Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.3324/haematol.006072 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
α9β1 integrin & its ligands as new potential biomarkers in FMF.
Indian J Med Res
July 2024
Department of Medical Pharmacology, Bursa Uludag University Faculty of Medicine, Nilufer-Bursa, Turkey.
Article Synopsis
- Familial Mediterranean Fever (FMF) is a hereditary illness that causes fever, stomach pain, and joint swelling, and colchicine is the main treatment but doesn’t cure it.
- In a study, they looked at blood samples from 50 people, including healthy individuals and those with active or inactive FMF, to measure certain markers tied to the disease.
- The results showed that some markers were higher in patients having FMF attacks compared to healthy people and those in remission, suggesting these markers could help in finding new ways to diagnose and treat FMF.
Interactions between integrin α9β1 and VCAM-1 promote neutrophil hyperactivation and mediate poststroke DVT.
Blood Adv
May 2024
Department of Pathology and Translational Pathobiology, Louisiana State University Health Sciences Center-Shreveport, Shreveport, LA.
Venous thromboembolic events are significant contributors to morbidity and mortality in patients with stroke. Neutrophils are among the first cells in the blood to respond to stroke and are known to promote deep vein thrombosis (DVT). Integrin α9 is a transmembrane glycoprotein highly expressed on neutrophils and stabilizes neutrophil adhesion to activated endothelium via vascular cell adhesion molecule 1 (VCAM-1).
View Article and Find Full Text PDFSVEP1 influences monocyte to macrophage differentiation via integrin α4β1/α9β1 and Rho/Rac signalling.
Biochim Biophys Acta Mol Cell Res
August 2023
Department of Cardiovascular Sciences, University of Leicester and National Institute for Health Research Leicester Biomedical Research Centre, Glenfield Hospital, Leicester LE3 9QP, United Kingdom. Electronic address:
Background: The large extracellular matrix protein SVEP1 mediates cell adhesion via integrin α9β1. Recent studies have identified an association between a missense variant in SVEP1 and increased risk of coronary artery disease (CAD) in humans and in mice Svep1 deficiency alters the development of atherosclerotic plaques. However how SVEP1 functionally contributes to CAD pathogenesis is not fully understood.
View Article and Find Full Text PDFVascular smooth muscle- and myeloid cell-derived integrin α9β1 does not directly mediate the development of atherosclerosis in mice.
Atherosclerosis
November 2022
Center for Cardiovascular Research, Division of Cardiology, Department of Medicine, Washington University School of Medicine, Saint Louis, MO, 63110, USA; McDonnell Genome Institute, Washington University School of Medicine, Saint Louis, MO, 63108, USA; Department of Genetics, Washington University School of Medicine, Saint Louis, MO, 63110, USA. Electronic address:
Background And Aims: Sushi, von Willebrand factor type A, EGF pentraxin domain-containing 1 (SVEP1), an extracellular matrix protein, is a human coronary artery disease locus that promotes atherosclerosis. We previously demonstrated that SVEP1 induces vascular smooth muscle cell (VSMC) proliferation and an inflammatory phenotype in the arterial wall to enhance the development of atherosclerotic plaque. The only receptor known to interact with SVEP1 is integrin α9β1, a cell surface receptor that is expressed by VSMCs and myeloid lineage-derived monocytes and macrophages.
View Article and Find Full Text PDFThe integrin ligand SVEP1 regulates GPCR-mediated vasoconstriction via integrins α9β1 and α4β1.
Br J Pharmacol
November 2022
Department of Cardiovascular Sciences, University of Leicester and National Institute for Health Research Leicester Biomedical Research Centre, Glenfield Hospital, Leicester, UK.
Background And Purpose: Vascular tone is regulated by the relative contractile state of vascular smooth muscle cells (VSMCs). Several integrins directly modulate VSMC contraction by regulating calcium influx through L-type voltage-gated Ca channels (VGCCs). Genetic variants in ITGA9, which encodes the α9 subunit of integrin α9β1, and SVEP1, a ligand for integrin α9β1, associate with elevated blood pressure; however, neither SVEP1 nor integrin α9β1 has reported roles in vasoregulation.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!