Caveolin 3 suppresses phosphorylation-dependent activation of sarcolemmal nNOS

Mutations of the caveolin 3 gene cause autosomal dominant limb-girdle muscular dystrophy (LGMD)1C. In mice, overexpression of mutant caveolin 3 leads to loss of caveolin 3 and results in myofiber hypotrophy in association with activation of neuronal nitric oxide synthase (nNOS) at the sarcolemma. He...
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Autor*in:	Ohsawa, Yutaka [verfasserIn] Ohtsubo, Hideaki [verfasserIn] Saito, Yoshihiko [verfasserIn] Nishimatsu, Shin-ichiro [verfasserIn] Hagiwara, Hiroki [verfasserIn] Murakami, Tatsufumi [verfasserIn] Nishino, Ichizo [verfasserIn] Sunada, Yoshihide [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2022

Schlagwörter:	caveolin 3 Neuronal nitric oxide synthase Myoblast fusion Exercise Myofiber hypertrophy Limb-girdle muscular dystrophy 1C

Übergeordnetes Werk:	Enthalten in: Biochemical and biophysical research communications - Orlando, Fla. : Academic Press, 1959, 628, Seite 84-90
Übergeordnetes Werk:	volume:628 ; pages:84-90

DOI / URN:	10.1016/j.bbrc.2022.08.066

Katalog-ID:	ELV008459576

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100	1		\|a Ohsawa, Yutaka \|e verfasserin \|0 (orcid)0000-0003-1643-4797 \|4 aut
245	1	0	\|a Caveolin 3 suppresses phosphorylation-dependent activation of sarcolemmal nNOS
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520			\|a Mutations of the caveolin 3 gene cause autosomal dominant limb-girdle muscular dystrophy (LGMD)1C. In mice, overexpression of mutant caveolin 3 leads to loss of caveolin 3 and results in myofiber hypotrophy in association with activation of neuronal nitric oxide synthase (nNOS) at the sarcolemma. Here, we show that caveolin 3 directly bound to nNOS and suppressed its phosphorylation-dependent activation at a specific residue, Ser1412 in the nicotinamide adenine dinucleotide phosphate (NADPH)−flavin adenine dinucleotide (FAD) module near the C-terminus of the reduction domain, in vitro. Constitutively active nNOS enhanced myoblast fusion, but not myogenesis, in vitro. Phosphorylation-dependent activation of nNOS occurred in muscles from caveolin 3-mutant mice and LGMD1C patients. Mating with nNOS-mutant mice exacerbated myofiber hypotrophy in the caveolin 3-mutant mice. In nNOS-mutant mice, regenerating myofibers after cardiotoxin injury became hypotrophic with reduced myoblast fusion. Administration of NO donor increased myofiber size and the number of myonuclei in the caveolin 3-mutant mice. Exercise also increased myofiber size accompanied by phosphorylation-dependent activation of nNOS in wild-type and caveolin 3-mutant mice. These data indicate that caveolin 3 inhibits phosphorylation-dependent activation of nNOS, which leads to myofiber hypertrophy via enhancing myoblast fusion. Hypertrophic signaling by nNOS phosphorylation could act in a compensatory manner in caveolin 3-deficient muscles.
650		4	\|a caveolin 3
650		4	\|a Neuronal nitric oxide synthase
650		4	\|a Myoblast fusion
650		4	\|a Exercise
650		4	\|a Myofiber hypertrophy
650		4	\|a Limb-girdle muscular dystrophy 1C
700	1		\|a Ohtsubo, Hideaki \|e verfasserin \|4 aut
700	1		\|a Saito, Yoshihiko \|e verfasserin \|4 aut
700	1		\|a Nishimatsu, Shin-ichiro \|e verfasserin \|0 (orcid)0000-0002-9824-1552 \|4 aut
700	1		\|a Hagiwara, Hiroki \|e verfasserin \|0 (orcid)0000-0002-8956-7649 \|4 aut
700	1		\|a Murakami, Tatsufumi \|e verfasserin \|0 (orcid)0000-0001-7851-6822 \|4 aut
700	1		\|a Nishino, Ichizo \|e verfasserin \|0 (orcid)0000-0001-9452-112X \|4 aut
700	1		\|a Sunada, Yoshihide \|e verfasserin \|4 aut
773	0	8	\|i Enthalten in \|t Biochemical and biophysical research communications \|d Orlando, Fla. : Academic Press, 1959 \|g 628, Seite 84-90 \|h Online-Ressource \|w (DE-627)254231691 \|w (DE-600)1461396-7 \|w (DE-576)103373039 \|x 0006-291X \|7 nnns
773	1	8	\|g volume:628 \|g pages:84-90
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936	b	k	\|a 35.70 \|j Biochemie: Allgemeines
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author_variant	y o yo h o ho y s ys s i n sin h h hh t m tm i n in y s ys
matchkey_str	article:0006291X:2022----::aelnsprsepopoyaineednatvt
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publishDate	2022
allfields	10.1016/j.bbrc.2022.08.066 doi (DE-627)ELV008459576 (ELSEVIER)S0006-291X(22)01203-7 DE-627 ger DE-627 rda eng 570 DE-600 BIODIV DE-30 fid 35.70 bkl 42.12 bkl Ohsawa, Yutaka verfasserin (orcid)0000-0003-1643-4797 aut Caveolin 3 suppresses phosphorylation-dependent activation of sarcolemmal nNOS 2022 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Mutations of the caveolin 3 gene cause autosomal dominant limb-girdle muscular dystrophy (LGMD)1C. In mice, overexpression of mutant caveolin 3 leads to loss of caveolin 3 and results in myofiber hypotrophy in association with activation of neuronal nitric oxide synthase (nNOS) at the sarcolemma. Here, we show that caveolin 3 directly bound to nNOS and suppressed its phosphorylation-dependent activation at a specific residue, Ser1412 in the nicotinamide adenine dinucleotide phosphate (NADPH)−flavin adenine dinucleotide (FAD) module near the C-terminus of the reduction domain, in vitro. Constitutively active nNOS enhanced myoblast fusion, but not myogenesis, in vitro. Phosphorylation-dependent activation of nNOS occurred in muscles from caveolin 3-mutant mice and LGMD1C patients. Mating with nNOS-mutant mice exacerbated myofiber hypotrophy in the caveolin 3-mutant mice. In nNOS-mutant mice, regenerating myofibers after cardiotoxin injury became hypotrophic with reduced myoblast fusion. Administration of NO donor increased myofiber size and the number of myonuclei in the caveolin 3-mutant mice. Exercise also increased myofiber size accompanied by phosphorylation-dependent activation of nNOS in wild-type and caveolin 3-mutant mice. These data indicate that caveolin 3 inhibits phosphorylation-dependent activation of nNOS, which leads to myofiber hypertrophy via enhancing myoblast fusion. Hypertrophic signaling by nNOS phosphorylation could act in a compensatory manner in caveolin 3-deficient muscles. caveolin 3 Neuronal nitric oxide synthase Myoblast fusion Exercise Myofiber hypertrophy Limb-girdle muscular dystrophy 1C Ohtsubo, Hideaki verfasserin aut Saito, Yoshihiko verfasserin aut Nishimatsu, Shin-ichiro verfasserin (orcid)0000-0002-9824-1552 aut Hagiwara, Hiroki verfasserin (orcid)0000-0002-8956-7649 aut Murakami, Tatsufumi verfasserin (orcid)0000-0001-7851-6822 aut Nishino, Ichizo verfasserin (orcid)0000-0001-9452-112X aut Sunada, Yoshihide verfasserin aut Enthalten in Biochemical and biophysical research communications Orlando, Fla. : Academic Press, 1959 628, Seite 84-90 Online-Ressource (DE-627)254231691 (DE-600)1461396-7 (DE-576)103373039 0006-291X nnns volume:628 pages:84-90 GBV_USEFLAG_U SYSFLAG_U GBV_ELV FID-BIODIV SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_224 GBV_ILN_252 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2336 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4313 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4393 35.70 Biochemie: Allgemeines 42.12 Biophysik AR 628 84-90
spelling	10.1016/j.bbrc.2022.08.066 doi (DE-627)ELV008459576 (ELSEVIER)S0006-291X(22)01203-7 DE-627 ger DE-627 rda eng 570 DE-600 BIODIV DE-30 fid 35.70 bkl 42.12 bkl Ohsawa, Yutaka verfasserin (orcid)0000-0003-1643-4797 aut Caveolin 3 suppresses phosphorylation-dependent activation of sarcolemmal nNOS 2022 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Mutations of the caveolin 3 gene cause autosomal dominant limb-girdle muscular dystrophy (LGMD)1C. In mice, overexpression of mutant caveolin 3 leads to loss of caveolin 3 and results in myofiber hypotrophy in association with activation of neuronal nitric oxide synthase (nNOS) at the sarcolemma. Here, we show that caveolin 3 directly bound to nNOS and suppressed its phosphorylation-dependent activation at a specific residue, Ser1412 in the nicotinamide adenine dinucleotide phosphate (NADPH)−flavin adenine dinucleotide (FAD) module near the C-terminus of the reduction domain, in vitro. Constitutively active nNOS enhanced myoblast fusion, but not myogenesis, in vitro. Phosphorylation-dependent activation of nNOS occurred in muscles from caveolin 3-mutant mice and LGMD1C patients. Mating with nNOS-mutant mice exacerbated myofiber hypotrophy in the caveolin 3-mutant mice. In nNOS-mutant mice, regenerating myofibers after cardiotoxin injury became hypotrophic with reduced myoblast fusion. Administration of NO donor increased myofiber size and the number of myonuclei in the caveolin 3-mutant mice. Exercise also increased myofiber size accompanied by phosphorylation-dependent activation of nNOS in wild-type and caveolin 3-mutant mice. These data indicate that caveolin 3 inhibits phosphorylation-dependent activation of nNOS, which leads to myofiber hypertrophy via enhancing myoblast fusion. Hypertrophic signaling by nNOS phosphorylation could act in a compensatory manner in caveolin 3-deficient muscles. caveolin 3 Neuronal nitric oxide synthase Myoblast fusion Exercise Myofiber hypertrophy Limb-girdle muscular dystrophy 1C Ohtsubo, Hideaki verfasserin aut Saito, Yoshihiko verfasserin aut Nishimatsu, Shin-ichiro verfasserin (orcid)0000-0002-9824-1552 aut Hagiwara, Hiroki verfasserin (orcid)0000-0002-8956-7649 aut Murakami, Tatsufumi verfasserin (orcid)0000-0001-7851-6822 aut Nishino, Ichizo verfasserin (orcid)0000-0001-9452-112X aut Sunada, Yoshihide verfasserin aut Enthalten in Biochemical and biophysical research communications Orlando, Fla. : Academic Press, 1959 628, Seite 84-90 Online-Ressource (DE-627)254231691 (DE-600)1461396-7 (DE-576)103373039 0006-291X nnns volume:628 pages:84-90 GBV_USEFLAG_U SYSFLAG_U GBV_ELV FID-BIODIV SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_224 GBV_ILN_252 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2336 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4313 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4393 35.70 Biochemie: Allgemeines 42.12 Biophysik AR 628 84-90
allfields_unstemmed	10.1016/j.bbrc.2022.08.066 doi (DE-627)ELV008459576 (ELSEVIER)S0006-291X(22)01203-7 DE-627 ger DE-627 rda eng 570 DE-600 BIODIV DE-30 fid 35.70 bkl 42.12 bkl Ohsawa, Yutaka verfasserin (orcid)0000-0003-1643-4797 aut Caveolin 3 suppresses phosphorylation-dependent activation of sarcolemmal nNOS 2022 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Mutations of the caveolin 3 gene cause autosomal dominant limb-girdle muscular dystrophy (LGMD)1C. In mice, overexpression of mutant caveolin 3 leads to loss of caveolin 3 and results in myofiber hypotrophy in association with activation of neuronal nitric oxide synthase (nNOS) at the sarcolemma. Here, we show that caveolin 3 directly bound to nNOS and suppressed its phosphorylation-dependent activation at a specific residue, Ser1412 in the nicotinamide adenine dinucleotide phosphate (NADPH)−flavin adenine dinucleotide (FAD) module near the C-terminus of the reduction domain, in vitro. Constitutively active nNOS enhanced myoblast fusion, but not myogenesis, in vitro. Phosphorylation-dependent activation of nNOS occurred in muscles from caveolin 3-mutant mice and LGMD1C patients. Mating with nNOS-mutant mice exacerbated myofiber hypotrophy in the caveolin 3-mutant mice. In nNOS-mutant mice, regenerating myofibers after cardiotoxin injury became hypotrophic with reduced myoblast fusion. Administration of NO donor increased myofiber size and the number of myonuclei in the caveolin 3-mutant mice. Exercise also increased myofiber size accompanied by phosphorylation-dependent activation of nNOS in wild-type and caveolin 3-mutant mice. These data indicate that caveolin 3 inhibits phosphorylation-dependent activation of nNOS, which leads to myofiber hypertrophy via enhancing myoblast fusion. Hypertrophic signaling by nNOS phosphorylation could act in a compensatory manner in caveolin 3-deficient muscles. caveolin 3 Neuronal nitric oxide synthase Myoblast fusion Exercise Myofiber hypertrophy Limb-girdle muscular dystrophy 1C Ohtsubo, Hideaki verfasserin aut Saito, Yoshihiko verfasserin aut Nishimatsu, Shin-ichiro verfasserin (orcid)0000-0002-9824-1552 aut Hagiwara, Hiroki verfasserin (orcid)0000-0002-8956-7649 aut Murakami, Tatsufumi verfasserin (orcid)0000-0001-7851-6822 aut Nishino, Ichizo verfasserin (orcid)0000-0001-9452-112X aut Sunada, Yoshihide verfasserin aut Enthalten in Biochemical and biophysical research communications Orlando, Fla. : Academic Press, 1959 628, Seite 84-90 Online-Ressource (DE-627)254231691 (DE-600)1461396-7 (DE-576)103373039 0006-291X nnns volume:628 pages:84-90 GBV_USEFLAG_U SYSFLAG_U GBV_ELV FID-BIODIV SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_224 GBV_ILN_252 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2336 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4313 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4393 35.70 Biochemie: Allgemeines 42.12 Biophysik AR 628 84-90
allfieldsGer	10.1016/j.bbrc.2022.08.066 doi (DE-627)ELV008459576 (ELSEVIER)S0006-291X(22)01203-7 DE-627 ger DE-627 rda eng 570 DE-600 BIODIV DE-30 fid 35.70 bkl 42.12 bkl Ohsawa, Yutaka verfasserin (orcid)0000-0003-1643-4797 aut Caveolin 3 suppresses phosphorylation-dependent activation of sarcolemmal nNOS 2022 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Mutations of the caveolin 3 gene cause autosomal dominant limb-girdle muscular dystrophy (LGMD)1C. In mice, overexpression of mutant caveolin 3 leads to loss of caveolin 3 and results in myofiber hypotrophy in association with activation of neuronal nitric oxide synthase (nNOS) at the sarcolemma. Here, we show that caveolin 3 directly bound to nNOS and suppressed its phosphorylation-dependent activation at a specific residue, Ser1412 in the nicotinamide adenine dinucleotide phosphate (NADPH)−flavin adenine dinucleotide (FAD) module near the C-terminus of the reduction domain, in vitro. Constitutively active nNOS enhanced myoblast fusion, but not myogenesis, in vitro. Phosphorylation-dependent activation of nNOS occurred in muscles from caveolin 3-mutant mice and LGMD1C patients. Mating with nNOS-mutant mice exacerbated myofiber hypotrophy in the caveolin 3-mutant mice. In nNOS-mutant mice, regenerating myofibers after cardiotoxin injury became hypotrophic with reduced myoblast fusion. Administration of NO donor increased myofiber size and the number of myonuclei in the caveolin 3-mutant mice. Exercise also increased myofiber size accompanied by phosphorylation-dependent activation of nNOS in wild-type and caveolin 3-mutant mice. These data indicate that caveolin 3 inhibits phosphorylation-dependent activation of nNOS, which leads to myofiber hypertrophy via enhancing myoblast fusion. Hypertrophic signaling by nNOS phosphorylation could act in a compensatory manner in caveolin 3-deficient muscles. caveolin 3 Neuronal nitric oxide synthase Myoblast fusion Exercise Myofiber hypertrophy Limb-girdle muscular dystrophy 1C Ohtsubo, Hideaki verfasserin aut Saito, Yoshihiko verfasserin aut Nishimatsu, Shin-ichiro verfasserin (orcid)0000-0002-9824-1552 aut Hagiwara, Hiroki verfasserin (orcid)0000-0002-8956-7649 aut Murakami, Tatsufumi verfasserin (orcid)0000-0001-7851-6822 aut Nishino, Ichizo verfasserin (orcid)0000-0001-9452-112X aut Sunada, Yoshihide verfasserin aut Enthalten in Biochemical and biophysical research communications Orlando, Fla. : Academic Press, 1959 628, Seite 84-90 Online-Ressource (DE-627)254231691 (DE-600)1461396-7 (DE-576)103373039 0006-291X nnns volume:628 pages:84-90 GBV_USEFLAG_U SYSFLAG_U GBV_ELV FID-BIODIV SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_224 GBV_ILN_252 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2336 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4313 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4393 35.70 Biochemie: Allgemeines 42.12 Biophysik AR 628 84-90
allfieldsSound	10.1016/j.bbrc.2022.08.066 doi (DE-627)ELV008459576 (ELSEVIER)S0006-291X(22)01203-7 DE-627 ger DE-627 rda eng 570 DE-600 BIODIV DE-30 fid 35.70 bkl 42.12 bkl Ohsawa, Yutaka verfasserin (orcid)0000-0003-1643-4797 aut Caveolin 3 suppresses phosphorylation-dependent activation of sarcolemmal nNOS 2022 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Mutations of the caveolin 3 gene cause autosomal dominant limb-girdle muscular dystrophy (LGMD)1C. In mice, overexpression of mutant caveolin 3 leads to loss of caveolin 3 and results in myofiber hypotrophy in association with activation of neuronal nitric oxide synthase (nNOS) at the sarcolemma. Here, we show that caveolin 3 directly bound to nNOS and suppressed its phosphorylation-dependent activation at a specific residue, Ser1412 in the nicotinamide adenine dinucleotide phosphate (NADPH)−flavin adenine dinucleotide (FAD) module near the C-terminus of the reduction domain, in vitro. Constitutively active nNOS enhanced myoblast fusion, but not myogenesis, in vitro. Phosphorylation-dependent activation of nNOS occurred in muscles from caveolin 3-mutant mice and LGMD1C patients. Mating with nNOS-mutant mice exacerbated myofiber hypotrophy in the caveolin 3-mutant mice. In nNOS-mutant mice, regenerating myofibers after cardiotoxin injury became hypotrophic with reduced myoblast fusion. Administration of NO donor increased myofiber size and the number of myonuclei in the caveolin 3-mutant mice. Exercise also increased myofiber size accompanied by phosphorylation-dependent activation of nNOS in wild-type and caveolin 3-mutant mice. These data indicate that caveolin 3 inhibits phosphorylation-dependent activation of nNOS, which leads to myofiber hypertrophy via enhancing myoblast fusion. Hypertrophic signaling by nNOS phosphorylation could act in a compensatory manner in caveolin 3-deficient muscles. caveolin 3 Neuronal nitric oxide synthase Myoblast fusion Exercise Myofiber hypertrophy Limb-girdle muscular dystrophy 1C Ohtsubo, Hideaki verfasserin aut Saito, Yoshihiko verfasserin aut Nishimatsu, Shin-ichiro verfasserin (orcid)0000-0002-9824-1552 aut Hagiwara, Hiroki verfasserin (orcid)0000-0002-8956-7649 aut Murakami, Tatsufumi verfasserin (orcid)0000-0001-7851-6822 aut Nishino, Ichizo verfasserin (orcid)0000-0001-9452-112X aut Sunada, Yoshihide verfasserin aut Enthalten in Biochemical and biophysical research communications Orlando, Fla. : Academic Press, 1959 628, Seite 84-90 Online-Ressource (DE-627)254231691 (DE-600)1461396-7 (DE-576)103373039 0006-291X nnns volume:628 pages:84-90 GBV_USEFLAG_U SYSFLAG_U GBV_ELV FID-BIODIV SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_224 GBV_ILN_252 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2336 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4313 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4393 35.70 Biochemie: Allgemeines 42.12 Biophysik AR 628 84-90
language	English
source	Enthalten in Biochemical and biophysical research communications 628, Seite 84-90 volume:628 pages:84-90
sourceStr	Enthalten in Biochemical and biophysical research communications 628, Seite 84-90 volume:628 pages:84-90
format_phy_str_mv	Article
bklname	Biochemie: Allgemeines Biophysik
institution	findex.gbv.de
topic_facet	caveolin 3 Neuronal nitric oxide synthase Myoblast fusion Exercise Myofiber hypertrophy Limb-girdle muscular dystrophy 1C
dewey-raw	570
isfreeaccess_bool	false
container_title	Biochemical and biophysical research communications
authorswithroles_txt_mv	Ohsawa, Yutaka @@aut@@ Ohtsubo, Hideaki @@aut@@ Saito, Yoshihiko @@aut@@ Nishimatsu, Shin-ichiro @@aut@@ Hagiwara, Hiroki @@aut@@ Murakami, Tatsufumi @@aut@@ Nishino, Ichizo @@aut@@ Sunada, Yoshihide @@aut@@
publishDateDaySort_date	2022-01-01T00:00:00Z
hierarchy_top_id	254231691
dewey-sort	3570
id	ELV008459576
language_de	englisch
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author	Ohsawa, Yutaka
spellingShingle	Ohsawa, Yutaka ddc 570 fid BIODIV bkl 35.70 bkl 42.12 misc caveolin 3 misc Neuronal nitric oxide synthase misc Myoblast fusion misc Exercise misc Myofiber hypertrophy misc Limb-girdle muscular dystrophy 1C Caveolin 3 suppresses phosphorylation-dependent activation of sarcolemmal nNOS
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topic_title	570 DE-600 BIODIV DE-30 fid 35.70 bkl 42.12 bkl Caveolin 3 suppresses phosphorylation-dependent activation of sarcolemmal nNOS caveolin 3 Neuronal nitric oxide synthase Myoblast fusion Exercise Myofiber hypertrophy Limb-girdle muscular dystrophy 1C
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title	Caveolin 3 suppresses phosphorylation-dependent activation of sarcolemmal nNOS
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title_full	Caveolin 3 suppresses phosphorylation-dependent activation of sarcolemmal nNOS
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title_sort	caveolin 3 suppresses phosphorylation-dependent activation of sarcolemmal nnos
title_auth	Caveolin 3 suppresses phosphorylation-dependent activation of sarcolemmal nNOS
abstract	Mutations of the caveolin 3 gene cause autosomal dominant limb-girdle muscular dystrophy (LGMD)1C. In mice, overexpression of mutant caveolin 3 leads to loss of caveolin 3 and results in myofiber hypotrophy in association with activation of neuronal nitric oxide synthase (nNOS) at the sarcolemma. Here, we show that caveolin 3 directly bound to nNOS and suppressed its phosphorylation-dependent activation at a specific residue, Ser1412 in the nicotinamide adenine dinucleotide phosphate (NADPH)−flavin adenine dinucleotide (FAD) module near the C-terminus of the reduction domain, in vitro. Constitutively active nNOS enhanced myoblast fusion, but not myogenesis, in vitro. Phosphorylation-dependent activation of nNOS occurred in muscles from caveolin 3-mutant mice and LGMD1C patients. Mating with nNOS-mutant mice exacerbated myofiber hypotrophy in the caveolin 3-mutant mice. In nNOS-mutant mice, regenerating myofibers after cardiotoxin injury became hypotrophic with reduced myoblast fusion. Administration of NO donor increased myofiber size and the number of myonuclei in the caveolin 3-mutant mice. Exercise also increased myofiber size accompanied by phosphorylation-dependent activation of nNOS in wild-type and caveolin 3-mutant mice. These data indicate that caveolin 3 inhibits phosphorylation-dependent activation of nNOS, which leads to myofiber hypertrophy via enhancing myoblast fusion. Hypertrophic signaling by nNOS phosphorylation could act in a compensatory manner in caveolin 3-deficient muscles.
abstractGer	Mutations of the caveolin 3 gene cause autosomal dominant limb-girdle muscular dystrophy (LGMD)1C. In mice, overexpression of mutant caveolin 3 leads to loss of caveolin 3 and results in myofiber hypotrophy in association with activation of neuronal nitric oxide synthase (nNOS) at the sarcolemma. Here, we show that caveolin 3 directly bound to nNOS and suppressed its phosphorylation-dependent activation at a specific residue, Ser1412 in the nicotinamide adenine dinucleotide phosphate (NADPH)−flavin adenine dinucleotide (FAD) module near the C-terminus of the reduction domain, in vitro. Constitutively active nNOS enhanced myoblast fusion, but not myogenesis, in vitro. Phosphorylation-dependent activation of nNOS occurred in muscles from caveolin 3-mutant mice and LGMD1C patients. Mating with nNOS-mutant mice exacerbated myofiber hypotrophy in the caveolin 3-mutant mice. In nNOS-mutant mice, regenerating myofibers after cardiotoxin injury became hypotrophic with reduced myoblast fusion. Administration of NO donor increased myofiber size and the number of myonuclei in the caveolin 3-mutant mice. Exercise also increased myofiber size accompanied by phosphorylation-dependent activation of nNOS in wild-type and caveolin 3-mutant mice. These data indicate that caveolin 3 inhibits phosphorylation-dependent activation of nNOS, which leads to myofiber hypertrophy via enhancing myoblast fusion. Hypertrophic signaling by nNOS phosphorylation could act in a compensatory manner in caveolin 3-deficient muscles.
abstract_unstemmed	Mutations of the caveolin 3 gene cause autosomal dominant limb-girdle muscular dystrophy (LGMD)1C. In mice, overexpression of mutant caveolin 3 leads to loss of caveolin 3 and results in myofiber hypotrophy in association with activation of neuronal nitric oxide synthase (nNOS) at the sarcolemma. Here, we show that caveolin 3 directly bound to nNOS and suppressed its phosphorylation-dependent activation at a specific residue, Ser1412 in the nicotinamide adenine dinucleotide phosphate (NADPH)−flavin adenine dinucleotide (FAD) module near the C-terminus of the reduction domain, in vitro. Constitutively active nNOS enhanced myoblast fusion, but not myogenesis, in vitro. Phosphorylation-dependent activation of nNOS occurred in muscles from caveolin 3-mutant mice and LGMD1C patients. Mating with nNOS-mutant mice exacerbated myofiber hypotrophy in the caveolin 3-mutant mice. In nNOS-mutant mice, regenerating myofibers after cardiotoxin injury became hypotrophic with reduced myoblast fusion. Administration of NO donor increased myofiber size and the number of myonuclei in the caveolin 3-mutant mice. Exercise also increased myofiber size accompanied by phosphorylation-dependent activation of nNOS in wild-type and caveolin 3-mutant mice. These data indicate that caveolin 3 inhibits phosphorylation-dependent activation of nNOS, which leads to myofiber hypertrophy via enhancing myoblast fusion. Hypertrophic signaling by nNOS phosphorylation could act in a compensatory manner in caveolin 3-deficient muscles.
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title_short	Caveolin 3 suppresses phosphorylation-dependent activation of sarcolemmal nNOS
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author2	Ohtsubo, Hideaki Saito, Yoshihiko Nishimatsu, Shin-ichiro Hagiwara, Hiroki Murakami, Tatsufumi Nishino, Ichizo Sunada, Yoshihide
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up_date	2024-07-06T19:46:21.093Z
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fullrecord_marcxml	<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">ELV008459576</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20230524132118.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">230508s2022 xx \|\|\|\|\|o 00\| \|\|eng c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.1016/j.bbrc.2022.08.066</subfield><subfield code="2">doi</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)ELV008459576</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(ELSEVIER)S0006-291X(22)01203-7</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rda</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="082" ind1="0" ind2="4"><subfield code="a">570</subfield><subfield code="q">DE-600</subfield></datafield><datafield tag="084" ind1=" " ind2=" "><subfield code="a">BIODIV</subfield><subfield code="q">DE-30</subfield><subfield code="2">fid</subfield></datafield><datafield tag="084" ind1=" " ind2=" "><subfield code="a">35.70</subfield><subfield code="2">bkl</subfield></datafield><datafield tag="084" ind1=" " ind2=" "><subfield code="a">42.12</subfield><subfield code="2">bkl</subfield></datafield><datafield tag="100" ind1="1" ind2=" "><subfield code="a">Ohsawa, Yutaka</subfield><subfield code="e">verfasserin</subfield><subfield code="0">(orcid)0000-0003-1643-4797</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Caveolin 3 suppresses phosphorylation-dependent activation of sarcolemmal nNOS</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">2022</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zzz</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">Computermedien</subfield><subfield code="b">c</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">Online-Ressource</subfield><subfield code="b">cr</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Mutations of the caveolin 3 gene cause autosomal dominant limb-girdle muscular dystrophy (LGMD)1C. In mice, overexpression of mutant caveolin 3 leads to loss of caveolin 3 and results in myofiber hypotrophy in association with activation of neuronal nitric oxide synthase (nNOS) at the sarcolemma. Here, we show that caveolin 3 directly bound to nNOS and suppressed its phosphorylation-dependent activation at a specific residue, Ser1412 in the nicotinamide adenine dinucleotide phosphate (NADPH)−flavin adenine dinucleotide (FAD) module near the C-terminus of the reduction domain, in vitro. Constitutively active nNOS enhanced myoblast fusion, but not myogenesis, in vitro. Phosphorylation-dependent activation of nNOS occurred in muscles from caveolin 3-mutant mice and LGMD1C patients. Mating with nNOS-mutant mice exacerbated myofiber hypotrophy in the caveolin 3-mutant mice. In nNOS-mutant mice, regenerating myofibers after cardiotoxin injury became hypotrophic with reduced myoblast fusion. Administration of NO donor increased myofiber size and the number of myonuclei in the caveolin 3-mutant mice. Exercise also increased myofiber size accompanied by phosphorylation-dependent activation of nNOS in wild-type and caveolin 3-mutant mice. These data indicate that caveolin 3 inhibits phosphorylation-dependent activation of nNOS, which leads to myofiber hypertrophy via enhancing myoblast fusion. 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Caveolin 3 suppresses phosphorylation-dependent activation of sarcolemmal nNOS

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