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13 results on '"KOWARSKI S"'

1. Meta‐analysis of individual‐patient data from EVAR‐1, DREAM, OVER and ACE trials comparing outcomes of endovascular or open repair for abdominal aortic aneurysm over 5 years

Author

Powell, J. T., Sweeting, M. J., Ulug, P., Blankensteijn, J. D., Lederle, F. A., Becquemin, J.‐P., Greenhalgh, R. M., Greenhalgh, R. M., Beard, J. D., Buxton, M. J., Brown, L. C., Harris, P. L., Powell, J. T., Rose, J. D. G., Russell, I. T., Sculpher, M. J., Thompson, S. G., Lilford, R.J., Bell, P. R. F., Greenhalgh, R. M., Whitaker, S.C., Poole‐Wilson, the late P.A., Ruckley, C. V., Campbell, W. B., Dean, M. R. E., Ruttley, M. S. T., Coles, E. C., Powell, J. T., Halliday, A., Gibbs, S. J., Brown, L. C., Epstein, D., Sculpher, M. J., Thompson, S. G., Hannon, R. J., Johnston, L., Bradbury, A. W., Henderson, M. J., Parvin, S. D., Shepherd, D. F. C., Greenhalgh, R. M., Mitchell, A. W., Edwards, P. R., Abbott, G. T., Higman, D. J., Vohra, A., Ashley, S., Robottom, C., Wyatt, M. G., Rose, J. D. G., Byrne, D., Edwards, R., Leiberman, D. P., McCarter, D. H., Taylor, P. R., Reidy, J. F., Wilkinson, A. R., Ettles, D. F., Clason, A. E., Leen, G. L. S., Wilson, N. V., Downes, M., Walker, S. R., Lavelle, J. M., Gough, M. J., McPherson, S., Scott, D. J. A., Kessell, D. O., Naylor, R., Sayers, R., Fishwick, N. G., Harris, P. L., Gould, D. A., Walker, M. G., Chalmers, N. C., Garnham, A., Collins, M. A., Beard, J. D., Gaines, P. A., Ashour, M. Y., Uberoi, R., Braithwaite, B., Whitaker, S. C., Davies, J. N., Travis, S., Hamilton, G., Platts, A., Shandall, A., Sullivan, B. A., Sobeh, M., Matson, M., Fox, A. D., Orme, R., Yusef, W., Doyle, T., Horrocks, M., Hardman, J., Blair, P. H. B., Ellis, P. K., Morris, G., Odurny, A., Vohra, R., Duddy, M., Thompson, M., Loosemore, T. M. L., Belli, A. M., Morgan, R., Adiseshiah, M., Brookes, J. A. S., McCollum, C. N., Ashleigh, R., Aukett, M., Baker, S., Barbe, E., Batson, N., Bell, J., Blundell, J., Boardley, D., Boyes, S., Brown, O., Bryce, J., Carmichael, M., Chance, T., Coleman, J., Cosgrove, C., Curran, G., Dennison, T., Devine, C., Dewhirst, N., Errington, B., Farrell, H., Fisher, C., Fulford, P., Gough, M., Graham, C., Hooper, R., Horne, G., Horrocks, L., Hughes, B., Hutchings, T., Ireland, M., Judge, C., Kelly, L., Kemp, J., Kite, A., Kivela, M., Lapworth, M., Lee, C., Linekar, L., Mahmood, A., March, L., Martin, J., Matharu, N., McGuigen, K., Morris‐Vincent, P., Murray, S., Murtagh, A., Owen, G., Ramoutar, V., Rippin, C., Rowley, J., Sinclair, J., Spencer, S., Taylor, V., Tomlinson, C., Ward, S., Wealleans, V., West, J., White, K., Williams, J., Wilson, L., Grobbee, D. E., Blankensteijn, J. D., Bak, A. A. A., Buth, J., Pattynama, P. M., Verhoeven, E. L. G., van Voorthuisen, A. E., Blankensteijn, J. D., Balm, R., Buth, J., Cuypers, P. W. M., Grobbee, D. E., Prinssen, M., van Sambeek, M. R. H. M., Verhoeven, E. L. G., Baas, A. F., Hunink, M. G., van Engelshoven, J. M., Jacobs, M. J. H. M., de Mol, B. A. J. M., van Bockel, J. H., Balm, R., Reekers, J., Tielbeek, X., Verhoeven, E. L. G., Wisselink, W., Boekema, N., Heuveling, L. M., Sikking, I., Prinssen, M., Balm, R., Blankensteijn, J. D., Buth, J., Cuypers, P. W. M., van Sambeek, M. R. H. M., Verhoeven, E. L. G., de Bruin, J. L., Baas, A. F., Blankensteijn, J. D., Prinssen, M., Buth, J., Tielbeek, A.V., Blankensteijn, J. D., Balm, R., Reekers, J. A., van Sambeek, M. R. H. M., Pattynama, P., Verhoeven, E. L. G., Prins, T., van der Ham, A. C., van der Velden, J. J. I. M., van Sterkenburg, S. M. M., ten Haken, G. B., Bruijninckx, C. M. A., van Overhagen, H., Tutein Nolthenius, R. P., Hendriksz, T. R., Teijink, J. A. W., Odink, H. F., de Smet, A. A. E. A., Vroegindeweij, D., van Loenhout, R. M. M., Rutten, M. J., Hamming, J. F., Lampmann, L. E. H., Bender, M. H. M., Pasmans, H., Vahl, A. C., de Vries, C., Mackaay, A. J. C., van Dortmont, L. M. C., van der Vliet, A. J., Schultze Kool, L. J., Boomsma, J. H. B., van Dop, H. R., de Mol van Otterloo, J. C. A., de Rooij, T. P. W., Smits, T. M., Yilmaz, E. N., Wisselink, W., van den Berg, F. G., Visser, M. J. T., van der Linden, E., Schurink, G. W. H., de Haan, M., Smeets, H. J., Stabel, P., van Elst, F., Poniewierski, J., Vermassen, F. E. G., Lederle, F. A., Freischlag, J. A., Kohler, T. R., Latts, E., Matsumura, J., Padberg, F. T., Jr, Kyriakides, T. C., Swanson, K. M., Guarino, P., Peduzzi, P., Antonelli, M., Cushing, C., Davis, E., Durant, L., Joyner, S., Kossack, the late A., Kyriakides, T. C., LeGwin, Mary, McBride, V., OʼConnor, T., Poulton, J., Stratton, the late S., Zellner, S., Snodgrass, A. J., Thornton, J., Swanson, K. M., Haakenson, C. M., Stroupe, K.T., Jonk, Y., Hallett, J. W., Hertzer, N., Towne, J., Katz, D. A., Karrison, T., Matts, J. P., Marottoli, R., Kasl, S., Mehta, R., Feldman, R., Farrell, W., Allore, H., Perry, E., Niederman, J., Randall, F., Zeman, M., Beckwith, the late D., OʼLeary, T. J., Huang, G. D., Latts, E., Bader, M., Ketteler, E. R., Kingsley, D. D., Marek, J. M., Massen, R. J., Matteson, B. D., Pitcher, J. D., Langsfeld, M., Corson, J. D., Goff, J. M., Jr, Kasirajan, K., Paap, C., Robertson, D. C., Salam, A., Veeraswamy, R., Milner, R., Kasirajan, K., Guidot, J., Lal, B. K., Busuttil, S. J., Lilly, M. P., Braganza, M., Ellis, K., Patterson, M. A., Jordan, W. D., Whitley, D., Taylor, S., Passman, M., Kerns, D., Inman, C., Poirier, J., Ebaugh, J., Raffetto, J., Chew, D., Lathi, S., Owens, C., Hickson, K., Dosluoglu, H. H., Eschberger, K., Kibbe, M. R., Baraniewski, H. M., Matsumura, J., Endo, M., Busman, A., Meadows, W., Evans, M., Giglia, J. S., El Sayed, H., Reed, A. B., Ruf, M., Ross, S., Jean‐Claude, J. M., Pinault, G., Kang, P., White, N., Eiseman, M., Jones, the late R., Timaran, C. H., Modrall, J. G., Welborn, M. B., III, Lopez, J., Nguyen, T., Chacko, J. K. Y., Granke, K., Vouyouka, A. G., Olgren, E., Chand, P., Allende, B., Ranella, M., Yales, C., Whitehill, T. A., Krupski, the late W. C., Nehler, M. R., Johnson, S. P., Jones, D. N., Strecker, P., Bhola, M. A., Shortell, C. K., Gray, J. L., Lawson, J. H., McCann, R., Sebastian, M.W., Kistler Tetterton, J., Blackwell, C., Prinzo, P. A., Lee, N., Padberg, F. T., Jr, Cerveira, J. J., Lal, B. K., Zickler, R. W., Hauck, K. A., Berceli, S. A., Lee, W. A., Ozaki, C. K., Nelson, P. R., Irwin, A. S., Baum, R., Aulivola, B., Rodriguez, H., Littooy, F. N., Greisler, H., OʼSullivan, M. T., Kougias, P., Lin, P. H., Bush, R. L., Guinn, G., Bechara, C., Cagiannos, C., Pisimisis, G., Barshes, N., Pillack, S., Guillory, B., Cikrit, D., Lalka, S. G., Lemmon, G., Nachreiner, R., Rusomaroff, M., OʼBrien, E., Cullen, J. J., Hoballah, J., Sharp, W. J., McCandless, J. L., Beach, V., Minion, D., Schwarcz, T. H., Kimbrough, J., Ashe, L., Rockich, A., Warner‐Carpenter, J., Moursi, M., Eidt, J. F., Brock, S., Bianchi, C., Bishop, V., Gordon, I. L., Fujitani, R., Kubaska, S. M., III, Behdad, M., Azadegan, R., Ma Agas, C., Zalecki, K., Hoch, J. R., Carr, S. C., Acher, C., Schwarze, M., Tefera, G., Mell, M., Dunlap, B., Rieder, J., Stuart, J. M., Weiman, D. S., Abul‐Khoudoud, O., Garrett, H. E., Walsh, S. M., Wilson, K. L., Seabrook, G. R., Cambria, R. A., Brown, K. R., Lewis, B. D., Framberg, S., Kallio, C., Barke, R. A., Santilli, S. M., dʼAudiffret, A. C., Oberle, N., Proebstle, C., Johnson, L. L., Jacobowitz, G. R., Cayne, N., Rockman, C., Adelman, M., Gagne, P., Nalbandian, M., Caropolo, L. J., Pipinos, I. I., Johanning, J., Lynch, T., DeSpiegelaere, H., Purviance, G., Zhou, W., Dalman, R., Lee, J. T., Safadi, B., Coogan, S. M., Wren, S. M., Bahmani, D. D., Maples, D., Thunen, S., Golden, M. A., Mitchell, M. E., Fairman, R., Reinhardt, S., Wilson, M. A., Tzeng, E., Muluk, S., Peterson, N. M., Foster, M., Edwards, J., Moneta, G. L., Landry, G., Taylor, L., Yeager, R., Cannady, E., Treiman, G., Hatton‐Ward, S., Salabsky, the late B., Kansal, N., Owens, E., Estes, M., Forbes, B. A., Sobotta, C., Rapp, J. H., Reilly, L. M., Perez, S. L., Yan, K., Sarkar, R., Dwyer, S. S., Perez, S., Chong, K., Kohler, T. R., Hatsukami, T. S., Glickerman, D. G., Sobel, M., Burdick, T. S., Pedersen, K., Cleary, P., Back, M., Bandyk, D., Johnson, B., Shames, M., Reinhard, R. L., Thomas, S. C., Hunter, G. C., Leon, L. R., Jr, Westerband, A., Guerra, R. J., Riveros, M., Mills, J. L., Sr, Hughes, J. D., Escalante, A. M., Psalms, S. B., Day, N. N., Macsata, R., Sidawy, A., Weiswasser, J., Arora, S., Jasper, B. J., Dardik, A., Gahtan, V., Muhs, B. E., Sumpio, B. E., Gusberg, R. J., Spector, M., Pollak, J., Aruny, J., Kelly, E. L., Wong, J., Vasilas, P., Joncas, C., Gelabert, H. A., DeVirgillio, C., Rigberg, D. A., Cole, L., Becquemin, J.‐P., Marzelle, J., Becquemin, J.‐P., Sapoval, M., Becquemin, J.‐P., Favre, J.‐P., Watelet, J., Lermusiaux, P., Sapoval, M., Lepage, E., Hemery, F., Dolbeau, G., Hawajry, N., Cunin, P., Harris, P., Stockx, L., Chatellier, G., Mialhe, C., Fiessinger, J.‐N., Pagny, L., Kobeiter, H., Boissier, C., Lacroix, P., Ledru, F., Pinot, J.‐J., Deux, J.‐F., Tzvetkov, B., Duvaldestin, P., Watelet, J., Jourdain, C., David, V., Enouf, D., Ady, N., Krimi, A., Boudjema, N., Jousset, Y., Enon, B., Blin, V., Picquet, J., LʼHoste, P., Thouveny, F., Borie, H., Kowarski, S., Pernes, J.‐M., Auguste, M., Becquemin, J.‐P., Desgranges, P., Allaire, E., Marzelle, J., Kobeiter, H., Meaulle, P.‐Y., Chaix, D., Juliae, P., Fabiani, J. N., Chevalier, P., Combes, M., Seguin, A., Belhomme, D., Sapoval, M., Baque, J., Pellerin, O., Favre, J. P., Barral, X., Veyret, C., Watelet, J., Peillon, C., Plissonier, D., Thomas, P., Clavier, E., Lermusiaux, P., Martinez, R., Bleuet, F., C, Dupreix, Verhoye, J. P., Langanay, T., Heautot, J. F., Koussa, M., Haulon, S., Halna, P., Destrieux, L., Lions, C., Wiloteaux, S., Beregi, J. P., Bergeron, P., Pinot, J.‐J., Patra, P., Costargent, A., Chaillou, P., DʼAlicourt, A., Goueffic, Y., Cheysson, E., Parrot, A., Garance, P., Demon, A., Tyazi, A., Pillet, J.‐C., Lescalie, F., Tilly, G., Steinmetz, E., Favier, C., Brenot, R., Krause, D., Cercueil, J. P., Vahdat, O., Sauer, M., Soula, P., Querian, A., Garcia, O., Levade, M., Colombier, D., Cardon, J.‐M., Joyeux, A., Borrelly, P., Dogas, G., Magnan, P.‐É., Branchereau, A., Bartoli, J.‐M., Hassen‐Khodja, R., Batt, M., Planchard, P.‐F., Bouillanne, P.‐J., Haudebourg, P., Bayne, J., Gouny, P., Badra, A., Braesco, J., Nonent, M., Lucas, A., Cardon, A., Kerdiles, Y., Rolland, Y., Kassab, M., Brillu, C., Goubault, F., Tailboux, L., Darrieux, H., Briand, O., Maillard, J.‐C., Varty, K., and Cousins, C.

Published
2017
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2. Isolation of the protein IMCal, a vitamin D-dependent membrane component of the intestinal transport mechanism for calcium.

Author

Schachter D and Kowarski S

Subjects
Animals, Biological Transport, Active, Membrane Proteins isolation & purification, Molecular Weight, Rats, Calcium metabolism, Calcium-Binding Proteins isolation & purification, Intestinal Mucosa metabolism, S100 Calcium Binding Protein G isolation & purification
Abstract

Regulation of the intestinal absorption of calcium by vitamin D in the rat involves the synthesis or maintenance of specific membrane proteins. A particulate preparation derived from duodenal mucosal homogenates or isolated microvillus membranes contains at least three vitamin D-dependent activities: calcium binding, p-nitrophenylphosphatase, and calcium-dependent ATPase. The membrane calcium-binding activity correlates closely with calcium transport. Solubilization and biochemical purification have led to the separation of the calcium-binding from the enzymatic activities and to the isolation of the calcium-binding protein (CaBP). This membrane protein has an apparent molecular weight of approximately 200,000 in 0.1% Triton X-100 and yields a monomeric subunit of molecular weight 20,500 in sodium dodecyl sulfate. The new protein, named IMCal, is clearly distinguished from the soluble CaBP found in mucosal homogenates and has a higher affinity for calcium than does the soluble protein. The hypothesis is proposed that IMCal is involved in the facilitated entry of calcium into the enterocyte from the lumen of the intestine.

Published
1982

3. Intestinal membrane calcium-binding protein. Vitamin D-dependent membrane component of the intestinal calcium transport mechanism.

Author

Kowarski S and Schachter D

Subjects
4-Nitrophenylphosphatase metabolism, Amino Acids analysis, Animals, Biological Transport, Active, Calcium metabolism, Calcium pharmacology, Calcium-Transporting ATPases metabolism, Duodenum metabolism, Intestinal Mucosa drug effects, Jejunum metabolism, Male, Molecular Weight, Rats, S100 Calcium Binding Protein G isolation & purification, Calcium-Binding Proteins metabolism, Intestinal Mucosa metabolism, S100 Calcium Binding Protein G metabolism
Abstract

A particulate fraction of rat intestinal mucosal homogenates, termed the "calcium-binding complex," contains three vitamin D-dependent activities: calcium binding of high affinity, calcium-dependent adenosine triphosphatase, and p-nitrophenylphosphatase. These particulate activities vary concordantly with intestinal calcium transport, suggesting that they represent membrane components of the translocation mechanism. The particulate was solubilized with 1-butanol and the activities were resolved partially by gel filtration and by DEAE-cellulose and spheroidal hydroxyl-apatite column chromatography. The Ca-binding activity was separated from the enzymes and isolated as a protein of molecular weight approximately 200,000, as estimated by gel filtration in 0.1% Triton X-100. The membrane protein, named IMCal (intestinal membrane calcium-binding protein), was dissociated with sodium dodecyl sulfate to yield a monomer of molecular weight 20,500 which is clearly distinguishable from the soluble calcium-binding protein (molecular weight 11,500) of rat mucosa. The apparent dissociation constants of Ca2+ of IMCal and of the soluble calcium-binding protein were estimated as 0.37 microM and 2.25 microM, respectively. The vitamin D-dependent activities of the calcium-binding complex are present in isolated intestinal microvillus membranes and may mediate the translocation of calcium from the intestinal lumen to the cytosol.

Published
1980

4. Vitamin D-dependent, particulate calcium-binding activity and intestinal calcium transport.

Author

Kowarski S and Schachter D

Subjects
Adenosine Triphosphatases metabolism, Aging, Animals, Biological Transport, Calcium pharmacology, Cell Fractionation, Chemical Phenomena, Chemistry, Chromatography, Gel, Cycloheximide pharmacology, Duodenum analysis, Duodenum metabolism, Intestinal Mucosa enzymology, Jejunum analysis, Jejunum metabolism, Male, Rats, Stimulation, Chemical, Temperature, Ultracentrifugation, Calcium metabolism, Carrier Proteins isolation & purification, Intestinal Mucosa metabolism, Vitamin D physiology
Abstract

A vitamin D-dependent calcium-binding activity of relatively high molecular weight has been identified in the particulate fraction of rat small intestinal mucosa. The Ca-binding activity is sedimented at 140,000 X g after treatment of the mucosal particulate fraction with Triton X-114. Intestinal brush-border suspensions can also be used as starting material. The Ca-binding component is inactivated by heat and repeated freeze-thawing and consists of one or more protein complexes in the range of 0.5-1.0 million mol wt as indicated by gel filtration. The Ca-binding activity correlates positively with known features of the intestinal Ca transport mechanism, as demonstrated by studies of the distribution in the small intestine and the effects of vitamin D, dietary Ca, cycloheximide treatment, and rat age. It is suggested that the component might function in the transit of Ca across the brush-border surface to the cytosol of intestinal mucosal cells.

Published
1975
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5. Active transport of zinc and identification of zinc-binding protein in rat jejunal mucosa.

Author

Kowarski S, Blair-Stanek CS, and Schachter D

Subjects
Animals, Biological Transport, Active, Calcium metabolism, Chromatography, Gel, Duodenum metabolism, Hexoses physiology, Ileum metabolism, Iodoacetates pharmacology, Male, Nitrophenols pharmacology, Oxygen, Proteins isolation & purification, Rats, Serous Membrane metabolism, Sodium physiology, Vitamin D pharmacology, Intestinal Mucosa metabolism, Jejunum metabolism, Protein Binding, Zinc metabolism
Published
1974
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6. Decreased content of integral membrane calcium-binding protein (IMCAL) in tissues of the spontaneously hypertensive rat.

Author

Kowarski S, Cowen LA, and Schachter D

Subjects
Animals, Antibodies, Monoclonal immunology, Erythrocyte Membrane analysis, Hypertension genetics, Intestinal Mucosa analysis, Kidney analysis, Liver analysis, Male, Muscles analysis, Myocardium analysis, Rats, Rats, Inbred WKY metabolism, S100 Calcium Binding Protein G immunology, Testis analysis, Calcium metabolism, Calcium-Binding Proteins analysis, Hypertension metabolism, Rats, Inbred SHR metabolism, Rats, Inbred Strains metabolism, S100 Calcium Binding Protein G analysis
Abstract

Prior studies report that plasma membranes of the spontaneously hypertensive rat (Okamoto-Aoki strain) bind less calcium than do the corresponding preparations from Wistar Kyoto controls. The possibility that the differences result from a decrease in the content of integral membrane calcium-binding protein (IMCAL) was explored by the application of immunoassays with polyclonal antisera and a mouse monoclonal antibody. IMCAL binds calcium with relatively high affinity, and its content in many rat tissues is regulated by vitamin D and the level of dietary calcium. Immunoassays of tissue IMCAL demonstrate significant reductions in content in the erythrocyte ghost, intestinal mucosa, kidney, heart, testis, and liver of the spontaneously hypertensive rat as compared to the control strains. The decreases are observed both at 4-5 weeks of age, before the onset of severe hypertension and at 8-9 weeks in the presence of severe hypertension. Moreover, the magnitude of the decrease in erythrocyte IMCAL can account for much of the decrease in the calcium-binding capacity of erythrocyte membranes reported by others. The results are especially significant because an abnormality in the membrane binding of calcium and in the regulation of cytosolic calcium ion concentration could underlie the pathogenesis of the hypertension.

Published
1986
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7. Tissue distribution and vitamin D dependence of IMCAL in the rat.

Author

Kowarski S, Cowen LA, Takahashi MT, and Schachter D

Subjects
Animals, Calcitriol pharmacology, Calcium, Dietary pharmacology, Cell Membrane metabolism, Intestinal Mucosa cytology, Intestinal Mucosa metabolism, Male, Rats, Rats, Inbred Strains, Time Factors, Tissue Distribution, Vitamin D Deficiency metabolism, S100 Calcium Binding Protein G metabolism
Abstract

Integral membrane calcium-binding protein (IMCAL) is a vitamin D-dependent integral membrane protein that binds calcium with relatively high affinity (J. Biol. Chem. 225: 10834-10840, 1980). Specific immunoassays for IMCAL utilizing rabbit polyclonal and mouse monoclonal antibodies were developed and applied to studies of its tissue distribution and regulation by vitamin D3 and dietary calcium in the rat. The results indicate that vitamin D-dependent, cross-reactive protein is present in small intestinal mucosa, cecal mucosa, bone, kidney, brain, testis, heart, lung, spleen, and skin. Rats maintained on a low- (0.02%) compared with & high- (2.0%) calcium diet had significantly higher content of IMCAL in duodenal mucosa, cecal mucosa, bone, kidney, brain, testis, and heart. Treatment of rats on the high-calcium diet with 1,25-dihydroxyvitamin D3 increased the IMCAL content of the duodenal mucosa, cecal mucosa, and kidney. The widespread tissue distribution of vitamin D-dependent IMCAL, its close correlation in intestinal mucosa with the calcium transport mechanism, and its occurrence in isolated preparations of enterocyte plasma membranes (microvillus and basolateral membranes) suggest that the protein is involved in the regulation of calcium flux in a number of cell types.

Published
1987
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10. VITAMIN D3: DIRECT ACTION ON THE SMALL INTESTINE OF THE RAT.

Author

SCHACHTER D, KOWARSKI S, and FINKELSTEIN JD

Subjects
Animals, Biological Transport, Rats, Calcium, Cholecalciferol, Duodenum, Intestine, Small, Metabolism, Pharmacology, Research, Vitamin D Deficiency
Abstract

Vitamin D(3) placed directly into loops of rat duodenum in vitamin D deficient animals increases markedly the subsequent transport of calcium by slices of the duodenal loop in vitro. Under similar conditions the same dose of vitamin given intravenously or placed in a jejunal loop has little or no effect on the duodenal tissue. Thus the vitamin acts directly on the small intestine without prior activation in another organ.

Published
1964
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12. Effects of vitamin D on phosphate transport and incorporation into mucosal constituents of rat intestinal mucosa.

Author

Kowarski S and Schachter D

Subjects
Animals, Calcium metabolism, Duodenum metabolism, Jejunum metabolism, Lipids biosynthesis, Male, Nucleic Acids biosynthesis, Phosphorus Isotopes, Protein Biosynthesis, Rats, Time Factors, Vitamin D Deficiency metabolism, Biological Transport, Active drug effects, Intestinal Absorption drug effects, Intestinal Mucosa metabolism, Phosphates metabolism, Vitamin D pharmacology
Published
1969

13. Vitamin D and adenosine triphosphatase dependent on divalent cations in rat intestinal mucosa.

Author

Kowarski S and Schachter D

Subjects
Adenosine Triphosphatases isolation & purification, Animals, Calcium pharmacology, Cations, Divalent, Duodenum analysis, Duodenum enzymology, Edetic Acid pharmacology, Glucosidases isolation & purification, Glucosidases metabolism, Injections, Subcutaneous, Intestinal Mucosa analysis, Intestinal Mucosa drug effects, Magnesium pharmacology, Male, Proteins isolation & purification, Rats, Starvation enzymology, Stimulation, Chemical, Sucrase isolation & purification, Sucrase metabolism, Vitamin D administration & dosage, Vitamin D Deficiency enzymology, Adenosine Triphosphatases metabolism, Intestinal Mucosa enzymology, Vitamin D pharmacology
Abstract

Intestinal brush borders prepared from vitamin D-deficient rats demonstrate increased susceptibility in vitro to fragmentation by shear forces or to loss of microvillus enzymes on treatment with EDTA. These effects are relatively nonspecific and are also observed in normal rats starved for 48 h. They may underlie prior observations that purport to demonstrate a vitamin D-dependent increase in brush border Ca-dependent ATPase. In addition, however, vitamin D increases ATPase activity dependent on certain divalent cations, including Ca and Zn, in whole-particulate suspensions pelleted by high-speed centrifugation of mucosal homogenates. This action is independent of changes in other microvillus enzymes, i.e. disaccharidases, and tissue distribution and cation specificity studies support the hypothesis that the mucosal whole-particulate ATPase is related to transport of Ca, Zn, and possibly other divalent cations.

Published
1973
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