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  • 1
    Online Resource
    Online Resource
    SAGE Publications ; 2001
    In:  Journal of Histochemistry & Cytochemistry Vol. 49, No. 5 ( 2001-05), p. 657-662
    In: Journal of Histochemistry & Cytochemistry, SAGE Publications, Vol. 49, No. 5 ( 2001-05), p. 657-662
    Abstract: Salivary carbonic anhydrase VI (CA VI) appears to contribute to taste function by protecting taste receptor cells (TRCs) from apoptosis. The serous von Ebner's glands locating in the posterior tongue deliver their saliva into the bottom of the trenches surrounding the TRC-rich circumvallate and foliate papillae. Because these glands deliver their saliva directly into the immediate vicinity of TRCs, we investigated whether CA VI is secreted by the von Ebner's glands, using immunochemical techniques. The immunohistochemical results showed that CA VI is present in the serous acinar cells, ductal cells, and ductal content of von Ebner's glands and in the demilune and ductal cells plus ductal content of rat lingual mucous glands. More importantly, CA VI was also detected in taste buds and in the taste pores. Western blotting of saliva collected from the orifices of human von Ebner's glands and CAs purified from rat von Ebner's glands confirmed that CA VI is expressed in these glands and secreted to the bottom of the trenches surrounding the circumvallate and foliate papillae. These findings are consistent with the hypothesis that locally secreted CA VI is implicated in the paracrine modulation of taste function and TRC apoptosis. (J Histochem Cytochem 49:657–662, 2001)
    Type of Medium: Online Resource
    ISSN: 0022-1554 , 1551-5044
    Language: English
    Publisher: SAGE Publications
    Publication Date: 2001
    detail.hit.zdb_id: 218208-7
    detail.hit.zdb_id: 1421306-0
    SSG: 12
    Location Call Number Limitation Availability
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  • 2
    In: Journal of Histochemistry & Cytochemistry, SAGE Publications, Vol. 48, No. 12 ( 2000-12), p. 1601-1608
    Abstract: Carbonic anhydrase isozyme XII (CA XII) is a novel membrane-associated protein with a potential role in von Hippel–Lindau carcinogenesis. Although Northern blotting has revealed positive signal for CA XII in normal human kidney, this is the first study to demonstrate its cellular and subcellular localization along the human nephron and collecting duct. Immunohistochemistry with a polyclonal antibody (PAb) raised against truncated CA XII revealed distinct staining in the basolateral plasma membrane of the epithelial cells in the thick ascending limb of Henle and distal convoluted tubules, and in the principal cells of the collecting ducts. A weak basolateral signal was also detected in the epithelium of the proximal convoluted tubules. In addition to the normal kidney specimens, this immunohistochemical study included 31 renal tumors. CA XII showed moderate or strong plasma membrane-associated expression in most oncocytomas and clear-cell carcinomas. The segmental, cellular, and subcellular distribution of CA XII along the human nephron and collecting duct suggests that it may be one of the key enzymes involved in normal renal physiology, particularly in the regulation of water homeostasis. High expression of CA XII in some renal carcinomas may contribute to its role in von Hippel–Lindau carcinogenesis.
    Type of Medium: Online Resource
    ISSN: 0022-1554 , 1551-5044
    Language: English
    Publisher: SAGE Publications
    Publication Date: 2000
    detail.hit.zdb_id: 218208-7
    detail.hit.zdb_id: 1421306-0
    SSG: 12
    Location Call Number Limitation Availability
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  • 3
    In: Journal of Histochemistry & Cytochemistry, SAGE Publications, Vol. 51, No. 9 ( 2003-09), p. 1217-1224
    Abstract: Membrane-associated carbonic anhydrase (CA) has a crucial role in renal HCO 3 − absorption. CA activity has been localized to both luminal and basolateral membranes of the tubule epithelial cells. CA XII is a transmembrane isoenzyme that has been demonstrated in the basolateral plasma membrane of human renal, intestinal, and reproductive epithelia. The present study was designed to demonstrate the distribution of CA XII expression in the rodent kidney. A new polyclonal antibody to recombinant mouse CA XII was used in both Western blotting and immunohistochemistry. Western blotting analysis revealed a 40–45-kD polypeptide in CA XII-expressing CHO cells and isolated membranes of mouse and rat kidney. Immunofluorescence staining localized CA XII in the basolateral plasma membranes of S1 and S2 proximal tubule segments. Abundant basolateral staining of CA XII was seen in a subpopulation of cells in both cortical and medullary collecting ducts. Double immunofluorescence staining identified these cells as H + -secreting type A intercalated cells. The localization of CA XII in the peritubular space of proximal tubules suggests that it may play a role in renal HCO 3 − absorption, whereas the function of CA XII in the type A intercalated cells needs further investigation.
    Type of Medium: Online Resource
    ISSN: 0022-1554 , 1551-5044
    Language: English
    Publisher: SAGE Publications
    Publication Date: 2003
    detail.hit.zdb_id: 218208-7
    detail.hit.zdb_id: 1421306-0
    SSG: 12
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
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