Aging but not dietary restriction alters the activation-induced apoptosis in rat T cells.
The aim of this study was to determine if aging or dietary restriction (DR) alters activation-induced cell death, which is known to regulate cell proliferation and eliminate the high number of activated cells during an immune response. Splenic T cells were isolated from young (4-6 months) and old (25-26 months) Fischer 344 rats that had free access to food, ad libitum (AL), and from dietary-restricted (DR) old (25-26 months) rats that beginning at 6 weeks of age were fed 60% (40% food-restricted) of the diet consume by the AL rats. T cells were incubated with anti-CD3 antibody, or staphylococcal enterotoxin B (primary stimulus) for 72-96 h, followed by restimulation with anti-CD3 (secondary stimulus) for 72 h. Activation-induced apoptosis was assessed by DNA fragmentation and the expression of Fas/CD95 receptor and Fas ligand (Fas-L) was measured by flow cytometry. We found that the amount of DNA fragmentation was significantly (P<0.05) higher in the stimulated and restimulated T cells from AL old rats and DR old rats compared to young rats. The increase in DNA fragmentation with age was paralleled by an increase in the proportion of the cells expressing Fas and Fas-L. However, DR had no significant effect on the age-related increase in DNA fragmentation or the expression of Fas or Fas-L. We also measured the levels of Bcl-2 and Bax protein and found that the level of Bcl-2 decreased and Bax increased with age and that DR had no effect on the age-related changes in the level of Bcl-2 or Bax protein. These results demonstrate that aging but not DR alters activation-induced apoptosis in rat T cells.
Geriatric Research, Education, and Clinical Center (182), South Texas Veterans Health Care System, Audie L. Murphy Veterans Hospital, San Antonio, TX 78284, USA. pahlavani@uthscsa.edu
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Vargas
D000375:Aging / Q000502:physiology*; D000818:Animals; D000954:Antigens, Surface / Q000096:biosynthesis / Q000378:metabolism; D017209:Apoptosis; D015153:Blotting, Western; D017252:CD3 Complex / Q000494:pharmacology; D002455:Cell Division; D053938:DNA Fragmentation; D004032:Diet; D004768:Enterotoxins / Q000494:pharmacology; D053222:Fas Ligand Protein; D005434:Flow Cytometry; D008297:Male; D008562:Membrane Glycoproteins / Q000096:biosynthesis / Q000378:metabolism; D011518:Proto-Oncogene Proteins / Q000096:biosynthesis / Q000378:metabolism; D019253:Proto-Oncogene Proteins c-bcl-2 / Q000096:biosynthesis / Q000378:metabolism; D051381:Rats; D011916:Rats, Inbred F344; D018089:Superantigens / Q000494:pharmacology; D013601:T-Lymphocytes / Q000502:physiology*; D051028:bcl-2-Associated X Protein; D019014:fas Receptor / Q000096:biosynthesis / Q000378:metabolism
D000954:Antigens, Surface; C494828:Bax protein, rat; D017252:CD3 Complex; D004768:Enterotoxins; D053222:Fas Ligand Protein; C505662:Faslg protein, rat; D008562:Membrane Glycoproteins; D011518:Proto-Oncogene Proteins; D019253:Proto-Oncogene Proteins c-bcl-2; D018089:Superantigens; D051028:bcl-2-Associated X Protein; D019014:fas Receptor; C031818:enterotoxin B, staphylococcal