Publications
64 results found
Episkopou V, 2005, SOX2 functions in adult neural stem cells, TRENDS IN NEUROSCIENCES, Vol: 28, Pages: 219-221, ISSN: 0166-2236
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- Citations: 189
Malas S, Postlethwaite M, Ekonomou A, et al., 2003, SOX1-deficient mice suffer from epilepsy associated with abnormal ventral forebrain development and olfactory cortex hyperexcitability, NEUROSCIENCE, Vol: 119, Pages: 421-432, ISSN: 0306-4522
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- Citations: 56
Graf D, Timmons PM, Hitchins M, et al., 2001, Evolutionary conservation, developmental expression, and genomic mapping of mammalian <i>Twisted gastrulation</i>, MAMMALIAN GENOME, Vol: 12, Pages: 554-560, ISSN: 0938-8990
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- Citations: 26
Niederländer C, Walsh JJ, Episkopou V, et al., 2001, Arkadia enhances nodal-related signalling to induce mesendoderm, NATURE, Vol: 410, Pages: 830-834, ISSN: 0028-0836
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- Citations: 62
Episkopou V, Arkell R, Timmons PM, et al., 2001, Induction of the mammalian node requires Arkadia function in the extraembryonic lineages, NATURE, Vol: 410, Pages: 825-830, ISSN: 0028-0836
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- Citations: 84
Buttery LDK, Bourne S, Xynos JD, et al., 2001, Differentiation of osteoblasts and <i>in vitro</i> bone formation from murine embryonic stem cells, TISSUE ENGINEERING, Vol: 7, Pages: 89-99, ISSN: 2152-4947
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- Citations: 314
van Bennekum AM, Wei SH, Gamble MV, et al., 2001, Biochemical basis for depressed serum retinol levels in transthyretin-deficient mice, JOURNAL OF BIOLOGICAL CHEMISTRY, Vol: 276, Pages: 1107-1113, ISSN: 0021-9258
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- Citations: 98
Bourne S, Buttery LDK, Xynos ID, et al., 2000, Selective differentiation of osteoblasts and in vitro bone formation from murine embryonic stem cells
A method for selective generation and enrichment of bone-forming osteoblasts from embryonic stem (ES) cells is described. Murine ES cell line was expanded in the presence of the differentiation inhibitors, LIF and inactivated murine fibroblast feeder layers. Cultures were fixed and stained with alizarin red to demonstrate the presence of mineral and were also stained by immunofluorescence for collagen-I and the osteoblast specific marker osteocalcin. Confocal microscopy investigation revealed the bone nodules to be composed of up to 100 cells within an extracelluar matrix of collagen-I and also osteocalcin.
Almeida Palha J, Fernandes R, Morreale de Escobar G, et al., 2000, Transthyretin Regulates Thyroid Hormone Levels in the Choroid Plexus, But Not in the Brain Parenchyma: Study in a Transthyretin-Null Mouse Model., Endocrinology, Vol: 141, Pages: 3267-3272
Palha JA, Fernandes R, de Escobar GM, et al., 2000, Transthyretin regulates thyroid hormone levels in the choroid plexus, but not in the brain parenchyma: Study in a transthyretin-null mouse model, ENDOCRINOLOGY, Vol: 141, Pages: 3267-3272, ISSN: 0013-7227
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- Citations: 53
Bourne S, Buttery LDK, Xynos ID, et al., 2000, Osteoblastic differentiation of murine embryonic stem cells., JOURNAL OF PATHOLOGY, Vol: 190, Pages: 20A-20A, ISSN: 0022-3417
Wood HB, Malas S, Nishiguchi S, et al., 2000, Sox1 is required for normal cell migration in the ventral telencephalon and loss of function leads to an epileptic phenotype, EUROPEAN JOURNAL OF NEUROSCIENCE, Vol: 12, Pages: 258-258, ISSN: 0953-816X
Constanti A, Postlethwaite M, Malas S, et al., 1999, Epileptiform activity recorded in olfactory cortical brain slices prepared from mice deficient in the Sox1 transcription factor gene, Journal of Pharmacy and Pharmacology, Vol: 51, ISSN: 0022-3573
Malas S, Duthie S, Deloukas P, et al., 1999, The isolation and high-resolution chromosomal mapping of human SOX14 and SOX21; two members of the SOX gene family related to SOX1, SOX2, and SOX3, MAMMALIAN GENOME, Vol: 10, Pages: 934-937, ISSN: 0938-8990
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- Citations: 26
Wood HB, Episkopou V, 1999, Comparative expression of the mouse <i>Sox1</i>, <i>Sox2</i> and <i>Sox3</i> genes from pre-gastrulation to early somite stages, MECHANISMS OF DEVELOPMENT, Vol: 86, Pages: 197-201, ISSN: 0925-4773
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- Citations: 423
Nishiguchi S, Wood H, Kondoh H, et al., 1998, <i>Sox1</i> directly regulates the γ-crystallin genes and is essential for lens development in mice, GENES & DEVELOPMENT, Vol: 12, Pages: 776-781, ISSN: 0890-9369
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- Citations: 224
Togashi S, Lim SK, Kawano H, et al., 1997, Serum amyloid P component enhances induction of murine amyloidosis, LABORATORY INVESTIGATION, Vol: 77, Pages: 525-531, ISSN: 0023-6837
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- Citations: 56
Malas S, Duthie SM, Mohri F, et al., 1997, Cloning and mapping of the human SOX1: a highly conserved gene expressed in the developing brain, MAMMALIAN GENOME, Vol: 8, Pages: 866-868, ISSN: 0938-8990
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- Citations: 24
Manson AL, Trezise AEO, MacVinish LJ, et al., 1997, Complementation of null CF mice with a human CFTR YAC transgene, EMBO JOURNAL, Vol: 16, Pages: 4238-4249, ISSN: 0261-4189
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- Citations: 65
Kohno K, Palha JA, Miyakawa K, et al., 1997, Analysis of amyloid deposition in a transgenic mouse model of homozygous familial amyloidotic polyneuropathy, AMERICAN JOURNAL OF PATHOLOGY, Vol: 150, Pages: 1497-1508, ISSN: 0002-9440
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- Citations: 77
Palha JA, Hays MT, Morreale de Escobar G, et al., 1997, Transthyretin is not essential for thyroxine to reach the brain and other tissues in transthyretin-null mice., Am J Physiol, Vol: 272, Pages: E485-E493, ISSN: 0002-9513
As part of a study on tissue uptake of thyroxine (T4) in a transthyretin (TTR)-null mouse strain, kinetic parameters of thyroxine metabolism in wild-type mice under normal physiological conditions are presented. Kinetic analysis of injected [(125)I]T4 showed that TTR-null mutants have markedly increased [(125)I]T4 transfer rate constants from plasma to the fast-exchange compartments of liver and kidney and from fast to slow kidney compartments. Transfer rates from plasma to brain, testes, and fat were little affected. The T4 tissue content in the mutants was greatly reduced in brain but relatively normal in liver and kidney. No major changes were observed in brain 3,3',5-triiodothyronine concentrations, suggesting that availability of this hormone is not markedly altered in the mutant mice. The low T4 brain content probably reflects the absence of T4-TTR complexes in the mutant choroid plexus and cerebrospinal fluid. This study indicates that TTR is not essential for T4 tissue uptake or for T4 to reach the brain across the choroid plexus-cerebrospinal fluid and/or blood-brain barriers.
Palha JA, Hays MT, deEscobar GM, et al., 1997, Transthyretin is not essential for thyroxine to reach the brain and other tissues in transthyretin-null mice, 76th Annual Meeting of the Endocrine-Society, Publisher: AMER PHYSIOLOGICAL SOC, Pages: E485-E493, ISSN: 0193-1849
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- Citations: 65
Palha JA, Hays MT, Morreale De Escobar G, et al., 1997, Transthyretin is not essential for thyroxine to reach the brain and other tissues in transthyretin-null mice, American Journal of Physiology - Endocrinology and Metabolism, Vol: 272, ISSN: 0193-1849
As part of a study on tissue uptake of thyroxine (T4) in a transthyretin (TTR)-null mouse strain, kinetic parameters of thyroxine metabolism in wild-type mice under normal physiological conditions are presented. Kinetic analysis of injected [125I]T4 showed that TTR-null mutants have markedly increased [125I]T4 transfer rate constants from plasma to the fast-exchange compartments of liver and kidney and from fast to slow kidney compartments. Transfer rates from plasma to brain, testes, and fat were little affected. The T4 tissue content in the mutants was greatly reduced in brain but relatively normal in liver and kidney. No major changes were observed in brain 3, 3', 5-triiodothyronine concentrations, suggesting that availability of this hormone is not markedly altered in the mutant mice. The low T4 brain content probably reflects the absence of T4-TTR complexes in the mutant choroid plexus and cerebrospinal fluid. This study indicates that TTR is not essential for T4 tissue uptake or for T4 to reach the brain across the choroid plexus-cerebrospinal fluid and/or blood-brain barriers.
Pasparakis M, Alexopoulou L, Episkopou V, et al., 1996, Immune and inflammatory responses in TNF alpha-deficient mice: A critical requirement for TNF alpha in the formation of primary B cell follicles, follicular dendritic cell networks and germinal centers, and in the maturation of the humoral immune response, Journal of Experimental Medicine, Vol: 184, Pages: 1397-1411, ISSN: 0022-1007
To investigate the role of TNF alpha in the development of in vivo immune response we have generated TNF alpha-deficient mice by gene targeting. Homozygous mutant mice are viable and fertile, develop lymph nodes and Peyer's patches and show no apparent phenotypic abnormalities, indicating that TNF alpha is not required for normal mouse development. In the absence of TNF alpha mice readily succumb to L. monocytogenes infections and show reduced contact hypersensitivity responses. Furthermore, TNF alpha knockout mice are resistant to the systemic toxicity of LPS upon D-galactosamine sensitization, yet they remain sensitive to high doses of LPS alone. Most interestingly, TNF alpha knockout mice completely lack splenic primary B cell follicles and cannot form organized follicular dendritic cell (FDC) networks and germinal centers. However, despite the absence of B cell follicles, Ig class-switching can still occur, yet deregulated humoral immune responses against either thymus-dependent (TD) or thymus-independent (TI) antigens are observed. Complementation of TNF alpha functioning by the expression of either human or murine TNF alpha transgenes is sufficient to reconstitute these defects, establishing a physiological role for TNF alpha in regulating the development and organization of splenic follicular architecture and in the maturation of the humoral immune response.
Malas S, Sartor M, Duthie S, et al., 1996, Genetic and physical mapping of the murine Sox1 gene, MAMMALIAN GENOME, Vol: 7, Pages: 620-621, ISSN: 0938-8990
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- Citations: 5
Matsuura S, Episkopou V, Hamvas R, et al., 1996, Xist expression from an Xist YAC transgene carried on the mouse Y chromosome, HUMAN MOLECULAR GENETICS, Vol: 5, Pages: 451-459, ISSN: 0964-6906
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- Citations: 31
Wei S, Episkopou V, Piantedosi R, et al., 1995, Studies on the metabolism of retinol and retinol-binding protein in transthyretin-deficient mice produced by homologous recombination., J Biol Chem, Vol: 270, Pages: 866-870, ISSN: 0021-9258
Tissue needs for retinoids are believed to be satisfied through the delivery in the circulation of retinol by its specific plasma transport protein, retinol-binding protein (RBP), which circulates as a 1-to-1 protein complex with transthyretin (TTR). The binding of RBP to TTR is thought to prevent filtration of retinol-RBP in the kidney and to play a role in secretion of RBP from hepatocytes. Recently a strain of mice (TTR-) that totally lacks immunoreactive TTR was produced by targeted mutagenesis. We have explored the effects of TTR deficiency on retinol and RBP metabolism in this mutant strain. In pooled plasma from the TTR- mice retinol levels averaged 6% of those of wild type animals. Similarly, plasma RBP in the TTR- mice was found to be 5% of wild type levels. Hepatic retinol and retinyl ester levels were similar for mutant and wild type mice, suggesting that the mutation affects neither the uptake nor storage of dietary retinol. Levels of retinol and retinyl esters in testis, kidney, spleen, and eye cups from TTR- mice were normal. Plasma all-trans-retinoic acid levels for the TTR- mice were 2.3-fold higher than those of wild type (425 versus 190 ng/dl). Kidney RBP levels were similar for the mutant and wild type mice and we were unable to detect intact RBP in urine from TTR- mice. Hepatic RBP levels in the TTR- mice were 60% higher than those of wild type mice (39.8 versus 25.0 micrograms of RBP/g of tissue). These data may suggest that there is a partial blockage in RBP secretion from TTR- hepatocytes that leads to lessened plasma levels of retinol-RBP.
Palha JA, Episkopou V, Maeda S, et al., 1994, Thyroid hormone metabolism in a transthyretin-null mouse strain., J Biol Chem, Vol: 269, Pages: 33135-33139, ISSN: 0021-9258
Transthyretin (TTR) is the principal carrier of thyroid hormones in rodent plasma and the major protein synthesized by the choroid plexus. Mice lacking TTR generated by targeted disruption (Episkopou, V., Maeda, S., Nishiguchi, S., Shimada, K., Gaitanaris, G. A., Gottesman, M. E., and Robertson, E. J. (1993) Proc. Natl. Acad. Sci. U.S.A. 90, 2375-2379) had a 50% decrease in total thyroxine (T4) plasma levels but had normal free hormone levels as compared to wild-type mice. In the mutant serum there was increased T4 binding to thyroxine-binding globulin. Thyroxine-binding globulin mRNA levels were the same in mutant and wild-type animals. Wild-type serum depleted of TTR also presented increased T4 binding to thyroxine-binding globulin, suggesting that TTR competes with thyroxine-binding globulin for T4 binding. Total and free triiodothyronine and thyrotoropin-stimulating hormone levels were not affected by the absence of TTR. Liver deiodinase-I activity, mRNA levels, and brain deiodinase-II activity were normal in the mutant mice, suggesting that the absence of TTR does not affect tissue thyroid hormone content. The low T4 levels found in the mutant mice sera cannot be accounted for by increased glucuronidation because the liver activity of UDP-glucuronosyltransferase was not affected in the TTR-deficient mice. We concluded that transthyretin-deficient mice are euthyroid in the absence of the major plasma T4 carrier. We ascribed this to the normal free hormone levels in the serum of the mutant mice. Our data, therefore, strongly supported the free hormone hypothesis for thyroxine uptake (Mendel, C. M. (1989) Endocr. Rev. 10, 232-274).
Episkopou V, Blaner WS, Kurlandisky SB, et al., 1994, Retinoid transport in rodents, Retinoids, Editors: Livrea, Vidali, Publisher: Birkhauser
Smith, JE, Milch, PO, Muto, Y., and Goodman, DS The plasma transport and metabolism of retinoic acid in the rat. Biochem. ... WS (1993) Plasma Retinol- Binding Protein, In: The Retinoids: Biology, Chemistry, and Medicine, 2nd Edition, ...
Bikoff EK, Huang LY, Episkopou V, et al., 1993, Defective major histocompatibility complex class II assembly, transport, peptide acquisition, and CD4+ T cell selection in mice lacking invariant chain expression., Journal of Experimental Medicine, Vol: 177, Pages: 1699-1712, ISSN: 0022-1007
We used gene targeting techniques to produce mice lacking the invariant chain associated with major histocompatibility complex (MHC) class II molecules. Cells from these mice show a dramatic reduction in surface class II, resulting from both defective association of class II alpha and beta chains and markedly decreased post-Golgi transport. The few class II alpha/beta heterodimers reaching the cell surface behave as if empty or occupied by an easily displaced peptide, and display a distinct structure. Mutant spleen cells are defective in their ability to present intact protein antigens, but stimulate enhanced responses in the presence of peptides. These mutant mice have greatly reduced numbers of thymic and peripheral CD4+ T cells. Overall, this striking phenotype establishes that the invariant chain plays a critical role in regulating MHC class II expression and function in the intact animal.
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