8 results on '"Francesco, Speciale"'
Search Results
2. QTc Interval and Mortality in a Population of SARS-2-CoV Infected Patients
- Author
-
Alessandro Vicentini, Lucrezia Masiello, Sabato D’Amore, Enrico Baldi, Stefano Ghio, Simone Savastano, Antonio Sanzo, Angela Di Matteo, Elena Maria Seminari, Marco Vincenzo Lenti, Matteo Bosio, Barbara Petracci, Laura Frigerio, Anna Sabena, Guido Tavazzi, Luigi Oltrona Visconti, Roberto Rordorf, Massimiliano Gnecchi, Rossana Totaro, Marco Ferlini, Alessandra Greco, Giulia Magrini, Laura Scelsi, Mauro Acquaro, Michela Coccia, Simonluca Digiacomo, Davide Foglia, Francesco Jeva, Claudio Montalto, Martina Moschella, Laura Pezza, Stefano Perlini, Claudia Alfano, Marco Bonzano, Federica Briganti, Giuseppe Crescenzi, Anna Giulia Falchi, Elena Maggi, Roberta Guarnone, Barbara Guglielmana, Ilaria Francesca Martino, Maria Serena Pioli Di Marco, Pietro Pettenazza, Federica Quaglia, Francesco Salinaro, Francesco Speciale, Ilaria Zunino, Giulia Sturniolo, Federico Bracchi, Elena Lago, Angelo Corsico, Davide Piloni, Giulia Accordino, Cecilia Burattini, Antonio Di Sabatino, Ivan Pellegrino, Simone Soriano, Giovanni Santacroce, Alessandro Parodi, Federica Borrelli de Andreis, Raffaele Bruno, Valentina Zuccaro, Francesco Moioli, Valentino Dammassi, and Riccardo Albertini
- Subjects
Male ,medicine.medical_specialty ,Time Factors ,Population ,Action Potentials ,medicine.disease_cause ,QT interval ,Risk Assessment ,Electrocardiography ,Heart Conduction System ,Heart Rate ,Risk Factors ,Physiology (medical) ,Internal medicine ,Heart rate ,medicine ,Humans ,education ,Coronavirus ,Aged ,Retrospective Studies ,education.field_of_study ,medicine.diagnostic_test ,business.industry ,COVID-19 ,Retrospective cohort study ,Atrial fibrillation ,Arrhythmias, Cardiac ,Middle Aged ,medicine.disease ,Prognosis ,Hospitalization ,Italy ,Female ,Cardiology and Cardiovascular Medicine ,Risk assessment ,business - Published
- 2020
3. Sarcoglycan Complex in Human Normal and Pathological Prostatic Tissue: An Immunohistochemical and RT-PCR Study
- Author
-
Debora Di Mauro, Giuseppe Santoro, Antonino Inferrera, Giuseppina Cutroneo, Carlo Magno, Angelo Favaloro, Arena Salvatore, Francesco Speciale, Placido Bramanti, Giuseppe Anastasi, Carmela Rinaldi, Mario Patricolo, and Fabio Trimarchi
- Subjects
musculoskeletal diseases ,congenital, hereditary, and neonatal diseases and abnormalities ,Pathology ,medicine.medical_specialty ,Histology ,Sarcoglycans ,Cadherin ,Myoepithelial cell ,Hyperplasia ,Biology ,musculoskeletal system ,medicine.disease ,Extracellular matrix ,medicine.anatomical_structure ,Prostate ,medicine ,Adenocarcinoma ,Immunohistochemistry ,Anatomy ,Ecology, Evolution, Behavior and Systematics ,Biotechnology - Abstract
The sarcoglycan complex is a trans-membrane system playing a key role in mechano-signaling the connection from the cytoskeleton to the extracellular matrix. While β-, δ-, and e-sarcoglycans are widely distributed, γ- and α-sarcoglycans are expressed exclusively in skeletal and cardiac muscle. Insufficient data are available on the distribution of sarcoglycans in nonmuscular tissue. In the present study, we used immunohistochemical and RT-PCR techniques to study the sarcoglycans also in normal human glandular tissue, a type of tissue never studied in relation to the sarcoglycan complex, with the aim of verifying the real wider distribution of this complex. To understand the role of sarcoglycans, we tested specimens collected from patients affected by benign prostatic hyperplasia and adenocarcinoma. For the first time, our results showed that all sarcoglycans are detectable in normal samples both in epithelial and in myoepithelial cells; in pathological prostate, sarcoglycans appeared severely reduced in number or were absent. These data demonstrated that all sarcoglycans have a wider distribution suggesting a new unknown role for these proteins. The decreased number of sarcoglycans, containing cadherin domain homologs in samples of prostate affected by hyperplasia, and the absence of proteins in prostate biopsies, in cases affected by adenocarcinoma, could be responsible for the loss of adhesion between epithelial cells, which in turn facilitates the progression of benign tumors and the invasive potential of malignant tumors. Anat Rec, 297:327–336, 2014. © 2013 Wiley Periodicals, Inc.
- Published
- 2013
- Full Text
- View/download PDF
4. Altered Cytoskeletal Structure of Smooth Muscle Cells in Ureteropelvic Junction Obstruction
- Author
-
Angelo Favaloro, Raimondo M. Cervellione, Vincenzo Di Benedetto, Francesco Speciale, Francesco Arena, Salvatore Arena, Silvia Grimaldi, Carlo Magno, Giuseppina Cutroneo, Debora Di Mauro, and Giuseppe Anastasi
- Subjects
Talin ,Integrins ,Pathology ,medicine.medical_specialty ,Pyeloplasty ,Urology ,medicine.medical_treatment ,Integrin ,smooth muscle ,Extracellular matrix ,Ureter ,Ureteropelvic junction ,Humans ,Medicine ,Myocyte ,Kidney Pelvis ,Dystroglycans ,Hydronephrosis ,Cytoskeleton ,biology ,Caspase 3 ,business.industry ,Cell adhesion molecule ,Infant ,Muscle, Smooth ,medicine.disease ,Immunohistochemistry ,medicine.anatomical_structure ,Child, Preschool ,biology.protein ,business ,Renal pelvis ,Ureteral Obstruction - Abstract
Ureteropelvic junction obstruction is one of the most common causes of hydronephrosis in children. A malfunction of smooth muscle cells is believed to be the underlying mechanism causing obstruction. We investigated the expression of some integrins, talin and β-dystroglycan, considered the main compound of smooth muscle cell cytoskeleton, and active caspase 3 at the level of the ureteropelvic junction obstruction.Specimens were obtained at pyeloplasty in 12 children with ureteropelvic junction obstruction. Six control specimens were obtained during organ explantation. Specimens were divided into renal pelvis, ureteropelvic junction and ureter below the obstruction. Western blot analysis of active caspase 3, and immunofluorescence and polymerase chain reaction analysis were performed for α7A, β1A, α7B and β1D integrins, talin and β-dystroglycan.Talin and β-dystroglycan were slightly impaired in ureteropelvic junction obstruction, while α7B and β1D integrins were severely reduced, and α7A, β1A and active caspase 3 were significantly enhanced compared to controls.We demonstrated activation of apoptosis and a critical alteration of cytoskeleton that might explain the altered function and the increased apoptosis in smooth muscle cells in ureteropelvic junction obstruction. The delayed rearrangement of the cytoskeleton of smooth muscle cells in ureteropelvic junction obstruction might be linked to a postnatal splicing from α7A and β1A to α7B and β1D integrins, respectively. This relationship could explain the common clinical scenario of spontaneous improvement of hydronephrosis in children with suspected ureteropelvic junction obstruction.
- Published
- 2011
- Full Text
- View/download PDF
5. Muscle adaptations in relation to different types of strength training: an application of diffusion tensor imaging technique
- Author
-
Magaudda, Ludovico, Diego, Buda, Francesco, Speciale, Silvia, Marino, DI MAURO, Debora, and Bramanti, Placido
- Subjects
Training ,Pre-exhaustion ,DTI ,Hypertrophy - Abstract
Several exercise methods are commonly used by fitness practitioners to increase muscle strength and body mass. Pre-exhaustion (PE) is a strength training method of combining two exercises, in which a single-joint exercise performed exhaustively is followed by a multi-joint exercise. The purpose of PE of the smaller muscle is to provide lower involvement of this muscle in the subsequent multi-joint exercise, thereby enabling greater participation of other muscles. Conversely, in the post-exhaustion (PO) method is reversed the sequence of the exercises: first a determined muscle is trained with a multi-joint exercise and after with a single-joint exercise (Augustsson et Al., 2003). The purpose of this study was to investigate the effects of pre-exhaustion and post-exhaustion methods on gastrocnemius muscles by Diffusion Tensor Imaging (DTI) and volumetric evaluation techniques. DTI allows for a non-invasive evaluation of water diffusion and its fractional anisotropy (FA) in tissues. Four adults men (aged 22 +/- 0.81) have been divided in two groups by two different strength trainings: pre-exhaustion method (PE) and post-exhaustion (PO) method. All subjects have been performed 3 days a week for 3 months of training. Before and after training they have been subjected to conventional T1-weighted magnetic resonance. Results, after both training protocols, have shown a growth of muscle volume differentiated in each subject, probably connected to individual variables. Moreover, we have observed that the volumetric changes are related to the FA mean and it can be assumed that this remodeling of the can’t exclude, in addition to hypertrophy, phenomena of hyperplasia., Italian Journal of Anatomy and Embryology, Vol. 120, No. 1 (Supplement) 2015
- Published
- 2015
- Full Text
- View/download PDF
6. Sarcoglycan Complex in Masseter and Sternocleidomastoid Muscles of Baboons: An Immunohistochemical Study
- Author
-
Daniele Bruschetta, Antonio Micali, Antonio Centofanti, D. Di Mauro, Francesco Trimarchi, Demetrio Milardi, Francesco Speciale, Angelo Favaloro, Giuseppina Rizzo, Giuseppe Santoro, Giuseppina Cutroneo, Giuseppe Anastasi, and Giovanna Vermiglio
- Subjects
musculoskeletal diseases ,Male ,Pathology ,medicine.medical_specialty ,congenital, hereditary, and neonatal diseases and abnormalities ,Histology ,Muscle Fibers, Skeletal ,Biophysics ,Hierarchy, Social ,Biology ,medicine.disease_cause ,Masseter muscle ,ranking ,Sarcoglycans ,Baboons, Evolution, Immunohistochemistry, Ranking, Sarcoglycan ,evolution ,Adaptation, Psychological ,medicine ,Animals ,Humans ,Sarcoglycan ,Muscle, Skeletal ,lcsh:QH301-705.5 ,Mutation ,Original Paper ,Microscopy, Confocal ,Masseter Muscle ,Cell Biology ,baboons ,musculoskeletal system ,Phenotype ,Immunohistochemistry ,Transmembrane protein ,lcsh:Biology (General) ,medicine.symptom ,Muscle contraction ,Muscle Contraction ,Papio - Abstract
The sarcoglycan complex consists of a group of single-pass transmembrane glycoproteins that are essential to maintain the integrity of muscle membranes. Any mutation in each sarcoglycan gene causes a series of recessive autosomal dystrophin-positive muscular dystrophies. Negative fibres for sarcoglycans have never been found in healthy humans and animals. In this study, we have investigated whether the social ranking has an influence on the expression of sarcoglycans in the skeletal muscles of healthy baboons. Biopsies of masseter and sternocleidomastoid muscles were processed for confocal immunohistochemical detection of sarcoglycans. Our findings showed that baboons from different social rankings exhibited different sarcoglycan expression profiles. While in dominant baboons almost all muscles were stained for sarcoglycans, only 55% of muscle fibres showed a significant staining. This different expression pattern is likely to be due to the living conditions of these primates. Sarcoglycans which play a key role in muscle activity by controlling contractile forces may influence the phenotype of muscle fibres, thus determining an adaptation to functional conditions. We hypothesize that this intraspecies variation reflects an epigenetic modification of the muscular protein network that allows baboons to adapt progressively to a different social status.
- Published
- 2015
7. Sarcoglycan complex in human normal and pathological prostatic tissue: An immunohistochemical and RT-PCR study
- Author
-
Giuseppina, Cutroneo, Placido, Bramanti, Angelo, Favaloro, Giuseppe, Anastasi, Fabio, Trimarchi, Debora, Di Mauro, Carmela, Rinaldi, Francesco, Speciale, Antonino, Inferrera, Giuseppe, Santoro, Salvatore, Arena, Mario, Patricolo, and Carlo, Magno
- Subjects
Adult ,Male ,Histology ,Evolution ,Biopsy ,Prostatic Hyperplasia ,Epithelial cells ,Adenocarcinoma ,Behavior and Systematics ,Sarcoglycans ,80 and over ,Cell Adhesion ,Humans ,Prostate ,Prostatic adenocarcinoma ,Prostatic hyperplasia ,Aged ,Aged, 80 and over ,Disease Progression ,Immunohistochemistry ,Middle Aged ,Prostatectomy ,Prostatic Neoplasms ,Reverse Transcriptase Polymerase Chain Reaction ,Anatomy ,Biotechnology ,Ecology, Evolution, Behavior and Systematics ,Ecology - Abstract
The sarcoglycan complex is a trans-membrane system playing a key role in mechano-signaling the connection from the cytoskeleton to the extracellular matrix. While b-, d-, and e-sarcoglycans are widely distributed, g- and a-sarcoglycans are expressed exclusively in skeletal and cardiac muscle. Insufficient data are available on the distribution of sarcoglycans in nonmuscular tissue. In the present study, we used immunohistochemical and RT-PCR techniques to study the sarcoglycans also in normal human glandular tissue, a type of tissue never studied in relation to the sarcoglycan complex, with the aim of verifying the real wider distribution of this complex. To understand the role of sarcoglycans, we tested specimens collected from patients affected by benign prostatic hyperplasia and adenocarcinoma. For the first time, our results showed that all sarcoglycans are detectable in normal samples both in epithelial and in myoepithelial cells; in pathological prostate, sarcoglycans appeared severely reduced in number or were absent. These data demonstrated that all sarcoglycans have a wider distribution suggesting a new unknown role for these proteins. The decreased number of sarcoglycans, containing cadherin domain homologs in samples of prostate affected by hyperplasia, and the absence of proteins in prostate biopsies, in cases affected by adenocarcinoma, could be responsible for the loss of adhesion between epithelial cells, which in turn facilitates the progression of benign tumors and the invasive potential of malignant tumors.
- Published
- 2014
8. Sarcoglycans in the normal and pathological breast tissue of humans: an immunohistochemical and molecular study
- Author
-
Giuseppina Cutroneo, Francesco Speciale, Angelo Favaloro, Giovanna Vermiglio, Alba Arco, Mara Gioffrè, and Giuseppe Santoro
- Subjects
musculoskeletal diseases ,Adult ,congenital, hereditary, and neonatal diseases and abnormalities ,Pathology ,medicine.medical_specialty ,Histology ,Breast Neoplasms ,Biology ,Extracellular matrix ,Breast Diseases ,Young Adult ,Imaging, Three-Dimensional ,Breast Fibroadenoma ,Sarcoglycans ,medicine ,Humans ,Breast ,Fibrocystic Breast Disease ,Electrophoresis, Agar Gel ,Cadherin ,Reverse Transcriptase Polymerase Chain Reaction ,Myoepithelial cell ,Middle Aged ,musculoskeletal system ,medicine.disease ,Fibroadenoma ,Immunohistochemistry ,Sarcoglycan Benign breast tumors Immunohistochemical study Molecular study ,Gene Expression Regulation ,Tumor progression ,Female ,Anatomy - Abstract
The sarcoglycan complex, consisting of α-, β-, γ-, δ- and ε-sarcoglycans, is a multimember transmembrane system providing a mechanosignaling connection from the cytoskeleton to the extracellular matrix. Whereas the expression of α- and γ-sarcoglycan is restricted to striated muscle, other sarcoglycans are widely expressed. Although many studies have investigated sarcoglycans in all muscle types, insufficient data are available on the distribution of the sarcoglycan complex in nonmuscle tissue. On this basis, we used immunohistochemical and RT-PCR techniques to study preliminarily the sarcoglycans in normal glandular breast tissue (which has never been studied in the literature on these proteins) to verify the effective wider distribution of this complex. Moreover, to understand the role of sarcoglycans, we also tested samples obtained from patients affected by fibrocystic mastopathy and breast fibroadenoma. Our data showed, for the first time, that all sarcoglycans are always detectable in all normal samples both in epithelial and myoepithelial cells; in pathological breast tissue, all sarcoglycans appeared severely reduced. These data demonstrated that all sarcoglycans, not only β-, δ-, and ε-sarcoglycans, have a wider distribution, implying a new unknown role for these proteins. Moreover, in breast diseases, sarcoglycans containing cadherin domain homologs could provoke a loss of strong adhesion between epithelial cells, permitting and facilitating the degeneration of these benign breast tumors into malignant tumors. Consequently, sarcoglycans could play an important and intriguing role in many breast diseases and in particular in tumor progression from benign to malignant.
- Published
- 2011
Catalog
Discovery Service for Jio Institute Digital Library
For full access to our library's resources, please sign in.