-
Je něco špatně v tomto záznamu ?
DiaPASEF proteotype analysis indicates changes in cell growth and metabolic switch induced by caspase-9 inhibition in chondrogenic cells
P. Lapcik, B. Vesela, D. Potesil, K. Dadakova, M. Zapletalova, P. Benes, P. Bouchal, E. Matalova
Jazyk angličtina Země Německo
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
36960851
DOI
10.1002/pmic.202200408
Knihovny.cz E-zdroje
- MeSH
- apoptóza * MeSH
- chondrocyty * metabolismus MeSH
- kaspasa 9 metabolismus farmakologie MeSH
- kaspasy metabolismus farmakologie MeSH
- signální transdukce MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
Caspase-9 is the major apical caspase responsible for triggering the intrinsic apoptotic pathway. Our previous study indicated that specific inhibition of caspase-9 caused microscopically evident alterations in appearance of the primary chondrogenic cultures which cannot be explained by decrease in apoptosis. To describe a complex molecular background of this effect, proteomics analysis of control and caspase-9 inhibitor-treated chondrogenic cultures were performed. Proteins were extracted, identified and quantified using LC-MS in both data dependent and data independent acquisition (DIA) mode. While directDIA analysis of diaPASEF data obtained using timsTOF Pro LC-MS system revealed 7849 protein groups (Q-value <0.01), a parallel analysis of iTRAQ-2DLC-MS3 and conventional DIA-MS data identified only 5146 and 4098 protein groups, respectively, showing diaPASEF a superior method for the study. The detailed analysis of diaPASEF data disclosed 236/551 significantly down-/up-regulated protein groups after caspase-9 inhibition, respectively (|log2FC|>0.58, Q value <0.05). Classification of downregulated proteins revealed changes in extracellular matrix organization, collagen metabolism, and muscle system processes. Moreover, deregulations suggest a switch from glycolytic to lipid based metabolism in the inhibited cells. No essential changes were found in the proteins involved in apoptosis. The data indicate new non-apoptotic participation of caspases in chondrocyte homeostasis with potential applications in cartilage pathophysiology.
Department of Biochemistry Faculty of Science Masaryk University Brno Czech Republic
Department of Experimental Biology Faculty of Science Masaryk University Brno Czech Republic
Department of Physiology Faculty of Veterinary Medicine Veterinary University Brno Czech Republic
International Clinical Research Center St Anne's University Hospital Brno Czech Republic
- 000
- 00000naa a2200000 a 4500
- 001
- bmc23011245
- 003
- CZ-PrNML
- 005
- 20230801132914.0
- 007
- ta
- 008
- 230718s2023 gw f 000 0|eng||
- 009
- AR
- 024 7_
- $a 10.1002/pmic.202200408 $2 doi
- 035 __
- $a (PubMed)36960851
- 040 __
- $a ABA008 $b cze $d ABA008 $e AACR2
- 041 0_
- $a eng
- 044 __
- $a gw
- 100 1_
- $a Lapcik, Petr $u Department of Biochemistry, Faculty of Science, Masaryk University, Brno, Czech Republic
- 245 10
- $a DiaPASEF proteotype analysis indicates changes in cell growth and metabolic switch induced by caspase-9 inhibition in chondrogenic cells / $c P. Lapcik, B. Vesela, D. Potesil, K. Dadakova, M. Zapletalova, P. Benes, P. Bouchal, E. Matalova
- 520 9_
- $a Caspase-9 is the major apical caspase responsible for triggering the intrinsic apoptotic pathway. Our previous study indicated that specific inhibition of caspase-9 caused microscopically evident alterations in appearance of the primary chondrogenic cultures which cannot be explained by decrease in apoptosis. To describe a complex molecular background of this effect, proteomics analysis of control and caspase-9 inhibitor-treated chondrogenic cultures were performed. Proteins were extracted, identified and quantified using LC-MS in both data dependent and data independent acquisition (DIA) mode. While directDIA analysis of diaPASEF data obtained using timsTOF Pro LC-MS system revealed 7849 protein groups (Q-value <0.01), a parallel analysis of iTRAQ-2DLC-MS3 and conventional DIA-MS data identified only 5146 and 4098 protein groups, respectively, showing diaPASEF a superior method for the study. The detailed analysis of diaPASEF data disclosed 236/551 significantly down-/up-regulated protein groups after caspase-9 inhibition, respectively (|log2FC|>0.58, Q value <0.05). Classification of downregulated proteins revealed changes in extracellular matrix organization, collagen metabolism, and muscle system processes. Moreover, deregulations suggest a switch from glycolytic to lipid based metabolism in the inhibited cells. No essential changes were found in the proteins involved in apoptosis. The data indicate new non-apoptotic participation of caspases in chondrocyte homeostasis with potential applications in cartilage pathophysiology.
- 650 _2
- $a kaspasa 9 $x metabolismus $x farmakologie $7 D053453
- 650 12
- $a chondrocyty $x metabolismus $7 D019902
- 650 12
- $a apoptóza $7 D017209
- 650 _2
- $a signální transdukce $7 D015398
- 650 _2
- $a kaspasy $x metabolismus $x farmakologie $7 D020169
- 655 _2
- $a časopisecké články $7 D016428
- 655 _2
- $a práce podpořená grantem $7 D013485
- 700 1_
- $a Vesela, Barbora $u Laboratory of Odontogenesis and Osteogenesis, Institute of Animal Physiology and Genetics, Czech Academy of Sciences, Brno, Czech Republic
- 700 1_
- $a Potesil, David $u Proteomics core facility, Central European Institute for Technology, Masaryk University, Brno, Czech Republic
- 700 1_
- $a Dadakova, Katerina $u Laboratory of Odontogenesis and Osteogenesis, Institute of Animal Physiology and Genetics, Czech Academy of Sciences, Brno, Czech Republic
- 700 1_
- $a Zapletalova, Martina $u Laboratory of Odontogenesis and Osteogenesis, Institute of Animal Physiology and Genetics, Czech Academy of Sciences, Brno, Czech Republic
- 700 1_
- $a Benes, Petr $u Department of Experimental Biology, Faculty of Science, Masaryk University, Brno, Czech Republic $u International Clinical Research Center, St. Anne's University Hospital, Brno, Czech Republic
- 700 1_
- $a Bouchal, Pavel $u Department of Biochemistry, Faculty of Science, Masaryk University, Brno, Czech Republic
- 700 1_
- $a Matalova, Eva $u Laboratory of Odontogenesis and Osteogenesis, Institute of Animal Physiology and Genetics, Czech Academy of Sciences, Brno, Czech Republic $u Department of Physiology, Faculty of Veterinary Medicine, Veterinary University, Brno, Czech Republic
- 773 0_
- $w MED00007044 $t Proteomics $x 1615-9861 $g Roč. 23, č. 11 (2023), s. e2200408
- 856 41
- $u https://pubmed.ncbi.nlm.nih.gov/36960851 $y Pubmed
- 910 __
- $a ABA008 $b sig $c sign $y p $z 0
- 990 __
- $a 20230718 $b ABA008
- 991 __
- $a 20230801132911 $b ABA008
- 999 __
- $a ok $b bmc $g 1963568 $s 1197510
- BAS __
- $a 3
- BAS __
- $a PreBMC-MEDLINE
- BMC __
- $a 2023 $b 23 $c 11 $d e2200408 $e 20230407 $i 1615-9861 $m Proteomics $n Proteomics $x MED00007044
- LZP __
- $a Pubmed-20230718