Results 61 to 70 of about 140,500 (312)

Adaptor protein CIN85 potentiates the motility of osteosarcoma cells via the Akt/mTOR and MMP2‐COL3A1 axis

open access: yesMolecular Oncology, EarlyView.
CIN85 is highly expressed in osteosarcoma, particularly in metastatic lesions. Its overexpression increases cell migration and Matrigel invasion, while silencing CIN85 suppresses these behaviors. Transcriptome analysis shows that CIN85 regulates MMP2, COL3A1, and Akt/mTOR signaling. Targeting these pathways reverses CIN85‐induced motility, highlighting
Iryna Horak   +10 more
wiley   +1 more source

IL-1β-Induced Matrix Metalloprotease-1 Promotes Mesenchymal Stem Cell Migration via PAR1 and G-Protein-Coupled Signaling Pathway

open access: yesStem Cells International, 2018
Mesenchymal stem cells (MSCs) are known for homing to sites of injury in response to signals of cellular damage. However, the mechanisms of how cytokines recruit stem cells to target tissue are still unclear.
Ming-Siou Chen   +5 more
doaj   +1 more source

Angiotensin Type 2 Receptor Stimulation Ameliorates Left Ventricular Fibrosis and Dysfunction via Regulation of Tissue Inhibitor of Matrix Metalloproteinase 1/Matrix Metalloproteinase 9 Axis and Transforming Growth Factor β1 in the Rat Heart [PDF]

open access: yes, 2014
Left ventricular (LV) remodeling is the main reason for the development of progressive cardiac dysfunction after myocardial infarction (MI). This study investigated whether stimulation of the angiotensin type 2 receptor is able to ameliorate
Dahlöf, Bjorn   +10 more
core   +2 more sources

Tumor‐stromal crosstalk and macrophage enrichment are associated with chemotherapy response in bladder cancer

open access: yesFEBS Open Bio, EarlyView.
Chemoresistance in bladder cancer: Macrophage recruitment associated with CXCL1, CXCL5 and CXCL8 expression is characteristic of Gemcitabine/Cisplatin (Gem/Cis) Non‐Responder tumors (right side) while Responder tumors did not show substantial tumor‐stromal crosstalk (left side). All biological icons are attributed to Bioicons: carcinoma, cancerous‐cell‐
Sophie Leypold   +11 more
wiley   +1 more source

Matrix metalloproteinase-2, tissue inhibitor of matrix metalloproteinase-2, and transforming growth factor beta 1 in the aqueous humor and serum of patients with pseudoexfoliation syndrome

open access: yesClinical Ophthalmology, 2014
Selcuk Kara,1 Nilgun Yildirim,2 Ahmet Ozer,2 Omer Colak,3 Afsun Sahin21Department of Ophthalmology, Canakkale Onsekiz Mart University School of Medicine, Canakkale, 2Department of Ophthalmology, Eskisehir Osmangazi University Hospitals, Meselik ...
Kara S   +4 more
doaj  

Disparate Remodeling of the Extracellular Matrix and Proteoglycans in Failing Pediatric Versus Adult Hearts

open access: yesJournal of the American Heart Association: Cardiovascular and Cerebrovascular Disease, 2018
Background Dilated cardiomyopathy (DCM) is a common cause of heart failure in adult and pediatric patients, but the underlying mechanism may vary in adults and children, with few studies conducted to date.
Sayantan Jana   +7 more
doaj   +1 more source

Matrix Metalloproteinases and Glaucoma Treatment. [PDF]

open access: yes, 2020
Matrix metalloproteinases (MMPs) are a family of proteolytic enzymes that degrade extracellular matrix (ECM) components such as collagen and have important roles in multiple biological processes, including development and tissue remodeling, both in ...
Dibas, Mohammed   +3 more
core  

Epigenetic Regulation of Matrix Metalloproteinase-1 and -3 Expression in Mycobacterium tuberculosis Infection. [PDF]

open access: yes, 2017
In pulmonary tuberculosis (TB), the inflammatory immune response against Mycobacterium tuberculosis (Mtb) is associated with tissue destruction and cavitation, which drives disease transmission, chronic lung disease, and mortality.
Alland   +52 more
core   +2 more sources

Matrix metalloproteinase‐9 regulates cell adhesion and membrane protrusive activity of ovarian cancer cells

open access: yesFEBS Open Bio, EarlyView.
Matrix metalloproteinase‐9 (MMP9) drives ovarian cancer progression. Using MMP9‐null cells (M9‐KO) created from ovarian cancer cells, we found MMP9 loss did not block Epidermal Growth Factor (EGF)‐driven E‐cadherin dissolution or EMT but delayed and reduced EGF‐driven membrane protrusions. Transient MMP9 re‐expression drove membrane protrusion.
Claire Strauel   +8 more
wiley   +1 more source

MMP-2, MMP-9, TIMP-1, and TIMP-2 in the Peripheral Blood of Patients with Differentiated Thyroid Carcinoma

open access: yesCancer Management and Research, 2019
Wen-jing Zhang, Bing Song, Tao Yang Department of General Surgery, Tianjin First Central Hospital, Tianjin 300192, People’s Republic of ChinaCorrespondence: Bing Song Email song2002bing@163.comIntroduction: The objective of this study was to assess
Zhang W, Song B, Yang T
doaj  

Home - About - Disclaimer - Privacy