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Auteur : Grafiati
Publié le 11 mars 2023

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1

Montanic, Sendi, Michela Terdoslavich, Uros Rajcevic, Luigina De Leo, Serena Department of Medical Sciences, Uni, Vladka Curin Serbec et Sabina Passamonti. « Development and characterization of a novel mAb against bilitranslocase - a new biomarker of renal carcinoma ». Radiology and Oncology 47, no 2 (1 juin 2013) : 128–37. http://dx.doi.org/10.2478/raon-2013-0026.

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Background. Bilitranslocase (TC 2.A.65.1.1) is a bilirubin-specific membrane transporter, found on absorptive (stomach and intestine) and excretory (kidney and liver) epithelia and in vascular endothelium. Polyclonal antibodies have been raised in rabbits in the past, using a synthetic peptide corresponding to AA65-77 of rat liver bilitranslocase, as an antigen. Affinity-purified antibodies from immune sera have been found to inhibit various membrane transport functions, including the bilirubin uptake into human hepatocytes and the uptake of some flavonoids into human vascular endothelial cells. It was described by means of immunohistochemistry using polyclonal antibodies that bilitranslocase expression is severely down-regulated in clear cell renal carcinoma. The aim of our work was development and characterization of high-affinity, specific mAbs against bilitranslocase, which can be used as a potential diagnostic tool in renal cell carcinoma as well as in a wide variety of biological assays on different human tissues. Materials and methods. Mice were immunized with a multi-antigen peptide corresponding to segment 65-75 of predicted primary structure of the bilitranslocase protein. By a sequence of cloning, immune- and functional tests, we aimed at obtaining a specific monoclonal antibody which recognizes a 37 kDa membrane protein, and influences the transport activity of bilitranslocase. Results. On the basis of previous results, specific IgM monoclonal antibodies were produced in BALB/c mice, in order to further improve and extend the immunological approach to the study of bilitranslocase in renal cancer cells as well as to develop its potential diagnostics use. Conclusions. In this article we show an immunological approach, based on newly developed monoclonal antibodies, to a detailed biochemical and functional characterization of a protein whose gene and protein structure is still unknown. We were able to demonstrate our novel mAb as a tumor marker candidate of renal cell carcinoma, which may prove useful in the diagnostic procedures.
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Gentile, Sandro, Marcello Persico, Giulia Baldini, Giancarlo Lunazzi, Claudio Tiribelli et Gian Luigi Sottocasa. « The implication of bilitranslocase function in the impaired rifamycin SV metabolism in Gilbert's syndrome ». Clinical Science 68, no 6 (1 juin 1985) : 675–80. http://dx.doi.org/10.1042/cs0680675.

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1. The plasma disappearance rate and the increment in plasma unconjugated bilirubin after intravenous administration of 5.9 μmol of rifamycin SV (RSV)/kg body wt. were investigated in 51 subjects with Gilbert's syndrome and 35 control subjects of both sexes. 2. Both the plasma disappearance rate and the unconjugated hyperbilirubinaemia after RSV administration were higher (P<0.001) in Gilbert's syndrome. Females, both normal and with the syndrome, showed a significantly shorter t1/2 and a lower hyperbilirubinaemic response as compared with males. A linear correlation (P<0.001) was present between RSV plasma half-life and the hyperbilirubinaemic response. 3. In vitro, RSV was shown to inhibit sulphobromophthalein (BSP) uptake in rat liver plasma-membrane vesicles with a Ki of 20 μmol/l. Evidence that this effect was due to competition for bilitranslocase was sought on preparations of the purified protein. Under these experimental conditions, RSV inhibited BSP binding with a Ki of 17 μmol/l. 4. Since RSV competes with BSP for binding to bilitranslocase in vitro, the data are interpreted as suggesting that reduced bilitranslocase function might underlie the delayed RSV plasma clearance and the exacerbated unconjugated hyperbilirubinaemia present in Gilbert's syndrome.
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Passamonti, Sabina, Urska Vrhovsek et Fulvio Mattivi. « The interaction of anthocyanins with bilitranslocase ». Biochemical and Biophysical Research Communications 296, no 3 (août 2002) : 631–36. http://dx.doi.org/10.1016/s0006-291x(02)00927-0.

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Passamonti, Sabina, Lucia Battiston et Gian Luigi Sottocasa. « Gastric uptake of nicotinic acid by bilitranslocase ». FEBS Letters 482, no 1-2 (28 septembre 2000) : 167–68. http://dx.doi.org/10.1016/s0014-5793(00)02041-x.

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Passamonti, Sabina, et Gian Luigi Sottocasa. « Organization of functional groups of liver bilitranslocase ». Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 1041, no 2 (novembre 1990) : 195–200. http://dx.doi.org/10.1016/0167-4838(90)90065-n.

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Persico, M., C. Tiribelli, S. Gentile et M. Coltorti. « Impaired bilitranslocase (BTL) function in Gilbert's syndrome ». Journal of Hepatology 9 (janvier 1989) : S204. http://dx.doi.org/10.1016/0168-8278(89)90582-5.

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Torres, A. M., J. V. Rodriguez, G. C. Lunazzi et C. Tiribelli. « Carrier-mediated transport of tetrabromosulfonephthalein by rat liver plasma membrane vesicles ». American Journal of Physiology-Gastrointestinal and Liver Physiology 263, no 3 (1 septembre 1992) : G338—G344. http://dx.doi.org/10.1152/ajpgi.1992.263.3.g338.

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To investigate the molecular requirements and mechanisms for the hepatic uptake of phthaleins, the transport of tetrabromosulfonephthalein (TBS) was investigated in basolateral rat liver plasma membrane vesicles. TBS uptake was electrogenic as greatly accelerated by the creation of a positive-inside membrane potential by the addition of valinomycin in the presence of an inwardly directed potassium gradient. No effect was observed when the ionophore was added in the presence of a sodium gradient. The transport occurred into an osmotic-sensitive space and was saturable with an apparent Michaelis constant of 5.32 +/- 0.56 microM and a maximal velocity of 9.23 +/- 0.25 nmol.s-1.mg protein-1 (mean +/- SD, n = 3 experiments). TBS uptake was directly related to the extra-vesicular pH, indicating the deprotonated quinoid negative-charged form of the dye as the transported species. In contrast, TBS uptake was inversely related to the intravesicular pH, suggesting that protonation inside the vesicles may act as an efficient trap in transport process. Addition of polyclonal monospecific anti-bilitranslocase antibody to liver vesicles specifically inhibited TBS uptake rate (3.27 +/- 0.17 vs. 5.82 +/- 0.61 nmol.s-1.mg protein-1, n = 3, P less than 0.001). These data indicate that TBS is electrogenically transported across the liver cell plasma membrane by bilitranslocase. They also indicate that the presence of a negative charged group on the benzenic ring of the ligand is important in accounting for the transport.
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Župerl, Špela, Stefano Fornasaro, Marjana Novič et Sabina Passamonti. « Experimental determination and prediction of bilitranslocase transport activity ». Analytica Chimica Acta 705, no 1-2 (octobre 2011) : 322–33. http://dx.doi.org/10.1016/j.aca.2011.07.004.

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Sabina Passamonti, Lucia Battiston,. « On the mechanism of bilitranslocase transport inactivation by phenylmethylsulphonyl fluoride ». Molecular Membrane Biology 16, no 2 (janvier 1999) : 167–72. http://dx.doi.org/10.1080/096876899294625.

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Miccio, Maddalena, Gian Carlo Lunazzi, Bruno Gazzin et Gian Luigi Sottocasa. « Reconstitution of sulfobromophthalein transport in erythrocyte membranes induced by bilitranslocase ». Biochimica et Biophysica Acta (BBA) - Biomembranes 1023, no 1 (mars 1990) : 140–42. http://dx.doi.org/10.1016/0005-2736(90)90019-k.

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Passamonti, Sabina, Lucia Battiston et Gian Luigi Sottocasa. « Arginine residues are involved in the transport function of bilitranslocase ». Biochimica et Biophysica Acta (BBA) - Biomembranes 1025, no 2 (juin 1990) : 122–26. http://dx.doi.org/10.1016/0005-2736(90)90088-6.

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Passamonti, S., A. Vanzo, U. Vrhovsek, M. Terdoslavich, A. Cocolo, G. Decorti et F. Mattivi. « Hepatic uptake of grape anthocyanins and the role of bilitranslocase ». Food Research International 38, no 8-9 (octobre 2005) : 953–60. http://dx.doi.org/10.1016/j.foodres.2005.02.015.

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Perdih, Andrej, Amrita Roy Choudhury, Špela Župerl, Emilia Sikorska, Igor Zhukov, Tom Solmajer et Marjana Novič. « Structural Analysis of a Peptide Fragment of Transmembrane Transporter Protein Bilitranslocase ». PLoS ONE 7, no 6 (20 juin 2012) : e38967. http://dx.doi.org/10.1371/journal.pone.0038967.

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Delneri, A., R. Franca, M. Terdoslavich, S. Montanič, V. Čurin Šerbec, F. Tramer, M. Francese et S. Passamonti. « Identification and Functional Characterization of Bilitranslocase in Sea-Bass (Dicentrarchus labrax) Hepatopancreas ». Analytical Letters 44, no 18 (décembre 2011) : 2887–900. http://dx.doi.org/10.1080/00032719.2011.582548.

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Brandoni, Anabel, Gisela Di Giusto, Raffaella Franca, Sabina Passamonti et Adriana M. Torres. « Expression of Kidney and Liver Bilitranslocase in Response to Acute Biliary Obstruction ». Nephron Physiology 114, no 4 (2010) : p35—p40. http://dx.doi.org/10.1159/000276588.

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Terdoslavich, Michela, Inge de Graaf, Johannes Proost, Alessandra Cocolo, Sabina Passamonti et Geny Groothuis. « Bilitranslocase is Involved in the Uptake of Bromosulfophthalein in Rat and Human Liver ». Drug Metabolism Letters 6, no 3 (1 mars 2013) : 165–73. http://dx.doi.org/10.2174/1872312811206030003.

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Martinčič, R., K. Venko, Š. Župerl et M. Novič. « Chemometrics approach for the prediction of structure–activity relationship for membrane transporter bilitranslocase ». SAR and QSAR in Environmental Research 25, no 11 (22 octobre 2014) : 853–72. http://dx.doi.org/10.1080/1062936x.2014.962082.

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Ziberna, L., M. Lunder, F. Tramer, G. Drevenšek et S. Passamonti. « The endothelial plasma membrane transporter bilitranslocase mediates rat aortic vasodilation induced by anthocyanins ». Nutrition, Metabolism and Cardiovascular Diseases 23, no 1 (janvier 2013) : 68–74. http://dx.doi.org/10.1016/j.numecd.2011.02.005.

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Nicolin, Vanessa, Vittorio Grill, Fulvio Micali, Paola Narducci et Sabina Passamonti. « Immunolocalisation of bilitranslocase in mucosecretory and parietal cells of the rat gastric mucosa ». Journal of Molecular Histology 36, no 1-2 (février 2005) : 45–50. http://dx.doi.org/10.1007/s10735-004-2920-0.

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Choudhury, Amrita Roy, Emilia Sikorska, Johannes van den Boom, Peter Bayer, Łukasz Popenda, Kosma Szutkowski, Stefan Jurga et al. « Structural Model of the Bilitranslocase Transmembrane Domain Supported by NMR and FRET Data ». PLOS ONE 10, no 8 (20 août 2015) : e0135455. http://dx.doi.org/10.1371/journal.pone.0135455.

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Karawajczyk, Anna, Viktor Drgan, Nevenka Medic, Ganiyu Oboh, Sabina Passamonti et Marjana Novič. « Properties of flavonoids influencing the binding to bilitranslocase investigated by neural network modelling ». Biochemical Pharmacology 73, no 2 (janvier 2007) : 308–20. http://dx.doi.org/10.1016/j.bcp.2006.09.024.

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Venko, Katja, A. Roy Choudhury et Marjana Novič. « Computational Approaches for Revealing the Structure of Membrane Transporters : Case Study on Bilitranslocase ». Computational and Structural Biotechnology Journal 15 (2017) : 232–42. http://dx.doi.org/10.1016/j.csbj.2017.01.008.

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Vanzo, Andreja, Michela Terdoslavich, Anabel Brandoni, Adriana M. Torres, Urska Vrhovsek et Sabina Passamonti. « Uptake of grape anthocyanins into the rat kidney and the involvement of bilitranslocase ». Molecular Nutrition & ; Food Research 52, no 10 (octobre 2008) : 1106–16. http://dx.doi.org/10.1002/mnfr.200700505.

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Elias, M. M., G. C. Lunazzi, S. Passamonti, B. Gazzin, M. Miccio, G. Stanta, G. L. Sottocasa et C. Tiribelli. « Bilitranslocase localization and function in basolateral plasma membrane of renal proximal tubule in rat ». American Journal of Physiology-Renal Physiology 259, no 4 (1 octobre 1990) : F559—F564. http://dx.doi.org/10.1152/ajprenal.1990.259.4.f559.

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Bilirubin and phthalein dyes are taken up by the liver via a carrier-mediated mechanism operated at least in part by bilitranslocase (BTL). Because they also undergo renal transport, the presence and function of BTL was investigated in rat renal tubular plasma membrane vesicles. Transport of sulfobromophthalein (BSP) was enriched in basolateral domain of plasma membrane and followed the distribution pattern of Na(+)-K(+)-ATPase but not of gamma-glutamyltransferase. BSP uptake was inhibited by addition of monospecific antibodies raised against hepatic BTL. As in liver vesicles, BSP transport was electrogenic, being greatly accelerated by addition of valinomycin in presence of an inwardly directed K+ gradient. Apparent Km of BSP transport was 17 +/- 2 microM (n = 3 expts), one order of magnitude higher than that measured in liver; however, Vmax was similar to that described in liver vesicles (429 +/- 18 nmol BSP.mg protein-1.min-1, n = 3 expts). Competitive inhibition was observed with both unconjugated bilirubin (Ki, 2.9 +/- 0.2 microM) and rifamycin SV (Ki, 76 +/- 10 microM), known competitors for hepatic BTL-mediated transport of BSP. Immunoblotting studies with anti-BTL monospecific antibodies revealed presence of a single positive band only in basolateral-enriched membrane fraction; its apparent molecular mass was 37 kDa, virtually identical to that of hepatic protein. Immunohistochemistry confined presence of BTL to renal proximal tubules (RPT) We conclude that BTL is present in basolateral plasma membrane of RPT cells. Lower affinity of renal, compared with hepatic protein, for substrates might explain the marginal role of kidney in plasma clearance of bilirubin and cholephilic dyes.
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Maestro, A., M. Terdoslavich, A. Vanzo, A. Kuku, F. Tramer, V. Nicolin, F. Micali, G. Decorti et S. Passamonti. « Expression of bilitranslocase in the vascular endothelium and its function as a flavonoid transporter ». Cardiovascular Research 85, no 1 (25 août 2009) : 175–83. http://dx.doi.org/10.1093/cvr/cvp290.

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Passamonti, Sabina, Michela Terdoslavich, Alja Margon, Alessandra Cocolo, Nevenka Medic, Fulvio Micali, Giuliana Decorti et Mladen Franko. « Uptake of bilirubin into HepG2 cells assayed by thermal lens spectroscopy. Function of bilitranslocase ». FEBS Journal 272, no 21 (novembre 2005) : 5522–35. http://dx.doi.org/10.1111/j.1742-4658.2005.04949.x.

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Rodilla-Sala, E., G. C. Lunazzi, W. Stremmel et C. Tiribelli. « BSP-bilirubin binding protein, fatty acid binding protein and bilitranslocase are immunological distinct proteins ». Journal of Hepatology 11 (janvier 1990) : S53. http://dx.doi.org/10.1016/0168-8278(90)91545-8.

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Peresson, Carlo, Elisa Petrussa, Antonio Filippi, Federica Tramer, Sabina Passamonti, Uros Rajcevic, Sendi Montanič et al. « Involvement of mammalian bilitranslocase-like protein(s) in chlorophyll catabolism of Pisum sativum L. tissues ». Journal of Bioenergetics and Biomembranes 46, no 2 (9 février 2014) : 109–17. http://dx.doi.org/10.1007/s10863-014-9539-y.

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Battiston, Lucia, Sabina Passamonti, Annalisa Macagno et Gian Luigi Sottocasa. « The Bilirubin-Binding Motif of Bilitranslocase and Its Relation to Conserved Motifs in Ancient Biliproteins ». Biochemical and Biophysical Research Communications 247, no 3 (juin 1998) : 687–92. http://dx.doi.org/10.1006/bbrc.1998.8868.

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Torres, A. M., G. C. Lunazzi, W. Stremmel et C. Tiribelli. « Bilitranslocase and sulfobromophthalein/bilirubin-binding protein are both involved in the hepatic uptake of organic anions. » Proceedings of the National Academy of Sciences 90, no 17 (1 septembre 1993) : 8136–39. http://dx.doi.org/10.1073/pnas.90.17.8136.

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Passamonti, Sabina, Alessandra Cocolo, Enrico Braidot, Elisa Petrussa, Carlo Peresson, Nevenka Medic, Francesco Macri et Angelo Vianello. « Characterization of electrogenic bromosulfophthalein transport in carnation petal microsomes and its inhibition by antibodies against bilitranslocase ». FEBS Journal 272, no 13 (24 juin 2005) : 3282–96. http://dx.doi.org/10.1111/j.1742-4658.2005.04751.x.

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Bertolini, A., C. Peresson, E. Petrussa, E. Braidot, S. Passamonti, F. Macri et A. Vianello. « Identification and localization of the bilitranslocase homologue in white grape berries (Vitis vinifera L.) during ripening ». Journal of Experimental Botany 60, no 13 (12 juillet 2009) : 3861–71. http://dx.doi.org/10.1093/jxb/erp225.

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Ziberna, Lovro, Jong-Hun Kim, Cyril Auger, Sabina Passamonti et Valérie Schini-Kerth. « Role of endothelial cell membrane transport in red wine polyphenols-induced coronary vasorelaxation : involvement of bilitranslocase ». Food & ; Function 4, no 10 (2013) : 1452. http://dx.doi.org/10.1039/c3fo60160a.

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Passamonti, Sabina, Lucia Battiston et Gian Luigi Sottocasa. « Arylsulfonylation of bilitranslocase in plasma membranes from rat liver enables to discriminate between natural and artificial substrates ». Biochimica et Biophysica Acta (BBA) - Biomembranes 1323, no 1 (janvier 1997) : 130–36. http://dx.doi.org/10.1016/s0005-2736(96)00181-2.

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Braidot, E., E. Petrussa, A. Bertolini, C. Peresson, P. Ermacora, N. Loi, M. Terdoslavich, S. Passamonti, F. Macrì et A. Vianello. « Evidence for a putative flavonoid translocator similar to mammalian bilitranslocase in grape berries (Vitis vinifera L.) during ripening ». Planta 228, no 1 (26 mars 2008) : 203–13. http://dx.doi.org/10.1007/s00425-008-0730-4.

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Torres, A. M., N. Kaplowitz et C. Tiribelli. « Role of BSP/Bilirubin Binding Protein and Bilitranslocase in Glutathione Uptake in Rat Basolateral Liver Plasma Membrane Vesicles ». Biochemical and Biophysical Research Communications 200, no 2 (avril 1994) : 1079–85. http://dx.doi.org/10.1006/bbrc.1994.1560.

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Passamonti, Sabina, Michela Terdoslavich, Raffaella Franca, Andreja Vanzo, Federica Tramer, Enrico Braidot, Elisa Petrussa et Angelo Vianello. « Bioavailability of Flavonoids : A Review of Their Membrane Transport and the Function of Bilitranslocase in Animal and Plant Organisms ». Current Drug Metabolism 10, no 4 (1 mai 2009) : 369–94. http://dx.doi.org/10.2174/138920009788498950.

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Trebucobich, Mara Soledad, María Herminia Hazelhoff, Alberto A. Chevalier, Sabina Passamonti, Anabel Brandoni et Adriana Mónica Torres. « Protein expression of kidney and liver bilitranslocase in rats exposed to mercuric chloride—A potential tissular biomarker of toxicity ». Toxicology Letters 225, no 2 (mars 2014) : 305–10. http://dx.doi.org/10.1016/j.toxlet.2013.11.022.

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Passamonti, Sabina, Lucia Battiston et Gian Luigi Sottocasa. « Bilitranslocase can exist in two metastable forms with different affinities for the substrates. Evidence from cysteine and arginine modification ». European Journal of Biochemistry 253, no 1 (avril 1998) : 84–90. http://dx.doi.org/10.1046/j.1432-1327.1998.2530084.x.

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Venko, Katja, et Marjana Novič. « An In Silico Approach for Assessment of the Membrane Transporter Activities of Phenols : A Case Study Based on Computational Models of Transport Activity for the Transporter Bilitranslocase ». Molecules 24, no 5 (27 février 2019) : 837. http://dx.doi.org/10.3390/molecules24050837.

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Phenols are the most abundant naturally accessible antioxidants present in a human normal diet. Since numerous beneficial applications of phenols as preventive agents in various diseases were revealed, the evaluation of phenols bioavailability is of high interest of researchers, consumers and drug manufacturers. The hydrophilic nature of phenols makes a cell membrane penetration difficult, which imply an alternative way of uptake via membrane transporters. However, the structural and functional data of membrane transporters are limited, thus the in silico modelling is really challenging and urgent tool in elucidation of transporter ligands. Focus of this research was a particular transporter bilitranslocase (BTL). BTL has a broad tissue expression (vascular endothelium, absorptive and excretory epithelia) and can transport wide variety of poly-aromatic compounds. With available BTL data (pKi [mmol/L] for 120 organic compounds) a robust and reliable QSAR models for BTL transport activity were developed and extrapolated on 300 phenolic compounds. For all compounds the transporter profiles were assessed and results show that dietary phenols and some drug candidates are likely to interact with BTL. Moreover, synopsis of predictions from BTL models and hits/predictions of 20 transporters from Metrabase and Chembench platforms were revealed. With such joint transporter analyses a new insights for elucidation of BTL functional role were acquired. Regarding limitation of models for virtual profiling of transporter interactions the computational approach reported in this study could be applied for further development of reliable in silico models for any transporter, if in vitro experimental data are available.
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Peyrol, Julien, Grégory Meyer, Philippe Obert, Olivier Dangles, Laurent Pechère, Marie-Josèphe Amiot et Catherine Riva. « Involvement of bilitranslocase and beta-glucuronidase in the vascular protection by hydroxytyrosol and its glucuronide metabolites in oxidative stress conditions ». Journal of Nutritional Biochemistry 51 (janvier 2018) : 8–15. http://dx.doi.org/10.1016/j.jnutbio.2017.09.009.

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Peyrol, J., G. Meyer, P. Obert, O. Dangles, L. Pechere, M. J. Amiot-Carlin et C. Riva. « Involvement of bilitranslocase and beta-glucuronidase in the vascular protection by hydroxytyrosol and its glucuronide metabolites in oxidative stress conditions ». Archives of Cardiovascular Diseases Supplements 10, no 2 (avril 2018) : 231. http://dx.doi.org/10.1016/j.acvdsp.2018.02.121.

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Passamonti, Sabina, et Gian Luigi Sottocasa. « The sulfhydryl groups responsible for bilitranslocase transport activity respond to the interaction of the carrier with bilirubin and functional analogues ». Biochimica et Biophysica Acta (BBA) - Biomembranes 1021, no 1 (janvier 1990) : 9–12. http://dx.doi.org/10.1016/0005-2736(90)90376-y.

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Szutkowski, Kosma, Emilia Sikorska, Iulia Bakanovych, Amrita Roy Choudhury, Andrej Perdih, Stefan Jurga, Marjana Novič et Igor Zhukov. « Structural Analysis and Dynamic Processes of the Transmembrane Segment Inside Different Micellar Environments—Implications for the TM4 Fragment of the Bilitranslocase Protein ». International Journal of Molecular Sciences 20, no 17 (26 août 2019) : 4172. http://dx.doi.org/10.3390/ijms20174172.

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The transmembrane (TM) proteins are gateways for molecular transport across the cell membrane that are often selected as potential targets for drug design. The bilitranslocase (BTL) protein facilitates the uptake of various anions, such as bilirubin, from the blood into the liver cells. As previously established, there are four hydrophobic transmembrane segments (TM1–TM4), which constitute the structure of the transmembrane channel of the BTL protein. In our previous studies, the 3D high-resolution structure of the TM2 and TM3 transmembrane fragments of the BTL in sodium dodecyl sulfate (SDS) micellar media were solved using Nuclear Magnetic Resonance (NMR) spectroscopy and molecular dynamics simulations (MD). The high-resolution 3D structure of the fourth transmembrane region (TM4) of the BTL was evaluated using NMR spectroscopy in two different micellar media, anionic SDS and zwitterionic DPC (dodecylphosphocholine). The presented experimental data revealed the existence of an α -helical conformation in the central part of the TM4 in both micellar media. In the case of SDS surfactant, the α -helical conformation is observed for the Pro258–Asn269 region. The use of the zwitterionic DPC micelle leads to the formation of an amphipathic α -helix, which is characterized by the extension of the central α -helix in the TM4 fragment to Phe257–Thr271. The complex character of the dynamic processes in the TM4 peptide within both surfactants was analyzed based on the relaxation data acquired on 15 N and 31 P isotopes. Contrary to previously published and present observations in the SDS micelle, the zwitterionic DPC environment leads to intensive low-frequency molecular dynamic processes in the TM4 fragment.
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Battiston, Lucia, Annalisa Macagno, Sabina Passamonti, Fulvio Micali et Gian Luigi Sottocasa. « Specific sequence-directed anti-bilitranslocase antibodies as a tool to detect potentially bilirubin-binding proteins in different tissues of the rat ». FEBS Letters 453, no 3 (23 juin 1999) : 351–55. http://dx.doi.org/10.1016/s0014-5793(99)00736-x.

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Roy Choudhury, Amrita, Andrej Perdih, Špela Župerl, Emilia Sikorska, Tom Solmajer, Stefan Jurga, Igor Zhukov et Marjana Novič. « Structural elucidation of transmembrane transporter protein bilitranslocase : Conformational analysis of the second transmembrane region TM2 by molecular dynamics and NMR spectroscopy ». Biochimica et Biophysica Acta (BBA) - Biomembranes 1828, no 11 (novembre 2013) : 2609–19. http://dx.doi.org/10.1016/j.bbamem.2013.06.006.

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Miccio, M., G. Baldini, V. Basso, B. Gazzin, G. C. Lunazzi, C. Tiribelli et G. L. Sottocasa. « Bilitranslocase is the protein responsible for the electrogenic movement of sulfobromophthalein in plasma membrane vesicles from rat liver : immunochemical evidence using mono- and poly-clonal antibodies ». Biochimica et Biophysica Acta (BBA) - Biomembranes 981, no 1 (mai 1989) : 115–20. http://dx.doi.org/10.1016/0005-2736(89)90088-6.

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Golijanin, Dragan J., Jonah Marshall, Allison Cardin, Eric A. Singer, Ronald W. Wood, Jay E. Reeder, Guan Wu, Jorge L. Yao, Sabina Passamonti et Edward M. Messing. « BILITRANSLOCASE (BTL) IS IMMUNOLOCALISED IN PROXIMAL AND DISTAL RENAL TUBULES AND ABSENT IN RENAL CORTICAL TUMORS ACCURATELY CORRESPONDING TO INTRAOPERATIVE NEAR INFRARED FLUORESCENCE (NIRF) EXPRESSION OF RENAL CORTICAL TUMORS USING INTRAVENOUS INDOCYANINE GREEN (ICG) ». Journal of Urology 179, no 4S (avril 2008) : 137. http://dx.doi.org/10.1016/s0022-5347(08)60394-8.

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Bogožalec Košir, Alexandra, Tjaša Lukan, Mateja Kukovec, Sendi Montanič, Vivijana Snoj, Vladka Čurin Šerbec et Uroš Rajčević. « New monoclonal antibodies against bilitranslocase as a diagnostic tool in determining the progress of clear cell renal cell carcinoma ». Slovenian Medical Journal 86, no 5-6 (28 juin 2017). http://dx.doi.org/10.6016/zdravvestn.1548.

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Background: Monoclonal antibodies (mAbs) are an important tool in diagnostics and research, especially when we are dealing with a protein marker of unknown primary structure as in the case of bilitranslocase (BTL). BTL is also expressed on kidney cells, where it acts as an organic anion transporter. We have shown earlier that there are differences in bilitranslocase expression in normal kidney cells versus early grade kidney cancer.Methods: We developed monoclonal antibodies against extra- and intra-cellular domains of bilitranslocase protein model. To also gain a deeper insight in bilitranslocase expression in clinical samples, we assessed BTL expression in different grades of clear cell kidney cell carcinoma (ccRCC).Results: Both new monoclonal antibodies bind to a protein in UOK171 cells but not in the negative control. Binding of mAb is specifc. mAb produced by cell line 2A9/2E9 (peptide 298–310; intracellular domain) is more suitable for immunohistochemical analyses as it gives stronger intensity of binding than mAb produced by cell line 11C9/2G9 (peptide 235–246; extracellular domain). Antibody 2A9/2E9 stains bilitranslocase in proximal renal tubules of normal kidneys but not in the surrounding stroma. Staining decreases in grade I compared to normal kidney, gradually increases in grades II and III, and decreases again in grade IV of ccRCC tissue.Conclusions: Our results show that these antibodies can be used in different immunoassays. Furthermore, specificity and afnity of our mAbs allowed us to use them in the analysis of progressive grades of clear cell renal cell carcinoma in a limited number of patients. Tus, mAbs developed here can be used as a diagnostic tool that could help distinguish between early and late grades of clear cell renal cell carcinoma.
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« Electrogenic sulfobromophthalein (BSP) movements mediated by bilitranslocase in liver plasma membrane vesicles ». Journal of Hepatology 1 (janvier 1985) : S133. http://dx.doi.org/10.1016/s0168-8278(85)80338-x.

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