M. Kaariainen et al., Integrin and dystrophin associated adhesion protein complexes during regeneration of shearing-type muscle injury, NEUROMUSC D, 10(2), 2000, pp. 121-132
In shearing injury both the myofibres and connective tissue framework are b
reached and the muscle-tendon continuity is disrupted. During regeneration
the firm myofibre to extracellular matrix (ECM) adhesion must be re-establi
shed. We have analysed the expression of selected molecules implementing th
is adhesion in regenerating myofibres 2-56 days after transection of rat so
leus muscle using quantitative immunohistochemistry and Northern blotting.
beta 1 integrin mRNA level and alpha 7 integrin and vinculin immunoreactivi
ties were transiently increased in both the intact and regenerating parts o
f the transected myofibres by day 5-7 with normalization by day 10-14. Afte
r day 14, alpha 7 integrin and vinculin accumulated at the tips of the rege
nerating myofibres, indicating formation of new mini-myotendinous junctions
(mMTJ). Immunoreactivities for dystrophin and associated proteins as well
as merosin appeared in regenerating myotubes by day 3-4 reaching control le
vels by day 56. Our results suggest that integrin and dystrophin associated
molecules are complementary in myofibre-ECM adhesion. During regeneration,
ruptured myofibres temporarily reinforce their integrin mediated lateral a
dhesion until mMTJs are formed. Thereby the load on the newly formed scar a
nd the risk of rerupture are I educed. Dystrophin associated molecules appe
ar later and replace integrin on the lateral aspects, while both complexes
are abundant at the mMTJs. These molecular events correspond to our previou
s results on tensile strength. (C) 2000 Elsevier Science B.V. All lights re
served.