CV Lattes
ORCID
Secretaria da Saúde (São Paulo - Estado). Hospital das Clínicas da Faculdade de Medicina da USP (HCFMUSP). Instituto do Coração Professor Euryclides de Jesus Zerbini (INCOR) (Institutional affiliation from the last research proposal) Birthplace: Brazil
Francisco R. M. Laurindo graduated in Medicine by the University of São Paulo School of Medicine, São Paulo, Brazil , in 1978 and completed his residence training in Internal Medicine and Cardiology at the Heart Institute(Incor), University of São Paulo School of Medicine. After a period (1982-84) as associate physician at the same institution, he underwent research training in Physiology and Pharmacology at the Uniformed Services University of the Health Sciences, in Bethesda, Maryland (under Dr. Robert Goldstein, 1984-87). Back to the Heart Institute, University of São Paulo School of Medicine, he started an investigative research track focused on mechanisms of redox signaling processes in the vascular system. He obtained his PhD in 1992, supervised by Dr. Protásio da Luz. Thereafter, he conducted several research projects through independent financial support from research agencies. In 2001, he started, together with Dr. Protásio da Luz, the Vascular Biology Laboratory at the Heart Institute (Incor), University of São Paulo School of Medicine and became its Director in 2008, until presently. His major research interests have focused on understanding mechanisms and regulatory processes underlying the production of oxidant species in vascular cells and tissues and their physiological implications for vessel remodeling in disease. The most important contributions of his group have been the original description of shear stress-dependent generation of superoxide radical from the endothelium, the multi-level characterization of redox response to vascular injury and, particularly, the original discovery that the endoplasmic reticulum chaperone protein disulfide isomerase interacts functionally and physically with oxidant-generating NADPH oxidase complexes. This finding had relevant implications regarding the role of endoplasmic reticulum (patho)physiology on NADPH oxidase function and how redox processes regulate cell migration and vascular remodeling. More recently, Dr. Laurindo's group showed an important role for extracellular PDI in arterial remodeling after injury. Dr. Laurindo has authored or co-authored over 145 publications in peer-reviewed journals, cited >3500 times (h-index=35 (ISI)). He supervised 18 PhD students and 17 post-doctoral fellows, in addition to several undergraduate trainees. From 2008-14, he was the vice-coordinator of the National Institute for Science and Technology of Redox Processes in Biomedicine (CNPq/Fapesp) and since 2013 (until present) the Vice-coordinator and principal investigator of Cepid-Fapesp Redoxoma. He is a member of the Brazilian Academy of Sciences since 2012 and a member of its Board of Directors since 2016, a member of Fapesp Study Committee in Health Sciences from 2008-2016 and Fapesp Advisor Committee in Life Sciences since 2016, a member of Capes Federal Agency Committee (Medicine) from 1998-2017. He served as Council Member of the Society for Free Radical Biology and Medicine from 2010-2014 and belongs to the Editorial Board of Free Radical Biology and Medicine since 2008 and of Clinical Science since 2012. He has been an ad-hoc consultant for >35 publications and research agencies from Brazil and abroad. He was elected as vice-chair (2014) and chair (2016) of the Gordon Research Conference on Nox Family NADPH Oxidases. (Source: Lattes Curriculum)
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The study of redox processes has high potential to elucidate integrative mechanisms, due to the ubiquity and strength of their effects. Many studies involve the role of redox mechanisms in diseases. However, the complexity of this field has increased concerning structures, structure-function relations, methods, molecular and sub-cellular pathology of redox-regulated proteins, genomics, pr…
Redox processes strongly regulate (patho) physiological cell signaling, yet several fundamental underlying mechanisms remain unclear, including in particular the associated subcellular compartmentalization. The Shah group at KCI investigates endoplasmic reticulum (ER) signaling mechanisms and associated cardiovascular implications of Nox NAOPH oxidases, major cellular ROS enzyme sources. …
Redox homeostasis depends on the regulated production of reactive oxygen species (ROS) via enzymatic sources such as the Nox family NADPH oxidase complex, the main source of ROs in vascular cells. Recent studies from our laboratory disclosed an important role of PDI in the regulation of NADPH oxidase. The important functional effects of PDI in NADPH oxidase in a number of distinct cell ty…
The aim of this project is the development and implementation of Laser Induced Breakdown Spectroscopy (LIBS), an analytical technique based on sampling and excitation of atoms and molecules induced by laser. Most recently, LlBS has been considered a very promising analytical tool for in situ quantitative chemical analysis, either in industrial process as well as in the field. However, the…
(Only some records are available in English at this moment)
The vascular response to mechanical injury is a phenomena model that occurs in various vascular diseases. Certain mechanisms, such as redox signaling, may permeate the natural story of injury response and affect the variables of the final response. Data from our group lead to the general hypothesis that Protein-Disulfide Isomerase (PDIA1), a redox chaperone from the endoplasmic reticulum …
A fundamental problem in cellular physiology is understanding the control of cell and tissue remodeling, which involves fine adjustments and homeostasis equilibrium, together accounting for cell form and function in contexts of adhesion, migration and mechanoadaptation. Central pathways involved in the upstream control of these processes are unknown and may contribute to vascular disease.…
Our group has described several effects of PDIA1 (Protein Disulfide Isomerase) on the regulation of vascular redox signaling. These include production of oxidants by NADPH oxidases (Nox), regulation of the cytoskeleton, cell migration and differentiation. Increases in PDIA1expression are observed in the arterial wall in vascular diseases. However, the temporal evolution of the effects and…
(Only some records are available in English at this moment)
Filopodia-like cellular protrusions are observed in most cell types and may carry protein condensates, which eventually detach from them as microvesicles. These processes are highly redox-regulated and our group has identified that protein disulfide isomerase-A1 (PDIA1), a thiol-redox chaperone from the endoplasmic reticulum, is an important component of these protein condensates. PDIA1 i…
Diabetes is a chronic and epidemic disease with high socio-economical cost worldwide, being characterized by increased risk of cardiovascular disease (CVD) and thromboembolic event. Upon endothelial dysfunction, platelets bind to endothelial cells to precipitate thrombus formation in a process that is not fully understood. Specifically, it is still unclear which surface proteins regulate …
High Molecular Weight Protein Complexes (HMW-PCs) are important effectors and regulators of cell signaling by constituting important hubs in protein-protein interaction networks. Therefore, the detection and analysis of HMW-PCs in distinct physiological conditions can provide windows to uncover novel and unexpected signaling routes related to major cell functions. Redox-related proteins a…
(Only some records are available in English at this moment)
PDIA1 is a redox chaperone from thioredoxin superfamily with roles on redox protein folding in the endoplasmic reticulum. Work from our group has suggested additional redox signaling roles for PDIA1 (the PDI family prototype) related to the regulation of the cytoskeleton and signaling by RhoGTPases and their regulators such as RhoGDIs. In this context, we propose that the interaction betw…
Understanding molecular pathways involved in the redox regulation of endoplasmic reticulum-plasma membrane contacts (ER-PM) is an important goal for clarifying several aspects of the ER-related pathophysiology of Nox NADPH oxidases and, in particular, the interplay between PDIA1 and Noxes. Our group has previously described that PDIA1 is a major upstream regulator of Nox family, which are…
PDIA1 is an essential, multifunctional enzyme that assists oxidative folding in the ER. It enters cotranslationally into, and resides in, the ER owing to its N-terminal signal sequence and C-terminal KDEL motifs, respectively. Yet, part of PDIA1 is detected extracellularly, where it may control blood clotting and virus entry, and part is found in the cytosol, where it may impact cytoskele…
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 …
Protein Disulfide Isomerase (PDI) is a dithiol/disulfide oxidoreductase chaperone mainly from endoplasmic reticulum (ER), where it assists redox protein folding. Recent works indicate PDI involvement in redox cell signaling, bearing a close functional and physical interaction with the NADPH oxidase complex, the main cellular source of signaling oxidants. In Vascular smooth muscle cells (V…
(Only some records are available in English at this moment)
| 1 / 1 | Ongoing research grants |
| 10 / 5 | Completed research grants |
| 4 / 4 | Ongoing scholarships in Brazil |
| 51 / 18 | Completed scholarships in Brazil |
| 2 / 2 | Ongoing scholarships abroad |
| 8 / 8 | Completed scholarships abroad |
| 76 / 38 | All research grants and scholarships |
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