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At least 271 records · Page 15Linked to original sources
PubMed1991

Pathogenic anti-DNA idiotype (16/6 Id) in systemic lupus erythematosus.

Systemic lupus erythematosus (SLE) is regarded as a classical autoimmune disease. Despite this belief, no one has been able to induce the disease in naive animals, neither with DNA nor with anti-DNA antibodies. We report on the induction of SLE in BALB/c mice following immunization with a pathogenic anti-DNA idiotype (16/6 Id) or its anti-Id. We also report on a specific treatment with T suppressor cells specific for the 16/6 Id. The induction of SLE in naive mice with a pathogenic anti-DNA Id suggests an additional mechanism for the diversity of manifestations in this disease.

Animals↗
PubMed1978

[Comparative study of immunoelectrophoresis (IEF) and immunoelectroosmophoresis-immunodiffusion (IEOF-ID) used in the diagnosis of paracoccidioidomycosis].

Immunoelectroporesis (IEF) and immunoelectroosmophoresis-immunodiffusion (IEOP-ID) (1) were comparatively used in the diagnosis of 16 patients with mycologically proved paracocidioidomycosis. In IEF, 5 different precipitin arcs were found and identified with arabic numbers. Arc. '1', cathodic, present in all the patients, is assimilated to specific arcs previously described by other authors. In IEOP-ID both 'cathodic' and 'anodic' arcs were observed in all the sera. A high number of precipitin arcs were revealed by IEOP-ID technique in comparison to IEF in every case. This should be due to the presence of cathodic arcs 'I' and '2' of the immunoelectrophoregram at both sides of the IEOP-ID preparate.

Antigens, Fungal↗
PubMed2004

Id genes and proteins as promising targets in cancer therapy.

Since the identification of Id proteins more than a decade ago, much work has demonstrated their regulatory roles in development, cell fate and lineage determination, proliferation, differentiation, angiogenesis, invasion and migration. Recent studies reveal not only that Id protein expression is significantly correlated both with cancer progression and with overall prognosis, but also that it can be exploited as a therapeutic target. This review will focus on the recent advances in our understanding of the relationships between Id expression and cancer, as well as providing a rationale for developing therapeutic strategies using Ids as targets to treat metastatic cancers.

Animals↗
PubMed2006

Involvement of Sp-1 in the regulation of the Id-1 gene during trophoblast cell differentiation.

Id-1, a member of the helix-loop-helix transcription factor family, inhibits the differentiation of Rcho-1 cells, which were derived from rat choriocarcinoma and consist of trophoblast stem cells. Id-1 is expressed at a high level in undifferentiated trophoblast stem cells and then down-regulated during early differentiation, and is thought to be a key regulator in the trophoblast giant-cell differentiation pathway. In this study, we analyzed the signaling mechanism regulating the high expression levels of Id-1 in undifferentiated Rcho-1 cells. Promoter deletion analysis revealed that a 31-bp sequence (Box-2 region), located between -200 and -169bp in the Id-1 promoter is necessary for the promoter activity. Electrophoretic mobility shift assays and DNA affinity precipitation assays showed that Box-2-binding activity was decreased during differentiation and that Sp-1 protein bound to this sequence. The protein level of Sp-1 was decreased during the differentiation. These results suggest that the Sp-1 protein level may regulate the Box-2-binding activity and the trophoblast giant-cell differentiation.

Animals↗
PubMed1991

Expression of Id, a negative regulator of helix-loop-helix DNA binding proteins, is down-regulated at confluence and enhanced by dexamethasone in a mouse osteoblastic cell line, MC3T3E1.

The message of Id (for "inhibitor of DNA binding") was expressed in an osteoblastic cell line, MC3T3E1, when the cells were in early cultures, while undetectable after the cells became confluent. The abundance of Id message in MC3T3E1 cells in early cultures was increased when the cells were treated with dexamethasone. This effect was time and dose dependent in a range between 10(-11)M and 10(-7)M. Id message expression was not enhanced by TGF-beta, 1,25-dihydroxyvitamin D3, retinoic acid, interleukin 1-alpha, interleukin 6, tumor necrosis factor-alpha or parathyroid hormone. These observations indicate for the first time the presence of HLH protein family member, Id, in osteoblast-like cells and its regulation by dexamethasone.

Actins↗
PubMed2003

BMP induction of Id proteins suppresses differentiation and sustains embryonic stem cell self-renewal in collaboration with STAT3.

The cytokine leukemia inhibitory factor (LIF) drives self-renewal of mouse embryonic stem (ES) cells by activating the transcription factor STAT3. In serum-free cultures, however, LIF is insufficient to block neural differentiation and maintain pluripotency. Here, we report that bone morphogenetic proteins (BMPs) act in combination with LIF to sustain self-renewal and preserve multilineage differentiation, chimera colonization, and germline transmission properties. ES cells can be propagated from single cells and derived de novo without serum or feeders using LIF plus BMP. The critical contribution of BMP is to induce expression of Id genes via the Smad pathway. Forced expression of Id liberates ES cells from BMP or serum dependence and allows self-renewal in LIF alone. Upon LIF withdrawal, Id-expressing ES cells differentiate but do not give rise to neural lineages. We conclude that blockade of lineage-specific transcription factors by Id proteins enables the self-renewal response to LIF/STAT3.

Animals↗
PubMedDate not supplied

The Inventory of Drinking Situations (IDS) in current drinkers with different degrees of alcohol problems.

The Inventory of Drinking Situations (IDS) is a questionnaire developed to characterize the situations where alcoholics in treatment drank excessively. The purpose of the present study was to extend the understanding of this instrument as a research and diagnostic tool by applying it to drinking situations in individuals who have never been diagnosed as alcoholics, but who may have problems due to alcohol. Seventy-three current drinkers (32.1 +/- 9.98 years) were examined with a version of the IDS suitable for nonalcoholic individuals. Using the CAGE test we categorized the subjects in five groups according to their score. Correlational analysis revealed that the IDS subscale scores increased significantly with the severity of drinking problems. The CAGE score, the factor-derived scale Negative Situations, being male, and a preference for drinking alone were also correlated with the amount of alcohol consumed, while age was correlated with none of the variables of interest. To facilitate the analysis of the profiles of drinking situations, the IDS subscales underwent a factor analysis that rendered two factor-derived scales, suggesting that drinking occurs both in positive and in negative situations. In persons with more alcohol problems, according to their high CAGE scores, there was more drinking in negative situations that in positive ones. Accordingly, we confirmed that the profiles of drinking situations seen in problem drinkers indicated that situations related to negative emotions are more important determinants to drink. Implications of a shift from drinking in positive to drinking in negative emotional situations are discussed. We further substantiated the value of this test instrument for studies on drinking situations and for studies in nonalcoholic individuals.

Adult↗
PubMed2001

Id4 expression and its relationship to other Id genes during avian embryonic development.

We present the sequence and expression pattern of chick Id4 and compare its distribution to that of other vertebrate Id genes. At early stages, Id4 expression is discrete, with transcript transiently expressed in subsets of migrating neural crest cells, the dorsal myocardium, the segmental plate mesoderm, and the tail bud. Later, expression is also observed in the telencephalic vesicles and corneal epithelium. Of all the Id genes, Id4 exhibits the most restricted pattern in the developing nervous system, with little expression in the presumptive neural crest or placodes. Id4 appears in the neural tube much later than other Id genes. However, all four Id genes display overlapping patterns in the branchial arches and tail bud.

Amino Acid Sequence↗
PubMed2003

Id proteins in development, cell cycle and cancer.

Id proteins are important parts of signaling pathways involved in development, cell cycle and tumorigenesis. They were first shown to act as dominant negative antagonists of the basic helix-loop-helix family of transcription factors, which positively regulate differentiation in many cell lineages. The Id proteins do this by associating with the ubiquitous E proteins and preventing them from binding DNA or other transcription factors. Id proteins also associate with Ets transcription factors and the Rb family of tumor suppressor proteins, and are downstream targets of transforming growth factor beta and bone morphogenic protein signaling. Thus, the Id proteins have become important molecules for understanding basic biological processes as well as targets for potential therapeutic intervention in human disease.

Aging↗
PubMed1996

New loop-loop tertiary interactions in self-splicing introns of subgroup IC and ID: a complete 3D model of the Tetrahymena thermophila ribozyme.

BACKGROUND: Group I introns self-splice via two consecutive trans-esterification reactions in the presence of guanosine cofactor and magnesium ions. Comparative sequence analysis has established that a catalytic core of about 120 nucleotides is conserved in all known group I introns. This core is generally not sufficient for activity, however, and most self-splicing group I introns require non-conserved peripheral elements to stabilize the complete three-dimensional (3D) structure. The physico-chemical properties of group I introns make them excellent systems for unraveling the structural basis of the RNA-RNA interactions responsible for promoting the self-assembly of complex RNAs. RESULTS: We present phylogenetic and experimental evidence for the existence of three additional tertiary base pairings between hairpin loops within peripheral components of subgroup IC1 and ID introns. Each of these new long range interactions, called P13, P14 and P16, involves a terminal loop located in domain 2. Although domains 2 of IC and ID introns share very strong sequence similarity, their terminal loops interact with domains 5 and 9 (subgroup IC1) and domain 6 (subgroup ID). Based on these tertiary contacts, comparative sequence analysis, and published experimental results such as Fe(II)-EDTA protection patterns, we propose 3D models for two entire group I introns, the subgroup IC1 intron in the large ribosomal precursor RNA of Tetrahymena thermophila and the SdCob.1 subgroup ID intron found in the cytochrome b gene of Saccharomyces douglasii. CONCLUSIONS: Three-dimensional models of group I introns belonging to four different subgroups are now available. They all emphasize the modular and hierarchical organization of the architecture of group I introns and the widespread use of base-pairings between terminal hairpin loops for stabilizing the folded and active structures of large and complex RNA molecules.

Animals↗
PubMed2003

Effect of angiogenesis inhibition by Id loss and the contribution of bone-marrow-derived endothelial cells in spontaneous murine tumors.

Angiogenic defects in Id mutant mice inhibit the growth of tumor xenografts, providing a genetic model for antiangiogenic stress. Our work tests the consequences of such stress on progression of more physiological Pten+/- tumors. While tumor growth occurs despite impaired angiogenesis, disruption of vasculature by Id loss causes tumor cells to experience hypoxia and necrosis, the extent of which is tumor dependent. We show that bone-marrow-derived endothelial precursors contribute functionally to neovasculature of some but not all Pten+/- tumors, partially rescuing Id mutant phenotype. We demonstrate that loss of Id1 in tumor endothelial cells results in downregulation of several proangiogenic genes, including alpha6 and beta4 integrins, matrix metalloprotease-2, and fibroblast growth factor receptor-1. Inhibition of these factors phenocopies loss of Id in in vivo angiogenesis assays.

Animals↗
PubMed2001

The function of E- and Id proteins in lymphocyte development.

Helix-loop-helix proteins are essential factors for lymphocyte development and function. In particular, E-proteins are crucial for commitment of lymphoid progenitors to the B- and T-cell lineages. E-proteins are negatively regulated by the Id class of helix-loop-helix proteins. The Id proteins function as dominant-negative inhibitors of E-proteins by inhibiting their ability to bind DNA. Here, we review the role of E-proteins and their Id protein antagonists in lymphocyte proliferation and developmental progression. In addition, we discuss how E-protein activity and Id gene expression are regulated by T-cell receptor (TCR) and pre-TCR-mediated signalling.

Animals↗
PubMed2001

Id proteins in cell cycle control and cellular senescence.

The Id family of helix-loop-helix (HLH) proteins are thought to affect the balance between cell growth and differentiation by negatively regulating the function of basic-helix-loop-helix (bHLH) transcription factors. Although it has been suggested for some time that Id is involved in cell cycle regulation, little is known about the molecular mechanism of this control. Recent studies, however, have revealed that Id binds to important cell cycle regulatory proteins other than bHLH proteins. Two such proteins, pRB (retinoblastoma tumour suppressor protein) family proteins and Ets-family transcription factors are known to play key roles in cell cycle regulation, transformation and tumour suppression. Through the characterization of these pathways we will begin to understand the mechanisms by which Id controls normal and abnormal cell cycle progression.

Animals↗
PubMed1997

Aminoglycoside 2'-N-acetyltransferase genes are universally present in mycobacteria: characterization of the aac(2')-Ic gene from Mycobacterium tuberculosis and the aac(2')-Id gene from Mycobacterium smegmatis.

The genus Mycobacterium comprises clinically important pathogens such as M. tuberculosis, which has reemerged as a major cause of morbidity and mortality world-wide especially with the emergence of multidrug-resistant strains. The use of fast-growing species such as Mycobacterium smegmatis has allowed important advances to be made in the field of mycobacterial genetics and in the study of the mechanisms of resistance in mycobacteria. The isolation of an aminoglycoside-resistance gene from Mycobacterium fortuitum has recently been described. The aac(2')-Ib gene is chromosomally encoded and is present in all isolates of M. fortuitum. The presence of this gene in other mycobacterial species is studied here and genes homologous to that of M. fortuitum have been found in all mycobacterial species studied. In this report, the cloning of the aac(2')-Ic gene from M. tuberculosis H37Rv and the aac(2')-Id gene from M. smegmatis mc(2)155 is described. Southern blot hybridizations have shown that both genes are present in all strains of this species studied to date. In addition, the putative aac(2')-Ie gene has been located in a recent release of the Mycobacterium leprae genome. The expression of the aac(2')-Ic and aac(2')-Id genes has been studied in M. smegmatis and only aac(2')-Id is correlated with aminoglycoside resistance. In order to elucidate the role of the aminoglycoside 2'-N-acetyltransferase genes in mycobacteria and to determine whether they are silent resistance genes or whether they have a secondary role in mycobacterial metabolism, the aac(2')-Id gene from M. smegmatis has been disrupted in the chromosome of M. smegmatis mc(2)155. The disruptant shows an increase in aminoglycoside susceptibility along with a slight increase in the susceptibility to lysozyme.

Acetyltransferases↗
PubMed2003

Angiogenesis impairment in Id-deficient mice cooperates with an Hsp90 inhibitor to completely suppress HER2/neu-dependent breast tumors.

Id proteins bind basic helix-loop-helix transcription factors and function as dominant negative inhibitors of gene expression. Id1 and Id3 are required for the recruitment of bone marrow-derived endothelial cell precursors and tumors transplanted into Id-deficient mice demonstrate impaired angiogenesis. Mouse mammary tumor virus-neu mice were bred with Id1-/-Id3+/- mice to ascertain the role of Id1 and Id3 in mammary tumorigenesis in a more physiologically relevant model. In mammary tumors from these mice, Id1 and Id3 expression was restricted to the vascular endothelium. Id1 and Id3 deficiency did not prevent or delay tumor formation but did alter tumor phenotype. The tumors that developed in the Id-deficient mice were larger and cystic with a viable rim of tumor cells surrounding a nonviable core of cellular debris. The Hsp90 chaperone protein is required for cellular survival under condition of environmental stress and for the stability of the neu oncogene. 17-Allylamino-17-demethoxygeldanamycin, an Hsp90 inhibitor, was used to treat these mice. Whereas 17-allylamino-17-demethoxygeldanamycin only modestly delayed the growth of established mammary tumors in WT mice for Id, tumor suppression was dramatically more effective in an Id1- or Id3-deficient background. These data suggest that tumorigenesis can occur in a background of defective angiogenesis but that tumors developing in such an environment may be especially sensitive to inhibitors of neu and stress-activated survival pathways. Thus angiogenesis inhibitors in combination with inhibitors of Hsp90 function should be evaluated for the treatment of advanced breast cancer.

Animals↗
PubMed1994

Id proteins control growth induction in mammalian cells.

Id1, Id2, and Id3 (HLH462) dimerize with members of the basic helix-loop-helix protein family, but due to the absence of the basic region, the resulting heterodimers cannot bind DNA. Therefore Id-type proteins negatively regulate DNA binding of the basic helix-loop-helix proteins. Here we report that Id1, Id2, and Id3 are induced shortly after serum stimulation in arrested NIH 3T3. Antisense oligonucleotides against the Id mRNAs delay the reentry of arrested cells into the cell cycle elicited by stimulation with serum or growth factors. Antisense oligonucleotides against all three Id mRNAs are more effective than individual ones. Combined, these results indicate that Id proteins are involved in the control of growth induction.

3T3 Cells↗
PubMed1994

Id-1 as a possible transcriptional mediator of muscle disuse atrophy.

Disuse of muscle leads to atrophy of the fibers. This atrophy is correlated with reduced transcription. We found that when muscle was denervated or paralyzed with a nerve impulse block, the mRNA for Id-1, a negative regulator of transcription, was increased 2- to 7-fold. To test the effect of high Id-1 levels in active muscles, we made transgenic mice in which Id-1 was overexpressed under control of regulatory elements which confer tissue- and fiber-type-specific expression in differentiated muscle cells. Fiber types with high transgene expression were atrophic compared to those in wild-type litter mates. In contrast, fiber types with low transgene expression displayed hypertrophy, presumably caused by an overload due to reduced strength in atrophic synergistic fibers. Apart from the selective effects on fiber caliber, the muscle tissue showed no signs of pathology, and apart from a characteristic slightly lower body weight, the transgenic animals looked and behaved normally. We suggest that in the mature muscle, Id-1 may be involved in regulating muscle fiber size at the transcriptional level during disuse.

Animals↗
PubMed1999

Immortalization of primary human keratinocytes by the helix-loop-helix protein, Id-1.

Basic helix-loop-helix (bHLH) DNA-binding proteins have been demonstrated to regulate tissue-specific transcription within multiple cell lineages. The Id family of helix-loop-helix proteins does not possess a basic DNA-binding domain and functions as a negative regulator of bHLH proteins. Overexpression of Id proteins within a variety of cell types has been shown to inhibit their ability to differentiate under appropriate conditions. We demonstrate that ectopic expression of Id-1 leads to activation of telomerase activity and immortalization of primary human keratinocytes. These immortalized cells have a decreased capacity to differentiate as well as activate phosphorylation of the retinoblastoma protein. Additionally, these cells acquire an impaired p53-mediated DNA-damage response as a late event in immortalization. We conclude that bHLH proteins play a pivotal role in regulating normal keratinocyte growth and differentiation, which can be disrupted by the immortalizing functions of Id-1 through activation of telomerase activity and inactivation of the retinoblastoma protein.

Catalytic Domain↗