Extracellular matrix alterations in brains lacking four of its components
Open accessAbstract
The organization of the brain extracellular matrix appears to be based on aggregates of hyaluronan and proteoglycans, connected by oligomeric glycoproteins. Mild phenotypical consequences were reported from several mouse strains lacking components of this matrix such as neurocan, brevican, tenascin-R, and tenascin-C. To further challenge the flexibility of the extracellular matrix network of the brain, mice lacking all four brain extracellular matrix molecules were generated, which were found to be viable and fertile. Analysis of the brains of 1-month-old quadruple KO mice revealed increased protein levels of fibulin-1 and fibulin-2. Histochemical analysis showed an unusual parenchymal deposition of these fibulins. The quadruple KO mice also displayed obvious changes in the pattern of deposition of hyaluronan. Further, an almost quadruple knockout like extracellular environment was noticed in the brains of triple knockout mice lacking both tenascins and brevican, since these brains had strongly reduced levels of neurocan.
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The first study describing the quadruple knockout mouse revealed an upregulation of fibulin-1 and fibulin-2 in the brains of one month old mice.
“The first study describing this knockout mouse revealed an upregulation of the proteins fibulin-1 and fibulin-2 in the brains of one month old mice28.”
From Elimination of the four extracellular matrix molecules tenascin-C, tenascin-R, brevican and neurocan alters the ratio of excitatory and inhibitory synapses (2019) · cites this paper as [28]
Altered hyaluronan deposition occurs in the mutant ECM.
“This is accompanied by an altered hyaluronan deposition in the mutant ECM28.”
From Elimination of the four extracellular matrix molecules tenascin-C, tenascin-R, brevican and neurocan alters the ratio of excitatory and inhibitory synapses (2019) · cites this paper as [28]
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- Authors
- Rauch, U., Zhou, X.-H., & Roos, G.
- Affiliations
- Lund University (SE)
- Corresponding author
- Rauch, Uwe
- ORCID
- Rauch, Uwe
- Venue
- Biochemical and Biophysical Research Communications
- Publisher
- Elsevier BV
- Published
- 2005-03
- Volume
- 328
- Issue
- 2
- Pages
- 608-617
- ISSN
- 0006-291X (ISSN-L)
- OpenAlex
- W2086582222
- Cited by
- 88
- References
- 51
- Citations by year
- 2025: 2 · 2024: 4 · 2023: 4 · 2022: 5 · 2021: 3 · 2020: 4 · 2019: 3 · 2018: 1 · 2017: 7 · 2016: 5 · 2015: 1 · 2014: 5 · 2013: 4 · 2012: 2
- FWCI
- 3.66
- Type
- journal article
- Language
- en
- Open access
- green
- lup.lub.lu.se
- Licence
- Locations
- Biochemical and Biophysical Research Communications (publishedVersion)
- PubMed (publishedVersion)
- Lund University Publications (Lund University) (submittedVersion, other-oa)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Proteoglycans and glycosaminoglycans research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
- Health Sciences › Medicine › Rheumatology › Bone and Dental Protein Studies
- Keywords
- brain extracellular matrix, neurocan, brevican, tenascin-R, tenascin-C, fibulin-1, fibulin-2, proteoglycans, triple knockout mice
- MeSH terms
- Animals, Brain, Calcium-Binding Proteins, Extracellular Matrix, Hyaluronic Acid, Nerve Tissue Proteins, Chondroitin Sulfate Proteoglycans, Tissue Distribution, Extracellular Matrix Proteins, Mice, Knockout, Tenascin, Lectins, C-Type, Mice, Neurocan, Brevican
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