-
Something wrong with this record ?
Proteomic analysis of the extracellular matrix in idiopathic pes equinovarus
M. Ošt'ádal, A. Eckhardt, J. Herget, I. Mikšík, P. Dungl, J. Chomiak, M. Frydrychová, M. Burian,
Language English Country Netherlands
Document type Journal Article
NLK
ProQuest Central
from 1997-01-01 to 1 year ago
Medline Complete (EBSCOhost)
from 2011-01-01 to 1 year ago
Health & Medicine (ProQuest)
from 1997-01-01 to 1 year ago
- MeSH
- Amino Acids analysis MeSH
- Extracellular Matrix Proteins metabolism MeSH
- Infant MeSH
- Collagen metabolism MeSH
- Humans MeSH
- Clubfoot metabolism pathology therapy MeSH
- Proteomics methods MeSH
- Transforming Growth Factor beta metabolism MeSH
- Check Tag
- Infant MeSH
- Humans MeSH
- Male MeSH
- Female MeSH
- Publication type
- Journal Article MeSH
Idiopathic pes equinovarus is a congenital deformity of the foot and lower leg defined as a fixation of the foot in adduction, supination, and varus. Although the pathogenesis of clubfoot remains unclear, it has been suggested that fibroblasts and growth factors are involved. To directly analyze the protein composition of the extracellular matrix in contracted tissue of patients with clubfoot. A total of 13 infants with idiopathic clubfoot treated with the Ponseti method were included in the present study. Tissue samples were obtained from patients undergoing surgery for relapsed clubfeet. Contracted tissues were obtained from the medial aspect of the talonavicular joint. Protein was extracted after digestion and delipidation using zip-tip C18. Individual collagenous fractions were detected using a chemiluminescent assay. Amino acid analysis of tissue samples revealed a predominance of collagens, namely collagen types I, III, and VI. The high content of glycine and h-proline suggests a predominance of collagens I and III. A total of 19 extracellular matrix proteins were identified. The major result of the present study was the observation that the extracellular matrix in clubfoot is composed of an additional 16 proteins, including collagens V, VI, and XII, as well as the previously described collagen types I and III and transforming growth factor β. The characterization of the general protein composition of the extracellular matrix in various regions of clubfoot may help in understanding the pathogenesis of this anomaly and, thus, contribute to the development of more efficacious therapeutic approaches.
References provided by Crossref.org
- 000
- 00000naa a2200000 a 4500
- 001
- bmc15031626
- 003
- CZ-PrNML
- 005
- 20240905114127.0
- 007
- ta
- 008
- 151005s2015 ne f 000 0|eng||
- 009
- AR
- 024 7_
- $a 10.1007/s11010-014-2300-3 $2 doi
- 035 __
- $a (PubMed)25472880
- 040 __
- $a ABA008 $b cze $d ABA008 $e AACR2
- 041 0_
- $a eng
- 044 __
- $a ne
- 100 1_
- $a Ošt'ádal, Martin $u Department of Orthopaedics, 1st Faculty of Medicine, University Hospital Bulovka, Charles University, Budínova 2, 180 00, Prague 8, Czech Republic, martinostadal@yahoo.com.
- 245 10
- $a Proteomic analysis of the extracellular matrix in idiopathic pes equinovarus / $c M. Ošt'ádal, A. Eckhardt, J. Herget, I. Mikšík, P. Dungl, J. Chomiak, M. Frydrychová, M. Burian,
- 520 9_
- $a Idiopathic pes equinovarus is a congenital deformity of the foot and lower leg defined as a fixation of the foot in adduction, supination, and varus. Although the pathogenesis of clubfoot remains unclear, it has been suggested that fibroblasts and growth factors are involved. To directly analyze the protein composition of the extracellular matrix in contracted tissue of patients with clubfoot. A total of 13 infants with idiopathic clubfoot treated with the Ponseti method were included in the present study. Tissue samples were obtained from patients undergoing surgery for relapsed clubfeet. Contracted tissues were obtained from the medial aspect of the talonavicular joint. Protein was extracted after digestion and delipidation using zip-tip C18. Individual collagenous fractions were detected using a chemiluminescent assay. Amino acid analysis of tissue samples revealed a predominance of collagens, namely collagen types I, III, and VI. The high content of glycine and h-proline suggests a predominance of collagens I and III. A total of 19 extracellular matrix proteins were identified. The major result of the present study was the observation that the extracellular matrix in clubfoot is composed of an additional 16 proteins, including collagens V, VI, and XII, as well as the previously described collagen types I and III and transforming growth factor β. The characterization of the general protein composition of the extracellular matrix in various regions of clubfoot may help in understanding the pathogenesis of this anomaly and, thus, contribute to the development of more efficacious therapeutic approaches.
- 650 _2
- $a aminokyseliny $x analýza $7 D000596
- 650 _2
- $a pes equinovarus $x metabolismus $x patologie $x terapie $7 D003025
- 650 _2
- $a kolagen $x metabolismus $7 D003094
- 650 _2
- $a extracelulární matrix - proteiny $x metabolismus $7 D016326
- 650 _2
- $a ženské pohlaví $7 D005260
- 650 _2
- $a lidé $7 D006801
- 650 _2
- $a kojenec $7 D007223
- 650 _2
- $a mužské pohlaví $7 D008297
- 650 _2
- $a proteomika $x metody $7 D040901
- 650 _2
- $a transformující růstový faktor beta $x metabolismus $7 D016212
- 655 _2
- $a časopisecké články $7 D016428
- 700 1_
- $a Eckhardt, Adam
- 700 1_
- $a Herget, Jan
- 700 1_
- $a Mikšík, Ivan
- 700 1_
- $a Dungl, Pavel
- 700 1_
- $a Chomiak, Jiří
- 700 1_
- $a Frydrychová, Monika
- 700 1_
- $a Burian, Michal $7 xx0322189
- 773 0_
- $w MED00003385 $t Molecular and cellular biochemistry $x 1573-4919 $g Roč. 401, č. 1-2 (2015), s. 133-9
- 856 41
- $u https://pubmed.ncbi.nlm.nih.gov/25472880 $y Pubmed
- 910 __
- $a ABA008 $b sig $c sign $y a $z 0
- 990 __
- $a 20151005 $b ABA008
- 991 __
- $a 20240905114122 $b ABA008
- 999 __
- $a ok $b bmc $g 1092502 $s 914752
- BAS __
- $a 3
- BAS __
- $a PreBMC
- BMC __
- $a 2015 $b 401 $c 1-2 $d 133-9 $e 20141204 $i 1573-4919 $m Molecular and cellular biochemistry $n Mol Cell Biochem $x MED00003385
- LZP __
- $a Pubmed-20151005