-
Je něco špatně v tomto záznamu ?
Instability restricts signaling of multiple fibroblast growth factors
M. Buchtova, R. Chaloupkova, M. Zakrzewska, I. Vesela, P. Cela, J. Barathova, I. Gudernova, R. Zajickova, L. Trantirek, J. Martin, M. Kostas, J. Otlewski, J. Damborsky, A. Kozubik, A. Wiedlocha, P. Krejci,
Jazyk angličtina Země Švýcarsko
Typ dokumentu časopisecké články, práce podpořená grantem
NLK
PubMed Central
od 1997
ProQuest Central
od 1997-01-01 do 2017-12-31
Medline Complete (EBSCOhost)
od 2000-01-01
Health & Medicine (ProQuest)
od 1997-01-01 do 2017-12-31
- MeSH
- chondrosarkom genetika metabolismus patologie MeSH
- cirkulární dichroismus MeSH
- fibroblastové růstové faktory chemie klasifikace genetika metabolismus MeSH
- krysa rodu rattus MeSH
- lidé MeSH
- mutace genetika MeSH
- mutantní proteiny chemie metabolismus MeSH
- nádorové buňky kultivované MeSH
- nádory kostí genetika metabolismus patologie MeSH
- nádory prsu genetika metabolismus patologie MeSH
- proliferace buněk * MeSH
- signální transdukce * MeSH
- stabilita proteinů MeSH
- teplota MeSH
- zvířata MeSH
- Check Tag
- krysa rodu rattus MeSH
- lidé MeSH
- ženské pohlaví MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
Fibroblast growth factors (FGFs) deliver extracellular signals that govern many developmental and regenerative processes, but the mechanisms regulating FGF signaling remain incompletely understood. Here, we explored the relationship between intrinsic stability of FGF proteins and their biological activity for all 18 members of the FGF family. We report that FGF1, FGF3, FGF4, FGF6, FGF8, FGF9, FGF10, FGF16, FGF17, FGF18, FGF20, and FGF22 exist as unstable proteins, which are rapidly degraded in cell cultivation media. Biological activity of FGF1, FGF3, FGF4, FGF6, FGF8, FGF10, FGF16, FGF17, and FGF20 is limited by their instability, manifesting as failure to activate FGF receptor signal transduction over long periods of time, and influence specific cell behavior in vitro and in vivo. Stabilization via exogenous heparin binding, introduction of stabilizing mutations or lowering the cell cultivation temperature rescues signaling of unstable FGFs. Thus, the intrinsic ligand instability is an important elementary level of regulation in the FGF signaling system.
Citace poskytuje Crossref.org
- 000
- 00000naa a2200000 a 4500
- 001
- bmc15031405
- 003
- CZ-PrNML
- 005
- 20170620083132.0
- 007
- ta
- 008
- 151005s2015 sz f 000 0|eng||
- 009
- AR
- 024 7_
- $a 10.1007/s00018-015-1856-8 $2 doi
- 035 __
- $a (PubMed)25854632
- 040 __
- $a ABA008 $b cze $d ABA008 $e AACR2
- 041 0_
- $a eng
- 044 __
- $a sz
- 100 1_
- $a Buchtová, Marcela $u Department of Anatomy, Histology and Embryology, University of Veterinary and Pharmaceutical Sciences, Brno, Czech Republic. $7 xx0043736
- 245 10
- $a Instability restricts signaling of multiple fibroblast growth factors / $c M. Buchtova, R. Chaloupkova, M. Zakrzewska, I. Vesela, P. Cela, J. Barathova, I. Gudernova, R. Zajickova, L. Trantirek, J. Martin, M. Kostas, J. Otlewski, J. Damborsky, A. Kozubik, A. Wiedlocha, P. Krejci,
- 520 9_
- $a Fibroblast growth factors (FGFs) deliver extracellular signals that govern many developmental and regenerative processes, but the mechanisms regulating FGF signaling remain incompletely understood. Here, we explored the relationship between intrinsic stability of FGF proteins and their biological activity for all 18 members of the FGF family. We report that FGF1, FGF3, FGF4, FGF6, FGF8, FGF9, FGF10, FGF16, FGF17, FGF18, FGF20, and FGF22 exist as unstable proteins, which are rapidly degraded in cell cultivation media. Biological activity of FGF1, FGF3, FGF4, FGF6, FGF8, FGF10, FGF16, FGF17, and FGF20 is limited by their instability, manifesting as failure to activate FGF receptor signal transduction over long periods of time, and influence specific cell behavior in vitro and in vivo. Stabilization via exogenous heparin binding, introduction of stabilizing mutations or lowering the cell cultivation temperature rescues signaling of unstable FGFs. Thus, the intrinsic ligand instability is an important elementary level of regulation in the FGF signaling system.
- 650 _2
- $a zvířata $7 D000818
- 650 _2
- $a nádory kostí $x genetika $x metabolismus $x patologie $7 D001859
- 650 _2
- $a nádory prsu $x genetika $x metabolismus $x patologie $7 D001943
- 650 12
- $a proliferace buněk $7 D049109
- 650 _2
- $a chondrosarkom $x genetika $x metabolismus $x patologie $7 D002813
- 650 _2
- $a cirkulární dichroismus $7 D002942
- 650 _2
- $a ženské pohlaví $7 D005260
- 650 _2
- $a fibroblastové růstové faktory $x chemie $x klasifikace $x genetika $x metabolismus $7 D005346
- 650 _2
- $a lidé $7 D006801
- 650 _2
- $a mutantní proteiny $x chemie $x metabolismus $7 D050505
- 650 _2
- $a mutace $x genetika $7 D009154
- 650 _2
- $a stabilita proteinů $7 D055550
- 650 _2
- $a krysa rodu Rattus $7 D051381
- 650 12
- $a signální transdukce $7 D015398
- 650 _2
- $a teplota $7 D013696
- 650 _2
- $a nádorové buňky kultivované $7 D014407
- 655 _2
- $a časopisecké články $7 D016428
- 655 _2
- $a práce podpořená grantem $7 D013485
- 700 1_
- $a Chaloupkova, Radka
- 700 1_
- $a Zakrzewska, Malgorzata
- 700 1_
- $a Veselá, Ivana $7 xx0214541
- 700 1_
- $a Cela, Petra
- 700 1_
- $a Barathova, Jana
- 700 1_
- $a Gudernova, Iva
- 700 1_
- $a Zajickova, Renata
- 700 1_
- $a Trantirek, Lukas
- 700 1_
- $a Martin, Jorge
- 700 1_
- $a Kostas, Michal
- 700 1_
- $a Otlewski, Jacek
- 700 1_
- $a Damborsky, Jiri
- 700 1_
- $a Kozubik, Alois
- 700 1_
- $a Wiedlocha, Antoni
- 700 1_
- $a Krejci, Pavel
- 773 0_
- $w MED00001078 $t Cellular and molecular life sciences CMLS $x 1420-9071 $g Roč. 72, č. 12 (2015), s. 2445-59
- 856 41
- $u https://pubmed.ncbi.nlm.nih.gov/25854632 $y Pubmed
- 910 __
- $a ABA008 $b sig $c sign $y a $z 0
- 990 __
- $a 20151005 $b ABA008
- 991 __
- $a 20170620083550 $b ABA008
- 999 __
- $a ok $b bmc $g 1092281 $s 914531
- BAS __
- $a 3
- BAS __
- $a PreBMC
- BMC __
- $a 2015 $b 72 $c 12 $d 2445-59 $e 20150218 $i 1420-9071 $m Cellular and molecular life sciences $n Cell Mol Life Sci $x MED00001078
- LZP __
- $a Pubmed-20151005