High-activity carbonic anhydrase isoenzyme (CA II) in human gallbladder epitheliumT Juvonen, S Parkkila, AK Parkkila, O Niemela, LH Lajunen, MI Kairaluoma, P Peramaki and H Rajaniemi Department of Surgery, University of Oulu, Finland. Acidification of bile is one of the factors that prevents calcium precipitation and thereby gallstone formation. Carbonic anhydrase II (CA II) has previously been shown to be one of the key factors in the human alimentary tract that regulates the acid-base balance. We demonstrated CA II expression in the human gallbladder epithelium using immunohistochemical techniques, elucidated the CA II content of the epithelium by digital image analysis of the immunohistochemically stained enzyme in samples from 16 patients undergoing cholecystectomy, and correlated the results with the calcium content of the gallstones. Nine patients had symptomatic gallstone disease and seven an acalculous, histologically normal gallbladder. The patients were classified into two groups on the basis of the calcium content of their gallstones: no gallstones or gallstones containing no calcium (Group 1) and gallstones with 2-87% calcium by weight (Group 2). The immunohistochemical techniques showed distinct epithelial CA II- positive staining in most of the gallbladder samples, but digital image analysis revealed distinct variations in staining intensity among them. The median staining intensity index was significantly higher in Group 1 (0.4463) than in Group 2 (0.2376; p = 0.0262). The results suggest that CA II is abundantly expressed in the normal gallbladder epithelium and that decreased expression may be associated with the formation of calcified gallstones. These findings are relevant to the pathogenesis of gallstone disease.
Volume 42,
Issue 10,
pp. 1393-1397,
10/01/1994
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R. M. Morphew, H. A. Wright, E. J. LaCourse, D. J. Woods, and P. M. Brophy Comparative Proteomics of Excretory-Secretory Proteins Released by the Liver Fluke Fasciola hepatica in Sheep Host Bile and during in Vitro Culture ex Host Mol. Cell. Proteomics, June 1, 2007; 6(6): 963 - 972. [Abstract] [Full Text] [PDF] |
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L. Alvarez, M. Fanjul, N. Carter, and E. Hollande Carbonic Anhydrase II Associated with Plasma Membrane in a Human Pancreatic Duct Cell Line (CAPAN-1) J. Histochem. Cytochem., August 1, 2001; 49(8): 1045 - 1054. [Abstract] [Full Text] [PDF] |
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S. Parkkila, A.-K. Parkkila, J. Saarnio, J. Kivelä, T. J. Karttunen, K. Kaunisto, A. Waheed, W. S. Sly, O. Türeci, I. Virtanen, et al. Expression of the Membrane-associated Carbonic Anhydrase Isozyme XII in the Human Kidney and Renal Tumors J. Histochem. Cytochem., December 1, 2000; 48(12): 1601 - 1608. [Abstract] [Full Text] |
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J. Saarnio, S. Parkkila, A.-K. Parkkila, A. Waheed, M. C. Casey, X. Y. Zhou, S. Pastoreková, J. Pastorek, T. Karttunen, K. Haukipuro, et al. Immunohistochemistry of Carbonic Anhydrase Isozyme IX (MN/CA IX) in Human Gut Reveals Polarized Expression in the Epithelial Cells with the Highest Proliferative Capacity J. Histochem. Cytochem., April 1, 1998; 46(4): 497 - 504. [Abstract] [Full Text] |
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