Immunoelectron microscopy of carbonic anhydrase isozyme VI in rat submandibular gland: comparison with isozymes I and II.

Ogawa, Yuzo; Chang, Chee Keong; Kuwahara, Hideki; Hong, Sung-Soo; Toyosawa, Satoru; Yagi, T.

doi:10.1177/40.6.1588027

Cited by 40 publications

(53 citation statements)

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“…Thus, the immunoreactivities of the CAs appear to differ between animals based on respiratory function. Using immunoelectron microscopy, Ogawa et al determined that two types of CA-VI exist: a cytosolic enzyme and a secretory enzyme [10]. In the present study, both types of CA-VI most likely reacted to the anti-CA-VI antiserum, which may account for the similar pattern of distribution of CA-II and CA-VI in the respiratory tract cells.…”

supporting

confidence: 60%

Immunohistochemical Localization and Gene Expression of Carbonic Anhydrase Isoenzymes CA-II and CA-VI in Canine Lower Airways and Lung

Sugiura

Oishi

Amasaki

et al. 2009

The Journal of Veterinary Medical Science

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ABSTRACT. The immunohistolocalization and gene expression of carbonic anhydrase (CA) isoenzymes CA-II and CA-VI in the canine lower airways and lung were examined using specific canine CA-II and CA-VI antisera and the RT-PCR method. Laryngeal, tracheal and bronchial epithelia, serous acinar and bronchiolar secretory cells and pulmonary great alveolar cells showed immunopositive reactions to anti-CA-II and anti-CA-VI antisera. However, all mucous cells showed immunonegative reactions. The physiological roles of CA-II and CA-VI in the lower airways and lung may involve the maintenance of pH balance and the protection of mucosal surfaces against the acidic milieu.KEY WORDS: canine respiratory tract, carbonic anhydrase, immunohistochemistry, RT-PCR.

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supporting

confidence: 60%

Immunohistochemical Localization and Gene Expression of Carbonic Anhydrase Isoenzymes CA-II and CA-VI in Canine Lower Airways and Lung

Sugiura

Oishi

Amasaki

et al. 2009

The Journal of Veterinary Medical Science

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“…respiratory tract against the excessive acidity of the respiratory milieu [19]. Ogawa et al [22] described that there were two types of CA-VI, differentiated by their subcellular localizations. The first type is found in serous granules, while the second type is found diffusely in the cytoplasm.…”

Section: Discussionmentioning

confidence: 99%

Immunohistolocalization and Gene Expression of Secretory Carbonic Anhydrase Isoenzyme CA-VI in Canine Nasal Cavity

Sugiura

Ichihara

Nishita

et al. 2008

The Journal of Veterinary Medical Science

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ABSTRACT. Immunolocalization of the secretory form of carbonic anhydrase isoenzyme, CA-VI were studied using a specific canine CA-VI antiserum, and CA-VI mRNA signals were also investigated using the reverse-transcriptase polymerase chain reaction (RT-PCR) in canine nasal mucosal epithelia and glands. Immunoreactivity to CA-VI was positive throughout the mucosal epithelial cells and in the cytoplasm of serous acinar and ductal epithelial cells of the nasal mucosa and glands, including the vestibule of the nose, but the mucous acinar cells of the glands were immunonegative. We detected CA-VI gene transcripts in the same regions as the CA-VI immunoreactivity. The physiological roles of CA-VI in the nasal mucosal epithelium and glands might maintain bicarbonate levels in nasal secretions and protect the mucosa against acid. KEY WORDS: canine nasal cavity, CA-VI, immunohistochemistry, mRNA.

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“…From some animals, submandibular gland, liver, and blood were obtained. The tissues were immediately frozen in liquid nitrogen and stored at Ϫ 80C until used, and the blood was directly processed to prepare erythrocyte lysate according to the method described previously (Ogawa et al 1992).…”

Section: Methodsmentioning

confidence: 99%

Carbonic Anhydrase VI in the Mouse Nasal Gland

Kimoto¹,

Iwai²,

Maeda³

et al. 2004

J Histochem Cytochem.

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S U M M A R YWestern blotting analysis of mouse nasal tissue using a specific anti-mouse secreted carbonic anhydrase (CA VI) antibody has shown that CA VI is present in this tissue. A single immunoreactive band of 42 kD was observed, as has been found previously for salivary tissues. RT-PCR analysis has shown that nasal mucosa expressed CA VI mRNA. By immunohistochemistry (IHC), CA VI was observed in acinar cells, in duct contents of the anterior gland of the nasal septum, and in the lateral nasal gland. The Bowman's gland, the posterior gland of the nasal septum, and the maxillary sinus gland were negative. Immunoreactivity was also observed in the mucus covering the respiratory and olfactory mucosa and in the lumen of the nasolacrimal duct. In contrast, an anti-rat CA II antibody (that crossreacts with the mouse enzyme) stained only known CA II-positive cells and an occasional olfactory receptor neuron. These results indicate that CA VI is produced by the nasal gland and is secreted over the nasal mucosa. By reversible hydration of CO 2 , CA VI is presumed to play a role in mucosal functions such as CO 2 sensation and acid-base balance. It may also play a role in olfactory function as a growth factor in maturation of the olfactory epithelial cells.

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Immunoelectron microscopy of carbonic anhydrase isozyme VI in rat submandibular gland: comparison with isozymes I and II.

Cited by 40 publications

References 1 publication

Immunohistochemical Localization and Gene Expression of Carbonic Anhydrase Isoenzymes CA-II and CA-VI in Canine Lower Airways and Lung

Immunohistochemical Localization and Gene Expression of Carbonic Anhydrase Isoenzymes CA-II and CA-VI in Canine Lower Airways and Lung

Immunohistolocalization and Gene Expression of Secretory Carbonic Anhydrase Isoenzyme CA-VI in Canine Nasal Cavity

Carbonic Anhydrase VI in the Mouse Nasal Gland

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