Novel contribution to clubfoot pathogenesis: The possible role of extracellular matrix proteins
Jazyk angličtina Země Spojené státy americké Médium print-electronic
Typ dokumentu srovnávací studie, časopisecké články, práce podpořená grantem
Grantová podpora
17-31564A
The Ministry of Health of the Czech Republic, Department Program for Research and Development - International
n. 336218
Charles University in Prague, project GA UK - International
RVO:67985823
Charles University in Prague, Specific University Research - International
n. SVV 260440
Charles University in Prague, Specific University Research - International
n. 217116002
The KZCR, a.s., Czech Republic, IGP KZ - International
PubMed
30615219
DOI
10.1002/jor.24211
Knihovny.cz E-zdroje
- Klíčová slova
- clubfoot, collagen, extracellular matrix, fibrosis, proteomics,
- MeSH
- dítě MeSH
- extracelulární matrix - proteiny metabolismus MeSH
- hmotnostní spektrometrie MeSH
- kalcinóza MeSH
- lidé MeSH
- pes equinovarus etiologie metabolismus MeSH
- předškolní dítě MeSH
- prospektivní studie MeSH
- proteom MeSH
- transformující růstový faktor beta metabolismus MeSH
- Check Tag
- dítě MeSH
- lidé MeSH
- mužské pohlaví MeSH
- předškolní dítě MeSH
- ženské pohlaví MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- srovnávací studie MeSH
- Názvy látek
- betaIG-H3 protein MeSH Prohlížeč
- extracelulární matrix - proteiny MeSH
- proteom MeSH
- transformující růstový faktor beta MeSH
Idiopathic pes equinovarus (clubfoot) is a congenital deformity of the feet and lower legs. Clubfoot belongs to a group of fibro-proliferative disorders but its origin remains unknown. Our study aimed to achieve the first complex proteomic comparison of clubfoot contracted tissue of the foot (medial side; n = 16), with non-contracted tissue (lateral side; n = 13). We used label-free mass spectrometry quantification and immunohistochemistry. Seven proteins were observed to be significantly upregulated in the medial side (asporin, collagen type III, V, and VI, versican, tenascin-C, and transforming growth factor beta induced protein) and four in the lateral side (collagen types XII and XIV, fibromodulin, and cartilage intermediate layer protein 2) of the clubfoot. Comparison of control samples from cadavers brought only two different protein concentrations (collagen types I and VI). We also revealed pathological calcification and intracellular positivity of transforming growth factor beta only in the contracted tissue of clubfoot. Most of the 11 differently expressed proteins are strongly related to the extracellular matrix architecture and we assume that they may play specific roles in the pathogenesis of this deformity. These proteins seem to be promising targets for future investigations and treatment of this disease. © 2019 Orthopaedic Research Society. Published by Wiley Periodicals, Inc. J Orthop Res.
2nd Faculty of Medicine Department of Physiology Charles University Prague Czech Republic
Biomedical Research Institute Hasselt University Diepenbeek Belgium
Department of Orthopedics Masaryk Hospital Usti nad Labem Czech Republic
Faculty of Physical Education and Sport Charles University Prague Czech Republic
Faculty of Science Department of Analytical Chemistry Charles University Prague Czech Republic
Institute of Physiology of the Czech Academy of Sciences v v i Videnska 1083 Prague Czech Republic
Citace poskytuje Crossref.org
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