Ask about this productRelated genes to: SAE1 Blocking Peptide
- Gene:
- SAE1 NIH gene
- Name:
- SUMO1 activating enzyme subunit 1
- Previous symbol:
- -
- Synonyms:
- AOS1, FLJ3091, Sua1
- Chromosome:
- 19q13.32
- Locus Type:
- gene with protein product
- Date approved:
- 2006-10-31
- Date modifiied:
- 2014-11-18
Related products to: SAE1 Blocking Peptide
Related articles to: SAE1 Blocking Peptide
- Alkyl shikimates (SAEs) bearing linear and branched alkyl groups (R) ranging from CH to CH were synthesized and assayed for proliferative activity toward human dermal fibroblasts; proliferation increase (PRA), measured using a CCK-8 assay kit, was used as the primary endpoint. Several SAEs exhibited significant PRA, depending on the concentration added to the culture medium and alkyl group structure. However, shikimic acid (SA) added to the culture medium did not induce fibroblast proliferation. SAEs with CH, CH, and CH alkyl groups (SAE-1, SAE-2, and SAE-3a,b) induced a 30-50% increase in cell proliferation at a concentration of 5.5 mM, while SAEs with a CH groups (SAE-4a,b,c) showed low PRA and those with a CH groups (SAE-5a,b,c) exhibited strong cytotoxicity (CYT: decrease in cell viability) at this concentration. The proliferation rates of SAEs at 5.5 mM correlated significantly with their calculated log P (ClogP) values, which reflect hydrophobicity and cell membrane permeability (quadratic regression; coefficient of determination, r = 0.977-0.953. Based on these results, we proposed a mechanism in which membrane-permeable SAEs could form complexes with carboxylesterase (CES) present in dermal fibroblasts and be subsequently hydrolyzed into SA and alcohols (ALs) intracellularly, with the resulting SA potentially inducing PRA. In contrast, SA added extracellularly cannot enter cells due to its high hydrophilicity and therefore cannot induce PRA. In order to evaluate the stability of the proposed complexes, we estimated binding energies between CES and SAEs by quantum mechanical methods; however, the results showed no significant differences in binding energy attributable to alkyl chain length or steric effects of the SAE alkyl groups. The most plausible explanation for the differences in PRA among SAEs is that intracellularly regenerated SA promotes fibroblast proliferation, whereas the regenerated ALs may cause CYT. Alkyl group-dependent differences in AL toxicity may account for the concentration-dependent variation in SAE-induced PRA. In fact, when the CYT of linear alkyl alcohols (ALs-1, 2, 3a, 4a, and 5a) was measured by CCK-8 at a concentration of 100 mM, the results showed that differences in AL alkyl chain length significantly influenced cell viability, which was consistent with their ClogP values (CYT order; R = CH > CH > CH > CH ≥ CH). - Source: PubMed
Publication date: 2026/06/02
Morishita HidetadaUmezawa KojiKojima Masanobu - Idiopathic inflammatory myopathies (IIMs) are autoimmune, systemic diseases that affect skeletal muscles. The causes are not fully understood. IIMs present with proximal weakness, elevated muscle enzymes (primarily creatine phosphokinase, or CPK), and multiorgan involvement, often pulmonary. Muscle tissue shows leukocyte infiltration, and specific autoantibodies are present. We aimed to investigate the possible association between the rs16944 polymorphism and the risk of developing IIMs. - Source: PubMed
Publication date: 2026/04/01
García-De la Torre IgnacioMendoza-Lujambio IreneAndrade-Ortega LiliaVazquez-Del Mercado MónicaLamadrid-Gámez KarinaPérez-Rostro CelsoPérez-Covarrubias Daniel - Small ubiquitin-related modifiers (SUMOs) are covalently conjugated onto the proteome and serve as signaling molecules in many aspects of eukaryotic cell biology, from and to . The conjugatable SUMO variants, SUMO1 and the almost identical SUMO2 and SUMO3 (designated SUMO2/3), are processed by an E1(SAE1:SAE2)-E2(UBC9)-E3 enzyme cascade to produce SUMO-modified proteins. The prerogative of the SUMO biology field is to identify and study the specific proteins undergoing SUMOylation, which grants us insights into the biological pathway of interest. This protocol was developed using the human osteosarcoma cell line U2OS to enable the investigation of SUMO conjugates in mitosis, the cell division phase of the cell cycle. We enrich the cell population for mitotic cells, which are isolated and subjected to stringent lysis conditions involving a high concentration of SDS and DTT in RIPA buffer, to promote complete protein denaturation. The lysates in high SDS RIPA buffer are diluted to reduce the overall SDS concentration and undergo conventional immunoprecipitation using SUMO1- or SUMO2/3-specific antibodies bound to protein A/G agarose beads. The samples are then compatible with downstream readouts such as western blots and mass spectrometry. This protocol detects endogenous SUMOylated proteins and avoids exogenous SUMO overexpression, which can alter SUMO conjugate formation. Furthermore, this denaturing protocol ensures only SUMOylated proteins are immunoprecipitated, and not their interactors. Key features • Purifies endogenous SUMO-modified proteins by building on Becker et al. [1]. • Enriches and isolates cells in mitosis using nocodazole and mitotic shake-off. • 1% SDS RIPA lysis promotes robust denaturation ahead of SUMO-specific immunoprecipitation. • Compatible with downstream readouts such as western blots and mass spectrometry. - Source: PubMed
Publication date: 2026/04/05
Walker Alexandra KLanz Alexander JMorris Joanna R - The 2023 International Myositis Assessment and Clinical Studies Group (IMACS) guidelines introduced a standardized risk-stratification model for cancer screening in idiopathic inflammatory myopathies (IIM). However, real-world data on their application remain limited. This study aimed to evaluate the effectiveness of IMACS-based risk stratification in predicting malignancy and assess adherence to cancer screening recommendations in a multicentric Italian IIM cohort. - Source: PubMed
Pellico Maria RosaBochicchio CristinaIannone ClaudiaCavalli SilviaMagi IlariaBatani VeronicaTonutti AntonioGrazzini SilviaDella Pina SilviaGatti AlessiaSette ManuelMinniti AntoninaDe Santis MariaCeribelli AngelaConticini EdoardoCavazzana IlariaCampochiaro CorradoDe Luca GiacomoCaporali RobertoDel Papa Nicoletta - SSc is a proteopathy with limited diagnostic and therapeutic options. This study aimed to uncover structural protein alterations in dermal fibroblasts from diffuse cutaneous (dc)SSc patients using a novel method: limited proteolysis-MS (LiP-MS). - Source: PubMed
Li JingyaAbegg DanielMalinovska LilianaRudnik MichałDistler OliverBłyszczuk PrzemysławPicotti PaolaKania Gabriela