Age-dependent ultrastructural alterations and biochemical response of rat skeletal muscle after hypoxic or hyperoxic treatments.
This work deals with the antioxidant enzymatic response and the ultrastructural aspects of the skeletal muscle of young and aged rats kept under hypoxic or hyperoxic normobaric conditions. It is in fact well known that the supply of oxygen at concentrations higher or lower than those occurring under normal conditions can promote oxidative processes that can cause tissue damage. The enzymes investigated were both those directly involved in reactive oxygen species (ROS) scavenging (superoxide dismutase, catalase and selenium-dependent glutathione peroxidase), and those challenged with the detoxication of cytotoxic compounds produced by the action of ROS on biological molecules (glutathione transferase, glyoxalase I, glutathione reductase), in order to obtain a comparative view of the defence strategies used with respect to aging. Our results support the hypothesis that one of the major contributors to the aging process is the oxidative damage produced at least in part by an impairment of the antioxidant enzymatic system. This makes the aged organism particularly susceptible to oxidative stress injury and to the related degenerative diseases, especially in those tissues with high demand for oxidative metabolism.
Amicarelli
F
F
Dipartimento di Biologia di Base ed Applicata, Università di L'Aquila, Italy. cellular@univaq.it
Ragnelli
A M
AM
Aimola
P
P
Bonfigli
A
A
Colafarina
S
S
Di Ilio
C
C
Miranda
M
M
D000375:Aging / Q000378:metabolism* / Q000473:pathology; D000818:Animals; D002374:Catalase / Q000032:analysis; D005979:Glutathione Peroxidase / Q000032:analysis; D005982:Glutathione Transferase / Q000032:analysis; D018496:Hyperoxia / Q000201:enzymology* / Q000473:pathology; D000860:Hypoxia / Q000201:enzymology* / Q000473:pathology; D007791:Lactoylglutathione Lyase / Q000032:analysis; D008297:Male; D018482:Muscle, Skeletal / Q000201:enzymology* / Q000648:ultrastructure; D051381:Rats; D017208:Rats, Wistar; D013482:Superoxide Dismutase / Q000032:analysis