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The friction peak that occurs in tire-road sliding when the contact changes from wet to dry was previously attributed to capillary cohesion, van der Waals attraction, and surface roughness, but the detailed mechanisms have yet to be revealed. In this study, friction and static contact experiments were conducted using a custom-built in situ optical microtribometer, which allowed us to investigate the evolution of the friction, normal load, and contact area between a polydimethylsiloxane (PDMS) film and a silicon nitride ball during water volatilization. The friction coefficient increased by 100%, and the normal force dropped by 30% relative to those in the dry condition during the wet-to-dry transition. In static contact experiments, the probe indentation depth increased, and the normal load decreased by ∼60% as the water evaporated. Combining the friction and static contact results, we propose that the large friction peak that appeared in this study can be attributed to the combined effects of increased adhesive capillary force and increased plowing during the wet-to-dry transition. [ABSTRACT FROM AUTHOR]

A transient and unusually high friction coefficient always appears when the tire–road interface changes from wet to dry and has been known as the tacky regime. This paper aims to study the mechanism of such friction peak that appears in a hydrophilic contact between an oxidized silicon nitride (ox-Si3N4) sphere and a sheet of oxidized polydimethylsiloxane (ox-PDMS) film. The results found, in the tacky regime, the friction coefficient increased by 23% from the dry sliding condition. A threshold technique was used to quantify the real solid–solid contact area (Ar) and contact area with a water film less than 110 ± 2 nm thick (Af) during the tacky transition. A strong linear relation between the transient friction coefficient and the water film area ratio (Af/(Af + Ar)) is found. We proposed that the transient frictional force (1) consists of the solid–solid shear force and the capillary shear force, (2) could be analyzed with a simple rule-of-mixture model, and (3) is dominated by thin, high shear strength water films within the apparent contact area. Based on the proposed model, capillary bridges within the apparent contact area have a shear strength ~ 2 times of the solid–solid contact and contribute 40% to the transient friction force. [ABSTRACT FROM AUTHOR]

Collagen prolyl 4-hydroxylase (P4H) expression and collagen hydroxylation in cancer cells are necessary for breast cancer progression. Here, we show that P4H alpha 1 subunit (P4HA1) protein expression is induced in triple-negative breast cancer (TNBC) and HER2 positive breast cancer. By modulating alpha ketoglutarate (α-KG) and succinate levels P4HA1 expression reduces proline hydroxylation on hypoxia-inducible factor (HIF) 1α, enhancing its stability in cancer cells. Activation of the P4HA/HIF-1 axis enhances cancer cell stemness, accompanied by decreased oxidative phosphorylation and reactive oxygen species (ROS) levels. Inhibition of P4HA1 sensitizes TNBC to the chemotherapeutic agent docetaxel and doxorubicin in xenografts and patient-derived models. We also show that increased P4HA1 expression correlates with short relapse-free survival in TNBC patients who received chemotherapy. These results suggest that P4HA1 promotes chemoresistance by modulating HIF-1-dependent cancer cell stemness. Targeting collagen P4H is a promising strategy to inhibit tumor progression and sensitize TNBC to chemotherapeutic agents. Hyperactivation of HIF-1α is crucial in progression of triple-negative breast cancer, but how HIF-1α stability is maintained in a hypoxia-independent manner is unclear. Here, the authors show collagen prolyl-4-hydroylase 1 stabilises HIF-1α and is involved in chemoresistance in TNBC. [ABSTRACT FROM AUTHOR]

Pleckstrin homology domain and leucine rich repeat protein phosphatase 1 (PHLPP1) is a member of the serine/threonine family of phosphatases. It has been studied in organs including brain, heart, pancreas, adipose, breast, and prostate. Human PHLPP1 encodes two splice variants - PHLPP1α (~140-150 kDa) and PHLPP1β (~180-190 kDa). Commercial antibodies are widely used to characterize PHLPP1 proteins in cells/tissues. Here we validate five different antibodies to detect PHLPP1α/β by Western blot using PHLPP1 WT/KO mice. All antibodies recognize PHLPP1β in brain. Only a single antibody (Cosmo Bio Co) detects PHLPP1α (~145-150 kDa). The other four antibodies detect a non-specific signal at ~150 kDa as evidenced by its abundance in PHLPP1 KO tissues. Results suggest Cosmo antibody is a better reagent to detect PHLPP1α by Western blot. In contrast, we found it unsuitable for immunofluorescence applications in brain. Our findings caution interpretation of the ~150 kDa band detected by some PHLPP1 antibodies in rodent and human tissues. Results also recapitulate the importance of including molecular weight standards in Western blot data to simplify retrospective analysis. [ABSTRACT FROM AUTHOR]