Carbonic anhydrase-III immunohistochemical localization in human skeletal muscle

Shima, K; Tashiro, Kunio; Hibi, Nozomu; Tsutsumi, Yutaka; Hirai, Hidematsu

doi:10.1007/bf00703210

Cited by 61 publications

(17 citation statements)

References 7 publications

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“…In contrast to carbonic anhydrase III, which from biochemical, histochemical and functional studies is known to be present in the cytosol of red skeletal muscles (Register, Koester & Noltmann, 1978;Shima, Tashiro, Hibi, Tsukada & Hirai, 1983;Gros, Ganghoff, Scheid, Siffert, Teske & Kruger, 1984), this enzyme appears to be absent from the sarcoplasm as is suggested by histochemical and functional evidence (Ldnnerholm, 1980;Dermietzel, Leibstein, Siffert, Zamboglou & Gros, 1985;G. Gros, F. Ganghoff & P. Scheid, in preparation).…”

Section: Introductionmentioning

confidence: 91%

“…It is highly unlikely that the intracellular staining seen in Pls. 1 and 2 is due to carbonic anhydrase III because (i) this enzyme has an extremely low affinity towards sulphonamides (Sanyal et al 1982; see also Table 3) and is unlikely to be loaded to a larger degree with DNSA at the concentrations employed and (ii) carbonic anhydrase III is restricted to slow-twitch oxidative fibres and is cytosolic and homogeneously distributed across the fibre interior (Shima et al 1983). This is confirmed by the high sensitivity of s.r.…”

Section: Carbonic Anhydrase Associated With the Sarcoplasmic Reticulummentioning

confidence: 99%

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Carbonic anhydrase in the sarcoplasmic reticulum of rabbit skeletal muscle.

Bruns¹,

Dermietzel²,

Gros³

1986

The Journal of Physiology

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SUMMARY1. Sarcoplasmic reticulum vesicles and mitochondria were prepared from red and white skeletal muscles of the rabbit. The preparations were characterized in terms of their specific activities of citrate synthase, basal (Mg2+-dependent) and Ca2+-dependent ATPase (the latter two in the presence of NaN3 and ouabain), and their specific carbonic anhydrase activities were determined.2. Skeletal muscle mitochondria had high specific activities of citrate synthase (700-1200 mu. mg protein-1) and low carbonic anhydrase activities (0 1-0 4 u. ml mg protein-1). The latter are likely to be due to a contamination of the preparations with sarcoplasmic reticulum (s.r.)3. Preparations of s.r. vesicles showed negligible activities of citrate synthase and the expected differing patterns of basal and Ca2+-dependent ATPase in red and white muscles. Specific carbonic anhydrase activities in s.r. from both muscle types were high (2-4 u. ml mg protein-'). The highest carbonic anhydrase activity, 11 u. ml mg protein-1, was found in s.r. from rabbit m. masseter. The inhibition constant of s.r. carbonic anhydrase towards acetazolamide was 4-6 x 10-8 M and similar but not identical to that of cytosolic carbonic anhydrase II.4. It appears possible that the carbonic anhydrase II-like enzyme previously found by us in muscle homogenates (Siffert & Gros, 1982) originates from the s.r.5. Histochemical studies using the dansylsuphonamide method described previously (Dermietzel, Leibstein, Siffert, Zamboglou & Gros, 1985) showed an intracellular pattern of carbonic anhydrase staining compatible with the presence of the enzyme in s.r.: spots homogeneously distributed across the fibre crosssections in transversely sectioned fibres and thin, longitudinally oriented, bands in longitudinally sectioned fibres.6. It is estimated that s.r. carbonic anhydrase accelerates C02 hydration within the s.r. approximately 1000-fold. Thus, CO2 and HCO3-react fast enough to provide a rapid source and sink for protons leaving and entering the s.r. in exchange for Ca2+.

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Section: Introductionmentioning

confidence: 91%

Section: Carbonic Anhydrase Associated With the Sarcoplasmic Reticulummentioning

confidence: 99%

Carbonic anhydrase in the sarcoplasmic reticulum of rabbit skeletal muscle.

Bruns¹,

Dermietzel²,

Gros³

1986

The Journal of Physiology

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“…CA I1 is present in some species in fast muscles, e.g. the extensor digitonun longus (EDL), whereas CA I11 is abundant in slow red muscles such as the M. soleus (2)(3)(4)(5)(6)(7). Furthermore, a number of histological, biochemical, and physiological studies (8)(9)(10)(11)(12) indicate the existence of a membrane-bound CA in sarcolemma (SL) and sarcoplasmic reticulum (SR) of skeletal muscle cells.…”

Section: Introductionmentioning

confidence: 99%

Immunohistochemical localization of carbonic anhydrase IV in capillaries of rat and human skeletal muscle.

Sender

Gros

Waheed

et al. 1994

J Histochem Cytochem.

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We used plyclonal antisera raised in rabbits against membrane-bound rat lung and human lung carbonic anhydrase (CA) IV in immunofluorescence studies to stain aysections of rat soleus and extensor digitorum longus (EDL) and several human skeletal musdes. There was strong specific staining of capillaries in all musdes investigated. Several techniques were applied to verify this result. (a) Serial sections were either incubated with anti-CA IV/"E or processed for endothelial ATPase reaction. There was precise CO-localization of antibody marked structures and ATPase stained capillaries. (b) Human musde sections were double stained with anti-CA IV/"RIK and anti-von Willebrand factor (vWF)/HK. vWF, a capillary marker, and CA IV were localized at identical sites. (c) The CA IV was released from cap& lark by treatment with phosphatidylinositol specific phospholipase C, suggesting that the enzyme is anchored to the

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“…In the developing skeletal muscles in the human upper limb, type 1 fibers are at first few in number, but grow rapidly between 15 and 20 weeks of gestation, equal ling the number of type 2 fibers at 30 weeks of gestation [16]. In the present study, CA-III as the molecular marker of the type 1 fiber [8] appeared in the human extraocular muscles later than p-enolase, which is mainly localized in the type 2 fiber [3]. In addition, the number of CA-II1-imniunorcactive fibers increased and became almost equal to that of (3-enolase-immunorcactivc fibers from stage 21 to stage 23.…”

Section: Discussionmentioning

confidence: 90%

“…The third form of the enzyme, CA-III, is found in a high concentration in skeletal muscles [7], especially in type 1 fibers [8].…”

Section: Introductionmentioning

confidence: 99%

Immunohistochemical Study of Carbonic Anhydrase III in the Extraocular Muscles of Human Embryos

Oguni

Setogawa²,

Tanaka³

et al. 1992

Cells Tissues Organs

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The differentiation of extraocular muscles was studied immunohistochemically in externally normal human embryos (Carnegie stages 13-23), using antibodies to carbonic anhydrase (CA) III and β-enolase as the markers of type 1 and type 2 muscle fibers, respectively. At stage 18, some myoblasts were immunoreactive to β-enolase antibodies, however, CA-III immunoreactivity was not observed around the optic vesicle. At stage 20, CA-III immunoreactivity appeared in some muscle fibers of extraocular muscles. From stage 21 to stage 23, CA-III-immunoreactive fibers increased and almost equalled the number of β-enolase-immunoreactive fibers. These findings suggest that CA-III-immunoreactive type 1 fibers appear in the late stage of myogenesis compared with β-enolase-immunoreactive type 2 fibers.

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Carbonic anhydrase-III immunohistochemical localization in human skeletal muscle

Cited by 61 publications

References 7 publications

Carbonic anhydrase in the sarcoplasmic reticulum of rabbit skeletal muscle.

Carbonic anhydrase in the sarcoplasmic reticulum of rabbit skeletal muscle.

Immunohistochemical localization of carbonic anhydrase IV in capillaries of rat and human skeletal muscle.

Immunohistochemical Study of Carbonic Anhydrase III in the Extraocular Muscles of Human Embryos

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