Готові списки джерел за темами / Basiglio

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Добірка наукової літератури з теми "Basiglio"

Автор: Grafiati

Опубліковано: 10 березня 2023

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Статті в журналах з теми "Basiglio"

Bianconi, M., L. Ferraro, G. C. Traina, G. Zanoli, T. Antonelli, A. Guberti, R. Ricci, and L. Massari. "Pharmacokinetics and efficacy of ropivacaine continuous wound instillation after joint replacement surgery † †Declaration of interest. This work was supported by AstraZeneca, Basiglio, Milano, Italy. Presented in part at the Third European Congress of Orthopaedic Anaesthesia, 31 May–2 June 2001, London, UK." British Journal of Anaesthesia 91, no. 6 (December 2003): 830–35. http://dx.doi.org/10.1093/bja/aeg277.

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Chen, Li, Jiajia Bi, Masaaki Nakai, David Bunick, John F. Couse, Kenneth S. Korach та Romana A. Nowak. "Expression of basigin in reproductive tissues of estrogen receptor-α or -β null mice". REPRODUCTION 139, № 6 (червень 2010): 1057–66. http://dx.doi.org/10.1530/rep-10-0069.

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Basigin plays important roles in both male and female reproduction because basigin (Bsg) null male and female mice are infertile. The aim of the present study was to determine whether basigin expression in reproductive organs requires estrogen receptor-α (ESR1, ERα) or -β (ESR2, ERβ). Expression of basigin protein in the testis, ovary, and male and female reproductive tracts was studied in adult wild-type (WT),Esr1-null (αERKO), andEsr2-null (βERKO) mice by immunohistochemistry and immunoblotting. Basigin mRNA levels in ovary and uterus were examined by quantitative RT-PCR. In females, basigin protein expression was observed mainly in granulosa and interstitial cells of the ovary and epithelial cells of the proximal oviduct in all genotypes. Basigin protein was also expressed in the uterine epithelium at proestrus and estrus in WT and βERKO mice but not in αERKO mice. However, a higher level of basigin mRNA was observed in uteri of αERKO mice compared with WT and βERKO mice. In males, basigin was expressed in Leydig cells and all germ cells except spermatogonia in all genotypes. Basigin was present in epithelial cells lining the efferent ductules in WT and βERKO mice, but expression was greatly reduced in αERKO mice. In epididymal ducts, basigin expression was observed in epithelial cells in the caput and cauda in all genotypes. These data suggest that expression of basigin protein requires ESR1, but not ESR2, in the uterus and efferent ductules, but is independent of estrogen receptor in the ovary, oviduct, testis, and epididymis.

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Ding, Nai-Zheng, Cheng-Qiang He, and Zeng-Ming Yang. "Quantification of basigin mRNA in mouse oocytes and preimplantation embryos by competitive RT-PCR." Zygote 10, no. 3 (August 2002): 239–43. http://dx.doi.org/10.1017/s0967199402002319.

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Basigin is a member of the immunoglobulin superfamily and a key molecule related to mouse blastocyst implantation. Whether preimplantation mouse embryos express basigin mRNA is still unknown. The aim of this study was to use a quantitative competitive polymerase chain reaction to assess quantitatively the levels of basigin mRNA in mouse oocyte and preimplantation embryos. Basigin mRNA was detected in the oocyte and all the stages of preimplantation embryos. The levels of basigin mRNA were 0.0606 ± 0.0282 in the oocyte, 0.0102 ± 0.0036 in the zygote, 0.0007 ± 0.0003 in the 2-cell embryo, 0.0031 ± 0.0017 in the 4-cell embryo, 0.0084 ± 0.0024 in the 8-cell embryo, 0.0537 ± 0.0121 in the morula and 0.0392 ± 0.0161 attomoles in the blastocyst, respectively. The levels of basigin mRNA in the oocyte, morula and blastocyst were significantly higher than those in the zygote and embryos at the 2-cell, 4-cell and 8-cell stages. The high level of basigin expression in the blastocyst may play a role during embryo implantation.

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Albrechtsen, Reidar, Nicolai Wewer Albrechtsen, Sebastian Gnosa, Jeanette Schwarz, Lars Dyrskjøt, and Marie Kveiborg. "Identification of ADAM12 as a Novel Basigin Sheddase." International Journal of Molecular Sciences 20, no. 8 (April 22, 2019): 1957. http://dx.doi.org/10.3390/ijms20081957.

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The transmembrane glycoprotein basigin, a member of the immunoglobulin superfamily, stimulates matrix metalloproteinase (MMP)-mediated extracellular matrix (ECM) degradation and thereby drives cancer cell invasion. Basigin is proteolytically shed from the cell surface and high concentrations of soluble basigin in the blood dictates poor prognosis in cancer patients. A positive correlation between basigin and a disintegrin and metalloproteinase (ADAM)-12 in serum from prostate cancer patients has been reported. Yet, the functional relevance of this correlation is unknown. Here, we show that ADAM12 interacts with basigin and cleaves it in the juxtamembrane region. Specifically, overexpression of ADAM12 increases ectodomain shedding of an alkaline phosphatase-tagged basigin reporter protein from the cell surface. Moreover, CRISPR/Cas9-mediated knockout of ADAM12 in human HeLa carcinoma cells results in reduced shedding of the basigin reporter, which can be rescued by ADAM12 re-expression. We detected endogenous basigin fragments, corresponding to the expected size of the ADAM12-generated ectodomain, in conditioned media from ADAM12 expressing cancer cell-lines, as well as serum samples from a healthy pregnant donor and five bladder cancer patients, known to contain high ADAM12 levels. Supporting the cancer relevance of our findings, we identified several cancer-associated mutations in the basigin membrane proximal region. Subsequent in vitro expression showed that some of these mutants are more prone to ADAM12-mediated shedding and that the shed ectodomain can enhance gelatin degradation by cancer cells. In conclusion, we identified ADAM12 as a novel basigin sheddase with a potential implication in cancer.

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Li, Kailiang, and Romana A. Nowak. "The role of basigin in reproduction." Reproduction 159, no. 2 (February 2020): R97—R109. http://dx.doi.org/10.1530/rep-19-0268.

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Basigin is a highly glycosylated transmembrane protein that was originally identified as a product of tumor cells. Basigin is a potent inducer of matrix metalloproteinases (MMPs) and angiogenic factors such as vascular endothelial growth factor (VEGF). Basigin is also a chaperone protein for specific metabolite transporters in the plasma cell membrane such as the monocarboxylate transporters and is an important regulator of cell metabolism. Studies in reproductive model systems have demonstrated that basigin is expressed in the testis, ovary, uterus and placenta and is necessary for normal fertility in both males and females. Overexpression of basigin is associated with reproductive diseases including uterine leiomyomas and endometriosis. This review presents an overview of the literature regarding the physiological role of basigin in reproductive tissues and the mechanistic pathways involved in its actions.

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Chen, Li, Robert J. Belton, and Romana A. Nowak. "Basigin-Mediated Gene Expression Changes in Mouse Uterine Stromal Cells During Implantation." Endocrinology 150, no. 2 (February 1, 2009): 966–76. http://dx.doi.org/10.1210/en.2008-0571.

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Implantation of mouse embryos is dependent on the proliferation and differentiation of uterine stromal cells in a process called decidualization. Decidualization both supports and limits the invasion of the implanting embryo and is regulated in part by the expression of matrix metalloproteinases (MMPs) and their inhibitors, the tissue inhibitors of metalloproteinases (TIMPs). Molecules that alter the balance between MMP and TIMP expression could prevent implantation of the embryo. The membrane glycoprotein basigin (CD147/EMMPRIN), a known inducer of MMPs, is necessary for normal implantation in the mouse. The purpose of this study was to investigate the potential roles of basigin during implantation in the mouse. Using an in vitro stromal cell culture system, we found that recombinant human basigin protein (rBSG) increases MMP-3 and MMP-9 expression without altering TIMP-3 expression. Our results also showed rBSG induces expression of cytokines IL-1α/β and leukocyte chemoattractants, CCL3, CCL20, CXCL2, and CXCL5. More importantly, rBSG significantly suppressed stromal cell decidualization as shown by the inhibition of alkaline phosphatase-2 expression and activity by rBSG. However, rBSG did not affect stromal cell proliferation. Taken together, our data indicate that basigin mediates gene expression changes in mouse uterine stromal cells and suggests that temporal and spatial regulation of basigin expression may be involved in the recruitment of leukocytes to the mouse uterus during early pregnancy. The role of basigin during embryo implantation in mice is examined. Basigin regulates matrix metalloproteinase, IL-1, and leukocyte chemoattractant production by uterine stromal cells.

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Köpnick, Anna-Lena, Annika Jansen, Katharina Geistlinger, Nathan Hugo Epalle, and Eric Beitz. "Basigin drives intracellular accumulation of l-lactate by harvesting protons and substrate anions." PLOS ONE 16, no. 3 (March 26, 2021): e0249110. http://dx.doi.org/10.1371/journal.pone.0249110.

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Transmembrane transport of l-lactate by members of the monocarboxylate transporter family, MCT, is vital in human physiology and a malignancy factor in cancer. Interaction with an accessory protein, typically basigin, is required to deliver the MCT to the plasma membrane. It is unknown whether basigin additionally exerts direct effects on the transmembrane l-lactate transport of MCT1. Here, we show that the presence of basigin leads to an intracellular accumulation of l-lactate 4.5-fold above the substrate/proton concentrations provided by the external buffer. Using basigin truncations we localized the effect to arise from the extracellular Ig-I domain. Identification of surface patches of condensed opposite electrostatic potential, and experimental analysis of charge-affecting Ig-I mutants indicated a bivalent harvesting antenna functionality for both, protons and substrate anions. From these data, and determinations of the cytosolic pH with a fluorescent probe, we conclude that the basigin Ig-I domain drives lactate uptake by locally increasing the proton and substrate concentration at the extracellular MCT entry site. The biophysical properties are physiologically relevant as cell growth on lactate media was strongly promoted in the presence of the Ig-I domain. Lack of the domain due to shedding, or misfolding due to breakage of a stabilizing disulfide bridge reversed the effect. Tumor progression according to classical or reverse Warburg effects depends on the transmembrane l-lactate distribution, and this study shows that the basigin Ig-I domain is a pivotal determinant.

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Belton, Robert J., Li Chen, Fernando S. Mesquita, and Romana A. Nowak. "Basigin-2 Is a Cell Surface Receptor for Soluble Basigin Ligand." Journal of Biological Chemistry 283, no. 26 (April 22, 2008): 17805–14. http://dx.doi.org/10.1074/jbc.m801876200.

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Ovens, Matthew J., Christine Manoharan, Marieangela C. Wilson, Clarey M. Murray, and Andrew P. Halestrap. "The inhibition of monocarboxylate transporter 2 (MCT2) by AR-C155858 is modulated by the associated ancillary protein." Biochemical Journal 431, no. 2 (September 28, 2010): 217–25. http://dx.doi.org/10.1042/bj20100890.

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In mammalian cells, MCTs (monocarboxylate transporters) require association with an ancillary protein to enable plasma membrane expression of the active transporter. Basigin is the preferred binding partner for MCT1, MCT3 and MCT4, and embigin for MCT2. In rat and rabbit erythrocytes, MCT1 is associated with embigin and basigin respectively, but its sensitivity to inhibition by AR-C155858 was found to be identical. Using RT (reverse transcription)–PCR, we have shown that Xenopus laevis oocytes contain endogenous basigin, but not embigin. Co-expression of exogenous embigin was without effect on either the expression of MCT1 or its inhibition by AR-C155858. In contrast, expression of active MCT2 at the plasma membrane of oocytes was significantly enhanced by co-expression of exogenous embigin. This additional transport activity was insensitive to inhibition by AR-C155858 unlike that by MCT2 expressed with endogenous basigin that was potently inhibited by AR-C155858. Chimaeras and C-terminal truncations of MCT1 and MCT2 were also expressed in oocytes in the presence and absence of exogenous embigin. L-Lactate Km values for these constructs were determined and revealed that the TM (transmembrane) domains of an MCT, most probably TM7–TM12, but not the C-terminus, are the major determinants of L-lactate affinity, whereas the associated ancillary protein has little or no effect. Inhibitor titrations of lactate transport by these constructs indicated that embigin modulates MCT2 sensitivity to AR-C155858 through interactions with both the intracellular C-terminus and TMs 3 and 6 of MCT2. The C-terminus of MCT2 was found to be essential for its expression with endogenous basigin.

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Sakuragi, Takaharu, Ryuta Kanai, Akihisa Tsutsumi, Hirotaka Narita, Eriko Onishi, Kohei Nishino, Takuya Miyazaki, et al. "The tertiary structure of the human Xkr8–Basigin complex that scrambles phospholipids at plasma membranes." Nature Structural & Molecular Biology 28, no. 10 (October 2021): 825–34. http://dx.doi.org/10.1038/s41594-021-00665-8.

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AbstractXkr8–Basigin is a plasma membrane phospholipid scramblase activated by kinases or caspases. We combined cryo-EM and X-ray crystallography to investigate its structure at an overall resolution of 3.8 Å. Its membrane-spanning region carrying 22 charged amino acids adopts a cuboid-like structure stabilized by salt bridges between hydrophilic residues in transmembrane helices. Phosphatidylcholine binding was observed in a hydrophobic cleft on the surface exposed to the outer leaflet of the plasma membrane. Six charged residues placed from top to bottom inside the molecule were essential for scrambling phospholipids in inward and outward directions, apparently providing a pathway for their translocation. A tryptophan residue was present between the head group of phosphatidylcholine and the extracellular end of the path. Its mutation to alanine made the Xkr8–Basigin complex constitutively active, indicating that it plays a vital role in regulating its scramblase activity. The structure of Xkr8–Basigin provides insights into the molecular mechanisms underlying phospholipid scrambling.

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Більше джерел

Дисертації з теми "Basiglio"

Lee, Aimei Yen-Jia. "The glycoprotein Basigin in liver disease." Thesis, The University of Sydney, 2016. http://hdl.handle.net/2123/17163.

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Basigin (Bsg) is a membrane glycoprotein expressed by many different cell types. Bsg is instrumental in tissue development, extracellular matrix (ECM) remodelling, and has been implicated in numerous cancer types. The liver carries out many important functions and when injured, undergoes ECM remodelling. Persistent liver damage can lead to the development of fibrosis, cirrhosis, and hepatocellular carcinoma (HCC). Bsg is highly expressed within the liver, and membrane bound Bsg is known to be increased in liver disease and HCC. Bsg may also be solubilised via cleavage from the cell surface or secreted in microparticles (MPs) to exert its actions at distal locations. However, not much is known about soluble Bsg (solBsg) in liver disease and its progression. It is also not known whether the glycan structures on Bsg alter with liver disease, and there is a lack of knowledge about the expression of glycosylation-associated genes in the context of liver disease. Hence this thesis sought to investigate solBsg and glycosylation-associated genes in liver disease. The major findings of this thesis identified significant correlations between solBsg and liver diseases, as well as numerous characteristics of HCC. Further, it has been demonstrated that solBsg has the potential to be utilised as a biomarker in the progression of liver disease and HCC prognosis. The results have also demonstrated that glycosylation-associated genes within the liver are dysregulated in different liver diseases. It was also shown that different cytokines, which are prominent in an inflammatory liver environment, are involved in affecting the transcription of glycosylation-associated genes. Future research into the glycan structures of Bsg as its activities become malignant may enable the development of personalised novel therapies to target specific disease conditions.

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Pablo, Kristine Anne V. "Examination of the Mitochondrial Health of the Basigin Null Mouse Retina." UNF Digital Commons, 2011. http://digitalcommons.unf.edu/etd/387.

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Basigin gene products are cell adhesion molecules that are expressed by photoreceptor cells, Müller cells and endothelial cells of the mammalian retina. Previous studies have suggested that a lactate shuttle exists between the photoreceptor cells and the Müller cells, with Basigin being an essential component in this shuttle. Deletion of the Basigin gene in mice results in blindness with an eventual retinal degeneration. It was hypothesized that the lactate shuttle between photoreceptors and Müller cells does not form in Basigin null mice and that the blindness is attributed to faulty photoreceptor metabolism. Therefore, the purpose of this study was to determine whether the mitochondria of the Basigin null mice are metabolically active in the absence of the lactate shuttle. Mitochondrial health in the Basigin null mouse retina was assessed by a variety of assays, including ELISA analyses to measure Cytochrome c concentration and expression of autophagy-specific proteins. Mitotracker dyes were used to stain the mitochondria of Basigin null and normal retinas to determine the number of metabolically active mitochondria and the total number of mitochondria. The results showed that apoptosis and autophagy are not occurring in the Basigin null animals at a rate greater than that of the normal animals. The Mitotracker assay showed that there is a ~60% decrease in the total number of mitochondria in the null animals compared to their normal counterparts. A recalculation of the Cytochrome c assay in light of the reduced number of mitochondria in Basigin null mice revealed that apoptosis is likely occurring in these animals prior to the first signs of cytoarchitectural changes in the tissue. These results suggest that in the absence of the lactate shuttle in the Basigin null animals, the photoreceptors are unable to perform oxidative phosphorylation at the necessary rate, thus decreasing the number of mitochondria, which results in limited photoreceptor functionality, hence blindness.

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Köpnick, Anna-Lena [Verfasser], Eric [Akademischer Betreuer] Beitz, and Axel [Gutachter] Scheidig. "Fusion of human monocarboxylate transporter 1 with basigin and expression in S. cerevisiae : Is basigin more than a chaperone? / Anna-Lena Köpnick ; Gutachter: Axel Scheidig ; Betreuer: Eric Beitz." Kiel : Universitätsbibliothek Kiel, 2021. http://d-nb.info/1234981424/34.

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Brown, Josephine Michelle. "Characterization of the interaction between Basigin and the pattern recognition receptor TLR4." UNF Digital Commons, 2016. http://digitalcommons.unf.edu/etd/650.

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Toll-like receptors (TLRs) are a major group of pattern recognition receptors expressed on the surface of immune cells that recognize molecular patterns associated with all classes of pathogenic microorganisms. TLR4 recognizes the lipopolysaccharide component of Gram-negative bacterial cell walls and is the only TLR known to induce signaling through both the MyD88 and TRIF pathways. Basigin, a ubiquitous cell adhesion molecule, is a member of the immunoglobulin superfamily that has the ability to influence cell signaling mediated by the MyD88 and TRIF pathways, the same signaling pathways induced by the TLR4 receptor protein. Analysis of the Basigin protein sequence indicates the presence of a hydrophilic glutamate residue within the hydrophobic transmembrane domain, but no consensus binding sites for MyD88 or TRIF. The purpose of this study was to determine if Basigin uses TLR4 for signal transduction. It is hypothesized that Basigin interacts with TLR4 and that the glutamate residue plays a role in the interaction. Enzyme-linked immunosorbent binding assays were performed using endogenous TLR4 and recombinant Basigin proteins. These analyses demonstrated that binding of Basigin to TLR4 was significantly greater than that of the control protein and that the glutamate residue in the Basigin transmembrane domain does play a role in the interaction between Basigin and TLR4 as well as many hydrophobic residues in the Basigin transmembrane domain. The data suggest that Basigin interacts with TLR4 to influence signaling cascades using MyD88 and TRIF.

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Finch, NiCole A. "A Study of the Interaction Between the Basigin Transmembrane Domain and Monocarboxylate Transporter 1." UNF Digital Commons, 2007. http://digitalcommons.unf.edu/etd/182.

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It is thought that a lactate shuttle complex of Basigin gene products and Monocarboxylate transporter 1 (MCT1) is necessary for photoreceptor cell maturation and function. The purpose of this study was to investigate the assembly of the lactate shuttle by determining which amino acids within Basigin interact with MCT1. It has been hypothesized that these two membrane proteins interact via the transmembrane domain of Basigin. Therefore, a full-length histidine-tagged peptide of the transmembrane domain (24 amino acids), as well as histidine-tagged deletion mutants were generated using the pET1 02/0 vector (Invitrogen) to test for binding to MCT1 via enzyme-linked immunosorbent assay (ELISA). The probe containing the entire transmembrane domain of Basigin (amino acids 1 to 24) did interact with MCT1. An interaction was also observed when a probe containing amino acids 13 to 24 of the Basigin transmembrane domain was used. A comparable interaction was observed when amino acids 19 to 24 were used as a probe, but no signal was observed when amino acids 13 to 18 were used. This indicates that some or all of the six C-terminal amino acids of the Basigin transmembrane domain bind to MCT1. Site-directed mutagenesis of each of the six C-terminal amino acids, and subsequent ELISA analysis, . indicates that isoleucine - 20, isoleucine - 21, isoleucine - 23, and tyrosine - 24 interact with MCT1. Vlll

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Fong, Joseph D. "The Distinction of the Interactions Between the Transmembrane Domains of Basigin Gene Products and Monocarboxylate Transporters." UNF Digital Commons, 2018. https://digitalcommons.unf.edu/etd/788.

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Although it was once thought that neurons solely rely on glucose as a substrate for cellular energy production, it is now known that small monocarboxylate molecules, like pyruvate, lactate, and ketone bodies, are also utilized. Monocarboxylates are transported across plasma membranes via facilitated diffusion using a family of transport proteins known as monocarboxylate transporters (MCTs). Four MCTs (MCT1, MCT2, MCT3, and MCT4) are expressed within neural tissues. Expression of the MCTs has been tied to co-expression of a cell adhesion molecule belonging to the Basigin subset of the immunoglobulin superfamily (IgSF). Basigin gene products are known to interact with MCT1 and MCT4 in the mammalian neural retina and this association is essential to support the cellular energy needs of photoreceptors. A previous study indicated that Basigin gene products use hydrophobic amino acids within specific regions of the transmembrane domain to interact with MCT1. In the present study, it is hypothesized that the same amino acids within the transmembrane domain are used to interact with MCT4, but that no association exists with MCT2, which typically interacts with a different member of the IgSF subset. Therefore, the purpose of the present study was to assess the association between Basigin gene products and MCT4, and with MCT2. Recombinant proteins corresponding to the transmembrane domain of Basigin gene products were used in in vitro binding assays with endogenous MCT2 and MCT4 from mouse brain protein lysates. Contrary to the hypothesis, it was determined that the transmembrane domain of Basigin gene products binds to both MCT2 and MCT4 in vitro. Different amino acids within the transmembrane domain of Basigin gene products are used for each association and the pattern is different from that used in the association with MCT1. The data suggest that Basigin plays multiple roles in the nervous system.

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Gambon, Paul L. "Localization and characterization of the interactions between Basigin gene products and Monocarboxlate Transporters in the olfactory bulb of the mouse." UNF Digital Commons, 2011. http://digitalcommons.unf.edu/etd/126.

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Basigin, the mouse form of the human protein EMMPRIN, is commonly found as a transmembrane homodimer with carboxy termini in the cytosol and extracellular amino-termini. Because of its important role as a cell-to-cell junction molecule, and possible implications for cancer research, a Basigin null mouse was developed in 1996 by Igakura et al., to aid in the study of this protein. Their early research demonstrated that Basigin plays a large role in embryonic development. Mice lacking the Basigin gene are blind from the time of eye opening, and have demonstrated a lack of aversion to offensive odors such as acetic acid and isogine, as well as increased sensitivity to electric foot shock (Naruhashi et al., 1997). Further research demonstrated that Basigin is associated with cell-to-cell communication within the retina of the eye (Ochrietor et al., 2002), and in the olfactory system (Igakura et al., 1996). It is thought that Basigin acts as a chaperone for several Monocarboxylate Transporters (MCTs), accompanying them for proper placement in the cell membrane. The focus of this current study is to explore the role and function of Basigin in the olfactory bulb of the mouse. Data from biochemical analysis of tissue samples show that MCTs in the olfactory bulb are unaffected by absence of Basigin. Further study involving immunohistochemistry reveals that MCT2 is the most abundant transporter present in normal olfactory bulbs, and that a metabolic defect does not likely underlie the anosmia exhibited by Basigin null mice.

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Little, L. Nicole. "Characterization of Basigin and the Interaction Between Embigin and Monocarboxylate Transporter -1, -2, and -4 (MCT1, MCT2, MCT4) in the Mouse Brain." UNF Digital Commons, 2011. http://digitalcommons.unf.edu/etd/384.

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Анотація:

Basigin and Embigin are members of the immunoglobulin superfamily that function as cell adhesion molecules. Studies of Basigin null mice revealed reproductive sterility, increased pain sensitivity, and blindness. It is thought that the mechanism causing blindness involves misexpression of monocarboxylate transporter 1 (MCT1) in the absence of Basigin. It is known that the transmembrane domain of Basigin interacts with MCT1. In the absence of Basigin, MCT1 does not localize to the plasma membrane of expressing cells and photoreceptor function is disrupted. Studies of the Basigin null mouse brain suggest that MCT1 is properly expressed, which suggests a separate mechanism causes the increased pain sensitivity in these animals, and also that a different protein directs MCT1 to the plasma membrane of expressing cells in mouse brain. Embigin is known to interact with MCT2 in neurons and with MCT1 in erythrocytes. It is not known, however, if Embigin normally interacts with MCT1 in the mouse brain or if Embigin acts to compensate for the lack of Basigin in the Basigin null animals. Therefore, the purpose of this study was to determine if Embigin normally interacts with MCT1, 2, or 4 in the mouse brain and if so, whether the interaction is similar to that between Basigin and MCT1. Expression of Basigin, Embigin, MCT1, MCT2, and MCT4 in mouse brain was assessed via immunoblotting and immunohistochemical analyses. In addition, recombinant protein probes corresponding to the Embigin transmembrane domain were generated for ELISA binding assays using endogenous mouse brain MCTs. It was determined that the proteins in question are rather ubiquitously expressed throughout the mouse brain, and that the cell adhesion molecules Basigin and Embigin may be co-expressed in the same cells as the MCT2 and MCT4 transporter proteins. In addition, it was determined that the Embigin transmembrane domain does not interact with the MCTs. The data therefore suggest that MCTs do not require Basigin or Embigin for plasma membrane expression in mouse brain.

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Marchiq, Ibtissam. "Hypoxie et métabolisme tumoral : analyse génétique et fonctionnelle des symporteurs H+/lactate et de leur chaperone, BASIGINE." Thesis, Nice, 2015. http://www.theses.fr/2015NICE4066/document.

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Анотація:

Le catabolisme exacerbé du glucose et de la glutamine est actuellement reconnu comme une caractéristique des cellules cancéreuses, qui leur procure un avantage prolifératif via la production et l’accumulation de plusieurs métabolites au niveau du microenvironnement. Parmi ces métabolites, l’acide lactique représente une molécule de signalisation clé, favorisant la migration et les métastases. Mon projet de thèse s’inscrit dans le contexte d’une étude du métabolisme glycolytique associé aux cellules tumorales à division rapide. Durant ce projet, nous nous sommes intéressés à la caractérisation génétique et fonctionnelle des transporteurs MCT (MonoCarboxylate Transporters) 1 et 4, qui sont des symporteurs H+/lactate dont l’expression membranaire et la fonctionnalité requièrent la liaison avec une protéine chaperonne : CD147/BASIGINE (BSG). Afin de mieux explorer la physiologie des complexes MCT/BSG, et valider le ciblage de l’export d’acide lactique comme une nouvelle approche anti-cancer, nous avons développé une stratégie visant à invalider le gène BSG et/ou MCT4, en utilisant la technologie des Zinc Finger Nucleases (ZFN), dans des lignées cellulaires cancéreuses humaines de côlon, poumon et glioblastome. D’abord, nous avons démontré, que l’effet pro-tumoral majeur de BSG est lié à son action directe sur la stabilisation des MCTs au niveau des tumeurs glycolytiques et non pas à la production des metalloprotéases. Ensuite, nous avons démontré pour la première fois que l’inhibition concomitante de MCT1 et MCT4 est nécessaire pour induire une baisse significative de la tumorigénécité in vivo
Enhanced glucose and glutamine catabolism has become a recognized feature of cancer cells, leading to accumulation of metabolites in the tumour microenvironment, which offers growth advantages to tumours. Among these metabolites is emerging as a key signalling molecule that plays a pivotal role in cancer cell migration and metastasis. In this thesis, we focused on the genetic and functional characterization of monocarboxylate transporters (MCT) 1 and 4, which are H+/lactate symporters that require an interaction with an ancillary protein, CD147/BASIGIN (BSG), for their plasma membrane expression and function. To further explore the physiology of MCT/BSG complexes and validate the blockade of lactic acid export as an anti-cancer strategy, we designed experiments using Zinc Finger Nuclease mediated BSG and/or MCT4 gene knockouts in human colon adenocarcinoma, lung carcinoma and glioblastoma cell lines. First of all, we demonstrated that the major protumoural action of BSG is to control the energetics of glycolytic tumours via MCT1/4 activity and not to produce matrix metalloproteases. Second, we showed for the first time that combined inhibition of both MCT1 and MCT4 transporters is required to achieve a significant reduction in the tumour growth in vivo. Moreover, our findings reported that disruption of the BSG gene dramatically reduced the plasma membrane expression and lactate transport activity of both MCT1 and MCT4, leading to increased accumulation of intracellular pools of lactic and pyruvic acids, decreased intracellular pH and reduced rate of glycolysis

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SOLIMANDO, ANNA RACHELE. "Il paesaggio delle aree agricole periurbane. Strumenti e progetti di tutela e valorizzazione." Doctoral thesis, 2010. http://hdl.handle.net/2158/592728.

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Книги з теми "Basiglio"

Shrestha, Brikha Raj. Role of the immunoglobulin superfamily member Basigin in sensory neuron dendrite morphogenesis in Drosophila. [New York, N.Y.?]: [publisher not identified], 2013.

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Частини книг з теми "Basiglio"

Joseph, Jeymohan, Robert L. Knobler, Fred D. Lublin, and Frank R. Burns. "Regulation of the Expression of Intercellular Adhesion Molecule-1 (ICAM-1) and the Putative Adhesion Molecule Basigin on Murine Cerebral Endothelial Cells by MHV-4 (JHM)." In Coronaviruses, 389–91. Boston, MA: Springer US, 1994. http://dx.doi.org/10.1007/978-1-4615-2996-5_60.

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Тези доповідей конференцій з теми "Basiglio"

Jeong, Jieun, Eunhee G. Kim, Jae Y. Cho, Eugene C. Yi, and Kristine M. Kim. "Role of basigin in adaptor protein mediated signaling pathways." In Bioscience and Medical Research 2013. Science & Engineering Research Support soCiety, 2013. http://dx.doi.org/10.14257/astl.2013.33.05.

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Kamal, Samaa, Matthew A. Firpo, Courtney L. Scaife, Adler G. Douglas, Kenneth M. Boucher, and Sean J. Mulvihill. "Abstract B23: Plasma basigin as an early detection biomarker for pancreatic adenocarcinoma." In Abstracts: AACR Special Conference on Pancreatic Cancer: Innovations in Research and Treatment; May 18-21, 2014; New Orleans, LA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-7445.panca2014-b23.

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Lappi, Douglas A., Leonardo Ancheta, and Romana A. Nowak. "Abstract 2244: Internalization of basigin-2, a poor prognosis marker, by a monoclonal antibody." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-2244.

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Bornhauser, Beat C., Jeannette Boutter, Peter Horvath, Martin Stanulla, and Jean-Pierre Bourquin. "Abstract 4597: Stroma-derived Basigin controls survival of leukemia cells through regulation of their redox state." In Proceedings: AACR 104th Annual Meeting 2013; Apr 6-10, 2013; Washington, DC. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1538-7445.am2013-4597.

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Ancheta, Leonardo R., and Douglas A. Lappi. "Abstract 5218: Basigin-2 (EMMPRIN), a prognostic marker, is a dynamic portal of entry into cancer cells." In Proceedings: AACR 102nd Annual Meeting 2011‐‐ Apr 2‐6, 2011; Orlando, FL. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1538-7445.am2011-5218.

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Floch, Renaud Le, Johanna Chiche, Ibtissam Marchiq, Tanesha Naiken, Karine Ilc, Marie-Pierre Simon, Danièle Roux, and Jacques Pouyssegur. "Abstract 3225: Growth inhibition of glycolytic tumors by targeting basigin/lactate-H+ symporters (MCTs): Metformin sensitizes MCT inhibition." In Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-3225.

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Spina, Raffaella, Dillon M. Voss, Kah Suan Lim, Constance J. Jeffery, and Eli E. Bar. "Abstract 5023: Disruption of Monocarboxylate transporter-4 Basigin interaction as an effective strategy to inhibit hypoxic response, tumor growth and vascularization, and stem cell phenotype in human glioblastomain vitroandin vivo." In Proceedings: AACR Annual Meeting 2017; April 1-5, 2017; Washington, DC. American Association for Cancer Research, 2017. http://dx.doi.org/10.1158/1538-7445.am2017-5023.

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