Interacting proteins: P29475 and Q13424 |
Pubmed |
SVM Score :0.73380271 |
An NH 2 terminal domain of nNOS directly interacts with alpha 1 syntrophin but not with other proteins in the dystrophin complex analyzed . 0.73380271^^^ |
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Interacting proteins: P29475 and Q13424 |
Pubmed |
SVM Score :0.76485542 |
Neuronal nitric oxide synthase ( nNOS ) has been shown previously to interact with alpha 1 syntrophin in the dystrophin complex of skeletal muscle . 0.76485542^^^ |
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Interacting proteins: P29475 and Q13424 |
Pubmed |
SVM Score :0.56999218 |
Neuronal nitric oxide synthase ( nNOS ) has a PSD 95 / Dlg / ZO 1 ( PDZ ) domain that can interact with multiple proteins . nNOS has been known to interact with PSD 95 and a related protein , PSD 93 , in brain and with alpha 1 syntrophin in skeletal muscle in mammals . 0.56999218^^^ |
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Interacting proteins: P29475 and Q13424 |
Pubmed |
SVM Score :0.58651 |
The results indicate that the C terminal extension peptide of the nNOS PDZ domain may represent a relatively independent structural unit in the mediation of the interaction between nNOS and PDZ domain containing proteins including PSD 95 and alpha 1 syntrophin . . 0.58651^^^ |
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Interacting proteins: P29475 and Q13424 |
Pubmed |
SVM Score :0.0 |
Similarly , in dystrophin deficient skeletal muscles from mdx mice both soluble and particulate nNOS was greatly reduced compared with C 57 control mice . nNOS mRNA was also reduced in mdx muscle in contrast to mRNA levels for a dystrophin binding protein , alpha 1 syntrophin . nNOS levels increased dramatically from 2 to 52 weeks of age in C 57 skeletal muscle , which may indicate a physiological role for NO in aging related processes . ^^^ |
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Interacting proteins: P29475 and Q13424 |
Pubmed |
SVM Score :0.0 |
We investigated the ultrastructural localization of alpha 1 syntrophin and neuronal nitric oxide synthase ( nNOS ) in normal human skeletal myofibers and analyzed their relation to each other and to dystrophin using single and double immunogold labeling electron microscopy . ^^^ Single immunolabeling showed antibodies to alpha 1 syntrophin and nNOS on the inner surface of the muscle plasma membrane , the sarcoplasmic side of plasma membrane invaginations , and the sarcoplasm near mitochondria of subsarcolemmal areas . ^^^ The epitopes of alpha 1 syntrophin and nNOS tended to be present in clusters . ^^^ Double immunolabeling revealed that epitope combinations of alpha 1 syntrophin dystrophin , alpha 1 syntrophin nNOS , and nNOS dystrophin occurred more frequently in doublet form than did other epitope combinations , such as alpha 1 syntrophin beta spectrin and nNOS beta spectrin . ^^^ Furthermore , nNOS formed doublets significantly more frequently with dystrophin ( 25 . 2 + / 3 . 3 % ) and alpha 1 syntrophin ( 26 . 0 + / 4 . 1 % ) than with beta spectrin ( 13 . 9 + / 2 . 3 % ; P < 0 . 05 ) . ^^^ |
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Interacting proteins: P29475 and Q13424 |
Pubmed |
SVM Score :0.0 |
Several studies have recently shown that the neuronal isoform of nitric oxide synthase ( nNOS ) is also located at the sarcolemma , and that this membrane localization is mediated through interactions of nNOS with one of the DAPs , namely alpha 1 syntrophin . ^^^ |
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Interacting proteins: P29475 and Q13424 |
Pubmed |
SVM Score :0.0 |
All three syntrophin isoforms have a PDZ domain that appears to participate in protein protein interactions at the plasma membrane . alpha 1 Syntrophin has additionally been shown to associate with neuronal nitric oxide synthase ( nNOS ) through PDZ domains in vitro . ^^^ These observations suggest that alpha 1 syntrophin may work as a modular adaptor protein that can link nNOS or other signaling enzyme to the sarcolemmal dystrophin complex . ^^^ In this study , we generated alpha 1 syntrophin knock out mice to clarify the interaction between alpha 1 syntrophin and nNOS in the skeletal muscle . ^^^ |
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Interacting proteins: P29475 and Q13424 |
Pubmed |
SVM Score :0.0 |
Specifically , nNOS is linked to alpha 1 syntrophin through PDZ domain interactions . ^^^ |
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Interacting proteins: P29475 and Q13424 |
Pubmed |
SVM Score :0.0 |
Complex formation between PSD 95 PDZ 2 and the nNOS PDZ was modelled on the basis of the crystal structure of the alpha 1 syntrophin PDZ / nNOS PDZ dimer . ^^^ |
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Interacting proteins: P29475 and Q13424 |
Pubmed |
SVM Score :0.0 |
We also analyzed the effects of mutating Asp 143 , a residue in the alphaB helix of alpha 1 syntrophin that forms a tertiary contact with the nNOS PDZ domain . ^^^ |
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Interacting proteins: P29475 and Q13424 |
Pubmed |
SVM Score :0.0 |
Association of neuronal nitric oxide synthase ( nNOS ) with alpha 1 syntrophin at the sarcolemma . alpha 1 syntrophin is a PDZ containing dystrophin associated protein , expressed predominantly in striated muscle and brain . alpha 1 syntrophin null mice generated by gene targeting technique showed no overt muscular dystrophic phenotype . ^^^ Thus , the alpha 1 syntrophin null mice are useful in the elucidation of the functional importance of nNOS targeting at the sarcolemma . ^^^ |
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Interacting proteins: P29475 and Q13424 |
Pubmed |
SVM Score :0.0 |
The results can be interpreted as indicating that , in general , NOS 1 targeting to the sarcolemma is dependent on particular members of the dystrophin complex , such as alpha 1 syntrophin , yet the expression and / or positioning of NOS 1 may be under the control of further factors , probably of neurogenic origin . ^^^ |
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Interacting proteins: P29475 and Q13424 |
Pubmed |
SVM Score :0.0 |
This paper shows the physical interaction between PMCA ( isoforms 1 and 4 ) and alpha 1 syntrophin and proposes a ternary complex of interaction between endogenous PMCA , alpha 1 syntrophin , and NOS 1 in cardiac cells . ^^^ The functionality of the interaction was demonstrated by investigating the inhibition of neuronal nitric oxide synthase 1 ( NOS 1 ) ; PMCA is a negative regulator of NOS 1 dependent NO production , and overexpression of alpha 1 syntrophin and PMCA 4 resulted in strongly increased inhibition of NO production . ^^^ |
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Interacting proteins: P29475 and Q13424 |
Pubmed |
SVM Score :0.0 |
NA |
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