PubMed Health⌕ Search

Biomedical subjects

D Christophe

Publications and source records attributed to D Christophe.

At least 19 recordsLinked to original sources

Structural and functional characterization of the two human ThOX/Duox genes and their 5'-flanking regions.

A crucial step in thyroid hormone synthesis is the oxidative coupling of iodide to thyroglobulin that is catalyzed by thyroperoxidase. The limiting factor of this reaction is the supply of hydrogen peroxide. The generation of hydrogen peroxide has been linked to an enzymatic system located at the apical pole of thyrocytes. This enzymatic activity is assumed to be exerted by NADPH oxidases encoded by two recently cloned genes hThOX1 and hThOX2. Both genes are expressed at high levels in thyrocytes. In this study we report the chromosomal organization of these two genes and the functional characterization of their respective promoter regions. The two human ThOX genes are arranged in a head to head configuration and are separated by a 16 kb-long region. Human ThOX1 and ThOX2 genes span 75 kb and are composed of 35 and 34 exons, respectively. The promoters of both genes do not resemble each other and differ from promoters of other known thyroid-specific genes. No TATA box is present in either ThOX gene promoter. Functional studies confirm that both promoters display significant transcriptional activities after transfection in differentiated thyroid cell lines. However, in contrast to that of thyroglobulin or Na(+)/I(-) symporter gene promoter, hThOX promoter activity is not restricted to thyroid cells. Additionally, functional studies show that both hThOX promoters are not positively controlled by cAMP.

5' Flanking Region↗

Identification of the gene encoding Brain Cell Membrane Protein 1 (BCMP1), a putative four-transmembrane protein distantly related to the Peripheral Myelin Protein 22 / Epithelial Membrane Proteins and the Claudins.

BACKGROUND: A partial cDNA clone from dog thyroid presenting a very significant similarity with an uncharacterized mouse EST sequence was isolated fortuitously. We report here the identification of the complete mRNA and of the gene, the product of which was termed "brain cell membrane protein 1" (BCMP1). RESULTS: The 4 kb-long mRNA sequence exhibited an open-reading frame of only 543 b followed by a 3.2 kb-long 3' untranslated region containing several AUUUA instability motifs. Analysis of the encoded protein sequence identified the presence of four putative transmembrane domains. Similarity searches in protein domain databases identified partial sequence conservations with peripheral myelin protein 22 (PMP22)/ epithelial membrane proteins (EMPs) and Claudins, defining the encoded protein as representative of the existence of a novel subclass in this protein family.Northern-blot analysis of the expression of the corresponding mRNA in adult dog tissues revealed the presence of a huge amount of the 4 kb transcript in the brain. An EGFP-BCMP1 fusion protein expressed in transfected COS-7 cells exhibited a membranous localization as expected. The sequences encoding BCMP1 were assigned to chromosome X in dog, man and rat using radiation hybrid panels and were partly localized in the currently available human genome sequence. CONCLUSIONS: We have identified the existence in several mammalian species of a gene encoding a putative four-transmembrane protein, BCMP1, wich defines a novel subclass in this family of proteins. In dog at least, the corresponding mRNA is highly present in brain cells. The chromosomal localization of the gene in man makes of it a likely candidate gene for X-linked mental retardation.

Journal Article↗

Suboptimal enhancer sequences are required for efficient bovine leukemia virus propagation in vivo: implications for viral latency.

Repression of viral expression is a major strategy developed by retroviruses to escape from the host immune response. The absence of viral proteins (or derived peptides) at the surface of an infected cell does not permit the establishment of an efficient immune attack. Such a strategy appears to have been adopted by animal oncoviruses such as bovine leukemia virus (BLV) and human T-cell leukemia virus (HTLV). In BLV-infected animals, only a small fraction of the infected lymphocytes (between 1 in 5,000 and 1 in 50,000) express large amounts of viral proteins; the vast majority of the proviruses are repressed at the transcriptional level. Induction of BLV transcription involves the interaction of the virus-encoded Tax protein with the CREB/ATF factors; the resulting complex is able to interact with three 21-bp Tax-responsive elements (TxRE) located in the 5' long terminal repeat (5' LTR). These TxRE contain cyclic AMP-responsive elements (CRE), but, remarkably, the "TGACGTCA" consensus is never strictly conserved in any viral strain (e.g.,AGACGTCA, TGACGGCA, TGACCTCA). To assess the role of these suboptimal CREs, we introduced a perfect consensus sequence within the TxRE and showed by gel retardation assays that the binding efficiency of the CREB/ATF proteins was increased. However, trans-activation of a luciferase-based reporter by Tax was not affected in transient transfection assays. Still, in the absence of Tax, the basal promoter activity of the mutated LTR was increased as much as 20-fold. In contrast, mutation of other regulatory elements within the LTR (the E box, NF-kappa B, and glucocorticoid- or interferon-responsive sites [GRE or IRF]) did not induce a similar alteration of the basal transcription levels. To evaluate the biological relevance of these observations made in vitro, the mutations were introduced into an infectious BLV molecular clone. After injection into sheep, it appeared that all the recombinants were infectious in vivo and did not revert into a wild-type virus. All of them, except one, propagated at wild-type levels, indicating that viral spread was not affected by the mutation. The sole exception was the CRE mutant; proviral loads were drastically reduced in sheep infected with this type of virus. We conclude that a series of sites (NF-kappa B, IRF, GRE, and the E box) are not required for efficient viral spread in the sheep model, although mutation of some of these motifs might induce a minor phenotype during transient transfection assays in vitro. Remarkably, a provirus (pBLV-Delta 21-bp) harboring only two TxRE was infectious and propagated at wild-type levels. And, most importantly, reconstitution of a consensus CRE, within the 21-bp enhancers increases binding of CREB/ATF proteins but abrogates basal repression of LTR-directed transcription in vitro. Suboptimal CREs are, however, essential for efficient viral spread within infected sheep, although these sites are dispensable for infectivity. These results suggest an evolutionary selection of suboptimal CREs that repress viral expression with escape from the host immune response. These observations, which were obtained in an animal model for HTLV-1, are of interest for oncovirus-induced pathogenesis in humans.

Activating Transcription Factor 1↗

A method for the large-scale cloning of nuclear proteins and nuclear targeting sequences on a functional basis.

We describe here a selection strategy allowing the cloning of sequences that contain a functional nuclear targeting signal. Our method relies on the use of green fluorescent protein fusion proteins to identify nuclear targeting sequences. Transfected cells expressing nuclear protein fusions were isolated on the basis of their nuclear fluorescence using flow cytometry and the transfected DNAs were recovered after bacterial transformation with total DNA from pools of sorted cells. Starting from a cDNA expression library, in which only 1% of the expressed proteins were nuclear, we obtained a 70-fold enrichment in nuclear protein-encoding clones after a single round of selection. Among the 63 clones that have been partially sequenced to date, 25 (40%) corresponded to known nuclear proteins and 13 (20%) to previously uncharacterized sequences. Despite their ability to target the green fluorescent protein marker to the cell nucleus, about half of the cloned sequences did not encode canonical basic or bipartite nuclear localization signals. The method can thus be applied to the large-scale cloning of functional nuclear targeting sequences, which opens the way to a wide investigation of nuclear import mechanisms and to the identification of previously unknown nuclear proteins.

Animals↗

Nuclear targeting of proteins: how many different signals?

The nuclear import of proteins into the cell nucleus involves the recognition of a nuclear localization signal sequence, borne by the protein to be transported, by complex molecules called importins, that will subsequently mediate the crossing over of the nuclear envelope. The most frequently encountered signal sequence is made up of short stretches of basic amino acid residues and is recognized by importins alpha and/or beta. Other signal sequences have been described, and some have been shown to mediate the association with importins other than importin alpha or beta. Recently, approaches have been developed that allow the cloning, on a functional basis, of sequences able to specify the nuclear localization of proteins. A variety of peptidic motifs of limited size which do not contain previously described signal sequences were isolated in such assays. It reveals that the spectrum of sequences that are able to target a protein to the cell nucleus may be wider than currently expected. It will probably also lead to the identification of novel target sequences for importins and will demonstrate the implication of additional members of this family of proteins in nuclear transport.

Amino Acid Sequence↗

Critical residues of the homeodomain involved in contacting DNA bases also specify the nuclear accumulation of thyroid transcription factor-1.

The N-terminal end of thyroid transcription factor-1 (TTF-1) homeodomain is composed of a stretch of five basic amino-acids that is conserved in both POU- and NK2-class homeodomains and constitutes a functional nuclear localization signal. By analyzing the cellular distribution of fusion proteins, composed of a jellyfish green fluorescent variant and different parts of TTF-1, we show here that the presence of this basic sequence is not sufficient by itself to confer complete nuclear accumulation. By mutagenesis, we identified a second region located in the center of the DNA recognition helix of the homeodomain that is also able to specify a predominantly nuclear localization of the chimeric proteins, independently of the presence of the basic NLS. The destruction, by mutagenesis, of both the basic stretch and the motif in the DNA recognition helix led to the total loss of nuclear accumulation, indicating that complete nuclear accumulation of TTF-1 results from the concerted action of these two proteic signals. Both of the regions of the homeodomain that are involved in nuclear targeting also encompass critical amino-acids responsible for DNA binding site recognition, as evidenced by the loss of DNA binding activity in vitro upon mutagenesis. Specifically, residues in the central part of the DNA recognition helix are involved in contacting bases in the major groove of DNA and are the most conserved in homeodomain proteins, suggesting that this part of the homeodomain could play a general role in the nuclear localization of members of this family of proteins.

Animals↗

A canonical nerve growth factor-induced gene-B response element appears not to be involved in the cyclic adenosine monophosphate-dependent expression of differentiation in thyrocytes.

The expression of transcriptionally active nerve growth factor-induced gene-B (NGFI-B) is rapidly induced in thyroid follicular cells in response to cAMP stimulation. As the transcription of thyrocyte-specific genes is controlled by the cAMP cascade, we have investigated a possible involvement of NGFI-B in this control. Recombinant adenoviruses driving the expression of either the intact NGFI-B protein or a truncated form of it that lacks the capacity to transactivate a NBRE-dependent promoter, were used to infect dog thyrocytes maintained in primary culture. Northern blot analysis of total RNA from infected cells revealed that the expression of NGFI-B was not sufficient to induce a significant accumulation of specific transcripts (thyroglobulin, thyroperoxidase, sodium-iodide symporter) in unstimulated thyrocytes. The overproduction of the transcriptionally inactive form of NGFI-B in thyrocytes maintained in the presence of forskolin after infection did not impair the accumulation of the thyroid-specific transcripts. These data show that NGFI-B does not control the expression of differentiation in thyrocytes by acting through a canonical NBRE. As a consequence, we must consider that either the expression of NGFI-B in cAMP-stimulated thyrocytes is not critically linked to the expression of differentiation or that NGFI-B is implicated in a regulatory mechanism which differs from its known action at the level of a NBRE.

Adenoviridae↗

Two binding sites for thyroid transcription factor 1 (TTF-1) determine the activity of the bovine thyroglobulin gene upstream enhancer element.

A thyroid-specific enhancer element located upstream from the bovine thyroglobulin gene had been shown to contain three contiguous regions that are protected by thyroid transcription factor 1 (TTF-1) in footprinting experiments in vitro. The functional relevance of the individual TTF-1 binding sites was investigated in a transient assay in primary cultured thyrocytes. Using reporter constructs containing synthetic oligonucleotides overlapping the protected sequences we were able to show that only two out of the three TTF-1 binding sites exhibit transcription enhancing activity. Within the context of the complete enhancer sequence, the central 'inactive' TTF-1 site could be deleted whithout any consequence on the activity of the enhancer in the assay, whereas the presence of both terminal 'active' TTF-1 sites had previously been shown to be strictly required for enhancer function. Our results thus show that the activity of the bovine thyroglobulin upstream enhancer relies on the presence of a pair of TTF-1 binding sites separated by about 30 bp. These results also emphasize the need to assess experimentally the functional relevance of TTF-1 binding sites identified in footprinting experiments.

Animals↗

TTF-2 does not appear to be a key mediator of the effect of cyclic AMP on thyroglobulin gene transcription in primary cultured dog thyrocytes.

TTF-2 is a thyroid-specific winged-helix transcription factor which has been proposed to play a key role in the hormonal control of thyroglobulin and thyroperoxidase genes transcription in FRTL-5 cells. We have analyzed TTF-2 DNA-binding activity in primary cultures of dog thyrocytes maintained in control condition or in the presence of the cAMP agonist forskolin. Binding of 35S-labelled nuclear proteins to the TTF-2 recognition sequence identified the presence of two molecular species of 41.5 and 42.5 kDa. TTF-2 DNA-binding activity was clearly detectable in nuclear extracts from unstimulated cells and appeared increased in forskolin-treated cells. Thus, the presence of TTF-2 DNA-binding activity does not correlate with the cAMP-dependent activity of thyroglobulin and thyroperoxidase genes in this cell system. In addition, the mutation of the TTF-2 binding site in the thyroglobulin promoter resulted in a very reduced but still clearly cAMP-dependent promoter activity when assayed by transient expression in the same cells. These results do not support a dominant role for TTF-2 in the cAMP-dependent control of thyroglobulin gene transcription in primary cultured thyrocytes.

Animals↗

Production of dog calcyphosine in bacteria and lack of phosphorylation by the catalytic subunit of protein kinase A in vitro.

Calcyphosine is a calcium-binding protein containing four EF-hand domains that is found in several epithelia and in some cells of the central nervous system. In thyroid follicular cells, calcyphosine is synthesized and phosphorylated in response to stimulation by thyrotropin and cAMP agonists. The cDNA coding for dog calcyphosine has been expressed in bacteria under the control of the T7 promoter. Recombinant calcyphosine was purified from crude bacterial lysates by a combination of anion-exchange and hydrophobic interaction chromatography. Phosphorylation assays using the purified catalytic subunit of protein kinase A and the recombinant or the native calcyphosine revealed that, contrary to a previous report, calcyphosine is not significantly phosphorylated by this enzyme in vitro.

Animals↗

Cloning and sequence analysis of human calcyphosine complementary DNA.

Calcyphosine, initially identified as thyroid protein p24, is a calcium-binding protein containing four EF-hand domains. It was first cloned and characterized in the dog and corresponds to R2D5 antigen in rabbit. Using the canine calcyphosine cDNA sequence as a probe, we have isolated its human counterpart from a thyroid cDNA library. The two sequences display a high degree of conservation, both at nucleotide and deduced amino acid levels. Sequence comparison with other proteins showed that the closest homologue of calcyphosine is the crustacean CCBP-23 protein. Northern blot analysis revealed that calcyphosine messenger RNA is much less abundant in human than in canine thyrocytes. Western blot experiments indicated that the amount of protein is also dramatically reduced in man compared to dog.

Amino Acid Sequence↗

A zinc-dependent DNA-binding activity co-operates with cAMP-responsive-element-binding protein to activate the human thyroglobulin enhancer.

Footprinting experiments involving the human thyroglobulin gene enhancer and thyroid nuclear extracts revealed a protected region called X2, containing an incomplete cAMP-responsive element (CRE). Band-shift experiments identified two binding activities recognizing the X2 element: a CRE-binding protein (CREB)/activating transcription factor (ATF) relative that binds the half CRE motif and a second factor that interacts with a G-rich motif located just upstream from the CRE. The first factor appears to be CREB itself, as indicated by the supershifting when using an antibody directed against CREB, and the second DNA-binding activity involved was shown to be zinc-dependent and exhibited an apparent molecular mass of 42-44 kDa in South-Western blotting experiments. This factor may represent a novel entity, which we named CAF, for 'CREB Associated Factor'. Three copies of X2 sequence conferred a strong cAMP-dependent transcriptional activation to a heterologous promoter in transient transfection assay in cAMP-stimulated primary thyrocytes and HeLa cells. Transfection experiments of constructs containing the X2 element mutated in either the CRE or the G-rich site showed that both motifs were required for this transcription activating function. Moreover, the combination of several individual X2 elements mutated in either the CRE or the G-rich motif did not exhibit full transcriptional activity. This suggests that, in the context of the X2 element, CREB requires a close interaction with CAF to achieve both basal and cAMP-dependent transcriptional activation.

Animals↗

Expression of a transactivation-deficient form of thyroid transcription factor I decreases the activity of co-transfected thyroglobulin and thyroperoxidase promoters.

Thyroid transcription factor I (TTF-1) plays a critical role in thyroid organogenesis and in the control of expression of several thyroid-specific genes, like those coding for thyroglobulin and thyroperoxidase. We have expressed the isolated DNA-binding homeodomain of TTF-1 in cultured thyroid cells by transient transfection. A specific reduction in the activity of co-transfected thyroglobulin and thyroperoxidase promoters was observed in the presence of the isolated TTF-1 homeodomain, as compared to their activity measured in the presence of a mutated homeodomain unable to bind DNA. The activity of the SV40 early promoter, used as a control, was only marginally affected in these experiments. The transactivation-deficient form of TTF-1 described here may thus be used for investigating other cellular processes that are dependent on TTF-1 transcriptional activity.

Cell Line↗

Pax 8 expression in primary cultured dog thyrocyte is increased by cyclic AMP.

Pax 8 proteins are paired domain-containing transcription factors expressed in thyroid, kidney, ovary, placenta and developing brain. Thyroglobulin (Tg) and thyroperoxidase (TPO) genes, which are specifically expressed in thyroid follicular cells, both harbor a Pax 8 binding site in their proximal promoter region. The transcription of these genes is, as is the expression of most of the other differentiated functions of the thyrocyte, positively regulated by thyrotropin (TSH) via a cyclic-AMP (cAMP)-dependent mechanism. However, no typical cAMP-responsive element has been detected in the promoter region of Tg and TPO genes. We therefore investigated whether Pax 8 activity itself could be regulated by cAMP, which would support a role for these factors in the cAMP-dependent expression of differentiation in thyroid cells. In this paper we show that the expression of Pax 8 mRNA and proteins are increased by treatment of the thyrocyte with forskolin. This suggests that Pax 8 could indeed participate in the mediation of the transcriptional activation of thyroid specific genes by cAMP. We also show that Pax 8 are nuclear phosphoproteins, although neither their phosphorylation, nor their nuclear translocation seem to be highly regulated by cAMP. During the course of this study, a new splicing variant of dog Pax 8, termed Pax 8g, has been isolated.

Amino Acid Sequence↗