Proteomic analysis in NSAIDs-treated primary cardiomyocytes

Seon Mi Baek, Jin Sook Ahn, Hae Sook Noh, Jae-Yong Park, Sang Soo Kang, Deok Ryong Kim

Research output: Contribution to journalArticle

11 Citations (Scopus)

Abstract

NSAIDs (non-steroidal anti-inflammatory drugs) are widely used for the treatment of a variety of inflammatory diseases, but many of them were withdrawn from the market due to their cardiovascular toxicity. In this study, we tried to identify proteins responding to the cellular toxicity in NSAIDs-treated primarily cultured cardiomyocytes using 2-D proteomic analysis. We used seven different NSAIDs (celecoxib, rofecoxib, valdecoxib, diclofenac, naproxen, ibuprofen, and meloxicam) possessing each different degree of cardiovascular risk. Overall protein spots were similar in all NSAIDs-treated cells although numbers of decreased proteins were about 2-fold higher in celecoxib or rofecoxib-treated cells than in cells incubated with other NSAIDs. Many stress-related proteins, cardiac muscle movement proteins and proteins involved in membrane organization have been isolated. Among them, Septin-8, a filament scaffolding protein, showed its specific expression pattern depending on the extent of drug toxicity. Its expression level was low in cells treated by relatively high toxic drugs such as celecoxib, diclofenac, valdecoxib, and rofecoxib. On the contrary, Septin-8 was similarly expressed in control cells in the presence of less toxic drugs such ibuprofen, naproxen, and meloxicam. This data suggests that Septin-8 differentially responds to each NSAID.

Original languageEnglish
Pages (from-to)721-732
Number of pages12
JournalJournal of Proteomics
Volume73
Issue number4
DOIs
Publication statusPublished - 2010 Feb 10
Externally publishedYes

Fingerprint

Cardiac Myocytes
Proteomics
Celecoxib
Anti-Inflammatory Agents
meloxicam
Septins
Pharmaceutical Preparations
Proteins
Naproxen
Toxicity
Diclofenac
Ibuprofen
Poisons
Cells
Muscle Proteins
Heat-Shock Proteins
Drug-Related Side Effects and Adverse Reactions
Myocardium
Muscle
Cell Count

Keywords

  • Cardiomyocytes
  • NSAID
  • Proteomic analysis
  • Septin-8

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry

Cite this

Baek, S. M., Ahn, J. S., Noh, H. S., Park, J-Y., Kang, S. S., & Kim, D. R. (2010). Proteomic analysis in NSAIDs-treated primary cardiomyocytes. Journal of Proteomics, 73(4), 721-732. https://doi.org/10.1016/j.jprot.2009.10.004

Proteomic analysis in NSAIDs-treated primary cardiomyocytes. / Baek, Seon Mi; Ahn, Jin Sook; Noh, Hae Sook; Park, Jae-Yong; Kang, Sang Soo; Kim, Deok Ryong.

In: Journal of Proteomics, Vol. 73, No. 4, 10.02.2010, p. 721-732.

Research output: Contribution to journalArticle

Baek, Seon Mi ; Ahn, Jin Sook ; Noh, Hae Sook ; Park, Jae-Yong ; Kang, Sang Soo ; Kim, Deok Ryong. / Proteomic analysis in NSAIDs-treated primary cardiomyocytes. In: Journal of Proteomics. 2010 ; Vol. 73, No. 4. pp. 721-732.
@article{d02158d707424e37aef6cb754da12457,
title = "Proteomic analysis in NSAIDs-treated primary cardiomyocytes",
abstract = "NSAIDs (non-steroidal anti-inflammatory drugs) are widely used for the treatment of a variety of inflammatory diseases, but many of them were withdrawn from the market due to their cardiovascular toxicity. In this study, we tried to identify proteins responding to the cellular toxicity in NSAIDs-treated primarily cultured cardiomyocytes using 2-D proteomic analysis. We used seven different NSAIDs (celecoxib, rofecoxib, valdecoxib, diclofenac, naproxen, ibuprofen, and meloxicam) possessing each different degree of cardiovascular risk. Overall protein spots were similar in all NSAIDs-treated cells although numbers of decreased proteins were about 2-fold higher in celecoxib or rofecoxib-treated cells than in cells incubated with other NSAIDs. Many stress-related proteins, cardiac muscle movement proteins and proteins involved in membrane organization have been isolated. Among them, Septin-8, a filament scaffolding protein, showed its specific expression pattern depending on the extent of drug toxicity. Its expression level was low in cells treated by relatively high toxic drugs such as celecoxib, diclofenac, valdecoxib, and rofecoxib. On the contrary, Septin-8 was similarly expressed in control cells in the presence of less toxic drugs such ibuprofen, naproxen, and meloxicam. This data suggests that Septin-8 differentially responds to each NSAID.",
keywords = "Cardiomyocytes, NSAID, Proteomic analysis, Septin-8",
author = "Baek, {Seon Mi} and Ahn, {Jin Sook} and Noh, {Hae Sook} and Jae-Yong Park and Kang, {Sang Soo} and Kim, {Deok Ryong}",
year = "2010",
month = "2",
day = "10",
doi = "10.1016/j.jprot.2009.10.004",
language = "English",
volume = "73",
pages = "721--732",
journal = "Journal of Proteomics",
issn = "1874-3919",
publisher = "Elsevier",
number = "4",

}

TY - JOUR

T1 - Proteomic analysis in NSAIDs-treated primary cardiomyocytes

AU - Baek, Seon Mi

AU - Ahn, Jin Sook

AU - Noh, Hae Sook

AU - Park, Jae-Yong

AU - Kang, Sang Soo

AU - Kim, Deok Ryong

PY - 2010/2/10

Y1 - 2010/2/10

N2 - NSAIDs (non-steroidal anti-inflammatory drugs) are widely used for the treatment of a variety of inflammatory diseases, but many of them were withdrawn from the market due to their cardiovascular toxicity. In this study, we tried to identify proteins responding to the cellular toxicity in NSAIDs-treated primarily cultured cardiomyocytes using 2-D proteomic analysis. We used seven different NSAIDs (celecoxib, rofecoxib, valdecoxib, diclofenac, naproxen, ibuprofen, and meloxicam) possessing each different degree of cardiovascular risk. Overall protein spots were similar in all NSAIDs-treated cells although numbers of decreased proteins were about 2-fold higher in celecoxib or rofecoxib-treated cells than in cells incubated with other NSAIDs. Many stress-related proteins, cardiac muscle movement proteins and proteins involved in membrane organization have been isolated. Among them, Septin-8, a filament scaffolding protein, showed its specific expression pattern depending on the extent of drug toxicity. Its expression level was low in cells treated by relatively high toxic drugs such as celecoxib, diclofenac, valdecoxib, and rofecoxib. On the contrary, Septin-8 was similarly expressed in control cells in the presence of less toxic drugs such ibuprofen, naproxen, and meloxicam. This data suggests that Septin-8 differentially responds to each NSAID.

AB - NSAIDs (non-steroidal anti-inflammatory drugs) are widely used for the treatment of a variety of inflammatory diseases, but many of them were withdrawn from the market due to their cardiovascular toxicity. In this study, we tried to identify proteins responding to the cellular toxicity in NSAIDs-treated primarily cultured cardiomyocytes using 2-D proteomic analysis. We used seven different NSAIDs (celecoxib, rofecoxib, valdecoxib, diclofenac, naproxen, ibuprofen, and meloxicam) possessing each different degree of cardiovascular risk. Overall protein spots were similar in all NSAIDs-treated cells although numbers of decreased proteins were about 2-fold higher in celecoxib or rofecoxib-treated cells than in cells incubated with other NSAIDs. Many stress-related proteins, cardiac muscle movement proteins and proteins involved in membrane organization have been isolated. Among them, Septin-8, a filament scaffolding protein, showed its specific expression pattern depending on the extent of drug toxicity. Its expression level was low in cells treated by relatively high toxic drugs such as celecoxib, diclofenac, valdecoxib, and rofecoxib. On the contrary, Septin-8 was similarly expressed in control cells in the presence of less toxic drugs such ibuprofen, naproxen, and meloxicam. This data suggests that Septin-8 differentially responds to each NSAID.

KW - Cardiomyocytes

KW - NSAID

KW - Proteomic analysis

KW - Septin-8

UR - http://www.scopus.com/inward/record.url?scp=74849088209&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=74849088209&partnerID=8YFLogxK

U2 - 10.1016/j.jprot.2009.10.004

DO - 10.1016/j.jprot.2009.10.004

M3 - Article

VL - 73

SP - 721

EP - 732

JO - Journal of Proteomics

JF - Journal of Proteomics

SN - 1874-3919

IS - 4

ER -