New concepts in basement membrane biology.
- Halfter W Department of Ophthalmology, University Hospital Basel, Switzerland.
- Oertle P Biozentrum and the Swiss Nanoscience Institute, University of Basel, Switzerland.
- Monnier CA Biozentrum and the Swiss Nanoscience Institute, University of Basel, Switzerland.
- Camenzind L Biozentrum and the Swiss Nanoscience Institute, University of Basel, Switzerland.
- Reyes-Lua M Department of Ophthalmology, University Hospital Basel, Switzerland.
- Hu H Department of Neurobiology and Physiology, Upstate University Hospital, SUNY University, Syracuse, NY, USA.
- Candiello J Department of Bioengeneering, University of Pittsburgh, PA, USA.
- Labilloy A Department of Renal Physiology, University of Pittsburgh, PA, USA.
- Balasubramani M Proteomics Core Facility of the University of Pittsburgh, PA, USA.
- Henrich PB Department of Ophthalmology, University Hospital Basel, Switzerland.
- Plodinec M Biozentrum and the Swiss Nanoscience Institute, University of Basel, Switzerland.
- 2015-08-25
Published in:
- The FEBS journal. - 2015
basal lamina
basement membrane
biomechanical properties
collagen IV
laminin
membrane asymmetry
nidogen
perlecan
Animals
Basement Membrane
Humans
Microscopy, Atomic Force
Proteomics
English
Basement membranes (BMs) are thin sheets of extracellular matrix that outline epithelia, muscle fibers, blood vessels and peripheral nerves. The current view of BM structure and functions is based mainly on transmission electron microscopy imaging, in vitro protein binding assays, and phenotype analysis of human patients, mutant mice and invertebrata. Recently, MS-based protein analysis, biomechanical testing and cell adhesion assays with in vivo derived BMs have led to new and unexpected insights. Proteomic analysis combined with ultrastructural studies showed that many BMs undergo compositional and structural changes with advancing age. Atomic force microscopy measurements in combination with phenotype analysis have revealed an altered mechanical stiffness that correlates with specific BM pathologies in mutant mice and human patients. Atomic force microscopy-based height measurements strongly suggest that BMs are more than two-fold thicker than previously estimated, providing greater freedom for modelling the large protein polymers within BMs. In addition, data gathered using BMs extracted from mutant mice showed that laminin has a crucial role in BM stability. Finally, recent evidence demonstrate that BMs are bi-functionally organized, leading to the proposition that BM-sidedness contributes to the alternating epithelial and stromal tissue arrangements that are found in all metazoan species. We propose that BMs are ancient structures with tissue-organizing functions and were essential in the evolution of metazoan species.
- Language
-
- English
- Open access status
- hybrid
- Identifiers
-
- DOI 10.1111/febs.13495
- PMID 26299746
- Persistent URL
- https://folia.unifr.ch/global/documents/73376
Statistics
Document views: 5
File downloads:
- fulltext.pdf: 0