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Published: 4 June 2021
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1

LAING, CHRISTOPHER JAMES. "Comparative Studies on Plasma Vitamin D Binding Protein." University of Sydney, 2000. http://hdl.handle.net/2123/359.

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The plasma vitamin D binding protein (DBP) is an a-glycoprotein, synthesised and secreted by the liver, which binds specifically vitamin D and its metabolites. The DBP molecule, has a single high affinity binding site for its ligands, and is present in blood in concentrations about 1000-fold greater than the sum of all its vitamin D ligands. Previous studies have not found any change in the concentration of DBP related to various derangements in mineral homeostasis. Therefore the general view is that DBP has a passive role in the physiology of vitamin D and its metabolites, and simply acts to solubilise and transport these hydrophobic ligands in the aqueous extracellular fluid. However, differences which have been described in its affinity for various vitamin D metabolites suggest that there have been evolutionary influences on the properties of this protein. Furthermore, plasma DBP concentration has been found to change in response to a number of physiological factors, such as changing sex steroid hormone secretion. The aim of the studies presented in this thesis was to investigate variation in the plasma concentration of the DBP in a range of vertebrate species, and in response to a variety of physiological factors. The results suggest that DBP may have an active role in regulating the bioavailability, and hence the utilisation and metabolism of its ligands. DBP concentration has traditionally been measured using immunological techniques. These techniques, although fast and simple, have a number of draw-backs which can be overcome by the use of assays which rely upon functional aspects of the DBP. A saturation binding assay was modified from those described previously. Using this technique, it was found that both the circulating concentration of the DBP and its affinity for 25-hydroxyvitamin D3 (25(OH)D3) varied significantly among a wide range of species of reptiles and birds. This variation did not reflect phylogenetic relationships among the study species, suggesting that the variation was more likely to be the result of selective pressure in response to individual ecological or physiological circumstance, rather than to random mutation. In support of this, both the plasma concentration of DBP, and its affinity for 25(OH)D3 were significantly associated with a number of ecological factors which might be considered to have some significance to vitamin D and calcium homeostasis. In addition, comparative binding data suggests that the ability of the DBP to bind 25-hydroxyvitamin D2 with equal affinity to 25(OH)D3 is an evolutionary innovation of mammalian vertebrates. In order to extend the idea of genetic variation in the concentration and affinity of plasma DBP, two strains of broiler (meat-type) chickens were studied. It was found that both the concentration and the affinity of plasma DBP for 25(OH)D3 was characteristic for each strain, emphasising the sensitivity of DBP to genetic variation. A number of factors have been found to modulate the genetically determined plasma concentration of DBP. Deficiencies of dietary protein and dietary energy, and variation in concentrations of sex steroids were found to affect the circulating concentration of DBP. However, species differences were still apparent, suggesting that the sensitivity of DBP to these physiological modifiers may have developed independently in different species, and may be secondary to genetic determinants of DBP properties. The plasma DBP concentration and specific binding affinity both determine the availability of its ligands for cellular uptake. It is likely that this process is complex, and involves a combination of protein mediated and non-mediated uptake events. This makes DBP a potentially important determinant of the biological actions of its ligands. The studies in this thesis have produced two main lines of argument supporting an active role for DBP in the regulation of vitamin D metabolism and utilisation. The first is that genetic variation in the properties of plasma DBP appears to be genetically determined, and is selected for, both at the between-species, and the within-species level, than it is to random mutation. Secondly, the ability of physiological and environmental factors to modify the circulating concentration of DBP suggests that this protein is responsive to homeostatic processes. It is proposed that DBP is an active regulator of the physiological economy of vitamin D and its metabolites by being itself regulated by a number of genetic and non-genetic factors.
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2

Robinson, Robert Charles. "Horse plasma vitamin D-binding protein : isolation and structural investigation." Thesis, University of British Columbia, 1990. http://hdl.handle.net/2429/30292.

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Vitamin D-binding protein (DBP) is an abundant serum protein, secreted by the liver, which transports vitamin D sterols and is part of an actin scavenging system. In this study, DBP was isolated from horse plasma in a highly reproducible, four step procedure: Affi-gel Blue affinity chromatography, gel filtration, hydroxy1apatite chromatography and anion exchange HPLC. 6-7 mg of DBP were obtained from 80 ml of plasma with a yield of 21-25%. The secondary structure of DBP was calculated from circular dichroism measurements to be 39% α-helix, 42% β-sheet and 19% random coil. A molecular mass of 53,000 ± 3,000 daltons was calculated from electrophoretic gels. Circular dichroism and fluorescence studies revealed that the disulphide bonds of DBP contribute substantial structural stabilization to the molecule with respect to thermal denaturation. Finally, acrylodan-labeled DBP was prepared. The fluorescence of this adduct was sensitive to the binding of actin and to the presence of dithiothreitol.
Science, Faculty of
Chemistry, Department of
Graduate
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3

Petrov, Brawnie Rebecca. "A New Role for Vitamin D Binding Protein in Bipolar Disorder." The Ohio State University, 2017. http://rave.ohiolink.edu/etdc/view?acc_num=osu1492642404941773.

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4

Göthe, Rosvall Ida. "Prevalence of two common vitamin D binding protein polymorphisms in a Swedish population." Thesis, Örebro universitet, Institutionen för hälsovetenskaper, 2016. http://urn.kb.se/resolve?urn=urn:nbn:se:oru:diva-51323.

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5

Kanan, Raed Mohammad. "Molecular genetics and biochemistry of vitamin D binding proteins in metabolic bone disease." Thesis, University of Newcastle Upon Tyne, 1999. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.287811.

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6

Otterbein, Ludovic R. "Etudes cristallographiques de l'actine et de la S100A6 humaine." Aix-Marseille 1, 2002. http://www.theses.fr/2002AIX11018.

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Dans la cellule eucaryote, l'actine est une protéine impliquée dans de nombreuses fonctions biologiques où elle joue un rôle dans la mobilité, la modification de l'aspect des cellules et dans la contraction musculaire. Nous avons déterminé la structure cristallographique de l'actine monomérique sous forme ADP à la résolution de 1,54 Å. Cette structure montre des changements conformationnels de la protéine lors de la libération du Pi du site catalytique. De plus, l'utilisation de la tétraméthylrhodamine-5-maléimide pour bloquer la polymérisation de l'actine permet dorénavant d'envisager la co-cristallisation de complexes de l'actine avec de nombreuses protéines qui interagissent avec celle-ci, mais qui contrairement à toutes celles étudiées jusqu'à présent ne permettent pas de prévenir sa polymérisation. Dans le muscle lisse, caldesmon, une protéine liant l'actine, joue un rôle important dans la régulation de la contraction musculaire. Cette protéine est régulée par des protéines liant le calcium, telles que la calmoduline et la S100A6. Nous avons déterminé les structures de la S100A6 avec et sans calcium. La liaison du calcium induit un large changement conformationnel ainsi qu'une modification des charges du dimère de S100A6 aboutissant à l'exposition de deux sites de liaison de cibles naturelles diamétralement opposés. Ces résultats permettent de classer la S100A6 et de manière plus globale les protéines S100 dans la famille des protéines "sensor" du calcium. La libération d'actine dans le flux sanguin peut être létal. Les structures de la "Vitamin D-binding protein" et de son complexe avec l'actine déterminées ici, apportent des informations importantes sur le rôle de l'actine dans le système de protection appelé "Actin-Scavenger System".
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7

Hasséssian, Harout. "A search for vitamin D dependent calcium binding proteins in the rat nervous system /." Thesis, McGill University, 1987. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=66112.

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8

KELLY, MICHAEL ALAN. "CHARACTERIZATION OF RECEPTORS AND BINDING PROTEINS FOR THE ACTIVE METABOLITES OF VITAMINS A AND D IN NORMAL AND RESISTANT CELLS (PRIMATE RESEARCH)." Diss., The University of Arizona, 1986. http://hdl.handle.net/10150/183919.

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Involvement of Cellular Retinoic Acid (CRABP) or Retinol (CRBP) Binding Proteins and 1,25-dihydroxyvitamin D₃ (1,25(OH)₂D₃) receptors in the response of cultured cells to retinoic acid and 1,25(OH)₂D₃ was examined. A new method for saturation analysis of CRABP and CRBP was applied to human tumors, human neuroblastoma cells, which retinoic acid causes to differentiate, and a bioselected subline resistant to retinoic acid. These data suggest that CRABP may not mediate cell differentiation by retinoic acid. In other studies, 1,25(OH)₂D₃ receptors and bioresponses were characterized in cultured primate cells. Rhesus monkey kidney cells (LLC-MK₂) were resistant to 1,25(OH)₂D₃-dependent induction of 25(OH)D-24-hydroxylase enzyme. The ED₅₀ in LLC-MK₂ cells was 10-100 fold higher than in other cultured cells. This resistance resulted from a low affinity receptor. Since the LLC-MK₂ variant receptor did not differ in size from the wild type rhesus 1,25(OH)₂D₃ receptor, (Mᵣ = 52 kDa) a subtle alteration in the receptor likely caused the decreased ligand affinity. Also of interest was the possible cellular resistance to 1,25(OH)₂D₃, in the owl monkey (Aotus trivurgatus), which generally occurs in new world primates. Owl monkey kidney (OMK) cells had the same content of receptors for 1,25(OH)₂D₃ and sensitivity to this hormone as cells from the rhesus monkey (old world primate). The ED₅₀ for induction of 24hydroxylase was 2-3 nM in both the OMK cells and the rhesus monkey fibroblasts. Both cells contained 2300 high affinity receptor molecules per cell, which bound DNA and were characterized by immunoblot as 52 kDa proteins. 1,25(OH)₂D₃ treatment increased the content of 1,25(OH)₂D₃ receptors in OMK cells, by increasing the synthesis of receptor mRNA. These data indicate the owl monkey is not resistant to 1,25(OH)₂D₃, unlike other new world primates. This finding was confirmed independently by demonstration that the owl monkey maintained mean serum 1,25(OH)₂D₃ levels (29 pg/ml) in the range of old world primates (33 pg/ml) and humans, in contrast to the elevated 1,25(OH)₂D₃ in other new world primates (97-129 pg/ml). This result suggests the alteration of 1,25(OH)₂D₃-endocrine dynamics in new world primates occurred subsequent to the evolutionary divergence of the owl monkey.
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9

Ousley, Amanda. "Engineering the human vitamin D receptor to bind a novel small molecule: investigating the structure-function relationship between human vitamin d receptor and various ligands." Diss., Georgia Institute of Technology, 2011. http://hdl.handle.net/1853/39580.

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The human vitamin D receptor (hVDR) is a member of the nuclear receptor superfamily, involved in calcium and phosphate homeostasis; hence implicated in a number of diseases, such as Rickets and Osteoporosis. This receptor binds 1α,25-dihydroxyvitamin D3 (also referred to as 1,25(OH)2D3) and other known ligands, such as lithocholic acid. Specific interactions between the receptor and ligand are crucial for the function and activation of this receptor, as implied by the single point mutation, H305Q, causing symptoms of Type II Rickets. In this work, further understanding of the significant and essential interactions between the ligand and the receptor were deciphered, through a combination of rational and random mutagenesis. A hVDR mutant, H305F, was engineered with increased sensitivity towards lithocholic acid, with an EC50 value of 10 µM and 40 + 14 fold activation in mammalian cell assays, while maintaining wild-type activity with 1,25(OH)2D3. Furthermore, via random mutagenesis, a hVDR mutant, H305F/H397Y, was discovered to bind a novel small molecule, cholecalciferol, a precursor in the 1α,25-dihydroxyvitamin D3 biosynthetic pathway, which does not activate wild-type hVDR. This variant, H305F/H397Y, binds and activates in response to cholecalciferol concentrations as low as 100 nM, with an EC50 value of 300 nM and 70 + 11 fold activation in mammalian cell assays.
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10

Reiswig, Jeffrey D. "Expression and regulation of vitamin D-dependent calcium binding proteins, calbindins, in the horse and cow female reproductive systems /." The Ohio State University, 1996. http://rave.ohiolink.edu/etdc/view?acc_num=osu1487942476405662.

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11

Coue, Martine. "Etude des effets de deux proteines associees a l'actine sur la polymerisation de l'actine." Paris 6, 1987. http://www.theses.fr/1987PA066318.

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L'etude des effets de deux proteines du serum, la gelsoline et de la proteine de liaison de la vitamine sur la polymerisation de l'actine a permis d'obtenir des informations: 1) sur le mecanisme d'action d'une proteine qui se fixe a un bout des filaments et qui les coupe et aussi d'une proteine qui se fixe uniquement au monomere d'actine 2) sur le mecanisme de la polymerisation au bout pointu des filaments d'actine. Ces resultats permettent de mieux envisager le role de la gelsoliune et la proteine de liaison de la vitamine d dans le serum
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12

Intrator, Sylvie. "Contribution à l'étude des cholécalcines 28k Da de rat, calcium-binding protein vitamine D-dépendante purification et caractérisation immunologique et biochimique." Grenoble 2 : ANRT, 1986. http://catalogue.bnf.fr/ark:/12148/cb37598447r.

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13

Intrator, Sylvie. "Contribution à l'étude des cholecalcines 28 kDa de rat (calcium-binding protein vitamine d-dépendante) : purification et caractérisation immunologique et biochimique." Paris 6, 1986. http://www.theses.fr/1986PA066263.

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14

McClelland, David Andrew. "The refolding of riboflavin binding protein." Thesis, University of Stirling, 1996. http://hdl.handle.net/1893/3408.

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Hen egg riboflavin binding protein (RfBP) acts as a source of riboflavin to the developing embryo. It is the most abundant vitamin binding protein in the egg white. Mutations giving rise to a lack of RfBP lead to embryo death at approximately 13 days. RfBP binds riboflavin tightly in a 1:1 ratio. On formation of this complex, the fluorescence of riboflavin is completely quenched; this quenching is thought to be due to the stacking of aromatic groups within the hydrophobic binding pocket. This quenching provides a convenient assay for the integrity of the riboflavin-binding site of the protein. RfBP consists of a single polypeptide chain of 219 amino acids of molecular mass 29.2 kDa. RfBP undergoes a number of post-translational modifications, namely: the formation of nine disulphide bonds, extensive glycosylation on Asn 36 and Asn 147, and the phosphorylation of eight serine side chains from between Ser 186 and Ser 197. The unfolding and refolding of RfBP was studied by denaturing in 6M guanidium chloride, followed by dilution in buffer, to start refolding. The processes were followed by both steady-state and stopped-flow circular dichroism and fluorescence spectroscopy. RfBP was found to readily unfold and refold, provided the disulphide bonds were intact. The regain of secondary structure was found to be too rapid to measure by the methods available (<12msec). The regain of tertiary structure was found to consist of 4 main phases, and a large proportion (80%) of the tertiary structure formed within 2 msec. The regain of riboflavin binding ability was complete at the end of the second phase, a reaction with a half-life of around 30 msec. In the presence and absence of riboflavin, the kinetics for the first 3 stages of tertiary structure changes seemed to be identical. In the presence of riboflavin, however, seemed to impede the completion of the final, very slow stage, with the refolding reaction only going to 95% completion. The dephosphorylation of the protein seemed to have no affect on this process. When the 9 disulphide bonds are reduced however, RfBP is unable to spontaneously reoxidise to a native-like state in the presence of an oxidised/reduced glutathione redox system. However, the addition of protein disulphide isomerase to the system increases significantly the yield of successfully reoxidised RfBP to about 50%. Attempts to prepare deglycosylated RfBP by chemical methods were unsuccessful since the treatment led to fragmentation of the polypeptide chain.
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15

Main, Ewan Ralph Gibson. "Studies on the immunosuppressant binding protein FKBP12 and the nuclear/steroid receptors vitamin D3 and oestrogen." Thesis, University of Cambridge, 2000. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.621749.

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16

Nishiyama, Akira. "Identification of thioredoxin-binding protein-2/vitamin D_3 up-regulated protein 1 as a nagative regulator of thioredoxin function and expression." Kyoto University, 1999. http://hdl.handle.net/2433/181259.

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17

Frey, Simone K. "Investigations on extra- and intracellular retinol-binding proteins." Phd thesis, Universität Potsdam, 2009. http://opus.kobv.de/ubp/volltexte/2009/3142/.

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The fat-soluble vitamin A, which is chemically referred to retinol (ROH), is known to be essential for the process of vision, the immune system but also for cell differentiation and proliferation. Recently, ROH itself has been reported to be involved in adipogenesis and a ROH transport protein, the retinol-binding protein 4 (RBP4), in insulin resistance and type 2 diabetes. However, there is still considerable scientific debate about this relation. With the increasing amount of studies investigating the relation of ROH in obesity and type 2 diabetes, basic research is an essential prerequisite for interpreting these results. This thesis enhances the knowledge on this relation by reviewing ROH metabolism on extra- and intracellular level. Aim 1: In the blood stream ROH is transported in a complex with RBP4 and a second protein, transthyretin (TTR), to the target cells. The levels of RBP4 and TTR are influenced by several factors but mainly by liver and kidney function. The reason for that is that liver and the kidneys are the sites of RBP4 synthesis and catabolism, respectively. Interestingly, obesity and type 2 diabetes involve disorders of the liver and the kidneys. Therefore the aim was to investigate factors that influence RBP4 and TTR levels in relation to obesity and type 2 diabetes (Part 1). Aim 2: Once arrived in the target cell ROH is bound to cellular retinol-binding protein type I (CRBP-I) and metabolised: ROH can either be stored as retinylesters or it can be oxidised to retinoic acid (RA). By acting as a transcription factor in the nucleus RA may influence processes such as adipogenesis. Therefore vitamin A has been postulated to be involved in obesity and type 2 diabetes. CRBP-I is known to mediate the storage of ROH in the liver, but the extra-hepatic metabolism and the functions of CRBP-I are not well known. This has been investigated in Part 2 of this work. Material & Methods: RBP4 and TTR levels were investigated by ELISA in serum samples of human subjects with overweight, type 2 diabetes, kidney or liver dysfunction. Molecular alterations of the RBP4 and TTR protein structure were analysed by MALDI-TOF mass spectrometry. The functions of intracellular CRBP-I were investigated in CRBP-I knock-out mice in liver and extra-hepatic tissues by measuring ROH levels as well as the levels of its storage form, the retinylesters, using reverse phase HPLC. The postprandial uptake of ROH into tissues was analysed using labelled ROH. The mRNA levels of enzymes that metabolize ROH were examined by real-time polymerase chain reaction (RCR). Results: The previous published results showing increased RBP4 levels in type 2 diabetic patients could not be confirmed in this work. However, it could be shown that during kidney dysfunction RBP4 levels are increased and that RBP4 and TTR levels are decreased during liver dysfunction. The important new finding of this work is that increased RBP4 levels in type 2 diabetic mice were increased when kidney function was decreased. Thus an increase in RBP4 levels in type 2 diabetes may be the effect of a reduced kidney function which is common in type 2 diabetes. Interestingly, during severe kidney dysfunction the molecular structure of RBP4 and TTR was altered in a specific manner which was not the case during liver diseases and type 2 diabetes. This underlines the important function of the kidneys in RBP4 metabolism. CRBP-I has been confirmed to be responsible for the ROH storage in the liver since CRBP-I knock-out mice had decreased ROH and retinylesters (the storage form of ROH) levels in the liver. Interestingly, in the adipose tissue (the second largest ROH storage tissue in the body) ROH and retinylesters levels were higher in the CRBP-I knock-out compared to the wild-type mice. It could be shown in this work that a different ROH binding protein, cellular retinol-binding protein type III, is upregulated in CRBP-I knock-out mice. Moreover enzymes were identified which mediate very efficiently ROH esterification in the adipose tissue of the knock-out mice. In the pancreas there was a higher postprandial ROH uptake in the CRBP-I knock-out compard to wild-type mice. Even under a vitamin A deficient diet the knock-out animals had ROH and retinylesters levels which were comparable to wild-type animals. These results underline the important role of ROH for insulin secretion in the pancreas. Summing up, there is evidence that RBP4 levels are more determined by kidney function than by type 2 diabetes and that specific molecular modifications occur during kidney dysfunction. The results in adipose tissue and pancreas of CRBP-I knock-out mice support the hypothesis that ROH plays an important role in glucose and lipid metabolism.
Vitamin A gehört zur Gruppe der fettlöslichen Vitamine und wird chemisch als Retinol bezeichnet. Es ist essentiell für den Prozess des Sehvorgangs und der Zelldifferenzierung und kann daher bestimmte Entwicklungsprozesse wie die Bildung des Fettgewebes beeinflussen. Aufgrund seiner Fettlöslichkeit muss Retinol im Blut (= extrazellulär) sowie in der Zelle (= intrazellulär) an sogenannte Transport-Moleküle, die Retinol-bindenden Proteine (RBPs) gebunden werden. Die zwei bekanntesten Vertreter der RBPs sind das Retinol-bindende Protein 4 (RBP4) und das intrazelluläre Retinol-bindende Protein Typ I (CRBP-I). RBP4 transportiert Vitamin A im Blut von der Leber zur Zielzelle und zum Abbauorgan für Vitamin A, der Niere. CRBP-I ist in der Leber für die Speicherung von Vitamin A zuständig. In den letzten Jahren wurden neben der Beteiligung des Retinols an der Bildung des Fettgewebes auch Studien veröffentlicht, in denen ein Zusammenhang zwischen erhöhten RBP4-Werte im Blut und Typ-2-Diabetes gezeigt wurde. Bis heute ist der mögliche Zusammenhang zwischen RBP4, CRBP-I und Übergewicht nicht ausreichend erforscht. Im ersten Teil der Arbeit war daher das Ziel, Einflussfaktoren, die zu Veränderungen der RBP4-Werte im Blut führen können, zu untersuchen. Dazu wurden Blutproben von Personen mit Übergewicht und/oder Typ-2-Diabetes und Patienten mit Nierenfunktionsstörungen oder mit Leberfunktionsstörungen analysiert. Es konnte gezeigt werden, dass bereits geringe Nierenfunktionsstörungen zu erhöhten RBP4-Konzentrationen im Blut führten. Bei Typ-2-Diabetikern, die sehr oft an Nierenfunktionsstörungen leiden, war eine Erhöhung der RBP4-Konzentration mit einer Abnahme der Nierenfunktion verbunden. Somit lässt sich zusammenfassen, dass nicht Typ-2-Diabetes sondern vielmehr die dabei auftretenden Nierenfunktionsstörungen zu einer Erhöhung der RBP4-Werte führen. Bei Lebererkrankten konnte ein Absinken der RBP4-Werte nachgewiesen werden, was der verminderten Bildung von RBP4 in der Leber bei diesen Patienten zuzuschreiben ist. Im zweiten Teil sollte der Frage nachgegangen werden, wie Retinol intrazellulär verstoffwechselt wird. Dabei lag der Fokus auf der Erforschung der bisher nicht bekannten Funktionen von CRBP-I im Fettgewebe und der Bauchspeicheldrüse. Zur Untersuchung der Funktionen von CRBP-I wurden Mäuse gezüchtet, bei denen das Gen für CRBP-I gelöscht wurde. Da CRBP-I für die Speicherung von Vitamin A in der Leber verantwortlich ist, zeigen diese Mäuse sehr geringe Vitamin-A-Speicher in der Leber. Das gleiche zeigte sich für die Bauchspeicheldrüse, die für die Sekretion von Insulin Vitamin A benötigt: In den Mäusen ohne CRBP-I waren die Retinol-Werte drastisch gesunken. Interessanterweise zeigte sich im Fettgewebe ein gegenteiliges Bild: Die Konzentrationen an Retinol und dessen Speicher waren in den Mäusen ohne CRBP-I höher im Vergleich zu den normalen Mäusen. Mit bestimmten Nachweismethoden konnte herausgefunden werden, dass Retinol im Fettgewebe an ein anderes RBP, das CRBP-III, gebunden wird und dadurch effektiver gespeichert werden kann als durch CRBP-I.
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18

Gliniak, Christy M. "The Role of the Retinol-Binding Protein Receptor STRA6 in Regulation of Diurnal Insulin Responses." Case Western Reserve University School of Graduate Studies / OhioLINK, 2017. http://rave.ohiolink.edu/etdc/view?acc_num=case1495817057084695.

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19

Dietzen, Matthias Michael [Verfasser], and Thomas [Akademischer Betreuer] Lengauer. "Modeling protein interactions in protein binding sites and oligomeric protein complexes / Matthias Michael Dietzen. Betreuer: Thomas Lengauer." Saarbrücken : Saarländische Universitäts- und Landesbibliothek, 2014. http://d-nb.info/1063330718/34.

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20

Angelo, Giana. "The role of heat shock protein 90 in the molecular mechanism of vitamin D action /." Thesis, Connect to Dissertations & Theses @ Tufts University, 2005.

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Thesis (Ph.D.)--Tufts University, 2005.
Adviser: Richard J. Wood. Submitted to the School of Nutrition Science and Policy. Includes bibliographical references. Access restricted to members of the Tufts University community. Also available via the World Wide Web;
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21

Juntunen, K. (Kari). "Functional and structural characterization of nuclear vitamin D receptor and its ligand binding domain." Doctoral thesis, University of Oulu, 2002. http://urn.fi/urn:isbn:9514268784.

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Abstract The hormonally active form of vitamin D, 1,25(OH)2D3, is involved in many biological functions throughout the body, such as regulation of calcium and phosphate homeostasis, bone remodeling and controlling cell proliferation and differentiation. Vitamin D receptor (VDR), a member of the nuclear hormone receptor (NHR) super family, mediates those genomic actions of 1,25 (OH)2D3 by actively repressing or activating its target genes. In the present study recombinant human nuclear VDR and its ligand binding domain (LBD) were expressed in Spodoptera frugiperda (Sf9) insect cells and in E.coli. Recombinant proteins were purified and their biochemical and biophysical properties were characterized. Recombinant VDR was shown to bind to the vitamin D response element (VDRE) of osteopontin and osteocalcin genes as a homodimer or as a heterodimer with the retinoid X receptor (RXR)-αΔAB. Full-length VDR and its LBD were demonstrated to bind natural ligand 1,25 (OH)2D3 with high affinity. The binding affinities of several vitamin D analogs were also determined. Ligand binding induced conformational change within the receptor was studied using several methods such as partial proteolytic digestion, small angle neutron scattering (SANS), native gel electrophoresis and circular dichroism (CD) spectroscopy. Results indicate that ligand binding induces conformational change within VDR and different 1,25(OH)2D3 analogs might induce a somewhat different conformation within the receptor. This is seen as an unequal capacity of analogs to stabilize receptor against proteases or heat and as differences in the promotion of receptor homodimerization. Compared to other nuclear hormone receptors, VDR presents a large insertion region at the N-terminal part of the LBD between helices H1 and H3, encoded by an additional exon. In the present study this additional exon was deleted and the properties of mutated LBD were compared to the wild type LBD. Biochemical analyses indicated that the mutant protein exhibits the same ligand binding, dimerization with RXR and transactivation properties as the wild-type VDR, suggesting that the insertion region does not affect these main functions. Furthermore, solution studies by small angle X-ray scattering indicated that the insertion region in the VDR locates on the surface of molecule and it is not structurally well ordered.
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22

Semenova, Ekaterina M. "Vitamin A and the retina : investigation of retinol delivery systems and retinol interactions with IRBP (interphotoreceptor retinoid-binding protein)." Thesis, University of Strathclyde, 2003. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.275194.

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23

Bass, Joseph. "The role of the vitamin D receptor in skeletal muscle protein metabolism." Thesis, University of Nottingham, 2017. http://eprints.nottingham.ac.uk/40166/.

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24

Zinnall, Ulrike [Verfasser]. "Functional characterization of the RNA-binding protein HDLBP / Ulrike Zinnall." Berlin : Humboldt-Universität zu Berlin, 2021. http://d-nb.info/1241116946/34.

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25

Sumiya, Michiko. "The XylF D-xylose binding protein transport system in Escherichia coli." Thesis, University of Cambridge, 1989. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.315994.

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26

Witcher, Michael. "Interaction of the anti-apoptotic protein BAG-1 with the vitamin D receptor." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1999. http://www.collectionscanada.ca/obj/s4/f2/dsk1/tape7/PQDD_0010/MQ52698.pdf.

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27

Simboli-Campbell, Maura E. "The role of protein kinase C in vitamin D-mediated effects in kidney." Thesis, University of Ottawa (Canada), 1993. http://hdl.handle.net/10393/6608.

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The role of the calcium/phospholipid-dependent serine/threonine kinase Protein Kinase C (PKC), in the effects of vitamin D on kidney was studied. Madin Darby Bovine Kidney (MDBK) cells, a normal epithelial-like cell line, were found to express the Vitamin D Receptor (VDR) and the vitamin D-dependent calcium binding protein Calbindin D-28K (CaBP D-28K). In MDBK cells, 1,25(OH)$\sb2\rm D\sb3$ increased PKC activity in a time- and dose-dependent manner as measured by two different phosphorylation assays. This activation appeared to result from translocation of PKC from the cytosol to the membrane and was accompanied by an increase in immunoreactive PKC in the membrane. PKC was also activated by short term exposure of MDBK cells to TPA, whereas PKC activity was completely down-regulated by long term exposure to TPA. Down-regulation of PKC activity was accompanied by a loss of immunoreactive PKC. The phorbol ester analogue 4$\alpha$PDD had no effect on PKC activity or amount. Concurrent with activation of PKC 1,25(OH)$\sb2\rm D\sb3$ homologously up-regulated the VDR and increased total immunoreactive CaBP D-28K in MDBK cells. In contrast, down-regulation of PKC activity in TPA treated cells was associated with decreased expression of the VDR and CaBP D-28K. The phorbol ester analogue 4$\alpha$PDD, which had no effect on PKC, did not affect the expression of the VDR or CaBP D-28K. Short term TPA treatment, which activated PKC, increased CaBP D-28K without altering VDR levels. The divergent effects of 1,25(OH)$\sb2\rm D\sb3$ and TPA were associated with differential regulation of PKC isozymes. Treatment of MDBK cells with 1,25(OH)$\sb2\rm D\sb3$ increased membrane association of PKC $\alpha,$ induced nuclear translocation of PKC $\beta$ and had no effect on PKC $\zeta.$ In contrast, long term treatment of MDBK cells with TPA induced down-regulation of PKC $\alpha,$ nuclear translocation of PKC $\beta,$ and decreased PKC $\zeta.$ Nuclear translocation of PKC $\beta$ by 1,25(OH)$\sb2\rm D\sb3$ treatment was accompanied by an increase in phosphorylation of endogenous nuclear proteins. However nuclear translocation of PKC $\beta$ by TPA treatment did not affect phosphorylation of endogenous nuclear proteins. The data have been incorporated into a model based on the hypothesis that the VDR could be a nuclear substrate for PKC $\beta$ and CaBP D-28K could be a cytosolic substrate for PKC $\alpha.$ This model predicts a novel role for PKC-dependent phosphorylations in the renal actions of 1,25(OH)$\sb2\rm D\sb3.$
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Lu, Cheng [Verfasser], and Gerhard [Akademischer Betreuer] Stock. "Modeling protein dynamics in solution: effects of ligand binding and crowding." Freiburg : Universität, 2016. http://d-nb.info/1119452643/34.

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29

Kiesel, Anja Sophie [Verfasser], and Johannes [Akademischer Betreuer] Söding. "Understanding protein-DNA binding events / Anja Sophie Kiesel ; Betreuer: Johannes Söding." München : Universitätsbibliothek der Ludwig-Maximilians-Universität, 2017. http://d-nb.info/1148276823/34.

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Schneider, Sebastian [Verfasser], Martin [Akademischer Betreuer] Zacharias, and Iris [Akademischer Betreuer] Antes. "Solvation of protein binding sites and optimisation of protein-protein complex prediction / Sebastian Schneider. Gutachter: Martin Zacharias ; Iris Antes. Betreuer: Martin Zacharias." München : Universitätsbibliothek der TU München, 2012. http://d-nb.info/1024567486/34.

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31

Engelke, Hanna C. "Coagulation protein FVIII binding to phospholipid membranes investigated by fluorescence correlation spectroscopy." Diss., kostenfrei, 2010. http://d-nb.info/1001732685/34.

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32

Hesse, Martina [Verfasser]. "Characterization of the binding properties of the Avian Coronavirus spike protein / Martina Hesse." Hannover : Bibliothek der Tierärztlichen Hochschule Hannover, 2015. http://d-nb.info/1073850358/34.

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33

Shinaberger, Christian S. "Hemodialysis patients-relationships with dietary protein and vitamin D dosage and impact on patient survival." Diss., Restricted to subscribing institutions, 2008. http://proquest.umi.com/pqdweb?did=1666908801&sid=1&Fmt=2&clientId=1564&RQT=309&VName=PQD.

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34

Wong, Kevin L. "Caveolae and Caveolin-1 are important for Vitamin D signalling." Thesis, Georgia Institute of Technology, 2010. http://hdl.handle.net/1853/37086.

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The most active form of Vitamin D, 1alpha,25(OH)2D3, modulates cells via receptor mediated mechanisms. While studies have elucidated the pathway via the classical nuclear Vitamin D Receptor (VDR), little is known about the membrane-associated Vitamin D Receptor (ERp60). Caveolae and its characteristic protein Caveolin-1 have been involved in many signaling pathways due to its specific structure and physical configuration. Other studies have shown that many components of the Vitamin D pathway have been found in caveolae. This study hypothesizes that caveolae and Caveolin-1 are important for the effects of 1,25 Vitamin D signaling via ERp60. Research up to date have shown that in rat and mouse growth zone chondrocytes, cells deprived of intact caveolae either through disruption through beta-Cyclodextrin or genetic knockout do not exhibit the characteristic responses to Vitamin D through ERp60 when compared to chondrocytes with functional caveolae. Studies using immunofluorescence co-localization and caveolae fractionation have shown that ERp60 is localized in the caveolae domains. Cellular fractionation was also performed to examine the localization of the ERp60 receptor in lipid rafts and caveolae. Histology and transmission electron microscopy were also used to examine the physiological importance of caveolae and Caveolin-1 in growth plate morphology and cellular characteristics.
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35

Kunstmann, Ruth Sonja [Verfasser], and Robert [Akademischer Betreuer] Seckler. "Design of a high-affinity carbohydrate binding protein / Ruth Sonja Kunstmann ; Betreuer: Robert Seckler." Potsdam : Universität Potsdam, 2017. http://d-nb.info/1218402830/34.

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Renner, Sonja [Verfasser], and Christian [Akademischer Betreuer] Haass. "Identification of ADAM10 5`UTR binding proteins : the RNA-binding protein Unr is involved in ADAM10 mRNA stability / Sonja Renner. Betreuer: Christian Haass." München : Universitätsbibliothek der Ludwig-Maximilians-Universität, 2014. http://d-nb.info/1053618514/34.

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Monroy, Ordoñez Elsa Beatriz [Verfasser], and Lutz [Akademischer Betreuer] Hein. "MicroRNAs regulate MeCP2, a methyl CpG binding protein, in the heart = MicroRNAs regulieren MeCP2, ein Methyl CpG bindendes Protein, im Herz." Freiburg : Universität, 2012. http://d-nb.info/1123474346/34.

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38

Schnell, David M. "VITAMIN D WORKS THROUGH THE LIPID DROPLET PROTEIN PLIN2 TO AUGMENT MITOCHONDRIAL FUNCTION IN SKELETAL MUSCLE." UKnowledge, 2018. https://uknowledge.uky.edu/pharmacol_etds/23.

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Vitamin D has been connected with increased intramyocellular lipid (IMCL) mitochondrial function in skeletal muscle. It is also shown to prevent lipotoxicity in several tissues, but this has not yet been examined in skeletal muscle. Perilipin 2 (PLIN2), a lipid droplet protein upregulated with vitamin D treatment, is integral to managing IMCL capacity and lipid oxidation in skeletal muscle. Increased lipid storage and oxidation is associated with increased tolerance to a hyperlipidic environment and resistance to lipotoxicity. Therefore, I hypothesized that vitamin D increases β-oxidation and lipid turnover though a PLIN2 mediated mechanism, thereby preventing lipotoxicity. This hypothesis was divided into two specific aims: 1) Characterize the effect of vitamin D and PLIN2 on lipid turnover and β-oxidation in mature myotubes, and 2) Determine the role of vitamin D and PLIN2 in regulating key markers of lipotoxicity. To address these aims, cells were treated with or without vitamin D, palmitate, and PLIN2 siRNA in an eight group, 2x2x2 design. Key experiments included quantitative real time polymerase chain reaction for markers of lipid accumulation, lipolysis, and lipotoxicity; Seahorse oxygen consumption assay; 14C-palmitate oxidation assay; and analyses of lipid accumulation and profile. Failure of the palmitate treatment to produce a reliable model for lipotoxicity resulted in negative data for Aim 2 of this dissertation and a focus on vitamin D and PLIN2 knockdown treatments as a four group, 2x2 model. Aim 1 showed that vitamin D reliably increases markers of lipolysis and lipid accumulation. Most of these markers were in turn decreased after PLIN2 knockdown, and DGAT2 exhibited an interaction effect between the two treatments. Contrary to our hypothesis and some published research, PLIN2 knockdown did not prevent lipid accumulation. Vitamin D increased oxygen consumption, especially consumption driven by mitochondrial complex II. PLIN2 knockdown decreased oxygen consumption and demonstrated an interaction effect specific to mitochondrial complex II. Data in this dissertation show that vitamin D increases mitochondrial function, and these effects are at least in part accomplished through a PLIN2 mediated mechanism. However, this work lacks the data required to make specific claims regarding β-oxidation and lipid turnover. This research is some of the first to show that PLIN2 knockdown carries negative impacts for skeletal muscle mitochondria and makes valuable contributions to general knowledge of how vitamin D and lipid storage impact muscle health and function. This ultimately provides additional evidence to advocate for vitamin D supplementation as a means of improving musculoskeletal health and function. Future research should investigate how vitamin D and PLIN2 impact markers of lipotoxicity in skeletal muscle.
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39

Kühnert, Julia [Verfasser], and Thomas [Akademischer Betreuer] Dobner. "SUMO-modification of the RNA-binding protein La enhances its binding to the translational start site of cyclin D1 / Julia Kühnert. Betreuer: Thomas Dobner." Hamburg : Staats- und Universitätsbibliothek Hamburg, 2013. http://d-nb.info/1030365970/34.

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Pleß, Ole [Verfasser], Achim [Gutachter] Leutz, Klaus [Gutachter] Scheidereit, and Thomas [Gutachter] Sommer. "Identifikation und Charakterisierung von Protein-Interaktionspartnern des Transkriptionsfaktors CCAAT/Enhancer Binding Protein beta / Ole Pleß ; Gutachter: Achim Leutz, Klaus Scheidereit, Thomas Sommer." Berlin : Humboldt-Universität zu Berlin, 2008. http://d-nb.info/1208078852/34.

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41

Krotzky, Timo [Verfasser], and Gerhard [Akademischer Betreuer] Klebe. "Methods for the Efficient Comparison of Protein Binding Sites and for the Assessment of Protein-Ligand Complexes / Timo Krotzky. Betreuer: Gerhard Klebe." Marburg : Philipps-Universität Marburg, 2015. http://d-nb.info/1076865607/34.

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42

Lim, Boon-Leong. "Cloning and expression of a C1q-binding protein and two of the collections (Collectin-43 and lung surfactant protein D)." Thesis, University of Oxford, 1994. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.239328.

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43

Vasile, Alexandra Iulia [Verfasser]. "Functional characterization of Pseudouridine synthase I and Y-box-binding protein 3 / Alexandra Iulia Vasile." Berlin : Freie Universität Berlin, 2016. http://d-nb.info/1099952220/34.

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44

Schacht, Teresa [Verfasser]. "Neuronal calcium-binding protein 2 (NECAB2): Charakterisierung eines striatalen Ca 2+ -bindenden Proteins / Teresa Schacht." Mainz : Universitätsbibliothek Mainz, 2017. http://d-nb.info/1141937689/34.

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45

Tisserant, Anne. "Analysis of the molecular basis underlying signal regulated splicing via the RNA binding protein Sam68." Karlsruhe Forschungszentrum Karlsruhe, 2007. http://d-nb.info/98506823X/34.

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46

Siebert, Matthias [Verfasser], and Johannes [Akademischer Betreuer] Söding. "Quantitative modeling and statistical analysis of protein-DNA binding sites / Matthias Siebert ; Betreuer: Johannes Söding." München : Universitätsbibliothek der Ludwig-Maximilians-Universität, 2016. http://d-nb.info/113104049X/34.

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47

Krapp, Christian [Verfasser]. "Guanylate binding protein 5 is an interferon-inducible inhibitor of HIV-1 infectivity / Christian Krapp." Ulm : Universität Ulm. Medizinische Fakultät, 2016. http://d-nb.info/1084767775/34.

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48

Lutzenberger, Manuel [Verfasser]. "Die Rolle von CCAAT/enhancer-binding protein delta (C/EBPD) in neurodegenerativen Erkrankungen / Manuel Lutzenberger." Berlin : Medizinische Fakultät Charité - Universitätsmedizin Berlin, 2016. http://d-nb.info/1084634228/34.

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49

Dunham, Shari Uldrich 1970. "Platinum-modified DNA : solution structure and protein-binding preferences of 1,2-intrastrand d(GpG) adducts." Thesis, Massachusetts Institute of Technology, 1997. http://hdl.handle.net/1721.1/44501.

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50

Kang, W. "Functional studies of SP-D in innate immunity, and its binding protein gp-340 in gastric epithelial development." Thesis, University of Oxford, 2002. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.249276.

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