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Biology subjects

Kamperman, M.

Publications and source records attributed to Kamperman, M..

2 recordsLinked to original sources

The Unfolded Protein Response Sensor PERK Mediates Mechanical Stress-induced Maturation of Focal Adhesion Complexes in Glioblastoma Cells

Stiffening of the brain extracellular matrix (ECM) in glioblastoma leads to mechanical stress, which is known to contribute to tumor formation and progression. Previously, we found that protein kinase R (PKR)-like endoplasmic reticulum kinase (PERK), a component of the unfolded protein response (UPR), plays a role in the adaptation of glioblastoma stem cells (GSCs) to matrix stiffness through PERK/FLNA dependent F-Actin remodeling. Here, we found that increases in matrix stiffness induces differentiation of GSCs that was not seen in PERK deficient GSCs. Furthermore, we investigated whether PERK is involved in detecting changes in matrix stiffness through focal adhesion complex (FAC) formation and maturation, which are instrumental for transmitting ECM dependent signaling. In PERK deficient GSCs, Vinculin and Tensin expression was decreased, while Talin and Integrin-{beta}1 expression was kept at the same level compared to PERK proficient cells. In addition, in the absence of PERK, Tubulin expression is sharply increased coupled with low Vimentin expression, which was observed as an opposite trend in the presence of PERK. In conclusion, our study reveals a novel role for PERK in regulating the formation of FACs during matrix stiffening, possibly associated with its regulatory capacity in F-Actin remodeling.

cancer biology↗

Resolving atomic-level dynamics and interactions of high-molecular weight hyaluronic acid in biomimetic ECM hydrogels by multidimensional solid-state NMR

High molecular weight (HMW) hyaluronic acid (HA) is a highly abundant natural polysaccharide and a fundamental component of the extracellular matrix (ECM). Its size and concentration regulate tissues macro- and microenvironments, and its upregulation is a hallmark feature of certain tumors. Yet, the conformational dynamics of HMW-HA and how it engages with components of the ECM microenvironment remain poorly understood on the molecular level. Probing the molecular structure and dynamics of HMW polysaccharides in a hydrated, physiological-like environment is crucial but also technically challenging. Here, we deploy advanced magic-angle-spinning (MAS) solid-state NMR (ssNMR) spectroscopy in combination with isotopic enrichment to enable an in-depth study of HMW-HA to address this challenge. This approach resolves multiple coexisting HA conformations and dynamics as a function of environmental conditions. By combining 13C-labeled HA with unlabeled ECM components, we detect by MAS NMR HA-specific changes in global and local conformational dynamics as a consequence of hydration and ECM interactions. These measurements reveal atom-specific variations in dynamics and structure of the N-acetylglucosamine (GlcNAc) moiety of HA. We discuss possible implications for interactions that stabilize the structure of HMW-HA and facilitate its recognition by HA-binding proteins. The described methods apply similarly to studies of the molecular structure and dynamics of HA in tumor contexts and in other biological tissues, as well as HMW-HA hydrogels and nanoparticles used for biomedical and/or pharmaceutical applications.

biophysics↗