Immunohistochemical localization of S100A1 and S100A6 in postnatally developing salivary glands of rats

Mori, Masahiko; Yamada, Kazuto; Ohomura, Hirotoshi; Kudeken, Wataru; Takai, Yoshiaki; Ilg, Evelyn C.; Schäfer, Beat W.; Heizmann, Claus W.

doi:10.1007/s004180050320

Cited by 15 publications

(16 citation statements)

References 25 publications

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“…The serous demilunes are well-differentiated at birth (Redman and Ball, 1978;Taga and Sesso, 1998). Postnatal increases in immunohistochemically demonstrated S100A1 and S100A6 proteins occur in the striated ducts (Mori et al, 1998). Demilune cells also variably react in rats prior to weaning.…”

Section: Comparison With Other Reports On Ductal Differentiation In Tmentioning

confidence: 97%

“…Postnatal increases in S100A1 and S100A6 proteins also occur in the striated ducts and GCTs (Mori et al, 1998). Physiologically, substantial reabsorption of Na ϩ and Cl Ϫ from the luminal fluid in these ducts has been demonstrated in submandibular glands of rats as young as one week after birth (Holzgreve et al, 1966).…”

Section: Comparison With Other Reports On Ductal Differentiation In Tmentioning

confidence: 98%

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Immunohistochemical localization of carbonic anhydrases I, II, and VI in the developing rat sublingual and submandibular glands

2000

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Carbonic anhydrase has been localized to the acini and ducts of mature rat salivary glands. This enzyme has been associated with ion transport, a prominent function of striated and excretory ducts in salivary glands, suggesting that it might be used as a marker of ductal differentiation. The purpose of this study was to immunohistochemically document developmental changes in carbonic anhydrase in the ducts of the rat sublingual and submandibular glands. Immunohistochemistry was performed with antibodies to human carbonic anhydrase isoenzymes I, II and VI on sections of sublingual and submandibular glands from rats at representative postnatal developmental ages. Reactions were weak in the ducts of both glands at 1 day, then progressively increased. By 42 days, reactions had the adult pattern of virtually none in the mucous or seromucous acini, moderate to strong in the striated and excretory ducts, and none to weak in the intercalated ducts. Weak to moderate reactions were observed in the granular convoluted tubules of the submandibular gland as they became recognizable at age 42 days. Reactions to carbonic anhydrase I and II antibodies also increased from none (1 day) to modest (42 days) in the demilunes of the sublingual gland. The order of reaction intensity of the antibodies was II > I > VI. When localized via these anti-human antibodies, carbonic anhydrase is a useful marker of the functional differentiation of the striated and excretory ducts of the developing rat sublingual and submandibular glands.

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Section: Comparison With Other Reports On Ductal Differentiation In Tmentioning

confidence: 97%

Section: Comparison With Other Reports On Ductal Differentiation In Tmentioning

confidence: 98%

Immunohistochemical localization of carbonic anhydrases I, II, and VI in the developing rat sublingual and submandibular glands

2000

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“…These new observations imply an additional role for guanylin possibly as a differentiation promoter (Cohen et al 1998;Pitari et al 2001) also in salivary glands. Acinar cells completed their differentiation 3 to 4 weeks after birth (Chang 1974;Cutler and Chaudry 1974;Yamashina and Mizuhira 1976;Mori et al 1998). Thus, we continued to observe guanylin immunoreactivity within the acini of parotid and submandibular glands till around D14.…”

Section: Discussionmentioning

confidence: 99%

Ontogeny of guanylin-immunoreactive cells in rat salivary glands

Vaccaro

Cetin

Renda

2004

Anatomy and Embryology

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Guanylin-like peptides regulate electrolyte/water transport through the epithelia. Moreover, these peptides possess antiproliferative activity and regulate the turnover of epithelial cells. In an earlier study we localized guanylin immunoreactivity in secretory ducts of adult rodent salivary glands. In this study we investigated the appearance and distribution pattern of this peptide during the development of rat salivary glands. Guanylin immunoreactivity appeared at the beginning of cell differentiation from solid bud, on embryonic day 17 in the submandibular and sublingual glands and after day 18 in the parotid gland. Guanylin immunoreactivity appeared first in ductal and acinar anlage: its cell distribution pattern and fate differed in these two compartments. In the duct cells guanylin immunoreactivity spread after the duct system developed, whereas in acinar cells it disappeared after cell differentiation. The guanylin immunoreactivity we detected in adult salivary duct cells accords with guanylin's role in regulating electrolyte and water transport through the various epithelia. It does so by activating guanylate cyclase-C receptor, increasing intracellular cGMP concentration, and phosphorylating the cystic fibrosis transmembrane conductance regulator (CFTR) protein by the cGMP-dependent protein kinase II. This signaling cascade couples to the ductal electrolyte/water secretion and modulates finally the electrolyte composition of the saliva. On the other hand, CFTR is also involved in mechanisms of cell growth, by regulating apoptosis, and promoting cell differentiation. The early diffuse guanylin immunoreactivity we observed in ducts and acinar anlage, before the secretory set is operative, suggests guanylin has a role in cell differentiation.

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“…S100A4 has also been examined in the developing mouse, but its expression was mainly found in the mesenchyme and not in brain tissues, which are mostly ectoderm-derived (Klingelhöfer et al, 1997). Other S100 proteins such as S100A1 and S100A8 have been analyzed in other developing structures but not in nervous tissues (Arcuri et al, 2002;Kiewtiz et al, 2000;Mori et al, 1998;Passey et al, 1999;Tatsumi et al, 1999;Timmons et al, 1993). Information on the expression in the CNS of other calcium binding proteins such as calbindin D-28k, parvalbumin, and calretinin is, however, more available (Coulin et al, 2001;Ding et al, 2000;Honig et al, 1996;Ulfig and Chan, 2001;Yew et al, 1997;Zecevic et al, 1999;Zecevic and Rakic, 2001).…”

Section: Introductionmentioning

confidence: 94%

Differential expression of S100 proteins in the developing human hippocampus and temporal cortex

Chan

Xia

Dacui³

et al. 2003

Microscopy Res & Technique

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S100 calcium binding proteins have long been known to express in the adult nervous system, but their distribution in the developing brain, especially the human fetal brain, is largely unknown. We used an immunohistochemical method to determine the expression of three S100 proteins, namely S100A4, S100A5, and S100A13, in the human fetal hippocampus and temporal cortex from 12 to 33 weeks of gestation. At 12 weeks, S100A5 was strongly expressed in the cells and fibers of the polymorphic, pyramidal, and molecular layers of the hippocampus. Thereafter, its expression decreased with age. In the temporal cortex, S100A5 expression was detected from 12 weeks onwards, peaked at 20 to 24 weeks, and then decreased with age. The horizontal fibers of the marginal zone were immunoreactive at all stages examined. S100A13 immunoreactivity was also detected in both cells and fibers of the hippocampus at 12 weeks, became slightly stronger at 20 weeks, and then decreased with age. In the temporal cortex, S100A13 immunoreactivity was also strong in all cellular layers at 12 to 24 weeks before it declined with age from 28 weeks onwards. Among the three proteins examined, S100A4 showed the weakest expression, which was detected in the cells and fibers of the hippocampus and the temporal cortex at all stages examined. Our results have demonstrated for the first time, in the human fetal hippocampus and temporal cortex, specific spatio-temporal patterns of expression of these proteins, all of which are likely to have different roles to play during development despite their pronounced sequence homology.

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Immunohistochemical localization of S100A1 and S100A6 in postnatally developing salivary glands of rats

Cited by 15 publications

References 25 publications

Immunohistochemical localization of carbonic anhydrases I, II, and VI in the developing rat sublingual and submandibular glands

Immunohistochemical localization of carbonic anhydrases I, II, and VI in the developing rat sublingual and submandibular glands

Ontogeny of guanylin-immunoreactive cells in rat salivary glands

Differential expression of S100 proteins in the developing human hippocampus and temporal cortex

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