Ask about this productRelated genes to: EGFL8 Blocking Peptide
- Gene:
- EGFL8 NIH gene
- Name:
- EGF like domain multiple 8
- Previous symbol:
- C6orf8
- Synonyms:
- NG3
- Chromosome:
- 6p21.32
- Locus Type:
- gene with protein product
- Date approved:
- 2002-08-02
- Date modifiied:
- 2016-10-05
Related products to: EGFL8 Blocking Peptide
Related articles to: EGFL8 Blocking Peptide
- To investigate the genetic causality between Human blood cell (HBC) traits and sporadic lymphangioleiomyomatosis (sLAM) by mediation joint multi-omics and eQTL Mendelian randomization analysis. - Source: PubMed
Publication date: 2026/01/27
Liu TianshuCai Yiting - Alzheimer's disease (AD) is a complex disorder with significant genetic contributions, yet only a limited number of risk loci have been conclusively identified. This research aimed to discover novel potential biomarkers for AD through multi-omics and brain pathology analysis. In this study, we investigated hippocampal molecular alterations in APP/PS1 mouse using transcriptomics and data-independent acquisition (DIA) proteomics. To further validate the involvement of differentially expressed genes (DEGs) and differentially expressed proteins (DEPs) in AD pathology and potential drug treatment, we performed an integrative analysis incorporating pathological data and protein-protein interaction networks. We identified 263 DEGs and 448 DEPs. Integrative transcriptomic and proteomic analyses revealed five co-upregulated DEGs/DEPs and one co-downregulated DEG/DEP. Comparison of KEGG pathway enrichment between the two datasets showed significant involvement in the complement and coagulation cascade, as well as neurodegeneration-multiple diseases. Furthermore, mRNA levels of LY86, CD180, and C1QB were strongly associated with amyloid-β plaque load in the AD mouse hippocampus. Protein-protein interaction analysis suggested that APP, LY86, CD180, and C1QB could serve as potential therapeutic targets for AD. The study identified three novel AD loci (EGFL8, ERMN, and CD180), with CD180 showing association with AD at both the expression and pathological levels, highlighting their potential roles in disease progression and therapeutic intervention. - Source: PubMed
Publication date: 2025/10/31
Zhao QingqingGou ChenLuo GuoshuaiDai ShujuanWang DanZhang ShifeiWang FengXu HuiHan YanbingWang Shitao - Previous research has highlighted the roles of epidermal growth factor-like (EGFL) 7 and EGFL8 in hepatocellular carcinoma (HCC), while EGFL9 has been implicated in other cancers such as breast cancer. Despite this, its role in HCC remains unexplored. This study aims to investigate EGFL9's impact on HCC progression. - Source: PubMed
Publication date: 2025/09/26
Li ZiyeFeng JingyangZhao LongchengWang LeiShen XiaobaoYuan WeiWang BailinWu Fan - Numerous extracellular matrix (ECM) proteins, referred to as the matrisome, are increased in Alzheimer's disease (AD). We recently demonstrated that many of these proteins colocalize with Aβ plaques and cerebral amyloid angiopathy (CAA), and some are present in dystrophic cellular processes within and around plaques. However, their precise roles in AD pathogenesis and their spatial and temporal distribution in postmortem brain tissue remain incompletely understood. Here, we performed a comprehensive immunohistochemistry analysis on postmortem brain samples spanning the spectrum of AD neuropathological change (ADNC: low, intermediate, and high). We assessed the accumulation of five matrisome proteins (MDK, SPOCK3, COL25aA1, SDC4, and EGFL8) across four brain regions differentially affected in AD (occipital cortex, hippocampus, striatum, and cerebellum) and examined their association with Aβ plaques, CAA, tau neurites, and neurofibrillary tangles (NFT). MDK in plaques increased consistently with ADNC severity across all regions. In contrast, SPOCK3, COL25A1, EGFL8, and SDC4 showed marked accumulation only in the occipital cortex and hippocampus, with sparse presence in the striatum and absence in the cerebellum. Notably, SPOCK3 exhibited pronounced regional specificity, with significantly higher levels in the hippocampus than in other areas. Morphological patterns of staining and degree of colocalization with Aβ and tau indicate that select matrisome proteins associate with either distinct types of Aβ deposits (neuritic versus diffuse plaques), while others may overlap more closely with tau pathology and/or dystrophic processes around plaques. Overall, our findings reveal region- and pathology-specific patterns of matrisome protein accumulation during AD progression. These proteins represent intriguing biomarkers of AD and are based on modeling studies potential therapeutic targets. - Source: PubMed
Publication date: 2025/07/24
Tsering WangchenPhilips Jennifer LGolde Todd EVillareal Jonathan AProkop Stefan - Numerous extracellular matrix (ECM) proteins, referred to as the matrisome, are increased in Alzheimer's disease (AD). We recently demonstrated that many of these proteins colocalize with Aβ plaques and cerebral amyloid angiopathy (CAA), and some are present in dystrophic cellular processes within and around plaques. However, their precise roles in AD pathogenesis and their spatial and temporal distribution in postmortem brain tissue remain incompletely understood. Here, we performed a comprehensive immunohistochemistry analysis on postmortem brain samples spanning the spectrum of AD neuropathological change (ADNC: low, intermediate, and high). We assessed the accumulation of five matrisome proteins (MDK, SPOCK3, COL25aA1, SDC4, and EGFL8) across four brain regions differentially affected in AD (occipital cortex, hippocampus, striatum, and cerebellum), and examined their association with Aβ plaques, CAA, tau neurites, and neurofibrillary tangles (NFT). MDK in plaques increased consistently with ADNC severity across all regions. In contrast, SPOCK3, COL25A1, EGFL8, and SDC4 showed marked accumulation only in the occipital cortex and hippocampus, with sparse presence in the striatum and absence in the cerebellum. Notably, SPOCK3 exhibited pronounced regional specificity, with significantly higher levels in the hippocampus than in other areas. Patterns of plaque staining and degree of colocalization indicate that select matrisome proteins associate with either distinct types of Aβ deposits (e.g, fibrillar and neuritic versus diffuse plaques), while others may correlate more closely with tau pathology and/or dystrophic processes around plaques. Overall, our findings reveal region- and pathology-specific patterns of these matrisome protein accumulation during AD progression. These proteins represent intriguing biomarkers of AD and based on modeling studies represent potential therapeutic targets. - Source: PubMed
Publication date: 2025/06/03
Tsering WangchenPhilips Jennifer LGolde Todd EVillareal Jonathan AProkop Stefan