Stretch-induced enhancement of active force (stretch activation, SA) is observed in striated muscles in general, and most conspicuously in insect flight muscle (IFM). It remains unclear whether a common mechanism underlies the SA of all-muscle types, or the SA of IFM relies on its highly specialized features. Recent studies suggest that IFM-specific isoforms of thin filament regulatory proteins (troponin and tropomyosin) are implicated in SA. Among others, IFM-specific troponin-I (troponin-H or TnH), with an unusually long Pro-Ala-rich extension at the C-terminus, has been speculated to transmit the mechanical signal of stretch to the troponin complex. To verify this hypothesis, it was removed by a specific endoproteinase in bumblebee IFM, expecting that it would eliminate SA while leaving intact the capacity for Ca2+-activated isometric force. Electrophoretic data showed that the extension was almost completely (97%) removed from IFM fibers after treatment. Unexpectedly, SA force was still conspicuous, and its rate of rise was not affected. Therefore, the results preclude the possibility that the extension is a main part of the mechanism of SA. This leaves open the possibility that SAs of IFM and vertebrate striated muscles, which lack the extension, operate under common basic mechanisms. (C) 2012 Elsevier Inc. All rights reserved.