José Alberto Carrodeguas

Universidad de Zaragoza

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Javier Sancho

Universidad de Zaragoza

Pascual López‐Buesa

Universidad de Zaragoza

Pedro Latorre‐Muro

Harvard University

Adrián Velazquez‐Campoy

Universidad de Zaragoza

Carmen Mesas Burgos

Karolinska Institutet

Sandra Salillas

Universidad de Zaragoza

Daniel Bogenhagen

Stony Brook University

María D. Díaz‐de‐Villegas

Universidad de Zaragoza

Ramón Hurtado‐Guerrero

Fundacion Agencia Aragonesa para la Investigacion y el Desarrollo

Eliette Touati

Institut Pasteur

Cooperative Institutions

Universidad de Zaragoza

Consejo Superior de Investigaciones Científicas

Instituto de Investigación Sanitaria Aragón

Instituto de Salud Carlos III

Centre National de la Recherche Scientifique

Centro de Investigación Biomédica en Red

Universitat de Barcelona

Weatherford College

Universidad Autónoma de Madrid

Inserm

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CRYSTAL STRUCTURE OF THE ACCESSORY SUBUNIT OF MURINE MITOCHONDRIAL POLYMERASE GAMMA

José Alberto Carrodeguas Karsten Theis Daniel Bogenhagen Caroline Kisker

10.2210/pdb1g5h/pdb

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The closed conformation of the LDL receptor is destabilized by the low Ca⁺⁺ concentration but favored by the high Mg⁺⁺ concentration in the endosome

FEBS Letters (2015)

Juan Martínez‐Oliván Xabier Arias‐Moreno Ramón Hurtado‐Guerrero José Alberto Carrodeguas Laura Miguel-Romero

The LDL receptor (LDLR) internalizes LDL and VLDL particles. In the endosomes, it adopts a closed conformation important for recycling, by interaction of two modules of the ligand binding domain (LR4–5) and a β‐propeller motif. Here, we investigate by SPR the interactions between those two modules and the β‐propeller. Our results indicate that the two modules cooperate to bind the β‐propeller. The binding is favored by low pH and by high [Ca ++ ]. Our data show that Mg ++ , at high concentration in the endosome, favors the formation of the closed conformation by replacing the structuring effect of Ca ++ in LR5. We propose a sequential model of LDL release where formation of the close conformation follows LDL release.

10.1016/j.febslet.2015.10.014

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Citations (7)

Allelic incidence in several pig breeds of a missense variant of pig melanocortin-4 receptor (MC4R) gene associated with carcass and productive traits; its relation to IGF2 genotype

Meat Science (2006)

Carmen Mesas Burgos José Alberto Carrodeguas C. Moreno J. Altarriba Luis Tarrafeta

Melanocortin 4 receptor

Large white

Linkage Disequilibrium

10.1016/j.meatsci.2005.11.007

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Citations (34)

Mitochondrial Transcription Initiation in the Crustacean Artemia franciscana

European Journal of Biochemistry (1997)

José Alberto Carrodeguas Carmen G. Vallejo

Mitochondrial transcription has been studied in several vertebrate organisms, but so far no report on mitochondrial transcription initiation in invertebrates has been published. Here we present an analysis of transcription initiation sites using in vivo ‐synthesized transcripts in the crustacean Artemia franciscana . The mitochondrial genome of Artemia has the same coding capacity as most animal mitochondrial genomes, and its overall organization is almost identical to that of Drosophila . Using in vitro capping, RNA mapping techniques and northern hybridization, we have identified a main initiation site for heavy‐strand transcription that matches the 5· end of 12S rRNA, on one end of the control region. This nascent RNA has an unusually small size and a highly heterogeneous 5· end. A second potential transcription‐initiation site has been located 250 bp upstream of the former, giving rise to a larger, less abundant RNA which also has an heterogeneous 5· end. The two sites have sequence similarity from which a consensus could be derived. Using the same methods we failed to identify any clear initiation site for transcription of the light strand, nevertheless a candidate has been located on the opposite side of the control region, with respect to the heavy‐strand initiation sites.

Transcription

10.1111/j.1432-1033.1997.0514a.x

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Citations (16)

DMSO affects Aβ_1–40's conformation and interactions with aggregation inhibitors as revealed by NMR

RSC Advances (2015)

Douglas V. Laurents David Pantoja‐Uceda Laura C. López José Alberto Carrodeguas Miguel Mompeán

DMSO alters Abeta's conformation and its recognition by inhibitors.

10.1039/c5ra12100k

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Two isoforms of PSAP/MTCH1 share two proapoptotic domains and multiple internal signals for import into the mitochondrial outer membrane

AJP Cell Physiology (2007)

Violeta Lamarca Antonio Sanz-Clemente Rosaura Pérez‐Pé Marı́a José Martı́nez-Lorenzo Nabil Halaihel

Presenilin 1-associated protein (PSAP) was first identified as a protein that interacts with presenilin 1. It was later reported that PSAP is a mitochondrial protein that induces apoptosis when overexpressed in cultured cells. PSAP is also known as mitochondrial carrier homolog 1 (Mtch1). In this study, we show that there are two proapoptotic PSAP isoforms generated by alternative splicing that differ in the length of a hydrophilic loop located between two predicted transmembrane domains. Using RT-PCR and Western blot assays, we determined that both isoforms are expressed in human and rat tissues as well as in culture cells. Our results indicate that PSAP is an integral mitochondrial outer membrane protein, although it contains a mitochondrial carrier domain conserved in several inner membrane carriers, which partially overlaps one of the predicted transmembrane segments. Deletion of this transmembrane segment impairs mitochondrial import of PSAP. Replacement of this segment with each of two transmembrane domains, with opposite membrane orientations, from an unrelated protein indicated that one of them allowed mitochondrial localization of the PSAP mutant, whereas the other one did not. Our interpretation of these results is that PSAP contains multiple mitochondrial targeting motifs dispersed along the protein but that a transmembrane domain in the correct position and orientation is necessary for membrane insertion. The amino acid sequence within this transmembrane domain may also be important. Furthermore, two independent regions in the amino terminal side of the protein are responsible for its proapoptotic activity. Possible implications of these findings in PSAP function are discussed.

Mitochondrial carrier

10.1152/ajpcell.00431.2006

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Citations (29)

Allelic frequencies of PRKAG3 in several pig breeds and its technological consequences on a Duroc × Landrace‐Large White cross

Journal of Animal Breeding and Genetics (2013)

A. Galve Carmen Mesas Burgos L. Varona José Alberto Carrodeguas Ángela Cánovas

Summary The allelic frequencies of PRKAG 3 gene (the RN gene) have been investigated in several pig breeds. R 200 Q mutation appear only in Hampshire pigs, whereas V 199 I mutation is most abundant in Iberian, P orco C elta or B izaro, and less in breeds selected for muscularity as D uroc, L andrace and P ietrain. A thorough study of phenotypic effects of V 1991 has been performed in a D uroc × L andrace‐ L arge W hite cross. 199 I homozygous pigs show increased p H 24 values in ham homogenates and loin (0.14 and 0.16 p H units, respectively) compared to 199 V homozygous ones. Meat of 199 I homozygous pigs exudates 42.6% less fluid and is darker (2.46 ‘ L ’‐value units). 199 I homozygous pigs are fatter (4.2 mm more backfat thickness) and contain less muscle mass in ham (1.0 percentage points) and shoulder (2.7 percentage points), than 199 V homozygous ones. 199 I homozygous pigs contain 7.3% less protein in the belly and 8.5% more fat in shoulder muscle mass than 199 V homozygous pigs. 199 I homozygous pigs have also superior functional properties: better gelling (22.8% larger G′ value) and emulsion capacities (14 percentage points less of total exuded fluid), and higher curing yield in the belly (6 percentage points more). These data support the adipogenic character of the V 199 I mutation. The advantages and disadvantages of selecting any of the two PRKAG 3 alleles for position 199 are discussed.

Loin

10.1111/jbg.12042

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Citations (14)

Compuestos para el tratamiento de enfermedades causadas por Helicobacter

Javier Sancho Sandra Salillas Ángel Lanas José Alberto Carrodeguas José A. Aı́nsa

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Benzbromarone, Quercetin, and Folic Acid Inhibit Amylin Aggregation

International Journal of Molecular Sciences (2016)

Laura López Olga Varea Susanna Navarro José Alberto Carrodeguas Natalia Sánchez de Groot

Human Amylin, or islet amyloid polypeptide (hIAPP), is a small hormone secreted by pancreatic β-cells that forms aggregates under insulin deficiency metabolic conditions, and it constitutes a pathological hallmark of type II diabetes mellitus. In type II diabetes patients, amylin is abnormally increased, self-assembled into amyloid aggregates, and ultimately contributes to the apoptotic death of β-cells by mechanisms that are not completely understood. We have screened a library of approved drugs in order to identify inhibitors of amylin aggregation that could be used as tools to investigate the role of amylin aggregation in type II diabetes or as therapeutics in order to reduce β-cell damage. Interestingly, three of the compounds analyzed-benzbromarone, quercetin, and folic acid-are able to slow down amylin fiber formation according to Thioflavin T binding, turbidimetry, and Transmission Electron Microscopy assays. In addition to the in vitro assays, we have tested the effect of these compounds in an amyloid toxicity cell culture model and we have found that one of them, quercetin, has the ability to partly protect cultured pancreatic insulinoma cells from the cytotoxic effect of amylin. Our data suggests that quercetin can contribute to reduce oxidative damage in pancreatic insulinoma β cells by modulating the aggregation propensity of amylin.

Amylin

Amyloid (mycology)

Thioflavin

10.3390/ijms17060964

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Exposure of any of two proapoptotic domains of presenilin 1-associated protein/mitochondrial carrier homolog 1 on the surface of mitochondria is sufficient for induction of apoptosis in a Bax/Bak-independent manner

European Journal of Cell Biology (2008)

Violeta Lamarca Isabel Marzo Antonio Sanz-Clemente José Alberto Carrodeguas

Mitochondrial apoptosis-induced channel

Bcl-2 Family

Bcl-2-associated X protein

10.1016/j.ejcb.2008.02.004

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Citations (19)