Ask about this productRelated genes to: CCDC52 antibody
- Gene:
- SPICE1 NIH gene
- Name:
- spindle and centriole associated protein 1
- Previous symbol:
- CCDC52
- Synonyms:
- SPICE
- Chromosome:
- 3q13.2
- Locus Type:
- gene with protein product
- Date approved:
- 2006-01-02
- Date modifiied:
- 2014-11-19
Related products to: CCDC52 antibody
Related articles to: CCDC52 antibody
- Keloids are the abnormal accumulation of collagen in the dermis, which leads to the formation of raised fibrous tissue at the site of injury and the development of a hard scar. The underlying pathological mechanisms associated with keloids have not been fully elucidated. In this study, two GEO datasets (GSE44270 and GSE7890) were employed alongside two machine learning algorithms, Support Vector Machine-Recursive Feature Elimination (SVM-RFE) and Random Forest, to identify diagnostic biomarkers associated with centrosome replication. Following identifying these biomarkers, researchers conducted a functional enrichment analysis to elucidate their biological significance and constructed a gene regulatory network to map their interactions. Furthermore, the study investigated the role of SPICE1 in keloid formation, utilizing a mouse model to explore its potential implications in this pathological process. Researchers identified ten diagnostic markers associated with centrosome replication, among which SPICE1 was significantly upregulated in keloid tissues and fibroblasts. In vivo experiments further demonstrated that the overexpression of SPICE1 promotes keloid formation. Additionally, functional enrichment analysis revealed a connection between these markers and immune cells, suggesting that the immune system may play a crucial role in the development of keloids. This study indicates that SPICE1 is a potential diagnostic marker and therapeutic target for keloids. It offers new insights into the pathological mechanisms of keloids and the development of novel treatments. - Source: PubMed
Publication date: 2025/04/01
Wang YinXia ZhengguoWang WengtingZhang JingsongHu ChaoWang FanWang JunLi Xiaojing - Osteosarcoma (OS) is recognized as a prevalent primary bone malignancy, particularly affecting adolescents during their growth spurts. Despite its clinical significance, the underlying biological characteristics and associated prognostic factors remain incompletely understood. The identification of novel molecular players involved in osteosarcoma progression could enhance our understanding of its pathogenesis and potentially inform patient management strategies. - Source: PubMed
Publication date: 2025/02/21
Tong WeilaiXie XinshengShu ZhiguoNie JiangboYang XianheYang FengLiu ZhiliLiu Jiaming - Osteosarcoma, a highly invasive and metastatic primary bone malignancy, remains a significant clinical challenge due to the limited improvement in overall survival despite advances in treatment strategies. This highlights the urgent need for the development of more effective therapeutic options. In response, we have developed a novel paclitaxel (PTX)-loaded nanodrug system, PLGA-CS-1@PTX, by incorporating a synthesized epoxy-tetrapeptide derivative (compound 1) with poly(lactic-co-glycolic acid) (PLGA) and chitosan (CS), forming the PLGA-CS-1 composite system. The system was thoroughly characterized for its physicochemical properties, including morphology, particle size, and in vitro release behavior. Scanning electron microscopy (SEM) confirmed the nanostructure of the particles, with particle sizes around 170 nm and a narrow PDI (<0.15), indicating a uniform distribution. In vitro release studies showed a pH-responsive release profile, with 84.8 % of PTX released at pH 5.4 after 65 h of incubation, compared to 68.1 % at pH 6.4 and 14.8 % at pH 7.4, demonstrating good drug release control in acidic environments. Biological assays demonstrated significant inhibition of osteosarcoma cell proliferation in both HOS and U2OS cell lines, with a dose-dependent reduction in SPICE1 expression, suggesting that PLGA-CS-1@PTX can effectively suppress the proliferative activity of osteosarcoma cells by modulating SPICE1 levels. The hydrophobic segment of the peptide enhanced the drug loading capacity and minimized side effects, improving the overall safety profile of the system. This composite system effectively integrates the strengths of each component, offering a promising, safe, and efficient strategy for osteosarcoma treatment with great potential for clinical application. - Source: PubMed
Publication date: 2025/02/04
Lin YunfeiWang Bing - Metastasis is an unavoidable event happened among almost all small cell lung cancer (SCLC) patients. However, the molecular driven factors have not been elucidated. Recently, a novel hydrolase called cell migration inducing hyaluronidase (CEMIP) triggered both migration and invasion in many tumors but not SCLC. Therefore, in this study, we verified that CEMIP promoted migration and invasion in SCLC and applied proteomics analysis to screen out potential target profiles and the signaling pathway related to CEMIP regulation. - Source: PubMed
Publication date: 2020/07/09
Li LiPan YingxingMo XiaoxiangWei TongtongSong JinjingLuo MinHuang GuolinTeng CuifangLiang KaiMao NaiquanYang Jie - Aurora kinases play a major role in mitosis by regulating diverse substrates. Defining their critical downstream targets is important in understanding Aurora kinase function. Here we have developed an unbiased computational approach to identify new Aurora kinase substrates based on phosphorylation site clustering, protein localization, protein structure, and species conservation. We validate the microtubule-associated proteins Clasp2, Elys, tubulin tyrosine ligase-like polyglutamylase residues 330-624 and spindle and centriole associated protein 1, residues 549-855 (SPICE1), as Aurora A and B kinases substrates in vitro. We also demonstrate that SPICE1 localization is regulated by Aurora kinases during mitosis. In the absence of Aurora kinase activity, SPICE1 remains at centrioles but does not target to the spindle. Similarly, a nonphosphorylatable SPICE1 mutant no longer localizes to the spindle. Finally, we show that misregulating SPICE1 phosphorylation results in abnormal centriole number, spindle multipolarity, and chromosome alignment defects. Overall, our work indicates that temporal and spatial Aurora kinase-mediated regulation of SPICE1 is important for correct chromosome segregation. In addition, our work provides a database-search tool that enables rapid identification of Aurora kinase substrates. - Source: PubMed
Publication date: 2018/11/28
Deretic JovanaKerr AlastairWelburn Julie P I