Enzyme histochemical and immunohistochemical localization of carbonic anhydrase as a marker of ductal differentiation in the developing rat parotid gland

Peagler, FD; Redman, RS; NcNutt, RL; Kruse, DH; Johansson, Ingegerd

doi:10.1002/(sici)1097-0185(199802)250:2<190::aid-ar9>3.0.co;2-7

Cited by 13 publications

(10 citation statements)

References 29 publications

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“…Rat and ovine salivary glands become mature structures after weaning [16,[19][20][21]. Our dot blot and immunohistological findings provide evidence that CA-VI is synthesized in the bovine mammary gland and ductal cells, and that it is secreted in milk during in early lactation period.…”

Section: Discussionmentioning

confidence: 51%

“…The lingual von Ebner's gland also contains CA-VI [11]. CA-VI is a secretory isozyme in saliva, and its expression is specific to the parotid and submandibular glands in humans, mice, rats, sheep and cattle [1,16,18,19] and to the lacrimal gland in rats and sheep [15,17]. According to Ogawa et al [15], CA-VI is synthesized in lacrimal glands, and secreted in very small amounts into lacrimal fluid.…”

Section: Discussionmentioning

confidence: 99%

“…CA-VI was purified from ovine [4], rat [3,13], human [8,12,14,18] and bovine saliva [1] and is thought to enhance the buffering capacity of the oral cavity [10]. Immunohistochemistry and in situ hybridization histochemistry have identified the acinar cells of the salivary gland as the origin of CA-VI in several species [1,14,15,19]. These studies have shown that CA-VI is present in acinar cells of the mammalian parotid and submandibular glands, from where it is secreted into the saliva.…”

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confidence: 99%

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Immunohistolocalization of Carbonic Anhydrase Isozyme (CA-VI) in Bovine Mammary Glands

Ichihara

Asari

Kasuya

et al. 2003

The Journal of Veterinary Medical Science

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ABSTRACT. The localization of bovine carbonic anhydrase isozyme VI (CA-VI) was examined immunohistochemically in bovine mammary glands during early lactation period (after 2-3 days of postpartum) and dry period (at about 2 months preparturition in adu lts), and young calves (at 30 and 150 days after birth) using specific CA-VI antiserum. The immunoreaction for anti-CA-VI antiserum was very weak in the mammary glands in young (prepubescent) calves. In dry period, CA-VI was also weakly expressed in secretory epithelial (acinar) and ductal cells. In contrast, the reaction was intense in mammary gland cells in early lactation period. Dot blotting analysis indicated that anti-CA-VI reacted positively to beastings and mature saliva, but weakly or not at all to milk during the dry per iod or calf saliva, respectively. The intense expression of CA-VI in the mammary glands in early lactation period might compensate for low levels of secretion from functionally and structurally immature salivary glands in young calves. KEY WORDS: bovine mammary gland, CA-VI, immunohistochemical localization.

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Section: Discussionmentioning

confidence: 51%

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

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Immunohistolocalization of Carbonic Anhydrase Isozyme (CA-VI) in Bovine Mammary Glands

Ichihara

Asari

Kasuya

et al. 2003

The Journal of Veterinary Medical Science

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“…The existence of a relationship between the expression of CA II and differentiated cell status has also been demonstrated in other human pancreatic duct cell lines (Frazier et al 1990) and for enzyme systems such as alkaline phosphatases (Fanjul et al 1991) or CA IV (Mahieu et al 1994;Mairal et al 1996) in this same cell model. In the same way, CA II in vivo is considered to be a marker for the tissue differentiation of excretory ducts in the developing rat parotid gland (Peagler et al 1998). In polarized Capan-1 cells, our immunocytochemical studies revealed CA II immunoreactivity on the microvilli.…”

Section: Discussionmentioning

confidence: 57%

Carbonic Anhydrase II Associated with Plasma Membrane in a Human Pancreatic Duct Cell Line (CAPAN-1)

Alvarez

Fanjul

Carter

et al. 2001

J Histochem Cytochem.

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S U M M A R YThe subcellular distribution of carbonic anhydrase II, either throughout the cytosol or in the cytoplasm close to the apical plasma membrane or vesicular compartments, suggests that this enzyme may have different roles in the regulation of pH in intra-or extracellular compartments. To throw more light on the role of pancreatic carbonic anhydrase II, we examined its expression and subcellular distribution in Capan-1 cells. Immunocytochemical analysis by light, confocal, and electron microscopy, as well as immunoblotting of cell homogenates or purified plasma membranes, was performed. A carbonic anhydrase II of 29 kD associated by weak bonds to the inner leaflet of apical plasma membranes of polarized cells was detected. This enzyme was co-localized with markers of Golgi compartments. Moreover, the defect of its targeting to apical plasma membranes in cells treated with brefeldin A was indicative of its transport by the Golgi apparatus. We show here that a carbonic anhydrase II is associated with the inner leaflet of apical plasma membranes and with the cytosolic side of the endomembranes of human cancerous pancreatic duct cells (Capan-1). These observations point to a role for this enzyme in the regulation of intraand extracellular pH.

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“…Considerable work has been done on acinar and myoepithelial differentiation in the developing rat parotid gland, but there have been only a few reports on ductal differentiation (Redman and Sreebny, 1971; Taga and Sesso, 1979; Bordeianu et al, 1983; Redman, 1987; Ogawa et al, 1998; Peagler et al, 1998). This investigation is part of a systematic study of ductal differentiation in this gland.…”

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confidence: 99%

Enzyme histochemical localization of Na+,K+-ATPase and NADH-DE in the developing rat parotid gland

Peagler

Redman

1999

Anat. Rec.

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Information on ductal differentiation in the developing rat parotid gland is sparse. Striated and excretory ducts are rich in a number of enzymes related to ion movement. The objective of this investigation was to delineate histochemically the chronology of two of these, ouabain-sensitive Na(+),K(+)-ATPase and NADH-DE, in the developing rat parotid gland. Parotid glands were excised from rats at representative ages from 20 days in utero to 42 days. Enzyme histochemistry was performed on air-dried frozen sections. For Na(+), K(+)-ATPase, some sections also were fixed in phosphate-buffered formalin. Ouabain blocked Na(+),K(+)-ATPase activity, and neither enzyme reacted without substrate. Weak Na(+),K(+)-ATPase reactions were initially seen in unfixed sections at 1 day, and increased steadily to the adult pattern of strong (concentrated basolaterally) in striated ducts and excretory ducts, respectively, and weak to modest (diffuse) in acini and intercalated ducts at 28 days. In fixed sections, localization was sharper but the reaction was somewhat reduced. NADH-DE was modest in terminal buds and ducts before birth, then progressively changed to the adult pattern of weak in acini and intercalated ducts and strong (concentrated basally and luminally) in striated and excretory ducts at 28 days. As demonstrated by enzyme histochemistry of Na(+),K(+)-ATPase and NADH-DE, differentiation of rat parotid striated ducts and excretory ducts occurs mainly between birth and 28 days. Anat Rec 256:72-77, 1999. Published 1999 Wiley-Liss, Inc.

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Enzyme histochemical and immunohistochemical localization of carbonic anhydrase as a marker of ductal differentiation in the developing rat parotid gland

Abstract: Carbonic anhydrase is a useful marker of the functional differentiation of the striated and excretory ducts of the developing rat parotid gland.

Cited by 13 publications

References 29 publications

Immunohistolocalization of Carbonic Anhydrase Isozyme (CA-VI) in Bovine Mammary Glands

Immunohistolocalization of Carbonic Anhydrase Isozyme (CA-VI) in Bovine Mammary Glands

Carbonic Anhydrase II Associated with Plasma Membrane in a Human Pancreatic Duct Cell Line (CAPAN-1)

Enzyme histochemical localization of Na+,K+-ATPase and NADH-DE in the developing rat parotid gland

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