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Titolo:
Association of soluble guanylate cyclase with the sarcolemma of mammalian skeletal muscle fibers
Autore:
Feussner, M; Richter, H; Baum, O; Gossrau, R;
Indirizzi:
Free Univ Berlin, Clin Benjamin Franklin, Dept Anat 2, D-14195 Berlin, Germany Free Univ Berlin Berlin Germany D-14195 Anat 2, D-14195 Berlin, Germany
Titolo Testata:
ACTA HISTOCHEMICA
fascicolo: 3, volume: 103, anno: 2001,
pagine: 265 - 277
SICI:
0065-1281(200107)103:3<265:AOSGCW>2.0.ZU;2-A
Fonte:
ISI
Lingua:
ENG
Soggetto:
NITRIC-OXIDE-SYNTHASE; DUCHENNE MUSCULAR-DYSTROPHY; I NOS-I; HEME OXYGENASE-2; EXPRESSION; SUBUNITS; ENZYME; DEFICIENT; REGION;
Keywords:
soluble guanylate cyclase; nitric oxide synthase-1; heme oxygenase-2; skeletal muscle; sarcolemma;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
41
Recensione:
Indirizzi per estratti:
Indirizzo: Gossrau, R Free Univ Berlin, Clin Benjamin Franklin, Dept Anat 2, Konigin Luise Str 15, D-14195 Berlin, Germany Free Univ Berlin Konigin Luise Str 15Berlin Germany D-14195 y
Citazione:
M. Feussner et al., "Association of soluble guanylate cyclase with the sarcolemma of mammalian skeletal muscle fibers", ACT HISTOCH, 103(3), 2001, pp. 265-277

Abstract

Previous investigations have shown that NO-producing nitric oxide synthase(NOS)-1 and GO-generating heme oxygenase (HO-2) are associated with the sarcolemma of skeletal muscle fibers in many mammalian species. Despite numerous roles ascribed to NO and possibly also CO in skeletal muscle, a specific receptor for both gases has hitherto not been found in myofibers. Therefore, in the present work the appearance of the alpha1, beta1 and beta2 subunits of soluble guanylate cyclase (sGC), the most commonly known receptor for NO and potentially also CO, was analysed in mammalian skeletal muscles using immunoblotting and immunohistochemistry. Immunoblotting with an antibody against the pi subunit of sGC revealed a band of 70 kDa corresponding to the molecular weight of this protein. Immunohistochemistry with antibodies against the alpha1, beta1 and beta2 sGC subunits showed that the larger part of positivity was present in the sarcolemma region of skeletal muscle fibers and colocalized with NOS-1 mainly in type II myofibers and with HO-2 intype I and type II myofibers. For the first time, sarcolemmal association of sGC and its colocalization with NOS-1 generating the sGC-activator NO and with HO-2 producing the potential sGC upregulator CO have been demonstrated in the present study. These results enable a better understanding of therole of NO and CO in myofibers and suggest a so far unknown molecular mechanism for the interaction of sGC with the sarcolemma.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 01/04/20 alle ore 20:14:48