Deletion of integrin α7 subunit does not aggravate the phenotype of laminin α2 chain-deficient mice.
(2015) In Scientific Reports 5.- Abstract
- Laminin-211 is a major constituent of the skeletal muscle basement membrane, exerting its biological functions by binding to cell surface receptors integrin α7β1 and dystroglycan (the latter is part of the dystrophin-glycoprotein complex). The importance of these molecules for normal muscle function is underscored by the fact that their respective deficiency leads to different forms of muscular dystrophy with different severity in humans and animal models. We recently demonstrated that laminin α2 chain and members of the dystrophin-glycoprotein complex have overlapping but non-redundant roles despite being part of the same adhesion complex. To analyse whether laminin-211 and integrin α7 subunit have non-redundant functions we generated... (More)
- Laminin-211 is a major constituent of the skeletal muscle basement membrane, exerting its biological functions by binding to cell surface receptors integrin α7β1 and dystroglycan (the latter is part of the dystrophin-glycoprotein complex). The importance of these molecules for normal muscle function is underscored by the fact that their respective deficiency leads to different forms of muscular dystrophy with different severity in humans and animal models. We recently demonstrated that laminin α2 chain and members of the dystrophin-glycoprotein complex have overlapping but non-redundant roles despite being part of the same adhesion complex. To analyse whether laminin-211 and integrin α7 subunit have non-redundant functions we generated mice deficient in laminin α2 chain and integrin α7 subunit (dy(3K)/itga7). We show that lack of both molecules did not exacerbate the severe phenotype of laminin α2-chain deficient animals. They displayed the same weight, survival and dystrophic pattern of muscle biopsy, with similar degree of inflammation and fibrosis. These data suggest that laminin-211 and integrin α7β1 have intersecting roles in skeletal muscle. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/8042632
- author
- Gawlik, Kinga LU and Durbeej-Hjalt, Madeleine LU
- organization
- publishing date
- 2015
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Scientific Reports
- volume
- 5
- article number
- 13916
- publisher
- Nature Publishing Group
- external identifiers
-
- pmid:26355035
- wos:000360978800001
- scopus:84941369362
- pmid:26355035
- ISSN
- 2045-2322
- DOI
- 10.1038/srep13916
- language
- English
- LU publication?
- yes
- id
- 4a3133fb-7a17-4249-8bc0-0e8cbb932399 (old id 8042632)
- alternative location
- http://www.ncbi.nlm.nih.gov/pubmed/26355035?dopt=Abstract
- date added to LUP
- 2016-04-01 13:05:27
- date last changed
- 2022-01-27 17:17:37
@article{4a3133fb-7a17-4249-8bc0-0e8cbb932399,
abstract = {{Laminin-211 is a major constituent of the skeletal muscle basement membrane, exerting its biological functions by binding to cell surface receptors integrin α7β1 and dystroglycan (the latter is part of the dystrophin-glycoprotein complex). The importance of these molecules for normal muscle function is underscored by the fact that their respective deficiency leads to different forms of muscular dystrophy with different severity in humans and animal models. We recently demonstrated that laminin α2 chain and members of the dystrophin-glycoprotein complex have overlapping but non-redundant roles despite being part of the same adhesion complex. To analyse whether laminin-211 and integrin α7 subunit have non-redundant functions we generated mice deficient in laminin α2 chain and integrin α7 subunit (dy(3K)/itga7). We show that lack of both molecules did not exacerbate the severe phenotype of laminin α2-chain deficient animals. They displayed the same weight, survival and dystrophic pattern of muscle biopsy, with similar degree of inflammation and fibrosis. These data suggest that laminin-211 and integrin α7β1 have intersecting roles in skeletal muscle.}},
author = {{Gawlik, Kinga and Durbeej-Hjalt, Madeleine}},
issn = {{2045-2322}},
language = {{eng}},
publisher = {{Nature Publishing Group}},
series = {{Scientific Reports}},
title = {{Deletion of integrin α7 subunit does not aggravate the phenotype of laminin α2 chain-deficient mice.}},
url = {{http://dx.doi.org/10.1038/srep13916}},
doi = {{10.1038/srep13916}},
volume = {{5}},
year = {{2015}},
}