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All relevant data are within the paper and its Supporting Information files. Introduction {#sec001} ============ Trabecular meshwork induced glucocorticoid response protein (TIGR) was identified almost 20 years ago by two independent groups \[[@pone.0206801.ref001], [@pone.0206801.ref002]\] desiring to understand genes upregulated following dexamethasone treatment, since steroid-induced glaucoma constitutes a major subset of glaucoma patients. At the time, Northern blots suggested high expression of TIGR in the eye as well as expression in skeletal muscle and heart \[[@pone.0206801.ref003]--[@pone.0206801.ref005]\]. Given the tissue distribution and considering that the N-terminal of the protein shares approximately 25% identity with myosin, *TIGR* was later renamed myocilin (*MYOC*). To date, *MYOC* is the gene with mutations most strongly-linked to glaucoma and is reported in approximately one-third of all juvenile open angle glaucoma (JOAG) patients \[[@pone.0206801.ref006]\] and up to 4% of all primary open angle glaucoma (POAG) cases \[[@pone.0206801.ref007], [@pone.0206801.ref008]\]. More than 70 pathological MYOC mutations have been reported and most are found in the C-terminal of the protein (refer to [http://www.myocilin.com](http://www.myocilin.com/)). The C-terminal of MYOC contains an olfactomedin (OLF) domain and shares 40% identity with the nearest OLF family member. Similar to most OLF family members, myocilin is a secreted protein, but MYOC with C-terminal pathological mutations are not secreted *in vitro* \[[@pone.0206801.ref009]\]. Despite intense study (for review see \[[@pone.0206801.ref010]\]), it is unknown definitively how mutant MYOC causes glaucoma and the function of wild-type (wt) MYOC has remained elusive. Several mouse models over-expressing wt MYOC or MYOC mutant proteins have been established to study intraocular pressure (IOP) and glaucoma disease development \[[@pone.0206801.ref011]--[@pone.0206801.ref014]\]. Although the eye and glaucoma have been the primary focus when studying pathological MYOC mutations, there is interest in knowing if *MYOC* mutations result in pathology in other tissues. Patients with POAG and a mutation in the *MYOC* gene have been reported to be phenotypically similar to other POAG patients without a *MYOC* mutation \[[@pone.0206801.ref015]\]. In 2002, Tamm stated that it was remarkable that patients with pathological *MYOC* mutations were at high-risk for glaucoma, but apparently had no other disease \[[@pone.0206801.ref010]\]. Could this be an area that has been overlooked? As such, studying MYOC in other tissues could provide missing insight into MYOC biology. Additionally, knowledge gained by studying myocilin in other tissues may assist physicians in early identification of patients suspected to carry a pathologic *MYOC* mutation. Myocilin transcripts are high in muscle \[[@pone.0206801.ref003]--[@pone.0206801.ref005]\] and a BAC transgenic mouse with 15-fold over-expression of wt mouse MYOC protein was reported to have skeletal muscle hypertrophy with an approximate 40% increase in gastrocnemius muscle weight \[[@pone.0206801.ref016]\]. Thus, it is possible that MYOC is impacting cells in tissues other than those of the eye. Our present study is the first to examine the impact of over-expressing MYOC with a pathologic mutation in skeletal muscle. We utilized a transgenic mouse with CMV-driven expression of cDNA encoding for the human MYOC Y437H mutant protein \[[@pone.0206801.ref014]\], which in humans is a severe *MYOC* mutation associated with JOAG \[[@pone.0206801.ref007], [@pone.0206801.ref017]\]. In the skeletal (gastrocnemius) muscle of these transgenic mice, we did not observe