Dataset Information

Human, ovarian epithelial cancer cell line, LC-MSMS

ABSTRACT: We investigated the functions of ECM1 subtypes ECM1a (inlcuding wild type and mutant) and ECM1b in ovarian cancer cell line HEYA8. While ECM1a is oncogenic, ECM1b is a tumor suppressor. To identify the molecules binding to ECM1a or ECM1b within cells, protein samples were generated by co-IP using HA antibody to pull down proteins potentially binding to ECM1a (HA-tagged) (samples: P20170700270A1/A2/A3/A4) or ECM1b (HA-tagged) (samples: P20170700270B1/B2/B3/B4) within cells indicated in gel image P20170700270. To identify more cell surface markers besides integrins alpha X and beta 2 binding to ECM1a-WT or ECM1a-MT, three batches of protein samples were generated by co-IP using HA antibody to pull down total proteins binding to ECM1a-WT or ECM1a-MT shown in gel image R20191201880, or to pull down membrane fractionation proteins binding to ECM1a-WT or ECM1a-MT indicated in gel image 20200100053, or to pull down membrane fractionation proteins of HEYA8 cells treated with ECM1a-WT or ECM1a-MT conditioned media binding to ECM1-WT or ECM1a-MT shown in gel image 20200100054.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Ovary Epithelium Cell Line, Epithelial Cell

DISEASE(S): Ovarian Cancer

SUBMITTER: Gong Yang

LAB HEAD: GONG YANG

PROVIDER: PXD025239 | Pride | 2021-05-27

REPOSITORIES: Pride

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Publications

Extracellular matrix protein-1 secretory isoform promotes ovarian cancer through increasing alternative mRNA splicing and stemness.

Yin Huijing H Wang Jingshu J Li Hui H Yu Yinjue Y Wang Xiaoling X Lu Lili L Lv Cuiting C Chang Bin B Jin Wei W Guo Wenwen W Ren Chunxia C Yang Gong G

Nature communications 20210709 1

Extracellular matrix protein-1 (ECM1) promotes tumorigenesis in multiple organs but the mechanisms associated to ECM1 isoform subtypes have yet to be clarified. We report in this study that the secretory ECM1a isoform induces tumorigenesis through the GPR motif binding to integrin αXβ2 and the activation of AKT/FAK/Rho/cytoskeleton signaling. The ATP binding cassette subfamily G member 1 (ABCG1) transduces the ECM1a-integrin αXβ2 interactive signaling to facilitate the phosphorylation of AKT/FAK ...[more]

PMID: 34244494

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Project description:Aims and introduction: Cardiac fibrosis is the hallmark of cardiac disease, particularly myocardial infarction (MI), and is one of the most prevalent causes of heart failure. MI is intricately linked to inflammation, extracellular matrix (ECM) remodelling, and cardiac fibrosis, however the mechanisms underpinning these events remain poorly understood. We recently identified that ECM1 has potential to play a key role in cardiac wound healing but the cellular origins in the heart and specific mechanisms of ECM1 in fibrosis remain elusive. Therefore, we investigated the spatiotemporal, cell specific, expression profile of ECM1 in the healthy and diseased mouse and human heart and investigate ECM1 dependent human cardiac fibroblast (HuCFb) cell signalling mechanisms. Methods and results: Western blotting, immunohistochemistry (IHC) and mRNA in-situ hybridisation revealed that ECM1 protein expression was significantly upregulated in human ischaemic and dilated heart failure patients, and predominantly localised interstitially to fibrotic, inflammatory, and peri-vascular areas. ECM1 specific analysis of the Litviňuková et al. (2020) single-cell and -nuclei RNA sequencing (sc/snRNAseq) dataset of healthy human hearts, and the Farbehi et al. (2019) scRNAseq dataset of mouse hearts post-MI demonstrated that ECM1 expression originates from fibroblasts, macrophages, and pericytes/vascular mural cells in the heart. Further, we identify that post-MI ECM1 is expressed in a temporal dynamic flux from unactivated fibroblasts in sham-operated mice, to M1 macrophages (M1MΦ) at day-3, and myofibroblasts and M2MΦ at day-7. Phosphoproteomics of ECM1 treated human cardiac fibroblast cells (HuCFb) alongside ECM1 to HuCFb cell surface protein binding pull-down and mass spectrometry, revealed that ECM1 signalling goes via proteins associated with Rho protein signal transduction, cell-cell adhesion, microtubule dynamics, and cell chemotaxis pathways, potentially initiated by ECM1 to CTNND1 binding on the cell surface. Further mechanistic analyses identified that ECM1 inhibits HuCFb cell migration and stimulates inflammatory (IL-6 and IL-1β mRNA expression), fibrotic (TGF-β1, TGF-β2 and Col1a2 mRNA expression), and non-canonical Wnt signalling pathways (Wnt5a mRNA expression and JNK1/2/3 and MYPT1 phosphorylation). Conclusions: This study demonstrates that ECM1 expression originates from macrophages and fibroblasts in the mouse and human heart. ECM1 has significant effects on HuCFb migration, inflammatory, fibrotic, Rho protein, and Wnt5a/non-canonical Wnt signalling pathways. Together, ECM1 plays an important role in cardiac wound healing and may represent a novel mechanism of inflammation-fibrosis crosstalk and progression post-MI.

			Action	DRS
	P20170700270.tif	Other
	P20170700270_A1.dat	Other
	P20170700270_A1.raw	Raw
	P20170700270_A1.xml	Xml
	P20170700270_B1.dat	Other