Ask about this productRelated genes to: SDCBP Blocking Peptide
- Gene:
- SDCBP NIH gene
- Name:
- syndecan binding protein
- Previous symbol:
- -
- Synonyms:
- SYCL, MDA-9
- Chromosome:
- 8q12.1
- Locus Type:
- gene with protein product
- Date approved:
- 1998-02-11
- Date modifiied:
- 2015-12-16
Related products to: SDCBP Blocking Peptide
Related articles to: SDCBP Blocking Peptide
- The intrinsic dynamic asymmetry between homologous PDZ domains in multidomain scaffold proteins offers insight into how they achieve multivalent partner recognition. Through a systematic x-ray crystallographic analysis of tandem PDZ1-PDZ2 domains in human syntenin-1 (SDCBP/MDA-9), we solved nine high-resolution structures and uncovered fundamental differences in conformational plasticity between these sequentially similar domains. Pairwise root mean square deviation (RMSD) analysis of 20 PDZ1 structures across multiple crystal forms revealed substantial structural variability concentrated in the Lys119-Ile125 and Ala181-Glu184 loops-key regions governing ligand specificity within PDZ1's binding cleft-whereas PDZ2 maintained remarkable structural conservation, indicating divergent evolutionary constraints on these tandem domains. Comparative analysis of isotropic B-factors and multistructure RMSD highlighted the limitations of B-factors alone and emphasized the value of multistructure comparisons for mapping dynamic landscapes. Molecular dynamics (MD) simulations implemented through GROMACS corroborate the crystallographic observations, showing elevated residue-specific fluctuation values in PDZ1's ligand-binding interface compared to analogous PDZ2 regions, and steady-state heteronuclear NOE measurements support enhanced loop flexibility in PDZ1 relative to PDZ2. Together, these findings indicate that PDZ1's conformational diversity represents an inherent biophysical property rather than a crystallographic artifact, suggest a functional division of labor in which PDZ1's structural plasticity enables broad ligand recognition via conformational selection while PDZ2's rigid architecture stabilizes the tandem domain arrangement, and provide an atomic-level framework for developing domain-selective therapeutics targeting syntenin-1 in cancer, viral infection, and neurodevelopmental disorders. - Source: PubMed
Ando NatsunoHanazono YuyaSakuma KoyaNumoto NobutakaHamajima RyuseiTenno TakeshiOshima AtsunoriIto NobutoshiHiroaki Hidekazu - Cytogenetics analysis of adipocytic tumours revealed varieties of chromosomal translocations beyond MDM2 amplification, so, this report aimed to identify these translocations and recognise the altered genes with their fusion partners. - Source: PubMed
Atta I SShafek S IAbdel-Hamid M - Bone metastasis is a frequent and incurable consequence of advanced prostate cancer (PC). This process originates through an interplay between disseminated tumor cells and heterogeneous bone resident cells in the metastatic niche. Melanoma differentiation associated gene-9 (mda-9/Syntenin) is a pro-metastatic gene expressed in multiple organs, including bone marrow-derived mesenchymal stromal cells (BM-MSCs), under both physiological and pathological conditions. MDA-9/Syntenin coordinates the interactions between tumor cells and BM-MSCs, which promote establishment of metastatic tumors in the bone niche. Considering the importance of protein-protein interactions in regulating MDA-9/Syntenin functions, we focused on developing small molecule inhibitors of these interactions. We describe the translational potential of IVMT-Rx-4, an intermediate synthesis product of PDZ1i, in inhibiting PC bone metastasis. IVMT-Rx-4 has similar bioactivity as PDZ1i but with improved druggable properties, e.g., higher solubility and lower efflux. It promotes potent anti-invasive and anti-metastatic effects by inhibiting the MDA-9/Syntenin dependent tumor-derived platelet derived growth factor, PDGF-AA, and its related signalling in BM-MSCs. In addition, the combination of IVMT-Rx-4 and docetaxel enhances survival in experimental bone metastasis models. These observations reinforce the concept that together with metastasis suppression, IVMT-Rx-4 can boost the effectiveness of standard-of-care treatment. Collectively, the present work provides a framework for translational strategies to ameliorate health complications and morbidity associated with advanced PC. - Source: PubMed
Publication date: 2026/03/21
Maji SantanuKumar AmitMannangatti PadmanabhanModi JinkalGunawardena MadelineLoPresti Marion QMukhopadhyay Nitai DBrown Anne MPangeni RudraXu QingguoSantos Webster LLi JiongDas Swadesh KFisher Paul B - Tuberculosis pleural effusion (TPE) accounts for 30 ~ 80% of all pleural effusions in developing countries and remains a major contributor to global morbidity and mortality. Although TPE is often absorbed after anti-tuberculosis treatment, approximately 60% of patients develop pleural thickening and pleural fibrosis. However, the underlying mechanisms of pleural fibrosis followed TPE remain poorly understood. In this study, firstly we found that exosomes isolated from TPE were associated with pleural fibrotic changes both in vivo and in vitro, accompanied by activation of the TGF-β signaling pathway. Disruption of exosomes or inhibition of exosome biogenesis attenuated these fibrotic responses. miRNA profiling revealed a distinct exosomal miRNA signature in TPE compared with transudative pleural effusion. Among these miRNAs, down-regulated miR-135b-5p was associated with increased SDCBP expression in pleural mesothelial cells (PMCs), while up-regulated miR-150-3p correlated with enhanced expression of the integrin ITGB6. In addition, miR-503-5p, miR-25-3p, miR-92a-3p and miR-424-3p were linked to reduced Smad7 and Smurf1 expression and decreased ubiquitination of TGF-βRI, collectively favoring TGF-β pathway. Together, these findings suggested that TPE-derived exosomal miRNAs converged on key regulatory nodes of TGF-β signaling and contributed to pleural fibrogenesis. This study provides mechanistic insight into post-tuberculous pleural fibrosis and supports exosomal miRNAs profile as a promising target for prevention and treatment of pleural fibrosis. - Source: PubMed
Publication date: 2026/02/03
Jiang Li-JuanZheng Yuan-YiLiang Li-MeiJia Zi-HengDu Rong-HuiHuang HaiDai XiyongCheng Pei-PeiZhao Li-QinLi QianJiang Ye-HanCui Xiao-LinYe Shu-YiHu Shi-HeZhang He-DeLian Chen-YueFeng XiaoSong Lin-JieYu FanHe Xin-LiangXiong LiangXiang FeiWang XiaorongLiu An-DongWang MengYe HongMa Wan-Li - Developing small molecule drugs to treat metastatic cancer remains challenging and relies on the identification of novel druggable targets within the multistep metastatic cascade. To this end, the pro-metastatic scaffolding protein, MDA-9/Syntenin-1 was identified and confirmed as a suitable target uniquely involved in the multiple stages of metastasis. Recently, the first-in class PDZ1 domain inhibitor for MDA-9, PDZ1i, was identified displaying significant anti-invasion activity improving survival in an in vivo glioblastoma and in multiple metastatic cancer mouse models. Herein, we report a focused library of substituted 1-(benzo[d]thiazol-2-yl)-3-phenylurea derivatives inspired by the anti-invasion and anti-metastatic agent, PDZ1i. Our studies revealed that 1-(benzo[d]thiazol-2-yl)-3-phenylurea analogs bearing 6-trifluoromethyl (3y) and 6-bromo (3aa) substituents display anti-invasion activity comparable to PDZ1i. However, compounds 3y and 3aa displayed overall decreased cancer cell selectivity and MDA-9 activity relative to PDZ1i. Nonetheless, the reported 1-(benzo[d]thiazol-2-yl)-3-phenylurea derivatives serve as promising starting points for future development of small molecule anti-invasion agents with potential to prevent and treat metastatic cancers. - Source: PubMed
Publication date: 2026/02/05
Gwinn Reilly KMannangatti PadmanabhanMir Shahid MaqboolKumari ShikhaLe Mai KDas Swadesh KFisher Paul BSantos Webster L