Thaís Larissa Araujo de Oliveira Silva

• Abstract

  HSP70 is an essential molecular chaperone for vascular physiology. Recently, we demonstrated that HSP70 plays a central role in vitro angiogenesis in primary human umbilical veins (HUVEC), coronary artery (HCAEC), and pulmonary artery (HPAEC) endothelial cells. Interestingly, we showed that HUVEC submitted to low oxygen concentrations (1%) for 24h under hypoxia reduced the expression of h…

  Modulation of heat shock protein expression in endothelial cells subjected to HSP70 inhibition, AP.R

• Abstract

  The molecular chaperone HSP70 is the most abundant chaperome member. In the vascular context there are only two know clients in endothelial cells (ECs): CLEC14a (C-type lectin domain family 14 member) and nucleolin, proteins associated to tumor angiogenesis. Loss-of-function experiments in static ECs promotes broader general effects like impairment of migration, tube formation, phosphoryl…

  Molecular chaperone HSP70 mediates proteostasis in endothelial cells response to hemodynamic force, AP.JP

• Standardization of BONCAT coupled to PLA in primary endothelial cells., BP.TT
• Standardization of BONCAT coupled to PLA in primary endothelial cells., BP.TT

• Abstract

  The 70 kDa heat shock protein (HSP70) is a versatile molecular chaperone that plays a role in protein folding, translocation of proteins to organelles, protein degradation by the ubiquitin proteasome system and also by autophagy. The HSP70 plays a role in endothelial cell migration VEGF2 induced and is important for tube formation showing its role in angiogenesis. Most of these studies fo…

  Effects of silencing of HSC70 and HSP70 on the response of endothelial cells in response to hemodynamic strength, BP.IC

(Only some records are available in English at this moment)

• Abstract

  Several intracellular chaperones have been shown to be secreted by distinct cellular types, including vascular, immune and tumor cells. Protein disulfide isomerase (PDI), as well as 70 and 90kDa heat shock protein (Hsp70 and Hsp90) families play extracellular roles in pathological conditions such as thrombosis, vascular remodeling and cancer survival and metastasis generation. Inhibition …

  Mechanisms and implications of selective cell-surface Grp94 inhibition in breast cancer cells, BE.EP.PD