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1. Plant-derived bioactives and oxidative stress-related disorders: a key trend towards health and longevity promotion

Author

Salehi B, Azzini E, Zucca P, Varoni EM, Kumar NVA, Dini L, Panzarini E, Rajkovic J, Fokou PVT, Peluso I, Prakash Mishra A, Nigam M, Rayess El, El Beyrouthy M, Setzer WN, Polito L, Iriti M, Sureda A, Quetglas-Llabres MM, Martorell M, Martins N, Estevinho LM, Taheri Y, Sharifi-Rad J, Salehi, B, Azzini, E, Zucca, P, Varoni, Em, Kumar, Nva, Dini, L, Panzarini, E, Rajkovic, J, Fokou, Pvt, Peluso, I, Prakash Mishra, A, Nigam, M, Rayess, El, El Beyrouthy, M, Setzer, Wn, Polito, L, Iriti, M, Sureda, A, Quetglas-Llabres, Mm, Martorell, M, Martins, N, Estevinho, Lm, Taheri, Y, and Sharifi-Rad, J

Published
2020

3. List of Contributors

Author

Aguiar, Odair, primary, Alkholy, Sarah Omar, additional, Allgrove, Judith, additional, Alqahtani, Samiah Naji, additional, Amini, Anna, additional, de Mello Andrade, Juliana Maria, additional, Andres-Lacueva, Cristina, additional, Aquilato, Andrea, additional, Arora, Rajesh, additional, Arranz, Sara, additional, Ashida, Hitoshi, additional, Avena, Paola, additional, Badole, Sachin L., additional, Baer-Dubowska, Wanda, additional, Bahrim, Gabriela, additional, Baliga, Manjeshwar Shrinath, additional, Barnes, Stephen, additional, Batista, Maria T., additional, Berhanu, Workalemahu Mikre, additional, Bhatia, Alka, additional, Bodhankar, Subhash L., additional, Bodnar, Lubomir, additional, Bolca, Selin, additional, Boto-Ordoñez, Maria, additional, Brizuela, Leyre, additional, Calhau, Conceição, additional, Carluccio, Maria Annunziata, additional, Carrasco-Pozo, Catalina, additional, Caruso, Anna, additional, Casaburi, Ivan, additional, Castro, Gerardo D., additional, Castro, José A., additional, Celep, Gulcin Sagdicoglu, additional, Chacko, Amala, additional, Chaudhari, Swapnil M., additional, Chen, Chung-Hwan, additional, Chen, Lixia, additional, Chiva-Blanch, Gemma, additional, Christensen, Kathrine Bisgaard, additional, Christensen, Lars Porskjær, additional, Chyu, Ming-Chien, additional, Cordova, Felina M., additional, Corona, Giulia, additional, Costa, G., additional, Cress, Brady F., additional, Crozier, Stephen J., additional, Cruz, M.T., additional, Cuvillier, Olivier, additional, Čvorović, Jovana, additional, Cyr, Lisa Danielle, additional, Czank, Charles, additional, D’Archivio, Massimo, additional, Davison, Glen, additional, De Caterina, Raffaele, additional, Deng, Guifang, additional, Devkar, Ranjitsinh V., additional, Doo, Taisha, additional, Doonan, Barbara, additional, Emami, Seyed Ahmad, additional, Estruch, Ramón, additional, Virgili, Fabio, additional, Falk, Michael, additional, Faria, Ana, additional, Farina, Grazia, additional, Fasolo, Daniel, additional, Fayad, Raja, additional, Ferreira, Maria Pontes, additional, Ferri, Claudio, additional, Forester, Sarah C., additional, Fornasaro, Stefano, additional, Cimino, Francesco, additional, Francis, Atul, additional, Francisco, V., additional, Fukuda, Itsuko, additional, Garcia-Aloy, Mar, additional, García-Mediavilla, María Victoria, additional, Gendron, Fidji, additional, Ghantasala, S., additional, Gil-Becerra, David, additional, Giovannini, Claudio, additional, Givigliano, Francesco, additional, Goldstein, Mark R., additional, Goel, Ajay, additional, Gollücke, Andréa Pittelli Boiago, additional, González-Gallego, Javier, additional, Govindaraghavan, Suresh, additional, Grassi, Davide, additional, Gunawardena, Dhanushka, additional, Guo, Honghui, additional, Habauzit, Véronique, additional, Haegeman, Guy, additional, He, Xiran, additional, Hegde, Mahabaleshwar V., additional, Heyninck, Karen, additional, Hsieh, Tze-chen, additional, Hurst, W. Jeffrey, additional, Iemma, Francesca, additional, Igoe, Ann, additional, Iglesias, Jacobo, additional, Ikeda, Ikuo, additional, Jadeja, Ravirajsinh N., additional, Jaffe, Russell, additional, Janda, Elzbieta, additional, Janel, Nathalie, additional, Jangam, Ganesh B., additional, Jayachander, Dipika, additional, Jiang, Fan, additional, Jirillo, Emilio, additional, Joo, Eun Ji, additional, Joseph, Nadhini, additional, Aguiar, Odair, additional, Juturu, Vijaya, additional, Kalekhan, Faizan, additional, Kamath, Krithika, additional, Karana, Rita, additional, Kaur, Kamaljeet, additional, Keating, Elisa, additional, Kennedy, David O., additional, Kerr, Jason, additional, Khaled, Mohd, additional, Khoo, Christina, additional, Khymenets, Olha, additional, Kim, Jiyoung, additional, Kobayashi, Makoto, additional, Kobori, Masuko, additional, Kochikuzhyil, Benson Mathai, additional, Koffas, Mattheos A.G., additional, Korniluk, Jan, additional, Kumar, Ashish, additional, Kumar, G., additional, Kumar, Yashwant, additional, Kumazawa, Yosho, additional, Kurien, Biji T., additional, Kwun, In-Sook, additional, Lambert, Joshua D., additional, Lamuela-Raventos, Rosa Maria, additional, Latheef, Latheesh, additional, Lee, Hyong Joo, additional, Lee, Ki Won, additional, Li, Huabin, additional, Li, Sha, additional, Llorach, Rafael, additional, Lopez, Victoria, additional, Maciel, María E., additional, Magrone, Thea, additional, Mani, Jayashree, additional, Marotta, Francesco, additional, Marquardt, Kristen Conrad, additional, Martel, Fátima, additional, Martínez, Verónica, additional, Maru, Girish B., additional, Mascitelli, Luca, additional, Masella, Roberta, additional, Maskarinec, Gertraud, additional, Massaro, Marika, additional, Masunov, Artëm E., additional, Mathew, Geetha, additional, Medina, Isabel, additional, Medina-Remón, Alexander, additional, Menaa, Abder, additional, Menaa, Bouzid, additional, Menaa, Farid, additional, Miglio, C., additional, Milenkovic, Dragan, additional, Mitjans, Montserrat, additional, Miura, Tomisato, additional, Mo, Huanbiao, additional, Mollace, Vincenzo, additional, Morand, Christine, additional, Moribito, G., additional, Mudgal, Piya Paul, additional, Münch, Gerald, additional, Murakami, Akira, additional, Nagasako-Akazome, Yoko, additional, Nayak, Yogendra, additional, Neves, B.M., additional, Noll, Christophe, additional, Nowak, Renata, additional, Nowacka, Natalia, additional, Odendaal, Antoinette Y., additional, Olech, Marta, additional, Ong, Khang Wei, additional, Osakabe, Naomi, additional, Paluszczak, Jarosław, additional, Parisi, Ortensia Ilaria, additional, Passamonti, Sabina, additional, Patil, Kalyani Y., additional, Pazos, Manuel, additional, Peluso, I., additional, Petry, Nicolai, additional, Pezzi, Vincenzo, additional, Piantanida, Marta, additional, Picci, Nevio, additional, Pimple, Bhushan P., additional, Pinto, John Thomas, additional, Pires, Vanessa Cardoso, additional, Prasain, Jeevan K., additional, Pravettoni, Valerio, additional, Primavesi, Laura, additional, Puoci, Francesco, additional, Quintans, Leandro N., additional, Rabassa, Montse, additional, Rai, Prajwith, additional, Rajeev, Antappa Govindaraju, additional, Rao, Suresh, additional, Rapeanu, Gabriela, additional, Rastmanesh, Reza, additional, Ravi, Rithin, additional, Restuccia, Donatella, additional, Ribeiro, Daniel Araki, additional, Rodrigo, Ramón, additional, Rotches-Ribalta, Maria, additional, Rouhani, Mae Nicole, additional, Saldanha, Elroy, additional, Saija, Antonella, additional, Sánchez-Campos, Sonia, additional, Saxena, Arpit, additional, Scazzocchio, Beatrice, additional, Schauss, Alexander G., additional, Scoditti, Egeria, additional, Scofield, R. Hal, additional, Serafini, Mauro, additional, Sharma, Rakesh, additional, Shen, Chwan-Li, additional, Shende, Pankaj S., additional, Shetty, Vaishaka, additional, Shivashankara, Arnadi Ramachandrayya, additional, Shoji, Toshihiko, additional, Simon, Paul, additional, Sinicropi, Maria Stefania, additional, Smith, Brenda J, additional, Sony, Dargi, additional, Speciale, Antonio, additional, Spencer, Jeremy P.E., additional, Stalmach, Angélique, additional, Stanciuc, Nicoleta, additional, Stover, Mitchel G, additional, Synowiec, Agnieszka, additional, Szarlej-Wcislo, Katarzyna, additional, Tajpara, P., additional, Tan, Benny Kwong Huat, additional, Tao, Ling, additional, Tayarani-Najaran, Nilufar, additional, Tayarani-Najaran, Zahra, additional, Thilakchand, Karadka Ramdas, additional, Tomás-Barberán, Francisco A., additional, Tomás-Navarro, María, additional, Tramer, Federica, additional, Tresserra-Rimbau, Anna, additional, Tréton, Jacques, additional, Tulipani, Sara, additional, Tuñón, María J., additional, Unnikrishnan, Mazhuvancherry K., additional, Urpi-Sarda, Mireia, additional, Valderas-Martínez, Palmira, additional, Vallejo, Fernando, additional, Vauzour, David, additional, Vázquez-Fresno, Rosa, additional, Venkatesh, Ponemone, additional, Veerapur, Veeresh, additional, Vinardell, M. Pilar, additional, Walker, Ross, additional, Watson, Ronald R., additional, Wcislo, Gabriel, additional, Wightman, Emma L., additional, Wilkins, John, additional, Wu, Erxi, additional, Wu, Joseph M, additional, Wu, Shan, additional, Xia, Enqin, additional, Xia, Min, additional, Yajima, Hiroaki, additional, Zanwar, Anand A., additional, and Ziberna, Lovro, additional

Published
2014
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9. The ADAMTS18 gene is responsible for autosomal recessive early onset severe retinal dystrophy

Author

Peluso, I., Conte, I., Testa, F., Dharmalingam, G., Pizzo, M., Collin, R.W.J., Meola, N., Barbato, S., Mutarelli, M., Ziviello, C., Barbarulo, A.M., Nigro, V., Melone, M.A., Simonelli, F., Banfi, S., Baere, E. de, Koenekoop, R.K., Leroy, B.P., Cremers, F.P., Kohl, S., Hamel, C., Ayuso, C., Wissinger, B., Inglehearn, C.F., Toomes, C., Hollander, A.I. den, Peluso, I., Conte, I., Testa, F., Dharmalingam, G., Pizzo, M., Collin, R. W. J., Meola, Nicola, Barbato, S., Mutarelli, M., Ziviello, C., Barbarulo, A. M., Nigro, V., Melone, M. A. B., Simonelli, F., Banfi, S., Peluso, I, Conte, I, Testa, F, Dharmalingam, G, Pizzo, M, Collin, Rwj, Meola, N, Barbato, S, Mutarelli, M, Ziviello, C, Barbarulo, Am, Nigro, V, Melone, M, Simonelli, F, and Banfi, S

Subjects
Genetics and epigenetic pathways of disease [NCMLS 6], Oryzias, PROTEIN, lcsh:Medicine, CHILDREN, ADAMTS Protein, DISEASE, MOLECULAR-GENETICS, ADAMTS Proteins, 0302 clinical medicine, Medicine and Health Sciences, Missense mutation, Knobloch syndrome, Genetics(clinical), Pharmacology (medical), Exome, Age of Onset, Genetics (clinical), Exome sequencing, Genetics, Medicine(all), 0303 health sciences, Inherited retinal dystrophies, General Medicine, ADAMTS18, Disease gene identification, 3. Good health, Human, EXPRESSION, ADAM Protein, Molecular Sequence Data, LEBER CONGENITAL AMAUROSIS, Genes, Recessive, Biology, ITALIAN PATIENTS, Polymorphism, Single Nucleotide, 03 medical and health sciences, Homozygosity mapping, Retinal Dystrophies, RETINITIS-PIGMENTOSA, KNOBLOCH SYNDROME, Retinitis pigmentosa, medicine, Animals, Humans, Amino Acid Sequence, Inherited retinal dystrophie, Medaka fish, 030304 developmental biology, Oryzia, Sequence Homology, Amino Acid, MUTATIONS, Genetic heterogeneity, Animal, Research, lcsh:R, Retinal Dystrophie, medicine.disease, ADAM Proteins, Mutation, Eye disorder, Genetics and epigenetic pathways of disease Genomic disorders and inherited multi-system disorders [NCMLS 6], 030217 neurology & neurosurgery
Abstract

BACKGROUND: Inherited retinal dystrophies, including Retinitis Pigmentosa and Leber Congenital Amaurosis among others, are a group of genetically heterogeneous disorders that lead to variable degrees of visual deficits. They can be caused by mutations in over 100 genes and there is evidence for the presence of as yet unidentified genes in a significant proportion of patients. We aimed at identifying a novel gene for an autosomal recessive form of early onset severe retinal dystrophy in a patient carrying no previously described mutations in known genes. METHODS: An integrated strategy including homozygosity mapping and whole exome sequencing was used to identify the responsible mutation. Functional tests were performed in the medaka fish (Oryzias latipes) model organism to gain further insight into the pathogenic role of the ADAMTS18 gene in eye and central nervous system (CNS) dysfunction. RESULTS: This study identified, in the analyzed patient, a homozygous missense mutation in the ADAMTS18 gene, which was recently linked to Knobloch syndrome, a rare developmental disorder that affects the eye and the occipital skull. In vivo gene knockdown performed in medaka fish confirmed both that the mutation has a pathogenic role and that the inactivation of this gene has a deleterious effect on photoreceptor cell function. CONCLUSION: This study reveals that mutations in the ADAMTS18 gene can cause a broad phenotypic spectrum of eye disorders and contribute to shed further light on the complexity of retinal diseases. Background: Inherited retinal dystrophies, including Retinitis Pigmentosa and Leber Congenital Amaurosis among others, are a group of genetically heterogeneous disorders that lead to variable degrees of visual deficits. They can be caused by mutations in over 100 genes and there is evidence for the presence of as yet unidentified genes in a significant proportion of patients. We aimed at identifying a novel gene for an autosomal recessive form of early onset severe retinal dystrophy in a patient carrying no previously described mutations in known genes.Methods: An integrated strategy including homozygosity mapping and whole exome sequencing was used to identify the responsible mutation. Functional tests were performed in the medaka fish (Oryzias latipes) model organism to gain further insight into the pathogenic role of the ADAMTS18 gene in eye and central nervous system (CNS) dysfunction.Results: This study identified, in the analyzed patient, a homozygous missense mutation in the ADAMTS18 gene, which was recently linked to Knobloch syndrome, a rare developmental disorder that affects the eye and the occipital skull. In vivo gene knockdown performed in medaka fish confirmed both that the mutation has a pathogenic role and that the inactivation of this gene has a deleterious effect on photoreceptor cell function.Conclusion: This study reveals that mutations in the ADAMTS18 gene can cause a broad phenotypic spectrum of eye disorders and contribute to shed further light on the complexity of retinal diseases.

Published
2013

10. Measurement and Clinical Significance of Biomarkers of Oxidative Stress in Humans

Author

Marrocco, Ilaria, Altieri, F., Peluso, I., Marrocco I. (ORCID:0000-0002-8225-2177), Marrocco, Ilaria, Altieri, F., Peluso, I., and Marrocco I. (ORCID:0000-0002-8225-2177)

Abstract

Oxidative stress is the result of the imbalance between reactive oxygen species (ROS) formation and enzymatic and nonenzymatic antioxidants. Biomarkers of oxidative stress are relevant in the evaluation of the disease status and of the health-enhancing effects of antioxidants. We aim to discuss the major methodological bias of methods used for the evaluation of oxidative stress in humans. There is a lack of consensus concerning the validation, standardization, and reproducibility of methods for the measurement of the following: (1) ROS in leukocytes and platelets by flow cytometry, (2) markers based on ROS-induced modifications of lipids, DNA, and proteins, (3) enzymatic players of redox status, and (4) total antioxidant capacity of human body fluids. It has been suggested that the bias of each method could be overcome by using indexes of oxidative stress that include more than one marker. However, the choice of the markers considered in the global index should be dictated by the aim of the study and its design, as well as by the clinical relevance in the selected subjects. In conclusion, the clinical significance of biomarkers of oxidative stress in humans must come from a critical analysis of the markers that should give an overall index of redox status in particular conditions.

Published
2017

11. Purine nucleoside phosphorylases from hyperthermophilic Archaea require a CXC motif forstability and folding

Author

CACCIAPUOTI, Giovanna, PORCELLI, Marina, PELUSO I., FUCCIO F., Cacciapuoti, Giovanna, Peluso, I., Fuccio, F., and Porcelli, Marina

Subjects
CXC motif, oxidative protein folding, 5'-deoxy-5'-methylthioadenosine phosphorylase, disulfide bond, hyperthermophilic proteins
Abstract

5'-Deoxy-5'-methylthioadenosine phosphorylase II from Sulfolobus solfataricus (SsMTAPII) and purine nucleoside phosphorylase from Pyrococcus furiosus (PfPNP) are hyperthermophilic purine nucleoside phosphorylases stabilized by intrasubunit disulfide bonds. In their C-terminus, both enzymes harbour a CXC motif analogous to the CXXC motif present at the active site of eukaryotic protein disulfide isomerase. By monitoring the refolding of SsMTAPII, PfPNP and their mutants lacking the C-terminal cysteine pair after guanidine-induced unfolding, we demonstrated that the CXC motif is required for the folding of these enzymes. Moreover, two synthesized CXC-containing peptides with the same amino acid sequences present in the C-terminal regions of SsMTAPII and PfPNP were found to act as in vitro catalysts of oxidative folding. These small peptides are involved in the folding of partially refolded SsMTAPII, PfPNP and their CXC-lacking mutants, with a concomitant recovery of their catalytic activity, thus indicating that the CXC motif is necessary to obtain complete reversibility from the unfolded state of the two proteins. The two CXC containing peptides are also able to reactivate scrambled RNaseA. The data obtained in the present study represent the first example of how the CXC motif improves both stability and folding in hyperthermophilic proteins with disulfide bonds.

Published
2009

14. Pyrimidine-specific ribonucleoside hydrolase from the archaeon Sulfolobus solfataricus: biochemical characterization and homology modeling

Author

Porcelli M, Concilio L, Peluso I, Marabotti A, Facchiano A, Cacciapuoti G., Porcelli, Marina, Concilio, L., Peluso, I., Marabotti, A., Facchiano, A., and Cacciapuoti, Giovanna

Subjects
Models, Molecular, Binding Sites, Sequence Homology, Amino Acid, Biochemical Phenomena, homology modeling, Molecular Sequence Data, Temperature, nucleoside hydrolase, Gene Expression, Biochemistry, Protein Structure, Tertiary, Substrate Specificity, nucleoside metabolism, Kinetics, hyperthermostability, Pyrimidines, Structural Homology, Protein, Sulfolobus solfataricus, Amino Acid Sequence, Protein Structure, Quaternary, N-Glycosyl Hydrolases, Sequence Alignment
Abstract

We report the characterization of the pyrimidine-specific ribonucleoside hydrolase from the hyperthermophilic archaeon Sulfolobus solfataricus (SsCU-NH). The gene SSO0505 encoding SsCU-NH was cloned and expressed in Escherichia coli and the recombinant protein was purified to homogeneity. SsCU-NH is a homotetramer of 140 kDa that recognizes uridine and cytidine as substrates. SsCU-NH shares 34% sequence identity with pyrimidine-specific nucleoside hydrolase from E. coli YeiK. The alignment of the amino acid sequences of SsCU-NH with nucleoside hydrolases whose 3D structures have been solved indicates that the amino acid residues involved in the calcium- and ribose-binding sites are preserved. SsCU-NH is highly thermophilic with an optimum temperature of 100 degrees C and is characterized by extreme thermodynamic stability (T(m) = 106 degrees C) and kinetic stability (100% residual activity after 1 h incubation at 90 degrees C). Limited proteolysis indicated that the only proteolytic cleavage site is localized in the C-terminal region and that the C-terminal peptide is necessary for the integrity of the active site. The structure of the enzyme determined by homology modeling provides insight into the proteolytic analyses as well as into mechanisms of thermal stability. This is the first nucleoside hydrolase from Archaea.

Published
2008

29. The Ceratitis capitata homologue of the Drosophila sex-determining gene Sex-lethal is structurally conserved, but not sex-specifically regulated

Author

SACCONE, GIUSEPPE, GIORDANO, ENNIO, POLITO, CATELLO, PELUSO I., ARTIACO D., Saccone, Giuseppe, Peluso, I., Artiaco, D., Giordano, Ennio, and Polito, Catello

Subjects
Drosophila melanogaster, Evolution, CERATITIS CAPITATA, Sex determination, diptera
Abstract

In Drosophila, Sxl functions as a binary switch in sex determination. Under the control of the primary sex-determining signal, it produces functional protein only in XX animals to implement female development. Here we report that, in contrast to Drosophila, the Sxl homologue in the Medfly, Ceratitis capitata, expresses the same mRNAs and protein isoforms in both XX and XY animals irrespective of the primary sex-determining signal. Also, experiments with two inducible transgenes demonstrate that the corresponding Ceratitis SXL product has no significant sex-transforming effects when expressed in Drosophila. Similar results have been obtained for the Sxl homologue of Musca domestica (Meise, M., Hilfiker-Kleiner, D., Brunner, C., DŁbendorfer, A., N¿thiger, R. and Bopp, D. (1998) Development 125, 1487-1494). Our findings suggest that Sxl acquired its master regulatory role in sex determination during evolution of the Acalyptratae group, most probably after phylogenetic divergence of the genus Drosophila from other genera of this group.

Published
1998

38. Molecular diagnosis of usher syndrome: application of two different next generation sequencing-based procedures

Author

Licastro, D., Mutarelli, M., Peluso, I., Neveling, K., Wieskamp, N., Rispoli, R., Vozzi, D., Athanasakis, E., D'Eustacchio, A., Pizzo, M., D'Amico, F., Ziviello, C., Simonelli, F., Fabretto, A., Scheffer, H., Gasparini, P., Banfi, S., Nigro, V., Licastro, D., Mutarelli, M., Peluso, I., Neveling, K., Wieskamp, N., Rispoli, R., Vozzi, D., Athanasakis, E., D'Eustacchio, A., Pizzo, M., D'Amico, F., Ziviello, C., Simonelli, F., Fabretto, A., Scheffer, H., Gasparini, P., Banfi, S., and Nigro, V.

Abstract

Contains fulltext : 108716.pdf (publisher's version ) (Open Access), Usher syndrome (USH) is a clinically and genetically heterogeneous disorder characterized by visual and hearing impairments. Clinically, it is subdivided into three subclasses with nine genes identified so far. In the present study, we investigated whether the currently available Next Generation Sequencing (NGS) technologies are already suitable for molecular diagnostics of USH. We analyzed a total of 12 patients, most of which were negative for previously described mutations in known USH genes upon primer extension-based microarray genotyping. We enriched the NGS template either by whole exome capture or by Long-PCR of the known USH genes. The main NGS sequencing platforms were used: SOLiD for whole exome sequencing, Illumina (Genome Analyzer II) and Roche 454 (GS FLX) for the Long-PCR sequencing. Long-PCR targeting was more efficient with up to 94% of USH gene regions displaying an overall coverage higher than 25x, whereas whole exome sequencing yielded a similar coverage for only 50% of those regions. Overall this integrated analysis led to the identification of 11 novel sequence variations in USH genes (2 homozygous and 9 heterozygous) out of 18 detected. However, at least two cases were not genetically solved. Our result highlights the current limitations in the diagnostic use of NGS for USH patients. The limit for whole exome sequencing is linked to the need of a strong coverage and to the correct interpretation of sequence variations with a non obvious, pathogenic role, whereas the targeted approach suffers from the high genetic heterogeneity of USH that may be also caused by the presence of additional causative genes yet to be identified.

Published
2012

45. The Ceratitis capitata homologue of the Drosophila sex-determining gene sex-lethal is structurally conserved, but not sex-specifically regulated.

Author

Saccone, G, Peluso, I, Artiaco, D, Giordano, E, Bopp, D, Polito, L C, Saccone, G, Peluso, I, Artiaco, D, Giordano, E, Bopp, D, and Polito, L C

Abstract

In Drosophila, Sxl functions as a binary switch in sex determination. Under the control of the primary sex-determining signal, it produces functional protein only in XX animals to implement female development. Here we report that, in contrast to Drosophila, the Sxl homologue in the Medfly, Ceratitis capitata, expresses the same mRNAs and protein isoforms in both XX and XY animals irrespective of the primary sex-determining signal. Also, experiments with two inducible transgenes demonstrate that the corresponding Ceratitis SXL product has no significant sex-transforming effects when expressed in Drosophila. Similar results have been obtained for the Sxl homologue of Musca domestica (Meise, M., Hilfiker-Kleiner, D., Brunner, C., DŁbendorfer, A., N¿thiger, R. and Bopp, D. (1998) Development 125, 1487-1494). Our findings suggest that Sxl acquired its master regulatory role in sex determination during evolution of the Acalyptratae group, most probably after phylogenetic divergence of the genus Drosophila from other genera of this group.

Published
1998

48. Role of the cholinergic system and of apamin-sensitive Ca[sup 2+] -activated K[sup +] channels on rabbit jejunum spontaneous activity and on the inhibitory effects of adrenoceptor agonists.

Author

Romanelli, L., Amico, M. C., Palmery, M., Peluso, I., Savini, G., Tucci, P., and Valeri, P.

Subjects
JEJUNUM, RABBITS, ADRENERGIC receptors, PARASYMPATHOMIMETIC agents
Abstract

Summary 1 One reason why rabbit jejunum is suitable for studying the mechanisms underlying the actions of the various neurotransmitters and their interactions is its spontaneous motility. The main regulator of spontaneous motility is the cholinergic system. How the cholinergic system regulates the spontaneous activity in the rabbit jejunum and how it affects the inhibitory action of α - and β -adrenoceptor agonists remains unclear. 2 We studied the influence of the cholinergic system and apamin-sensitive Ca[sup 2+] -activated K[sup +] channels on spontaneous contractions in the rabbit jejunum and on the inhibitory effects ofα [sub 1] - and β -adrenoceptor agonists. 3 In naïve tissues, atropine (ATR, 7.4 × 10[sup -8] m) and tetrodotoxin (8 × 10[sup -8] m) almost completely inhibited – to a similar extent – the amplitude of spontaneous activity. Despite the presence of ATR or TDX, tissue contraction gradually recovered to about 50% of the baseline amplitude within 5–10 min. When ATR or TDX, respectively, were added to the TDX- or ATR-treated tissues, the recovered activity decreased weakly but significantly. After washout and a 45-min rest the contraction amplitude returned to baseline values. A further exposure to ATR or TDX reduced the contraction to a level significantly lower than the one obtained after TDX or ATR added 5 min after ATR or TDX, respectively. In preparations prestimulated for 10 min with acetylcholine (ACh), ATR abolished the TDX-resistant recovered spontaneous activity. 4 Adrenaline (ADR, 0.5–5 × 10[sup -7] m) and phenylephrine (PHE, 1–10 × 10[sup -7] m) inhibited tissue motility in naïve and in ATR- and in TDX-exposed preparations. But whereas in naïve preparations the α [sub 1] -adrenoceptor antagonists completely antagonized inhibition induced by both drugs, in ATR- and TDX-exposed tissues they did so only partially for ADR. Agonist-induced inhibition had a rapid onset but rapidly faded; pendular movements took significantly longer to recover in ATR- and TDX-treated tissues than in naïve tissues. In tissues exposed for 2 min to ADR (0.5–5 × 10[sup -7] m) or PHE (1–10 × 10[sup -7] m), washout or addition of α [sub 1] -adrenoceptor antagonists caused an immediate short-lasting increase in contraction amplitude. 5 Apamin (APAM, 5 × 10[sup -9] m) caused a rapid and persistent increase in the amplitude of contractions. It also blocked the inhibitory responses to ADR and PHE, and removed washout-induced contractions. The APAM-induced increase in the contraction amplitude correlated with the increase obtained by washing out ADR or PHE. 6 Isoprenaline (at concentrations up to 2.8 × 10[sup -7] m) produced no inhibitory response in naïve tissues, but it invariably blocked (at a concentration of 0.7 × 10[sup -7] m) the recovered spontaneous activity (and sometimes depressed muscletone) in tissues exposed to ATR or TDX. Neither propranolol (3.4 × 10[sup -7] m) nor APAM (5 × 10[sup -9] m) counteracted these inhibitory effects. 7 These results indicate that spontaneous motility in the rabbit jejunum is predominantly mediated by neuronal release of ACh and by some other unidentified neuronal activity. Released ACh inhibits myogenic activity and strongly antagonizes β -adrenoceptor-induced APAM-insensitive inhibition but leaves α [sub 1] agonist-induced APAM-sensitive inhibition unchanged. [ABSTRACT FROM AUTHOR]

Published
2003
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50. Oxidant-induced pHi/Ca2+changes in rat aortic smooth muscle cells: The role of atrial natriuretic peptide

Author

De Vito, P., Di Nardo, P., Palmery, M., Peluso, I., Luly, P., and Baldini, P.M.

Abstract

The aim of this study was to investigate the effects of oxidative stress on PLD activity, [Ca2+]iand pHi levels and the possible relationship among them. Moreover, since atrial natriuretic peptide (ANP) protects against oxidant-induced injury, we investigated the potential protective role of the hormone in Rat Aortic Smooth Muscle (RASM) cells exposed to oxidative stress. Water-soluble 2,2′-Azobis (2hyphen;amidinopropane) dihydrochloride (AAPH) was used as free radical generating system, since it generates peroxyl radicals with defined reaction and the half time of peroxyl radicals is longer than other ROS. A significant increase of PLD activity was related to a significant decrease in pHi, while [Ca2+]ilevels showed an increase followed by a decrease after cell exposure to AAPH. [Ca2+]ichanges and pHi fall induced by AAPH were prevented by cadmium which inhibits a plasma membrane Ca2+ATPase coupled to Ca2+/H+exchanger, that operates the efflux of Ca2+coupled to H+influx. The involvement of PLD in pHi and [Ca2+]ichanges was confirmed by calphostin-c treatment, a potent inhibitor of PLD, which abolished all AAPH-induced effects. Pretreatment of RASM cells with pharmacological concentrations of ANP attenuated the AAPH effects on PLD activity as well as [Ca2+]iand pHi changes, while no effects were observed with physiological ANP concentrations, suggesting a possible role of the hormone as defensive effector against early events of the oxidative stress.

Published
2003
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