ArticlePloS one2011
Absence of aquaporin-4 in skeletal muscle alters proteins involved in bioenergetic pathways and calcium handling.
Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 25 citations in OpenAlex.
- Repeated heat exposure upregulates skeletal muscle aquaporin-4 expression in male mice.Physiological reports · 2026Article
- Article
- Aquaporin 4 Expression Level Is Decreased in Skeletal Muscles with Aging.The Kobe journal of medical sciences · 2023Article
- Assessing the Role of Aquaporin 4 in Skeletal Muscle Function.International journal of molecular sciences · 2023Review
- Aquaporins in Nervous System.Advances in experimental medicine and biology · 2023Article
- Corticospinal and peripheral responses to heat-induced hypo-hydration: potential physiological mechanisms and implications for neuromuscular function.European journal of applied physiology · 2022Review
- Signaling Mechanisms and Pharmacological Modulators Governing Diverse Aquaporin Functions in Human Health and Disease.International journal of molecular sciences · 2022Review
- Atrogin1-induced loss of aquaporin 4 in myocytes leads to skeletal muscle atrophy.Scientific reports · 2020Article
- Dysregulation of external globus pallidus-subthalamic nucleus network dynamics in parkinsonian mice during cortical slow-wave activity and activation.The Journal of physiology · 2020Article
- The expression of aquaporin-4 is regulated based on innervation in skeletal muscles.Journal of muscle research and cell motility · 2018Article
- Proteomic analysis reveals an impaired CaScientific reports · 2017Article
- Marked decrease of aquaporin-4 protein is independent of the changes in α1-syntrophin and TRPV4 levels in response to denervation-induced muscle atrophy in vivo.Journal of muscle research and cell motility · 2017Article
- Aquaporin-4 Protein Is Stably Maintained in the Hypertrophied Muscles by Functional Overload.Acta histochemica et cytochemica · 2016Article
- Systems analysis of transcriptional data provides insights into muscle's biological response to botulinum toxin.Muscle & nerve · 2014Article
- Aquaporin-4 knockout exacerbates corticosterone-induced depression by inhibiting astrocyte function and hippocampal neurogenesis.CNS neuroscience & therapeutics · 2014Article
- RETRACTED: AQP4-dependent water transport plays a functional role in exercise-induced skeletal muscle adaptations.PloS one · 2013Article
- Aquaporin-4 expression in distal myopathy with rimmed vacuoles.BMC neurology · 2012Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Aquaporin-4 (AQP4) is a water channel expressed at the sarcolemma of fast-twitch skeletal muscle fibers, whose expression is altered in several forms of muscular dystrophies. However, little is known concerning the physiological role of AQP4 in skeletal muscle and its functional and structural interaction with skeletal muscle proteome. Using AQP4-null mice, we analyzed the effect of the absence of AQP4 on the morphology and protein composition of sarcolemma as well as on the whole skeletal muscle proteome. Immunofluorescence analysis showed that the absence of AQP4 did not perturb the expression and cellular localization of the dystrophin-glycoprotein complex proteins, aside from those belonging to the extracellular matrix, and no alteration was found in sarcolemma integrity by dye extravasation assay. With the use of a 2DE-approach (BN/SDS-PAGE), protein maps revealed that in quadriceps, out of 300 Coomassie-blue detected and matched spots, 19 proteins exhibited changed expression in AQP4(-/-) compared to WT mice. In particular, comparison of the protein profiles revealed 12 up- and 7 down-regulated protein spots in AQP4-/- muscle. Protein identification by MS revealed that the perturbed expression pattern belongs to proteins involved in energy metabolism (i.e. GAPDH, creatine kinase), as well as in Ca(2+) handling (i.e. parvalbumin, SERCA1). Western blot analysis, performed on some significantly changed proteins, validated the 2D results. Together these findings suggest AQP4 as a novel determinant in the regulation of skeletal muscle metabolism and better define the role of this water channel in skeletal muscle physiology.
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