Cell death protection by 3-aminobenzamide and other poly(ADP-ribose)polymerase inhibitors: Different effects on human natural killer and lymphokine activated killer cell activities

D. Monti, A. Cossarizza, S. Salvioli, C. Franceschi, G. Rainaldi, E. Straface, R. Rivabene, W. Malorni

Research output: Contribution to journalArticle

Abstract

The death of target cells by cytotoxic effector cells is a relevant biological phenomenon, where cells are activated and a very quick apoptotic program occurs. In order to test the hypothesis that the nuclear enzyme poly(ADP-ribose)polymerase (PADPRP) plays a role in such a process, a variety of PADPRP inhibitors such as 3-aminobenzamide, nicotinamide, 4-aminobenzamide and luminol were used. All of them were able to strongly inhibit K562 target cell killing by human effector natural killer cells (NK) in a 4hr 51Cr release assay. PADPRP inhibitors were much less effective in protecting target cells when lymphokine activated killer cells (LAK) were used as effectors. These substances were active only when both target and effector cells were mixed, being ineffective on target or effector cells alone. On the whole, these data indicate that PADPRP is involved in the death of target cells. Moreover, the different sensitivity of NK and LAK activities to PADPRP inhibitors suggests that the molecular mechanisms underlying these two types of cytotoxicity are at least partially different.

Original languageEnglish
Pages (from-to)525-530
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume199
Issue number2
DOIs
Publication statusPublished - 1994

Fingerprint

Lymphokine-Activated Killer Cells
Cytoprotection
Lymphokines
Cell death
Cell Death
Poly(ADP-ribose) Polymerases
Luminol
Niacinamide
Natural Killer Cells
Cytotoxicity
Assays
Biological Phenomena
Cells
K562 Cells
Enzymes
Poly(ADP-ribose) Polymerase Inhibitors
3-aminobenzamide

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Cell death protection by 3-aminobenzamide and other poly(ADP-ribose)polymerase inhibitors : Different effects on human natural killer and lymphokine activated killer cell activities. / Monti, D.; Cossarizza, A.; Salvioli, S.; Franceschi, C.; Rainaldi, G.; Straface, E.; Rivabene, R.; Malorni, W.

In: Biochemical and Biophysical Research Communications, Vol. 199, No. 2, 1994, p. 525-530.

Research output: Contribution to journalArticle

@article{8ff4efdea17f4c2ebfb6c3a6d0a98473,
title = "Cell death protection by 3-aminobenzamide and other poly(ADP-ribose)polymerase inhibitors: Different effects on human natural killer and lymphokine activated killer cell activities",
abstract = "The death of target cells by cytotoxic effector cells is a relevant biological phenomenon, where cells are activated and a very quick apoptotic program occurs. In order to test the hypothesis that the nuclear enzyme poly(ADP-ribose)polymerase (PADPRP) plays a role in such a process, a variety of PADPRP inhibitors such as 3-aminobenzamide, nicotinamide, 4-aminobenzamide and luminol were used. All of them were able to strongly inhibit K562 target cell killing by human effector natural killer cells (NK) in a 4hr 51Cr release assay. PADPRP inhibitors were much less effective in protecting target cells when lymphokine activated killer cells (LAK) were used as effectors. These substances were active only when both target and effector cells were mixed, being ineffective on target or effector cells alone. On the whole, these data indicate that PADPRP is involved in the death of target cells. Moreover, the different sensitivity of NK and LAK activities to PADPRP inhibitors suggests that the molecular mechanisms underlying these two types of cytotoxicity are at least partially different.",
author = "D. Monti and A. Cossarizza and S. Salvioli and C. Franceschi and G. Rainaldi and E. Straface and R. Rivabene and W. Malorni",
year = "1994",
doi = "10.1006/bbrc.1994.1260",
language = "English",
volume = "199",
pages = "525--530",
journal = "Biochemical and Biophysical Research Communications",
issn = "0006-291X",
publisher = "Academic Press Inc.",
number = "2",

}

TY - JOUR

T1 - Cell death protection by 3-aminobenzamide and other poly(ADP-ribose)polymerase inhibitors

T2 - Different effects on human natural killer and lymphokine activated killer cell activities

AU - Monti, D.

AU - Cossarizza, A.

AU - Salvioli, S.

AU - Franceschi, C.

AU - Rainaldi, G.

AU - Straface, E.

AU - Rivabene, R.

AU - Malorni, W.

PY - 1994

Y1 - 1994

N2 - The death of target cells by cytotoxic effector cells is a relevant biological phenomenon, where cells are activated and a very quick apoptotic program occurs. In order to test the hypothesis that the nuclear enzyme poly(ADP-ribose)polymerase (PADPRP) plays a role in such a process, a variety of PADPRP inhibitors such as 3-aminobenzamide, nicotinamide, 4-aminobenzamide and luminol were used. All of them were able to strongly inhibit K562 target cell killing by human effector natural killer cells (NK) in a 4hr 51Cr release assay. PADPRP inhibitors were much less effective in protecting target cells when lymphokine activated killer cells (LAK) were used as effectors. These substances were active only when both target and effector cells were mixed, being ineffective on target or effector cells alone. On the whole, these data indicate that PADPRP is involved in the death of target cells. Moreover, the different sensitivity of NK and LAK activities to PADPRP inhibitors suggests that the molecular mechanisms underlying these two types of cytotoxicity are at least partially different.

AB - The death of target cells by cytotoxic effector cells is a relevant biological phenomenon, where cells are activated and a very quick apoptotic program occurs. In order to test the hypothesis that the nuclear enzyme poly(ADP-ribose)polymerase (PADPRP) plays a role in such a process, a variety of PADPRP inhibitors such as 3-aminobenzamide, nicotinamide, 4-aminobenzamide and luminol were used. All of them were able to strongly inhibit K562 target cell killing by human effector natural killer cells (NK) in a 4hr 51Cr release assay. PADPRP inhibitors were much less effective in protecting target cells when lymphokine activated killer cells (LAK) were used as effectors. These substances were active only when both target and effector cells were mixed, being ineffective on target or effector cells alone. On the whole, these data indicate that PADPRP is involved in the death of target cells. Moreover, the different sensitivity of NK and LAK activities to PADPRP inhibitors suggests that the molecular mechanisms underlying these two types of cytotoxicity are at least partially different.

UR - http://www.scopus.com/inward/record.url?scp=0028214198&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0028214198&partnerID=8YFLogxK

U2 - 10.1006/bbrc.1994.1260

DO - 10.1006/bbrc.1994.1260

M3 - Article

C2 - 8135793

AN - SCOPUS:0028214198

VL - 199

SP - 525

EP - 530

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 2

ER -