Immunohistochemistry of carbonic anhydrase isozymes (CA‐I, II and III) in canine salivary glands: a distributional and comparative assessment

Abstract

The immunohistolocalization of carbonic anhydrase isozymes (CA-I, II, III) in canine salivary glands was studied using antiserum against CA-I, II, III. In parotid glands, immunostaining intensely localized cytosolic CA-II antiserum throughout the cytoplasm of acinar secretory cells and ductal epithelial cells, especially in the striated duct region. CA-III reactivity in the glands was only seen selectively at the intercalated ductal cells. In contrast, no immunoreaction localized CA-I in the gland. In the submandibular and sublingual glands, CA-I, II, and III were all observed in the ductal segments of the glands, whereas serous demilune appeared devoid of all three cytosolic CA isozymes. In contrast, in zygomatic glands (i.e. dorsal buccal glands) all CA isozymes were observed in both serous demilune and ductal segments. In all of the salivary glands examined, no mucous acinar cells were found to be reactive for any CA.

Immunohistolocalization of Carbonic Anhydrase Isoenzymes (CA-I, -II and -III) in Canine Epididymis

“…The purification procedure for canine CA-I, II and III has been provided by the our previous reports, and we also previously raised antisera against purified canine CA-I, -II and -III isoenzymes [1,11,12]. The canine CAs antisera used in this study have also been recognized as to their immunological specificities [1].…”

“…CA-III (very low-activity ) has been discovered in the skeletal muscle as well as in the male rat liver [10,16]. CA-III is also found in the ductal cells of the salivary glands in the rat [13], hamster [13], dog [1], cow [2] and horse [3]. CA-III is particularly insensitive to inhibition by acetazolamide [19].…”

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

“…, Motoharu OISHI 1) , Tomoko AMASAKI 4) , Satoshi SOETA 5) , Nobutsune ICHIHARA 1) , Toshiho NISHITA 2) , Masaru MURAKAMI 3) , Hajime AMASAKI 5) and Masao ASARI 1) * 1) Departments of Anatomy, 2) Carbonic anhydrase (CA; EC4.2.1.1) is a zinc-containing metalloenzyme that has many functions, including macromolecule stabilization, gas exchange, acid-base balance, ion transport, and bone resorption [17]. About 14 CA isoenzymes are widely distributed in almost all mammalian species [4].…”

“…This sample collection procedure was approved by the Laboratory Animal Welfare committee of Azabu University and was based on their animal care and use programs. Canine CA-II and CA-VI antisera were purified as described [1,6] and then used in the double immunodiffusion method to determine the specificity of each antiserum [13]. The larynx (epiglottis), cervical and thoracic parts of the trachea, bifurcation of the trachea, principal bronchi and left caudal lobe with a lobar bronchus, and parotid gland as the positive control, were examined.…”

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

“…At least 14 distinct active isoenzymes of CA are widely distributed throughout mammalian organs [11]. Of these isoenzymes, only CA-VI occurs in secreted form, and it localizes to the digestive organs, specifically the parotid, submandibular and esophageal, lingual serous von Ebner's glands in sheep [8,9,31], rats [7,18,23], humans [13,18,20,24,29] and dogs [2,14,21]. Furthermore, the CA-VI isoenzyme has been identified in the lacrimal and mammary glands of rats [26], sheep [25] and cattle [12,16].…”