrin α8β1 and Potential Roles for This Integrin–Ligand Interaction in Kidney MorphogenesisMolecular Biology of the Cell, 1998
- Altered wound healing in mice lacking a functional osteopontin gene (spp1).Journal of Clinical Investigation, 1998
- Differential expression of five laminin α (1-5) chains in developing and adult mouse kidneyDevelopmental Dynamics, 1997
- The Laminin α Chains: Expression, Developmental Transitions, and Chromosomal Locations of α1-5, Identification of Heterotrimeric Laminins 8–11, and Cloning of a Novel α3 IsoformThe Journal of cell biology, 1997
- The Human Integrin α8β1 Functions as a Receptor for Tenascin, Fibronectin, and VitronectinPublished by Elsevier ,1995
- Integrin alpha 8 beta 1 promotes attachment, cell spreading, and neurite outgrowth on fibronectin.Molecular Biology of the Cell, 1995