Abstract
Interactions with the extracellular matrix (ECM) dictate cell fates. However, the complexity of dense ECM network and cell-surface molecules prevent the study of their dynamic interaction at the molecular level on living cells. Here, we focus on peptidyl prolyl cis/trans isomerases (PPIases) to dissect prolyl isomerization from other dynamic events. We reveal the contribution of PPIase on the mechanical properties of various ECM materials and on the dynamic cell–ECM interaction. To avoid complications associated with the existing spectroscopy-based methods such as light scattering, an assay was developed for detecting PPIase activity on living cell surface. This assay allows us to correlate PPIase activity with ECM development, and with the physiological and pathological states of the cells, including the functional properties of cancer cells and immune effector cells.
Highlights
Interactions with the extracellular matrix (ECM) dictate cell fates
To directly investigate the effect of peptidyl prolyl cis/trans isomerases (PPIases) on ECM dynamics, we tested the influence of PPIases on the gelation and stiffness of various ECM biomaterials using a rheometer
As the rearrangement of ECM network could be associated with a large amount of prolyl isomerization, it is unlikely that the effect involves only a specific peptidyl prolyl bond
Summary
Interactions with the extracellular matrix (ECM) dictate cell fates. the complexity of dense ECM network and cell-surface molecules prevent the study of their dynamic interaction at the molecular level on living cells. To avoid complications associated with the existing spectroscopy-based methods such as light scattering, an assay was developed for detecting PPIase activity on living cell surface. This assay allows us to correlate PPIase activity with ECM development, and with the physiological and pathological states of the cells, including the functional properties of cancer cells and immune effector cells. Whether PPIases directly regulate the structural dynamics of the dense polymer network of ECM and the complex cell surface proteins, affecting their interaction, has not been investigated so far to our knowledge. While the effect of catalyzed folding on ECM properties remains largely elusive, an assay for the direct detection of PPIase activity on living cells is still missing. A video abstract of this study is presented in Supplementary Movie 1
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