Immunocytochemical studies of aquaporin 4 in the skeletal muscle of mdx mouse

Liu, Jian Wu; Wakayama, Yoshihiro; Inoue, Masahiko; Shibuya, Seiji; Kojima, Hiroko; Jimi, Takahiro; Oniki, Hiroaki

doi:10.1016/s0022-510x(99)00051-9

Cited by 43 publications

(32 citation statements)

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“…AQP4 has been reported to be present in skeletal muscle tissue preferentially in type 2 fibers [Frigeri et al, 1998;Liu et al, 1999]. Subsequently, other AQP molecules, including AQP3 [Wakayama et al, 2002] and AQP7 [Wakayama et al, 2004], have been reported to be present in skeletal muscle tissue.…”

Section: Discussionmentioning

confidence: 99%

“…We have been interested in the expression and localization of AQPs in skel-182 etal myofibers. AQP3, AQP4 and AQP7 have been found to be expressed in the mature skeletal myofibers [Wakayama et al, 1990;Frigeri et al, 1998;Liu et al, 1999;Wakayama et al, 2002Wakayama et al, , 2004. With regard to AQP1 mRNA expression in the heart, Bondy et al [1993] reported that AQP1 mRNA was observed in the fetal rat heart from embryonic (E) day 14 to E16 and was greatly decreased after birth, although it was still diffusely detectable throughout the myocardium and endocardium.…”

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confidence: 99%

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Aquaporin 1: Examination of Its Expression and Localization in Normal Human Skeletal Muscle Tissue

Jimi

Wakayama²,

Inoue³

et al. 2006

Cells Tissues Organs

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To examine aquaporin 1 (AQP1) expression in skeletal muscle tissue precisely, we performed reverse transcription-polymerase chain reaction (RT-PCR) at RNA level and immunoblot analysis, immunohistochemistry and immunoelectron microscopy at protein level. The RT-PCR study of total RNA from normal human skeletal muscle showed a strong single band of AQP1. At the protein level we used two commercially available antibodies, both of which recognize the cytoplasmic domain of the AQP1 molecule. One antibody gave positive results. Immunoblot of muscle extract showed a 30-kDa band protein, the molecular weight of which corresponded to that of AQP1. Immunohistochemically, AQP1 was immunostained at the myofiber surface both in type 1 and type 2 myofibers with almost the same intensity, and its staining pattern was rather diffuse and irregular compared with that of the anti-dystrophin antibody. The endomysial endothelial cells were also immunolabeled. Immunoelectron microscopy revealed that the immunogold particles indicating the presence of the AQP1 molecule were present along the inside surface of the muscle plasma membrane. However, another antibody showed negative results except for the endomysial endothelial cells which were positively stained. We drew the conclusion that AQP1 is expressed at the endomysial capillary endothelial cell and further AQP1 may be expressed at the human skeletal myofiber plasma membrane.

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Section: Discussionmentioning

confidence: 99%

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confidence: 99%

Aquaporin 1: Examination of Its Expression and Localization in Normal Human Skeletal Muscle Tissue

Jimi

Wakayama²,

Inoue³

et al. 2006

Cells Tissues Organs

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“…Thus the concentration of AQP4 in adluminal endfoot membranes must depend on specific anchoring mechanisms. The first clue that the DAPC could be involved came with studies of mdx mice (44,90,202). These mice, which are deficient in dystrophin, showed reduced levels of AQP4 in skeletal muscles.…”

Section: Polarized Distributionmentioning

confidence: 99%

Physiological Roles of Aquaporin-4 in Brain

Nagelhus

Ottersen

2013

Physiological Reviews

596

520

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(AQP4) is one of the most abundant molecules in the brain and is particularly prevalent in astrocytic membranes at the blood-brain and brain-liquor interfaces. While AQP4 has been implicated in a number of pathophysiological processes, its role in brain physiology has remained elusive. Only recently has evidence accumulated to suggest that AQP4 is involved in such diverse functions as regulation of extracellular space volume, potassium buffering, cerebrospinal fluid circulation, interstitial fluid resorption, waste clearance, neuroinflammation, osmosensation, cell migration, and Ca 2ϩ signaling. AQP4 is also required for normal function of the retina, inner ear, and olfactory system. A review will be provided of the physiological roles of AQP4 in brain and of the growing list of data that emphasize the polarized nature of astrocytes.

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“…In addition, recent studies (1)(2)(3)(4)(5)(6)(7) have shown that the dystrophin complex is critical for the localization of a variety of signaling molecules to the skeletal muscle sarcolemma. Thus, the dystrophin complex functions as both a structural link to the extracellular matrix and as a scaffold that concentrates and stabilizes functionally inter-related signaling proteins at the muscle cell membrane.…”

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DAMAGE, a Novel α-Dystrobrevin-associated MAGE Protein in Dystrophin Complexes

Albrecht

Froehner

2004

Journal of Biological Chemistry

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Mice rendered null for ␣-dystrobrevin, a component of the dystrophin complex, have muscular dystrophy, despite the fact that the sarcolemma remains relatively intact (Grady, R. M., Grange, R. W., Lau, K. S., Maimone, M. M., Nichol, M. C., Stull, J. T., and Sanes, J. R. (1999) Nat. Cell Biol. 1, 215-220) Thus, ␣-dystrobrevin may serve a signaling function that is important for the maintenance of muscle integrity. We have identified a new dystrobrevin-associated protein, DAMAGE, that may play a signaling role in brain, muscle, and peripheral nerve. In humans, DAMAGE is encoded by an intronless gene located at chromosome Xq13.1, a locus that contains genes involved in mental retardation. DAM-AGE associates directly with ␣-dystrobrevin, as shown by yeast two-hybrid, and co-immunoprecipitates with the dystrobrevin-syntrophin complex from brain. This co-immunoprecipitation is dependent on the presence of ␣-dystrobrevin but not ␤-dystrobrevin. The DAMAGE protein contains a potential nuclear localization signal, 30 12-amino acid repeats, and two MAGE homology domains. The domain structure of DAMAGE is similar to that of NRAGE, a MAGE protein that mediates p75 neurotrophin receptor signaling and neuronal apoptosis (Salehi, A. H., Roux, P. P., Kubu, C. J., Zeindler, C., Bhakar, A., Tannis, L. L., Verdi, J. M., and Barker, P. A. (2000) Neuron 27, 279 -288). DAMAGE is highly expressed in brain and is present in the cell bodies and dendrites of hippocampal and Purkinje neurons. In skeletal muscle, DAMAGE is at the postsynaptic membrane and is associated with a subset of myonuclei. DAMAGE is also expressed in peripheral nerve, where it localizes along with other members of the dystrophin complex to the perineurium and myelin. These results expand the role of dystrobrevin and the dystrophin complex in membrane signaling and disease.The dystrophin glycoprotein complex links the actin cytoskeleton to the extracellular matrix in skeletal muscle. In addition, recent studies (1-7) have shown that the dystrophin complex is critical for the localization of a variety of signaling molecules to the skeletal muscle sarcolemma. Thus, the dystrophin complex functions as both a structural link to the extracellular matrix and as a scaffold that concentrates and stabilizes functionally inter-related signaling proteins at the muscle cell membrane.Part of the signaling function of the dystrophin complex may be mediated by the dystrobrevins. The role of the dystrobrevins in signaling is not fully understood; however, targeted disruption of the ␣-dystrobrevin gene in mice results in muscle pathology without the membrane fragility characteristic of dystrophin-deficient muscular dystrophy (8). These findings suggest that ␣-dystrobrevin is important for muscle function but in a non-structural way. Dystrobrevin has no enzymatic activity of its own; therefore, the involvement of dystrobrevin in signaling pathways is dependent on its interaction with other proteins.The dystrobrevins are transcribed from two separate genes, designated ␣ and ␤, that shar...

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Immunocytochemical studies of aquaporin 4 in the skeletal muscle of mdx mouse

Cited by 43 publications

References 29 publications

Aquaporin 1: Examination of Its Expression and Localization in Normal Human Skeletal Muscle Tissue

Aquaporin 1: Examination of Its Expression and Localization in Normal Human Skeletal Muscle Tissue

Physiological Roles of Aquaporin-4 in Brain

DAMAGE, a Novel α-Dystrobrevin-associated MAGE Protein in Dystrophin Complexes

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