Localization of nitric oxide synthase in human skeletal muscle

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Standard

Localization of nitric oxide synthase in human skeletal muscle. / Frandsen, Ulrik; Lopez-Figueroa, M.; Hellsten, Ylva.

I: Biochemical and Biophysical Research Communications, Bind 227, Nr. 1, 1996, s. 88-93.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Harvard

Frandsen, U, Lopez-Figueroa, M & Hellsten, Y 1996, 'Localization of nitric oxide synthase in human skeletal muscle', Biochemical and Biophysical Research Communications, bind 227, nr. 1, s. 88-93. https://doi.org/10.1006/bbrc.1996.1472

APA

Frandsen, U., Lopez-Figueroa, M., & Hellsten, Y. (1996). Localization of nitric oxide synthase in human skeletal muscle. Biochemical and Biophysical Research Communications, 227(1), 88-93. https://doi.org/10.1006/bbrc.1996.1472

Vancouver

Frandsen U, Lopez-Figueroa M, Hellsten Y. Localization of nitric oxide synthase in human skeletal muscle. Biochemical and Biophysical Research Communications. 1996;227(1):88-93. https://doi.org/10.1006/bbrc.1996.1472

Author

Frandsen, Ulrik ; Lopez-Figueroa, M. ; Hellsten, Ylva. / Localization of nitric oxide synthase in human skeletal muscle. I: Biochemical and Biophysical Research Communications. 1996 ; Bind 227, Nr. 1. s. 88-93.

Bibtex

@article{c325126032aa11df8ed1000ea68e967b,
title = "Localization of nitric oxide synthase in human skeletal muscle",
abstract = "The present study investigated the cellular localization of the neuronal type I and endothelial type III nitric oxide synthase in human skeletal muscle. Type I NO synthase immunoreactivity was found in the sarcolemma and the cytoplasm of all muscle fibres. Stronger immunoreactivity was expressed in the sarcolemma as well as the cytoplasm of type I muscle fibres. NADPH diaphorase activity confirmed a higher level of NO synthase activity in the sarcolemma as well as the cytoplasm of type I muscle fibers. Histochemical staining for cytochrome oxidase showed a staining pattern similar to that observed for type I NO synthase immunoreactivity and NADPH diaphorase activity. Type III NO synthase immunoreactivity was observed both in the endothelium of larger vessels and of microvessels. The results establish that human skeletal muscle expresses two different constitutive isoforms of NO synthase in different cellular compartments and suggest that NO may have specific actions in relation to its site of production. The localization of type I NO synthase in the vicinity of mitochondria supports a specific action of NO on mitochondrial respiration, whereas the localization of type III NO synthase in vascular endothelium is consistent with a role for NO in the control of blood flow in human skeletal muscle.",
author = "Ulrik Frandsen and M. Lopez-Figueroa and Ylva Hellsten",
note = "Keywords: Electron Transport Complex IV; Humans; Immunohistochemistry; Muscle, Skeletal; NADPH Dehydrogenase; Nitric Oxide Synthase",
year = "1996",
doi = "10.1006/bbrc.1996.1472",
language = "English",
volume = "227",
pages = "88--93",
journal = "Biochemical and Biophysical Research Communications",
issn = "0006-291X",
publisher = "Elsevier",
number = "1",

}

RIS

TY - JOUR

T1 - Localization of nitric oxide synthase in human skeletal muscle

AU - Frandsen, Ulrik

AU - Lopez-Figueroa, M.

AU - Hellsten, Ylva

N1 - Keywords: Electron Transport Complex IV; Humans; Immunohistochemistry; Muscle, Skeletal; NADPH Dehydrogenase; Nitric Oxide Synthase

PY - 1996

Y1 - 1996

N2 - The present study investigated the cellular localization of the neuronal type I and endothelial type III nitric oxide synthase in human skeletal muscle. Type I NO synthase immunoreactivity was found in the sarcolemma and the cytoplasm of all muscle fibres. Stronger immunoreactivity was expressed in the sarcolemma as well as the cytoplasm of type I muscle fibres. NADPH diaphorase activity confirmed a higher level of NO synthase activity in the sarcolemma as well as the cytoplasm of type I muscle fibers. Histochemical staining for cytochrome oxidase showed a staining pattern similar to that observed for type I NO synthase immunoreactivity and NADPH diaphorase activity. Type III NO synthase immunoreactivity was observed both in the endothelium of larger vessels and of microvessels. The results establish that human skeletal muscle expresses two different constitutive isoforms of NO synthase in different cellular compartments and suggest that NO may have specific actions in relation to its site of production. The localization of type I NO synthase in the vicinity of mitochondria supports a specific action of NO on mitochondrial respiration, whereas the localization of type III NO synthase in vascular endothelium is consistent with a role for NO in the control of blood flow in human skeletal muscle.

AB - The present study investigated the cellular localization of the neuronal type I and endothelial type III nitric oxide synthase in human skeletal muscle. Type I NO synthase immunoreactivity was found in the sarcolemma and the cytoplasm of all muscle fibres. Stronger immunoreactivity was expressed in the sarcolemma as well as the cytoplasm of type I muscle fibres. NADPH diaphorase activity confirmed a higher level of NO synthase activity in the sarcolemma as well as the cytoplasm of type I muscle fibers. Histochemical staining for cytochrome oxidase showed a staining pattern similar to that observed for type I NO synthase immunoreactivity and NADPH diaphorase activity. Type III NO synthase immunoreactivity was observed both in the endothelium of larger vessels and of microvessels. The results establish that human skeletal muscle expresses two different constitutive isoforms of NO synthase in different cellular compartments and suggest that NO may have specific actions in relation to its site of production. The localization of type I NO synthase in the vicinity of mitochondria supports a specific action of NO on mitochondrial respiration, whereas the localization of type III NO synthase in vascular endothelium is consistent with a role for NO in the control of blood flow in human skeletal muscle.

U2 - 10.1006/bbrc.1996.1472

DO - 10.1006/bbrc.1996.1472

M3 - Journal article

C2 - 8858108

VL - 227

SP - 88

EP - 93

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 1

ER -

ID: 18695014