Caspase activation in equine influenza virus induced apoptotic cell death

Chengbin Lin; Robert E. Holland; Jennifer C. Donofrio; Morgan H. McCoy; Lynn R. Tudor; Thomas M. Chambers

doi:10.1016/S0378-1135(01)00468-0

Caspase activation in equine influenza virus induced apoptotic cell death

Chengbin Lin, Robert E. Holland, Jennifer C. Donofrio, Morgan H. McCoy, Lynn R. Tudor, Thomas M. Chambers

Veterinary Science

Research output: Contribution to journal › Article › peer-review

47 Scopus citations

Abstract

Equine influenza virus (EIV) is the leading cause of acute respiratory infection in horses worldwide. In recent years, the precise mechanism by which influenza infection kills host cells is being re-evaluated. In this report, we examined whether caspases, a group of intracellular proteases, are activated following EIV infection and contribute to EIV-mediated cell death. Western blotting analysis indicated that a nuclear target of caspase-3, poly(ADP-ribose) polymerase (PARP) was proteolytically cleaved in EIV-infected MDCK cells, but not in mock-infected cells. In comparison with caspase-3 specific inhibitor Ac-DEVD-CHO, a general caspase inhibitor Boc-D-FMK provided much stronger inhibition of EIV-induced cytopathic effect and apoptosis. Our results suggest that EIV may activate more than one caspase. Caspase activation and cleavage of its cellular targets may play a critical role in EIV-mediated cytotoxicity.

Original language	English
Pages (from-to)	357-365
Number of pages	9
Journal	Veterinary Microbiology
Volume	84
Issue number	4
DOIs	https://doi.org/10.1016/S0378-1135(01)00468-0
State	Published - Feb 4 2002

Bibliographical note

Funding Information:
We wish to acknowledge Dr. Stephen Zimmer (Department of Microbiology and Immunology, University of Kentucky School of Medicine) for his helpful comments on this manuscript. We thank Dr. Judith Appleton (James A. Baker Institute for Animal Health, Cornell University) for the generous gift of F90 5 H1.25 antibody. We also thank Dr. Shu-Chen Cheng and Ms. Linda Obenauer-Kutner (Schering-Plough Research Institute) for help with the glossy prints. This work was supported in part by USDA/CRS project no. KY 014006. The investigation reported in this paper is in connection with a project of the Kentucky Agricultural Experiment Station (no. 99-14-107) and is published with approval of the director.

Keywords

Ac-DEVD-CHO
Boc-D-FMK
Caspases
Equine influenza virus (EIV)
Madin-Darby canine kidney (MDCK) cells
Poly(ADP-ribose) polymerase (PARP)

ASJC Scopus subject areas

Microbiology
General Veterinary

Access to Document

10.1016/S0378-1135(01)00468-0

Cite this

@article{d33b527c759a48b3beeba7d6bbacb690,

title = "Caspase activation in equine influenza virus induced apoptotic cell death",

abstract = "Equine influenza virus (EIV) is the leading cause of acute respiratory infection in horses worldwide. In recent years, the precise mechanism by which influenza infection kills host cells is being re-evaluated. In this report, we examined whether caspases, a group of intracellular proteases, are activated following EIV infection and contribute to EIV-mediated cell death. Western blotting analysis indicated that a nuclear target of caspase-3, poly(ADP-ribose) polymerase (PARP) was proteolytically cleaved in EIV-infected MDCK cells, but not in mock-infected cells. In comparison with caspase-3 specific inhibitor Ac-DEVD-CHO, a general caspase inhibitor Boc-D-FMK provided much stronger inhibition of EIV-induced cytopathic effect and apoptosis. Our results suggest that EIV may activate more than one caspase. Caspase activation and cleavage of its cellular targets may play a critical role in EIV-mediated cytotoxicity.",

keywords = "Ac-DEVD-CHO, Boc-D-FMK, Caspases, Equine influenza virus (EIV), Madin-Darby canine kidney (MDCK) cells, Poly(ADP-ribose) polymerase (PARP)",

author = "Chengbin Lin and Holland, {Robert E.} and Donofrio, {Jennifer C.} and McCoy, {Morgan H.} and Tudor, {Lynn R.} and Chambers, {Thomas M.}",

note = "Funding Information: We wish to acknowledge Dr. Stephen Zimmer (Department of Microbiology and Immunology, University of Kentucky School of Medicine) for his helpful comments on this manuscript. We thank Dr. Judith Appleton (James A. Baker Institute for Animal Health, Cornell University) for the generous gift of F90 5 H1.25 antibody. We also thank Dr. Shu-Chen Cheng and Ms. Linda Obenauer-Kutner (Schering-Plough Research Institute) for help with the glossy prints. This work was supported in part by USDA/CRS project no. KY 014006. The investigation reported in this paper is in connection with a project of the Kentucky Agricultural Experiment Station (no. 99-14-107) and is published with approval of the director.",

year = "2002",

month = feb,

day = "4",

doi = "10.1016/S0378-1135(01)00468-0",

language = "English",

volume = "84",

pages = "357--365",

number = "4",

}

TY - JOUR

T1 - Caspase activation in equine influenza virus induced apoptotic cell death

AU - Lin, Chengbin

AU - Holland, Robert E.

AU - Donofrio, Jennifer C.

AU - McCoy, Morgan H.

AU - Tudor, Lynn R.

AU - Chambers, Thomas M.

N1 - Funding Information: We wish to acknowledge Dr. Stephen Zimmer (Department of Microbiology and Immunology, University of Kentucky School of Medicine) for his helpful comments on this manuscript. We thank Dr. Judith Appleton (James A. Baker Institute for Animal Health, Cornell University) for the generous gift of F90 5 H1.25 antibody. We also thank Dr. Shu-Chen Cheng and Ms. Linda Obenauer-Kutner (Schering-Plough Research Institute) for help with the glossy prints. This work was supported in part by USDA/CRS project no. KY 014006. The investigation reported in this paper is in connection with a project of the Kentucky Agricultural Experiment Station (no. 99-14-107) and is published with approval of the director.

PY - 2002/2/4

Y1 - 2002/2/4

N2 - Equine influenza virus (EIV) is the leading cause of acute respiratory infection in horses worldwide. In recent years, the precise mechanism by which influenza infection kills host cells is being re-evaluated. In this report, we examined whether caspases, a group of intracellular proteases, are activated following EIV infection and contribute to EIV-mediated cell death. Western blotting analysis indicated that a nuclear target of caspase-3, poly(ADP-ribose) polymerase (PARP) was proteolytically cleaved in EIV-infected MDCK cells, but not in mock-infected cells. In comparison with caspase-3 specific inhibitor Ac-DEVD-CHO, a general caspase inhibitor Boc-D-FMK provided much stronger inhibition of EIV-induced cytopathic effect and apoptosis. Our results suggest that EIV may activate more than one caspase. Caspase activation and cleavage of its cellular targets may play a critical role in EIV-mediated cytotoxicity.

AB - Equine influenza virus (EIV) is the leading cause of acute respiratory infection in horses worldwide. In recent years, the precise mechanism by which influenza infection kills host cells is being re-evaluated. In this report, we examined whether caspases, a group of intracellular proteases, are activated following EIV infection and contribute to EIV-mediated cell death. Western blotting analysis indicated that a nuclear target of caspase-3, poly(ADP-ribose) polymerase (PARP) was proteolytically cleaved in EIV-infected MDCK cells, but not in mock-infected cells. In comparison with caspase-3 specific inhibitor Ac-DEVD-CHO, a general caspase inhibitor Boc-D-FMK provided much stronger inhibition of EIV-induced cytopathic effect and apoptosis. Our results suggest that EIV may activate more than one caspase. Caspase activation and cleavage of its cellular targets may play a critical role in EIV-mediated cytotoxicity.

KW - Ac-DEVD-CHO

KW - Boc-D-FMK

KW - Caspases

KW - Equine influenza virus (EIV)

KW - Madin-Darby canine kidney (MDCK) cells

KW - Poly(ADP-ribose) polymerase (PARP)

UR - http://www.scopus.com/inward/record.url?scp=0037016814&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0037016814&partnerID=8YFLogxK

U2 - 10.1016/S0378-1135(01)00468-0

DO - 10.1016/S0378-1135(01)00468-0

M3 - Article

C2 - 11750143

AN - SCOPUS:0037016814

SN - 0378-1135

VL - 84

SP - 357

EP - 365

JO - Veterinary Microbiology

JF - Veterinary Microbiology

IS - 4

ER -

Caspase activation in equine influenza virus induced apoptotic cell death

Abstract

Bibliographical note

Keywords

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this