Matrix metalloproteinase-9 deficiency results in decreased fiber cross-sectional area and alters fiber type distribution in mouse hindlimb skeletal muscle.
Matrix metalloproteinase-9 deficiency results in decreased fiber cross-sectional area and alters fiber type distribution in mouse hindlimb skeletal muscle.
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基质金属蛋白酶-9 缺乏导致纤维横截面积减少，并改变小鼠后肢骨骼肌的纤维类型分布。
DOI：
10.1159/000323654
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发表时间：
2011
期刊：
影响因子：
--
通讯作者：
Allen,DavidL
中科院分区：
文献类型：
--
作者：
Mehan,RyanS;Greybeck,BradleyJ;Emmons,Kayla;Byrnes,WilliamC;Allen,DavidL
基质金属蛋白酶（MMPs）在骨骼肌细胞外基质（ECM）的降解中起主要作用，特别是诱导型明胶酶MMP-9似乎对骨骼肌ECM在生长和修复过程中的重塑至关重要。在这里，我们确定了MMP-9基因失活对雌性小鼠胫骨前肌（TA），腓肠肌（GAST）和比目鱼肌（SOL）肌肉纤维类型和大小的影响。在TA中，肌球蛋白重链（MyHC）IIb表达纤维的横截面积（CSA）在MMP-9基因敲除小鼠中显著较小，而在GAST中，所有三种快速纤维类型的CSA均降低。在SOL中，表达MyHC I型的纤维在MMP-9缺失小鼠中显著较小。MyHC IIb型表达纤维的百分比在MMP-9 null小鼠的TA和GAST中显著增加，而MyHC IId表达纤维的百分比在MMP-9 null小鼠的GAST中显著降低。SOL中的纤维百分比在两个系之间没有显著差异。尽管这些变化的纤维大小和类型，在体内后肢力的生产没有改变MMP-9裸小鼠。同时，无论是组成型明胶酶MMP-2的表达，也没有IV型胶原的免疫组化染色显着改变MMP-9失活在任何肌肉检查。目前的研究表明，MMP-9失活导致成年小鼠后肢肌肉中纤维大小和类型的变化，这可能取决于间接机制，涉及减少骨生长或神经变化，以响应MMP-9失活。
Matrix metalloproteinases (MMPs) play a major role in the degradation of the extracellular matrix (ECM) of skeletal muscle, and the inducible gelatinase MMP-9 in particular appears to be critical for the remodeling of muscle ECM during growth and repair. Here we determined the effects of MMP-9 gene inactivation on fiber type and size in the tibialis anterior (TA), gastrocnemius (GAST), and soleus (SOL) muscles in female mice. In the TA, the cross-sectional area (CSA) of the myosin heavy chain (MyHC) IIb-expressing fibers was significantly smaller in MMP-9 null mice while in the GAST, CSA of all three fast fiber types was decreased. In the SOL, MyHC type I-expressing fibers were significantly smaller in the MMP-9 null mice. The percentage of MyHC type IIb-expressing fibers was significantly increased in the TA and GAST of MMP-9 null mice, while the percentage of MyHC IId-expressing fibers significantly decreased in the GAST of MMP-9 null mice. Fiber percentages in the SOL were not significantly different between the two lines. Despite these changes in fiber size and type, in vivo hindlimb force production was not changed in MMP-9 null mice. Meanwhile, neither expression of the constitutive gelatinase MMP-2 nor immunohistochemical staining for type IV collagen was significantly altered by MMP-9 inactivation in any muscles examined. The present study demonstrates that MMP-9 inactivation results in changes in fiber size and type in adult mouse hindlimb muscles that may depend on indirect mechanisms involving reduced bone growth or nerve changes in response to MMP-9 inactivation.
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