Id2 expression during apoptosis and satellite cell activation in unloaded and loaded quail skeletal muscles

Abstract

Inhibitor of differentiation-2 (Id2) is a basic helix-loop-helix protein that acts as a negative regulator of the myogenic regulatory transcription factor family, but Id2 has also been implicated in apoptosis in several cell lines. In this study, we tested the hypothesis that Id2 has a role in both apoptosis-associated muscle atrophy and muscle hypertrophy. A weight corresponding to 12% of the body weight was attached to one wing of Japanese quail to induce hypertrophy in the patagialis (PAT) muscle. Birds in group 1 were killed after 5 (n = 8), 7 (n = 10), or 14 days (n = 10) of loading. The left wing was loaded for 14 days in group 2 birds, and then the weight was removed and the PAT was examined after 7 (n = 10), 14 (n = 10), or 21 (n = 5) days of unloading. A time-released bromodeoxyuridine (BrdU) pellet was implanted subcutaneously with wing weighting to identify activated satellite cells during loading. The left wing was loaded for 14 days, unloaded for 14 days, and then the weight was reattached for a subsequent 7 (n = 10) or 14 days (n = 10) in group 3 birds. BrdU was implanted on the second loading phase in this group. Id2 mRNA as measured by kinetic PCR increased by 3.9-, 2.7-, and 1.6-fold, relative to control levels after 7, 14, and 21 days of unloading (group 2). Id2 protein as estimated by Western blots increased by 1.5-, 1.4-, and 0.75-fold after 7, 14, and 21 days of unloading (group 2). Muscle unloading induced apoptosis, because poly(ADP-ribose) polymerase-(PARP)-positive nuclei increased and caspase 8 levels increased by 2.6- and 1.7-fold after 7 or 14 days of unloading, respectively (group 2). Although BrdU-positive nuclei increased during loading (groups 1 and 3), 50% failed to survive during unloading (group 2). Id2 mRNA increased by 2.2- and 1.8-fold after 5 and 7 days of loading, respectively, but decreased to control levels by 14 days of loading in group 1. Id2 protein levels increased 2.1-fold after 5 days of loading (group 1). In contrast, Id2 did not increase in reloaded muscles of group 3 birds. These data suggest that Id2 may have a role in apoptosis-associated atrophy of skeletal muscles, but its role in muscle hypertrophy is less clear.

Myostatin inactivation induces a similar muscle molecular signature in double-muscled cattle as in mice

“…Daxx also interacts with the Fas receptor and potentiates its pro-apoptotic action (Yang et al, 1997). The Inhibitor of differentiation-2 (Id2) has been associated with apoptosis-associated atrophy of skeletal muscles (Alway et al, 2003). Conversely, the abundance of anti-apoptotic factors was increased in DM muscles.…”

Muscle memory and a new cellular model for muscle atrophy and hypertrophy

“…Adhihetty et al, 2007;Allen et al, 1997;Alway et al, 2003b;Meneses et al, 2014;Tews et al, 1997;Yoshimura and Harii, 1999). However, with such a technique it is difficult to distinguish between nuclei of different cell types, in particular satellite cells, which are located under the basal lamina of the muscle fibres.…”

Prevention of muscle wasting and osteoporosis: the value of examining novel animal models

“…Maximal caspase-3 and apoptosis-inducing factor expression was found in the soleus muscle of mice after 12 and 24 h of hindlimb suspension, respectively, which coincided with the highest levels of apoptotic DNA fragmentation (Ferreira et al, 2008). Further evidence that apoptosis is involved in the progression of muscle disuse atrophy arises from unilateral limb immobilisation studies in rats, mice and rabbits (Smith et al, 2000;Vazeille et al, 2008;Zhu et al, 2013), and a bird muscle loading/unloading model (Alway et al, 2003) (Table 3).…”