Publication: Matrix metalloproteinase
imbalance in muscle disuse atrophy
Authors
Giannelli, G. ; De Marzo, A. ; Marinosci, F. ; Antonaci, S.
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Publisher
Murcia : F. Hernández
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DOI
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info:eu-repo/semantics/article
Description
Abstract
Muscle atrophy commonly occurs as a
consequence of prolonged muscle inactivity, as observed
after cast immobilization, bed rest or space flights. The
molecular mechanisms responsible for muscle atrophy
are still unknown, but a role has been proposed for
altered permeability of the sarcolemma and of the
surrounding connective tissue. Matrix metalloproteinases
(MMPs) are a family of enzymes with
proteolytic activity toward a number of extracellular
matrix (ECM) components; they are inhibited by tissue
inhibitors of MMPs (TIMPs). In a rat tail-suspension
experimental model, we show that after fourteen days of
non-weight bearing there is increased expression of
MMP-2 in the atrophic soleus and gastrocnemius and
decreased expression of TIMP-2. In the same
experimental model the expression of Collagen I and
Collagen IV, two main ECM components present in the
muscles, was reduced and unevenly distributed in
unloaded animals. The difference was more evident in
the soleus than in the gastrocnemius muscle. This
suggests that muscle disuse induces a proteolytic
imbalance, which could be responsible for the
breakdown of basal lamina structures such as Collagen I
and Collagen IV, and that this leads to an altered
permeability with consequent atrophy. In conclusion, an
MMP-2/TIMP-2 imbalance could have a role in the
mechanism underlying muscle disuse atrophy; more
studies are needed to expand our molecular knowledge
on this issue and to explore the possibility of targeting
the proteolytic imbalance with MMP inhibitors.
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