European Journal of Applied Physiology

, Volume 100, Issue 4, pp 445–455

Calpain/calpastatin activities and substrate depletion patterns during hindlimb unweighting and reweighting in skeletal muscle

Authors

    • School of KinesiologyThe University of Western Ontario
    • Department of Kinesiology & Physical Education, Room 507, Bricker Academic BldgWilfrid Laurier University
  • Truls Raastad
    • Norwegian School of Sport Sciences
  • Ingrid Ugelstad
    • Norwegian School of Sport Sciences
  • Angelo N. Belcastro
    • School of KinesiologyThe University of Western Ontario
Original Article

DOI: 10.1007/s00421-007-0445-4

Cite this article as:
Enns, D.L., Raastad, T., Ugelstad, I. et al. Eur J Appl Physiol (2007) 100: 445. doi:10.1007/s00421-007-0445-4

Abstract

Unloading of skeletal muscle by hindlimb unweighting (HU) is characterized by atrophy, protein loss, and an elevation in intracellular Ca2+ levels that may be sufficient to activate Ca2+-dependent proteases (calpains). In this study, we investigated the time course of calpain activation and the depletion pattern of a specific structural protein (desmin) with unloading and subsequent reweighting. Rats underwent 12 h, 24 h, 72 h or 9 days of HU, followed by reweighting for either 0, 12 or 24 h. Total calpain-like activity was elevated with HU in skeletal muscle (P < 0.05) and was further enhanced with reweighting (P < 0.05). The increases in calpain-like activity were associated with a proportional increase in activity of the particulate fraction (P < 0.05). Activity of the μ-calpain isoform was elevated with 12 and 24 h of HU (P < 0.05) and returned to control levels thereafter. With reweighting, activities of μ-calpain were elevated above control levels for all HU groups except 9 days (P < 0.05). In contrast, minimal changes in m-calpain and calpastatin activity were observed with HU and reweighting. Although desmin depletion levels did not reach statistical significance, a significant inverse relationship was found between the μ-calpain/calpastatin ratio and the amount of desmin in isolated myofibrils (R = −0.83, P < 0.001). The results suggest that calpain activation is an early event during unloading in skeletal muscle, and that the majority of the increase in calpain activity can be attributed to the μ-isoform.

Keywords

ProteaseAtrophyHindlimb suspensionSkeletal muscle

Copyright information

© Springer-Verlag 2007