ArticleHistochemistry and cell biology2012
Fine-structural distribution of MMP-2 and MMP-9 activities in the rat skeletal muscle upon training: a study by high-resolution in situ zymography.
Article in Histochemistry and cell biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 33 citations in OpenAlex.
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- Antiatherogenic and plaque stabilizing effects of saffron ethanolic extract in atherosclerotic rabbits.BMC complementary medicine and therapies · 2025Article
- Effects of stretching on the basement membrane structure in the soleus muscle of Wistar rats.Medical molecular morphology · 2023Article
- RhoA within myofibers controls satellite cell microenvironment to allow hypertrophic growth.iScience · 2022Article
- Unravelling the Network of Nuclear Matrix Metalloproteinases for Targeted Drug Design.Biology · 2020Review
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- Fusion-Independent Satellite Cell Communication to Muscle Fibers During Load-Induced Hypertrophy.Function (Oxford, England) · 2020Article
- Paralogues of Mmp11 and Timp4 Interact during the Development of the Myotendinous Junction in the Zebrafish Embryo.Journal of developmental biology · 2019Article
- Intracellular Localization in Zebrafish Muscle and Conserved Sequence Features Suggest Roles for Gelatinase A Moonlighting in Sarcomere Maintenance.Biomedicines · 2019Article
- Doxycycline improves cage activity, but not exercised, supraspinatus tendon and muscle in a rat model.Journal of biomechanics · 2018Article
- Cathepsin K activity controls cardiotoxin-induced skeletal muscle repair in mice.Journal of cachexia, sarcopenia and muscle · 2018Article
- Nuclear matrix metalloproteinases: functions resemble the evolution from the intracellular to the extracellular compartment.Cell death discovery · 2017Review
- The Histochemistry and Cell Biology omnium-gatherum: the year 2015 in review.Histochemistry and cell biology · 2016Review
- Skeletal muscle as a therapeutic target for delaying type 1 diabetic complications.World journal of diabetes · 2015Review
- The expression and function of gelatinolytic activity at the rat neuromuscular junction upon physical exercise.Histochemistry and cell biology · 2015Article
- Effect of exercise training of different intensities on anti-inflammatory reaction in streptozotocin-induced diabetic rats.Biology of sport · 2014Article
- Article
- Dysregulation of matricellular proteins is an early signature of pathology in laminin-deficient muscular dystrophy.Skeletal muscle · 2014Article
- Matrix metalloproteinase-9 involvement in the structural plasticity of dendritic spines.Frontiers in neuroanatomy · 2014Review
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Matrix metalloproteinases (MMPs) are key regulators of extracellular matrix remodeling, but have also important intracellular targets. The purpose of this study was to examine the activity and subcellular localization of the gelatinases MMP-2 and MMP-9 in skeletal muscle of control and physically trained rats. In control hind limb muscle, the activity of the gelatinases was barely detectable. In contrast, after 5 days of intense exercise, in Soleus (Sol), but not Extensor digitorum longus (EDL) muscle, significant upregulation of gelatinolytic activity in myofibers was observed mainly in the nuclei, as assessed by high resolution in situ zymography. The nuclei of quiescent satellite cells did not contain the activity. Within the myonuclei, the gelatinolytic activity colocalized with an activated RNA Polymerase II. Also in Sol, but not in EDL, there were few foci of mononuclear cells with strongly positive cytoplasm, associated with apparent necrotic myofibers. These cells were identified as activated satellite cells/myoblasts. No extracellular gelatinase activity was observed. Gel zymography combined with subcellular fractionation revealed training-related upregulation of active MMP-2 in the nuclear fraction, and increase of active MMP-9 in the cytoplasmic fraction of Sol. Using RT-PCR, selective increase in MMP-9 mRNA was observed. We conclude that training activates nuclear MMP-2, and increases expression and activity of cytoplasmic MMP-9 in Sol, but not in EDL. Our results suggest that the gelatinases are involved in muscle adaptation to training, and that MMP-2 may play a novel role in myonuclear functions.
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