Literature DB >> 6422796

Immunolocalization of carbonic anhydrase isozymes in rat and mouse salivary and exorbital lacrimal glands.

R A Hennigar, B A Schulte, S S Spicer.   

Abstract

Carbonic anhydrase (CA) isozyme I and isozyme II have been localized with the immunoperoxidase bridge method in cells of mouse and rat salivary glands and exorbital lacrimal glands. Immunostaining proved optimal in Carnoy fixed specimens for some sites and in Bouin fixed glands for other sites. Staining in mouse largely resembled that in rat glands, but minor species differences were observed. Serous acinar cells in the submandibular gland stained uniformly and exclusively for CA I. From 50 to 100% of the serous acinar cells in the parotid glands evidenced content of both CA I and CA II. A minor population of serous acinar cells in the mouse exorbital lacrimal gland stained for CA I and CA II, but these glands in the rat failed to stain. Immunostaining was observed in ducts in Bouin fixed glands. Some cells in striated ducts of submandibular and sublingual glands stained for CA I and CA II and other cells in these ducts were negative. Such cellular heterogeneity was also observed in excretory ducts of submandibular and sublingual glands. These findings thus demonstrate the presence of CA in two morphologically and functionally diverse cell populations in rodent salivary glands. Immunolocalization of the CA isozymes in serous acinar cells and intercalated duct cells, presumably packaged in secretory granules, implies a role for this enzyme in salivary secretions whereas localization of CA in striated and excretory ducts suggests their traditional function in fluid and electrolyte transport.

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Year:  1983        PMID: 6422796     DOI: 10.1002/ar.1092070408

Source DB:  PubMed          Journal:  Anat Rec        ISSN: 0003-276X


  16 in total

1.  Carbonic anhydrase isozyme VI in rat lacrimal gland.

Authors:  Y Ogawa; S Toyosawa; T Inagaki; S S Hong; N Ijuhin
Journal:  Histochem Cell Biol       Date:  1995-05       Impact factor: 4.304

2.  Differential effects of aldosterone and ADH on intracellular electrolytes in the toad urinary bladder epithelium.

Authors:  R Rick; G Spancken; A Dörge
Journal:  J Membr Biol       Date:  1988-03       Impact factor: 1.843

3.  Tissue and species distribution of the secreted carbonic anhydrase isoenzyme.

Authors:  R T Fernley; P Darling; P Aldred; R D Wright; J P Coghlan
Journal:  Biochem J       Date:  1989-04-01       Impact factor: 3.857

4.  Histochemical localization of carbonic anhydrase in the trachea of the guinea pig.

Authors:  H Okamura; N Sugai; T Kanno; T Shimizu; I Ohtani
Journal:  Histochem Cell Biol       Date:  1996-08       Impact factor: 4.304

5.  Carbonic anhydrase activity in a calcium-mobilizing epithelium of the crustacean Orchestia cavimana during molting.

Authors:  J C Meyran; F Graf; J Fournié
Journal:  Histochemistry       Date:  1987

6.  Immunohistochemical study of carbonic anhydrase in mixed tumours from major salivary glands and skin.

Authors:  Y Noda; Y Takai; Y Iwai; M A Meenaghan; M Mori
Journal:  Virchows Arch A Pathol Anat Histopathol       Date:  1986

7.  The immunohistolocalization of carbonic anhydrase III in the submandibular gland of rats and hamsters.

Authors:  T Nishita; H Oshige; H Matsushita; Y Kano; M Asari
Journal:  Histochem J       Date:  1989-01

8.  Comparative immunohistolocalization of carbonic anhydrase isozymes I, II and III in the equine and bovine digestive tract.

Authors:  K Sasaki; S Igarashi; T Amasaki; H Amasaki; T Nishita; Y Kano; M Asari
Journal:  Histochem J       Date:  1993-04

9.  Acetylcholine-induced Na+ influx in the mouse lacrimal gland acinar cells: demonstration of multiple Na+ transport mechanisms by intracellular Na+ activity measurements.

Authors:  Y Saito; T Ozawa; A Nishiyama
Journal:  J Membr Biol       Date:  1987       Impact factor: 1.843

10.  Mouse carbonic anhydrase III: nucleotide sequence and expression studies.

Authors:  S Tweedie; Y Edwards
Journal:  Biochem Genet       Date:  1989-02       Impact factor: 1.890

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