Hydrogen peroxide and superoxide anion production during acetic acid-induced yeast programmed cell death

2007 ◽  
Vol 52 (3) ◽  
pp. 237-240 ◽  
Author(s):  
N. Guaragnella ◽  
L. Antonacci ◽  
S. Passarella ◽  
E. Marra ◽  
S. Giannattasio
Keyword(s):  
Hydrogen Peroxide ◽  
Cell Death ◽  
Acetic Acid ◽  
Programmed Cell Death ◽  
Superoxide Anion ◽  
Superoxide Anion Production ◽  
Anion Production

Hydrogen Peroxide Modulation of the Superoxide Anion Production by Stimulated Neutrophils

1998 ◽  
Vol 20 (1) ◽  
pp. 103-117 ◽  
Author(s):  
I. Dekaris ◽  
T. Marotti ◽  
R. C. Sprong ◽  
J. F.L. van Oirschot ◽  
B. S. Van Asbeck
Keyword(s):  
Hydrogen Peroxide ◽  
Superoxide Anion ◽  
Superoxide Anion Production ◽  
Anion Production

Lactate and P o 2 Modulate Superoxide Anion Production in Bovine Cardiac Myocytes

Circulation ◽  
1997 ◽  
Vol 96 (2) ◽  
pp. 614-620 ◽  
Author(s):  
Kamal M. Mohazzab-H. ◽  
Pawel M. Kaminski ◽  
Michael S. Wolin
Keyword(s):  
Cardiac Myocytes ◽  
Superoxide Anion ◽  
Superoxide Anion Production ◽  
Anion Production

scholarly journals Translation machinery reprogramming in programmed cell death in Saccharomyces cerevisiae

2021 ◽  
Vol 7 (1) ◽  
Author(s):  
Francesco Monticolo ◽  
Emanuela Palomba ◽  
Maria Luisa Chiusano
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cell Death ◽  
Acetic Acid ◽  
Programmed Cell Death ◽  
Differential Expression ◽  
Ribosomal Proteins ◽  
Relative Proportion ◽  
Duplication Event ◽  
Genome Duplication Event ◽  
Cell Death Pathway

AbstractProgrammed cell death involves complex molecular pathways in both eukaryotes and prokaryotes. In Escherichia coli, the toxin–antitoxin system (TA-system) has been described as a programmed cell death pathway in which mRNA and ribosome organizations are modified, favoring the production of specific death-related proteins, but also of a minor portion of survival proteins, determining the destiny of the cell population. In the eukaryote Saccharomyces cerevisiae, the ribosome was shown to change its stoichiometry in terms of ribosomal protein content during stress response, affecting the relative proportion between ohnologs, i.e., the couple of paralogs derived by a whole genome duplication event. Here, we confirm the differential expression of ribosomal proteins in yeast also during programmed cell death induced by acetic acid, and we highlight that also in this case pairs of ohnologs are involved. We also show that there are different trends in cytosolic and mitochondrial ribosomal proteins gene expression during the process. Moreover, we show that the exposure to acetic acid induces the differential expression of further genes coding for products related to translation processes and to rRNA post-transcriptional maturation, involving mRNA decapping, affecting translation accuracy, and snoRNA synthesis. Our results suggest that the reprogramming of the overall translation apparatus, including the cytosolic ribosome reorganization, are relevant events in yeast programmed cell death induced by acetic acid.

scholarly journals Opsonization of Actinobacillus actinomycetemcomitans by Immunoglobulin G Antibody Reactive with Phosphorylcholine

2002 ◽  
Vol 70 (11) ◽  
pp. 6485-6488 ◽  
Author(s):  
Donald Purkall ◽  
John G. Tew ◽  
Harvey A. Schenkein
Keyword(s):  
Streptococcus Pneumoniae ◽  
Immunoglobulin G ◽  
Oxidative Burst ◽  
Superoxide Anion ◽  
Polymorphonuclear Neutrophils ◽  
Actinobacillus Actinomycetemcomitans ◽  
Superoxide Anion Production ◽  
Protective Antibody ◽  
Anion Production ◽  
Human Sera

ABSTRACT We used two strains of Actinobacillus actinomycetemcomitans, one bearing phosphorylcholine (PC) (strain D045D-40) and one devoid of PC antigens (strain DB03A-42), as well as a nonencapsulated strain of Streptococcus pneumoniae (strain 39937), to examine the opsonic properties of physiological concentrations (⩽30 μg/ml) of purified human anti-PC immunoglobulin G (IgG). Anti-PC bound to both A. actinomycetemcomitans DO45D-40 and S. pneumoniae 39937 and induced superoxide anion production by polymorphonuclear neutrophils; induction of the oxidative burst was inhibited by antibodies to either CD16 or CD32. Thus, anti-PC IgG at concentrations present in most human sera promotes the opsonization of PC-expressing strains of A. actinomycetemcomitans in the absence of complement, implying that anti-PC may be a protective antibody against such strains of bacteria.

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