Disease relevance of Ids

• We have demonstrated that the human anti-DNA Ab O-81, of which Ids are commonly detected in renal glomeruli of active lupus nephritis, uses the V3-7 gene [1].
• This result suggested that many Ids with anti-dsDNA antibody activity may contribute to lupus pathogenesis in this strain of mouse [2].
• In sera, significant numbers of SLE, RA and patients with other autoimmune diseases are positive for both Ids [3].
• Mucopolysaccharidosis type II (MPSII; Hunter syndrome) is a lysosomal storage disorder caused by a deficiency in the enzyme iduronate 2-sulfatase (IDS) [4].
• BACKGROUND: Hunter syndrome, mucopolysaccharidosis type II (MPS II), is a X-linked inherited disorder caused by the deficiency of the enzyme iduronate-2-sulfatase (IDS), involved in the lysosomal catabolism of the glycosaminoglycans (GAG) dermatan and heparan sulfate [5].

Psychiatry related information on Ids

• Data from the various combinations of Id and anti-Id (and anti-isotype) were used to construct a low-resolution three-dimensional model that revealed not only the approximate locations of Ids on the surface of the antibody variable domains but also details of the geometry of Id-anti-Id interactions not otherwise available [6].

High impact information on Ids

• Ids bind to the ETS DNA-binding domain and disrupt the formation of DNA-bound complexes between TCFs and SRF on the c-fos serum response element (SRE) [7].
• Here, we show that inhibitors of differentiation/DNA binding (Ids), helix-loop-helix (HLH) transcription factors, negatively regulate TRANCE-induced osteoclast differentiation [8].
• We have characterized in detail the phenotype of IDS-deficient mice, a model of human MPSII [4].
• Although Ids affect myogenesis, neurogenesis, and B-cell development, little is known about their in vivo functions in epithelia [9].
• The cells expressing E1A and Ids undergo apoptosis after accumulation in S phase, suggesting that S phase events are perturbed by E1A and Ids [10].

Biological context of Ids

• Ids are inhibitory helix-loop-helix (HLH) transcription factors and expression of Id genes in osteoblasts is under the control of calciotropic agents such as BMP and vitamin D. However, the function of Ids during bone formation in vivo has not yet been elucidated [11].
• Since the main part of the individual populations was found to interact Fc-independently via Fab-located binding sites, we suppose that the dimers are for the most part complexes of idiotypic (Ids) and anti-idiotypic abs (anti-Ids) [12].
• In particular, expression of Ids and Math1 overlapped in cochlear progenitor cells before cellular differentiation, but a specific downregulation of Id expression was observed in individual cells that differentiated as hair cells [13].

Anatomical context of Ids

• The Ids gene was expressed in mouse islets and beta- and alpha-clonal cells, in which it was localized intracellularly in lysosomes [14].
• Identification of iduronate-2-sulfatase in mouse pancreatic islets [14].
• IDS has a potential role in the normal pathway of lysosomal degradation of secretory peptides and is likely to be essential to maintain pancreatic beta-cell function [14].
• In addition, progenitor cells in which the expression of Ids was maintained during the time period for hair cell differentiation were inhibited from developing as hair cells [13].
• Inhibitors of differentiation and DNA binding (Ids) regulate Math1 and hair cell formation during the development of the organ of Corti [13].

Associations of Ids with chemical compounds

• The transcriptional expression of Ids in mouse islets increased with glucose in a dose-dependent manner (11.5, 40.2, 88, and 179% at 5.5, 11.1, 16.7, and 24.4 mM, respectively, P < 0.01 for 16.7 and 24.4 mM glucose vs. 3 mM glucose) [14].
• The lysosomal enzyme iduronate-2-sulfatase (IDS) is expressed in pancreatic islets and is responsible for degradation of proteoglycans, such as perlecan and dermatan sulfate [14].
• These 15A-associated Ids are expressed by some heterologous human antimeningococcal B polysaccharide MAbs, and they also are independently expressed by two human MAbs that are specific for either the H. influenzae b polysaccharide or the i erythrocyte antigen and that utilize the kappa I-15A V region [15].
• The iduronate-2-sulfatase (IDS) is a lysosomal enzyme that acts on sulphate groups on C-2 positions of the iduronic acid residues of the mucopolysaccharides heparan sulphate and dermatan sulphate [16].

Other interactions of Ids

• These results indicate that the apoptotic processes elicited by these inducers are different and differently affected by wt and mutated p53 and by Ids [17].
• These results indicate a key role for Ids in the regulation of expression of Math1 and hair cell differentiation in the developing cochlea [13].

Analytical, diagnostic and therapeutic context of Ids

• A three-dimensional map of the positions of four idiotypic determinants (idiotopes or Ids) and an isotypic determinant was derived by transmission electron microscopy of negatively stained immune complexes [6].
• Thus, immunoelectron microscopy is a useful complement to serologic, biochemical, and genetic strategies for the topographical analysis of immunoglobulin Ids or other epitopes [6].
• Immunofluorescent staining revealed the presence of RT-72Id and RT-84Id positive immunoglobulin deposits in 18% and 45%, respectively, of the lupus renal sections compared with none in the disease control group, suggesting that these Ids may contribute to the pathology of the disease [3].
• In this study, by reverse transcriptase polymerase chain reaction (RT-PCR) we analyzed the expression of the two mRNA transcripts for the IDS gene in murine tissues, in various human cell-lines and in cells from some Hunter patients [16].

References