Lombardo, Verónica

GROUP LEADER NAME (as it appears in publications): 

Verónica A. Lombardo  (from 2017 I am member of the Binolfi group where I work with zebrafish as animal model)

AFFILIATION AND CURRENT POSITION:  

1) Instituto de Biología Molecular y Celular de Rosario, Consejo Nacional de Investigaciones Científicas y Técnicas and Universidad Nacional de Rosario, 2000 Rosario, Argentina.

2) Centro de Estudios Interdisciplinarios, Universidad Nacional de Rosario, 2000 Rosario, Argentina

Associate Researcher

TEL:* 54-341-4237070, ext. 649 (oficina )/ 614 (laboratorio)

EMAIL:* lombardo@ibr-conicet.gov.ar

WEB: http://www.ibr-conicet.gov.ar/laboratorios/biologia-estructural-celular/

GROUP NAME / RESEARCH INTEREST IN FEW WORDS: Cellular-structural biology Lab/ Regulation of CaMKII under conditions of oxidative stress - cardiac diseases.

SHORT SUMMARY OF RESEARCH INTEREST (MAX. 200 WORDS):  We use zebrafish as animal model to understand the role for the oxidative activation of Ca2+/calmodulin-dependent protein kinase II (CaMKII) in the pathogenesis of cardiac diseases, and its regulation by methionine sulfoxide reductase A (MSRA).

Note: please attach at the end of the form a longer description, with a maximum of 2000 words.

LIST OF UP TO FIVE RELEVANT PUBLICATIONS:

1- Lombardo V.A.*, Otten C.*, Abdelilah-Seyfried S. (2015). Large-scale zebrafish embryonic heart dissection for transcriptional analysis. J Vis Exp., (95), e52087, doi:10.3791/52087.  *equal contribution.

2- Dietrich AC*, Lombardo VA*, Veerkamp J, Priller F, Abdelilah-Seyfried S. (2014). Blood flow and Bmp control endocardial chamber morphogenesis. Dev Cell., 30:367–377. *equal contribution.

3- Lombardo V.A., Sporbert A., Abdelilah-Seyfried S. (2012). Cell tracking using photoconvertible proteins during zebrafish development. J Vis Exp, (67), e4350, DOI: 10.3791/4350.

4- Lombardo, V.A., Armas, P., Weiner, A.M.J. and Calcaterra, N.B. (2007). In vitro Embryonic Developmental Phosphorylation of the Cellular Nucleic acid Binding Protein by cAMP-dependent Protein Kinase and its Relevance for Biochemical Activities. FEBS J. 274: 485-497.

5- Armas, P., Cachero, S., Lombardo, V.A., Weiner, A.M.J., Allende, M.L. and Calcaterra, N.B. (2004). Zebrafish Cellular Nucleic Acid Binding Protein: Gene Structure and Developmental Behaviour. Gene 337:151-161.

GROUP MEMBERS (NAME, POSITION, EMAIL):*

Andrés Binolfi: Group leader (binolfi@ibr-conicet.gov.ar)

Verónica A. Lombardo: Associate Researcher (lombardo@ibr-conicet.gov.ar)

Magda Carolina Sánchez López: Post-doc (sanchezlopez@ibr-conicet.gov.ar)

Franco Agustín Biglione: doctoral student (francobiglione@hotmail.com)

FISH FACILITIES (TYPE OF FISH SYSTEM/TANKS, CAPACITY, ETC.)*

IBR-fish facility

FISH LINES KEPT IN STOCK 

AB wild type line

Tg(kdrl:EGFP)s843 endothelial/endocardial reporter line (Jin et al., 2005)

Tg(kdrl:nlsKIKGR)hsc7 endothelial/endocardial reporter line for photoconversion assays (Lazic and Scott, 2011)

Tg(myl7:EGFP)twu34 myocardial reporter line (Huang et al., 2003)

OTHER EQUIPMENT RELATED TO ZEBRAFISH RESEARCH*

MPPI microinjector

LAB EXPERTISE AND TECHNICAL CAPABILITIES (RELATED TO ZEBRAFISH RESEARCH)*

• Regular care, maintenance and breeding of zebrafish

• Transgenic line generation  and maintenance

• Genotyping of embryos and adult zebrafish

• Imaging of live and fixed zebrafish embryos by Confocal microscopy

• Cell lineage tracking by photoconversion

• Manual and large-scale heart dissection

• Pharmacological inhibition treatment

• Inducible gene expression (heat shock, Gal4-UAS system)

• Cell death and proliferation assay

• Whole mount immunohistochemistry

• In situ hybridization

• Gateway cloning

• Transcriptional expression analysis by Real-time PCR

• Image analysis by Fiji/ImageJ, Volocity, LSM browser

• Protein analysis by SDS-PAGE, Western blot

• Phosphorylation assay

• Protein expression and purification

• Molecular biology techniques

OTHER RELEVANT INFORMATION:*

Important notice: The idea is to make part of this information publicly available through the LAZEN webpage (PI name, affiliation, research interest, publications, link to the lab web page). Other information, such as telephone numbers and e-mail, as well as details on facilities (all marked with *), will only be shared within the Network. If you do not wish to share some part of the given information, please let us know.

Please, once filled, submit this form together with the PI’s CV to lazen@fcien.edu.uy

RESEARCH INTEREST (MAX. 2000 WORDS):

Oxidative stress plays an important role in the development of heart diseases. Elevated levels of Ca2+/calmodulin-dependent protein kinase II (CaMKII) expression and catalytic activity have been associated with several cardiac diseases, such as impaired Ca2 + homeostasis, heart failure, and arrhythmias; and in models of cardiac injury such as myocardial infarction and ischemia. Oxidation of CaMKII has been implicated in all these conditions, suggesting a critical role for the oxidative activation of CaMKII in the pathogenesis of cardiac diseases. Oxidation of CaMKII occurs via reactive oxygen species, and this reversible post-translational modification being via the enzyme methionine sulfoxide reductase A (MSRA). Studies in mice show that mutants for MSRA have increased CaMKII oxidation, cell death, and post-myocardial infarction mortality; whereas the overexpression of MSRA reduces the oxidation of CaMKII and prevents the pathological consequences of aldosterone and angiotensin II in myocardium. Despite the anatomical differences between the heart of fish and mammals, the similarity in the electrophysiology of zebrafish and humans supports its use to model human heart diseases. In addition, its transparency during the embryonic and larval stages, allows easy observation and monitoring of cardiac functions. In our lab, we are focus in to elucidate how different stress factors involved in cardiac diseases modulate the regulatory activity of CaMKII. Although phosphorylation and oxidation of methionines have been implicated in CaMKII activation independent of Ca2+/CaM, to date is not known whether there is a coordinated regulation of these post-translational modifications. Thus, we study the possible crosstalk between oxidation of methionines and phosphorylation during the activation of CaMKII under conditions of oxidative stress as a result of alterations in cardiac function using zebrafish as a animal model.