Results 81 to 90 of about 18,239 (220)

Cellular Signalling Networks in High Altitude Pulmonary Hypertension: From Canonical Pathways to Emerging Targets

Cell Proliferation, EarlyView.
This review elucidates the intricate cellular signalling networks involved in high‐altitude pulmonary hypertension (HAPH), integrating canonical pathways like HIF, MAPK and BMP with emerging targets such as Wnt/β‐catenin, Notch, Hippo‐YAP and IL‐6. It highlights potential therapeutic strategies targeting these pathways to mitigate vascular remodelling ...
Sheng Ding, Ju Chen, Zhaoyang Li, Yang Yu, Weijie Wang, Yan Liao, Jin Yang, Dianxiang Lu, Yujiang Fan   +8 more
wiley   +1 more source

Immobilized metal affinity chromatography co-purifies TGF-β1 with histidine-tagged recombinant extracellular proteins.

PLoS ONE, 2012
Extracellular recombinant proteins are commonly produced using HEK293 cells as histidine-tagged proteins facilitating purification by immobilized metal affinity chromatography (IMAC).
Jasvir Kaur, Dieter P Reinhardt
doaj   +1 more source

Extracellular matrix and proteolysis: mechanisms driving irreversible changes and shaping cell behavior

The FEBS Journal, EarlyView.
Irreversible ECM proteolysis by remodeling enzymes shapes development, homeostasis, and disease. ECM‐degrading proteases display cell specificity and are governed by shared mechanisms, exhibiting functional redundancy in generating matrikines, growth factors, and cytokines.
Inna Solomonov, Orit Kollet, Irit Sagi
wiley   +1 more source

Fibrillin-1 microfibril deposition is dependent on fibronectin assembly [PDF]

Journal of Cell Science, 2008
Newly deposited microfibrils strongly colocalise with fibronectin in primary fibroblasts. Microfibril formation is grossly inhibited by fibronectin depletion, but rescued by supplementation with exogenous cellular fibronectin. As integrin receptors are key determinants of fibronectin assembly, we investigated whether they also influenced microfibril ...
Kinsey, Rachel, Williamson, Matthew R., Chaudhry, Shazia, Mellody, Kieran T., McGovern, Amanda, Takahashi, Seiichiro, Shuttleworth, C. Adrian, Kielty, Cay M.   +7 more
openaire   +4 more sources

A guide to the types, structures, and multifaceted functions of matrix metalloproteinases in cancer

The FEBS Journal, EarlyView.
Matrix metalloproteinases (MMPs) orchestrate cancer progression and metastasis through proteolytic and non‐proteolytic actions. By remodeling the tumor microenvironment, enhancing growth factor availability, and modulating cell behavior, MMPs promote proliferation, migration or invasion, and epithelial‐to‐mesenchymal transition. Alongside extracellular
Zoi Piperigkou, Sylvia Mangani, Spyros Kremmydas, Nikolaos E. Koletsis, Nikos K. Karamanos   +4 more
wiley   +1 more source

P10.05 REDUCED MOLECULAR FLEXIBILITY IN THE LARGE ARTERIES OF DIABETIC RATS

Artery Research, 2009
In Type 1 and 2 diabetes tissue stiffening is evident from measurements of the gross mechanical properties of the vasculature. In general, pathological glycosylation of extracellular matrix proteins may play an important role in increasing stiffness in ...
R. Akhtar, N. Gardiner, J.K. Cruickshank, B. Derby, M.J. Sherratt   +4 more
doaj   +1 more source

Infection of the brown alga Ectocarpus siliculosus by the oomycete Eurychasma dicksonii induces oxidative stress and halogen metabolism [PDF]

, 2016
Acknowledgments We would like to thank the Aberdeen Proteome Facility, especially Phil Cash, David Stead and Evelyn Argo for assistance with 2D electrophoresis and mass spectrometry. M.S.
Asada, Austin, Bhadauria, Bouarab, Bréhélin, Butler, Chen, Chen, Cock, Cock, Collén, Contreras, Cosse, Crépineau, Dantuma, Dittami, Farmer, Farnham, Fosu-Nyarko, Franco, Gachon, Gachon, Goulitquer, Grenville-Briggs, Grenville-Briggs, Grenville-Briggs, Grenville-Briggs, Gschloessl, Heesch, Kav, Klochkova, Konotchick, Küpper, Küpper, Küpper, Küpper, Küpper, Küpper, Küpper, Küpper, Küpper, La Barre, Langenkämper, Le Bail, Matros, Mayer, Mithöfer, Müller, Nelson, Orozco-Cárdenas, Palmer, Park, Paul, Pearson, Pfaffl, Potin, Ritter, Roeder, Roy, Salgado, Santino, Schmidt, Sekimoto, Singh, Strittmatter, Strittmatter, Tan, Thomas, Thomas, Tonon, Tsirigoti, Tsirigoti, Uppalapati, Vidi, Vizcaíno, Weinberger, Weinberger, Weinberger, West, West, Yang, Youssef, Ytterberg, Zambounis, Zhou   +84 more
core   +1 more source

Behind the scenes: how the EMILIN/Multimerin family shapes the cancer landscape

The FEBS Journal, EarlyView.
The EMILIN/Multimerin family members regulate key hallmarks of cancer—including apoptosis, angiogenesis, metastasis, and tumor microenvironment remodeling. As indicated, their function in immune evasion, drug resistance, and metabolic reprogramming remains largely unexplored.
Evelina Poletto, Naike Casagrande, Emanuele Di Siena, Greta Carobolante, Lucrezia Camicia, Giorgia Schinello, Samanta Muzzin, Enrica Timis, Paola Spessotto, Maurizio Mongiat   +9 more
wiley   +1 more source

Fibulin-5 interacts with fibrillin-1 molecules and microfibrils [PDF]

Biochemical Journal, 2005
Fibulin-5 plays an important role in elastic fibre formation in vivo. We have investigated the molecular interactions between fibulin-5 and components of fibrillin-rich microfibrils which form a template for elastin. Fibulin-5 interacted in a dose-dependent manner with a fibrillin-1 N-terminal sequence and with tropoelastin, but not with MAGP-1 ...
Freeman, LJ, Lomas, A, Hodson, N, Sherratt, MJ, Mellody, KT, Weiss, AS, Shuttleworth, A, Kielty, CM   +7 more
openaire   +3 more sources

Angiotensin II type 1 receptor antagonists alleviate muscle pathology in the mouse model for laminin-alpha2-deficient congenital muscular dystrophy (MDC1A) [PDF]

, 2012
BACKGROUND: Laminin-alpha2-deficient congenital muscular dystrophy (MDC1A) is a severe muscle-wasting disease for which no curative treatment is available.
Lin, Shuo, Meinen, Sarina, Ruegg, Markus A.   +2 more
core   +1 more source