Last update 19 Sep 2024

ECM1

Last update 19 Sep 2024

Basic Info

Synonyms

ECM1, extracellular matrix protein 1, Secretory component p85

Introduction

Involved in endochondral bone formation as negative regulator of bone mineralization. Stimulates the proliferation of endothelial cells and promotes angiogenesis. Inhibits MMP9 proteolytic activity.

Drugs associated with ECM1

NCT-202

Target

ECM1

Mechanism

ECM1 inhibitors

Active Org.

NovaCell Technology, Inc.

Originator Org.

NovaCell Technology, Inc.

Active Indication

Breast Cancer [+2]

Inactive Indication-

Drug Highest PhasePreclinical

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

100 Clinical Results associated with ECM1

100 Translational Medicine associated with ECM1

0 Patents (Medical) associated with ECM1

517

Literatures (Medical) associated with ECM1

01 Oct 2024·Talanta

Au-decorated Ti3C2Tx/porous carbon immunoplatform for ECM1 breast cancer biomarker detection with machine learning computation for predictive accuracy

Article

Author: Khoso, Salim ; Karakuş, Selcan ; El-Bahy, Zeinhom M ; Tumrani, Sadam Hussain ; Soomro, Razium Ali ; Thabet, Hamdy Khamees ; Küçükdeniz, Tarık

Electrochemical immunosensors, surpassing conventional diagnostics, exhibit significant potential for cancer biomarker detection. However, achieving a delicate balance between signal sensitivity and operational stability, especially at the heterostructure interface, is crucial for practical immunosensors. Herein, porous carbon (PC) integration with Ti₃C₂T_x-MXene (MX) and gold nanoparticles (Au NPs) constructs a versatile immunosensing platform for detecting extracellular matrix protein-1 (ECM1), a breast cancer-associated biomarker. The inclusion of PC provided robust structural support, enhancing electrolytic diffusion with an expansive surface area while synergistically facilitating charge transfer with Ti₃C₂T_x. The biosensor optimized with 1.0 mg PC demonstrates a robust electrochemical redox response to the surface-bound thionine (th) redox probe, utilizing an inhibition-based strategy for ECM1 detection. The robust antibody-antigen interactions across the PC-integrated Ti₃C₂T_x-Au NPs platform (MX-Au-C-1) enabled robust ECM1 detection within 0.1-7.5 nM, with a low limit of detection (LOD) of 0.012 nM. The constructed biosensor shows improved operational stability with a 98.6 % current retention over 1 h, surpassing MXene-integrated (MX-Au) and pristine Au NPs (63.2 % and 44.3 %, respectively) electrodes. Moreover, the successful adaptation of the artificial neural network (ANN) model for predictive analysis of the generated DPV data further validates the accuracy of the biosensor, promising its future application in AI-powered remote health monitoring.

02 Aug 2024·Journal of Proteome Research

Extracellular Matrix Protein Signatures of the Outer and Inner Zones of the Rat Adrenal Cortex

Article

Author: Lotfi, Claudimara Ferini Pacicco ; Freitas, Danilo Henriques de Oliveira ; Auricino, Thais Barabba ; Kremer, Jean Lucas ; Palmisano, Giuseppe ; Bongiovani Rodrigues, Fernanda ; Santiago, Veronica Feijoli

This study analyzes the extracellular matrix (ECM) signatures of the outer (OF = capsule + subcapsular + zona glomerulosa cells) and inner fractions (IF = zona fasciculata cells) of the rat adrenal cortex, which comprise two distinct microenvironment niches. Proteomic profiles of decellularized OF and IF samples, male and female rats, identified 252 proteins, with 32 classified as ECM-component and ECM-related. Among these, 25 proteins were differentially regulated: 17 more abundant in OF, including Col1a1, Col1a2, Col6a1, Col6a2, Col6a3, Col12a1, Col14a1, Lama5, Lamb2, Lamc1, Eln, Emilin, Fbln5, Fbn1, Fbn2, Nid1, and Ltbp4, and eight more abundant in IF, including Col4a1, Col4a2, Lama2, Lama4, Lamb1, Fn1, Hspg2, and Ecm1. Eln, Tnc, and Nid2 were abundant in the female OF, while Lama2, Lama5, Lamb2, and Lamc1 were more abundant in the male IF. The complex protein signature of the OF suggests areas of tissue stress, stiffness, and regulatory proteins for growth factor signaling. The higher concentrations of Col4a1 and Col4a2 and their role in steroidogenesis should be further investigated in IF. These findings could significantly enhance our understanding of adrenal cortex functionality and its implications for human health and disease. Key findings were validated, and data are available in ProteomeXchange (PXD046828).

01 Aug 2024·Cancer Letters

Remodeling of tumor microenvironment by extracellular matrix protein 1a differentially regulates ovarian cancer metastasis

Article

Author: Xu, Xinyi ; Yang, Lina ; Yu, Yinjue ; Li, Xiaojing ; Lyu, Cuiting ; Wang, Jingshu ; Ren, Chunxia ; Yang, Gong ; Li, Hui ; Xin, Zhaochen

We previously reported that extracellular matrix protein 1 isoform a (ECM1a) promotes epithelial ovarian cancer (EOC) through autocrine signaling by binding to cell surface receptors αXβ2. However, the role of ECM1a as a secretory molecule in the tumor microenvironment is rarely reported. In this study, we constructed murine Ecm1-knockout mice and human ECM1a-knockin mice and further generated orthotopic or peritoneal xenograft tumor models to mimic the different metastatic stages of EOC. We show that ECM1a induces oncogenic metastasis of orthotopic xenograft tumors, but inhibits early-metastasis of peritoneal xenograft tumors. ECM1a remodels extracellular matrices (ECM) and promotes remote metastases by recruiting and transforming bone marrow mesenchymal stem cells (BMSCs) into platelet-derived growth factor receptor beta (PDGFRβ⁺) cancer-associated fibroblasts (CAFs) and facilitating the secretion of angiopoietin-like protein 2 (ANGPTL2). Competing with ECM1a, ANGPTL2 also binds to integrin αX through the P1/P2 peptides, resulting in negative effects on BMSC differentiation. Collectively, this study reveals the dual functions of ECM1a in remodeling of TME during tumor progression, emphasizing the complexity of EOC phenotypic heterogeneity and metastasis.

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ECM1

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