13 results on '"Majó G"'
Search Results
2. Sustainability benefits of RFID technology in Vietnamese fashion supply chain
- Author
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Rajkishore Nayak, Majo George, Irfan Ul Haq, and Hiep Cong Pham
- Subjects
RFID ,Sustainable fashion ,Fashion supply chain ,Environmental sustainability ,Social and economic benefits ,Vietnam ,Systems engineering ,TA168 ,Marketing. Distribution of products ,HF5410-5417.5 - Abstract
The growing need for sustainability in fashion production and retail operations has prompted the adoption of a variety of strategies, including the use of technology. Radio Frequency Identification (RFID) technology may shift economic dynamics and provide a more sustainable future in numerous industries, including fashion. Vietnam is one of the main fashion and textile manufacturing nations in South East Asia, where the manufacturing sectors face a number of obstacles in order to reach the triple bottom line of sustainability. As a result, using empirical research, this paper aimed to analyse the long-term advantages of RFID technology implementation. The research findings revealed that the adoption of RFID technology in Vietnamese fashion enterprises is in its infancy stage. Among a number of factors, cost of deploying RFID technology is found to be a critical barrier. Furthermore, companies that have used RFID have demonstrated that the speed, precision, and on-time information availability provided by RFID assists in reaching a variety of environmental, social, and economic advantages. Although this study discovered certain disadvantages of deploying RFID technology, the benefits obtained by RFID technology outweigh the disadvantages. The findings suggest that fashion industry should migrate to RFID due to the benefits of sustainability and transparency in the supply chain.
- Published
- 2022
- Full Text
- View/download PDF
3. Estudio de la superficie de limas de endodoncia sometidas a desinfección química mediante microscopia electrónica de barrido
- Author
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Navarro Majó, G., Mateos, M., Navarro, J.L., Canalda Sahli, Carlos, and Universitat de Barcelona
- Subjects
Disinfection ,Dental materials ,Corrosion and anti-corrosives ,Desinfecció ,Materials dentals ,Endodòncia ,Corrosió i anticorrosius ,Endodontics - Abstract
Se observaron al microscopio electró nico de barrido 40 limas de endodoncia de acero inoxidable después de ser sometidas a 10 ciclos de desinfección de 10 minutos cada ciclo, sumergidas en diferentes desinfectantes químicos. No se observó corrosión en la superficie de las limas en las circunstancias en que se realizó ese estudio.
- Published
- 1991
4. Trk neurotrophin receptor family immunoreactivity in rat and human pituitary tissues
- Author
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Aguado, F, primary, Majó, G, additional, Gómez de Aranda, I, additional, and Ferrer, I, additional
- Published
- 1998
- Full Text
- View/download PDF
5. Differential Distribution of Syntaxin Isoforms 1A and 1B in the Rat Central Nervous System
- Author
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Ruiz-Montasell, B., primary, Aguado, F., additional, Majó, G., additional, Chapman, E. R., additional, Canals, J. M., additional, Marsal, J., additional, and Blasi, J., additional
- Published
- 1996
- Full Text
- View/download PDF
6. Regulated secretion is impaired in AtT-20 endocrine cells stably transfected with botulinum neurotoxin type A light chain.
- Author
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Aguado, F, Gombau, L, Majó, G, Marsal, J, Blanco, J, and Blasi, J
- Abstract
Botulinum neurotoxin type A (BoNT/A) inhibits neurotransmitter release by specific cleavage of SNAP-25, a synaptosome-associated protein also expressed in the ACTH secretory cell line AtT-20. Expression of light chain BoNT/A (L-BoNT/A) gene transfected into AtT-20 cells resulted in a cleaved form of SNAP-25 indistinguishable from that generated by bona fide BoNT/A. L-BoNT/A-transfected cells showed no difference in replication rate, viability, or phenotype, compared with control AtT-20 cells. In contrast, L-BoNT/A-transfected cells could not be induced to secrete ACTH upon stimulation by 8-bromo-cAMP or KCl. In addition, alpha-latrotoxin induced ACTH release from control cells, but not from L-BoNT/A-transfected cells. These experiments suggest an important role for SNAP-25 in regulated secretion from AtT-20 cells and underline the usefulness of this cell system as a tool for the study of the molecular mechanism of peptide hormone secretion.
- Published
- 1997
7. Actualización en operatoria dental
- Author
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Navarro Majó, José Luis, Murtra Ferré, Jaime, Navarro Majó, G., and Universitat de Barcelona
- Subjects
Adhesius dentals ,Amalgames dentals ,Systematic reviews (Medical research) ,Dentistry ,Dental amalgams ,Ressenyes sistemàtiques (Investigació mèdica) ,Odontologia ,Dental adhesives - Abstract
Los autores revisan y comentan en este trabajo los artículos más relevantes y con más incidencia clínica seleccionados de entre las revistas más importantes durante el año 1988, referentes a amalgama dental, compuestos, adhesivos dentinarios e ionómeros de vidrio.
- Published
- 1989
8. Expression of synaptosomal-associated protein SNAP-25 in endocrine anterior pituitary cells
- Author
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Aguado F, Majó G, Ruiz-Montasell B, Josep M. Canals, Casanova A, Marsal J, and Blasi J
- Subjects
Male ,Botulinum Toxins ,Synaptosomal-Associated Protein 25 ,Qa-SNARE Proteins ,rab3 GTP-Binding Proteins ,Membrane Proteins ,Nerve Tissue Proteins ,Rats ,Immunoenzyme Techniques ,R-SNARE Proteins ,Rats, Sprague-Dawley ,GTP-Binding Proteins ,Pituitary Gland, Anterior ,Animals ,RNA, Messenger ,Cells, Cultured - Abstract
A growing body of evidence indicates that the fundamental molecular mechanism of exocytosis in the secretory pathway may be structurally similar in all eukaryotic cells. The synaptosomal-associated protein of 25 kDa (SNAP-25) is a plasma membrane protein involved in regulated exocytosis in neurons. In order to compare exocytotic components in neurons and endocrine cells, we have analyzed the expression of SNAP-25 in the rat anterior pituitary. Western blotting analysis documented the presence of SNAP-25 in anterior pituitary homogenates and cultured anterior pituitary cells. In addition to SNAP-25, other neuronal proteins involved in exocytosis (syntaxin, VAMP/synaptobrevin and Rab3A) were also detected in the anterior pituitary. The specific expression of SNAP-25 mRNA in anterior pituitary cells was also corroborated by Northern analysis. SNAP-25 immunoreactivity was located at the plasma membrane of endocrine anterior pituitary cells. Characteristically, patches of fine punctate deposits exhibited intense SNAP-25 immunoreactivity. Double-labeling immunocytochemistry revealed that SNAP-25 was mainly associated with gonadotroph cell populations. Furthermore, we demonstrate that in the anterior pituitary, SNAP-25 is selectively cleaved by clostridial neurotoxins. In conclusion, our results establish the presence of SNAP-25 in secretory anterior pituitary cells and suggest a potential role of this protein in the secretion of adenohypophysial hormone.
9. Exocytotic protein components in rat pituitary gland after long-term estrogen administration.
- Author
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Majó G, Lorenzo MJ, Blasi J, and Aguado F
- Subjects
- Animals, Blotting, Western, Cell Culture Techniques, Down-Regulation drug effects, Exocytosis physiology, Female, Immunoenzyme Techniques, Pituitary Gland, Anterior metabolism, Pituitary Neoplasms chemically induced, Prolactin metabolism, Rats, Rats, Inbred F344, Tumor Cells, Cultured, Estradiol pharmacology, Exocytosis drug effects, Neoplasm Proteins metabolism, Pituitary Neoplasms metabolism
- Abstract
Recently, a set of proteins involved in the docking and fusion machinery of secretory organelles has been identified in anterior pituitary cells. In this study we analyzed, by Western blotting and immunocytochemistry, the expression of several proteins involved in exocytosis after long-term administration of 17beta-estradiol (E2) in Fischer 344 rats. No differences were observed in the amount of synaptosomal-associated protein of 25 kDa, synaptobrevin 2, syntaxin 1, synaptotagmin I and Rab3a in total brain homogenates from treated rats after E2 administration. In striking contrast, the levels of all of these exocytotic proteins, including cellubrevin, were notably decreased in pituitary glands of E2-treated rats. In addition, no differences were observed in the in vitro basal and 8-Br-cAMP-induced prolactin (PRL) release between pituitary cells from control and E2-treated rats, whereas TRH-induced PRL release in anterior pituitary cells from E2-treated animals was higher than in control donors. In conclusion, this study shows that protein components of the exocytotic machinery are specifically down-regulated in the pituitary gland of E2-treated Fischer 344 rats.
- Published
- 1999
- Full Text
- View/download PDF
10. Synaptobrevin isoforms in secretory granules and synaptic-like microvesicles in anterior pituitary cells.
- Author
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Majó G, Aguado F, Blasi J, and Marsal J
- Subjects
- Animals, Antigens, Surface analysis, Cell Line, Centrifugation, Density Gradient, Female, Immunoblotting, Immunohistochemistry, Isomerism, Nerve Tissue Proteins analysis, R-SNARE Proteins, Rabbits, Rats, Rats, Sprague-Dawley, SNARE Proteins, Subcellular Fractions chemistry, Synaptosomal-Associated Protein 25, Syntaxin 1, Tetanus Toxin pharmacology, Vesicle-Associated Membrane Protein 3, Cytoplasmic Granules chemistry, Membrane Proteins analysis, Pituitary Gland, Anterior chemistry, Synaptic Membranes chemistry, Vesicular Transport Proteins
- Abstract
A set of synaptic proteins have been shown to be essential for the life cycle and exocytosis of synaptic vesicles at the nerve terminal. Recently, these proteins have also been identified in certain endocrine cells. Here we analysed the presence and location of some of these synaptic proteins in anterior pituitary cells. Immunoblotting data demonstrated that Rab3a, synaptotagmin, cellubrevin, synaptobrevin 2, syntaxin 1, SNAP-25 and synaptophysin were well represented in anterior pituitary cells as well as in the corticotroph cell line AtT-20. Cellubrevin was the most abundant synaptobrevin isoform present in pituitary cells. Moreover, both cellubrevin and synaptobrevin 2 took part of a protein complex involved in the fusion process in adenohypophyseal cells. Immunocytochemical and subcellular fractionation showed that cellubrevin, synaptobrevin 2, Rab3a and synaptotagmin were located in both secretory granules and synaptic-like microvesicles fractions. In contrast, SNAP-25 and syntaxin 1 were mainly associated with plasma membrane fractions. Therefore, these results suggest similar secretory mechanisms for synaptic vesicles and secretory organelles in both neuronal and endocrine cells.
- Published
- 1998
- Full Text
- View/download PDF
11. Immunocytochemical analysis of the synaptic proteins SNAP-25 and Rab3A in human pituitary adenomas. Overexpression of SNAP-25 in the mammmosomatotroph lineages.
- Author
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Majó G, Ferrer I, Marsal J, Blasi J, and Aguado F
- Subjects
- Acromegaly metabolism, Adolescent, Adult, Aged, Aged, 80 and over, Cushing Syndrome metabolism, Female, Fluorescent Antibody Technique, Humans, Immunoenzyme Techniques, Male, Middle Aged, Prolactinoma metabolism, Synaptosomal-Associated Protein 25, rab3 GTP-Binding Proteins, Adenoma metabolism, GTP-Binding Proteins metabolism, Membrane Proteins, Neoplasm Proteins metabolism, Nerve Tissue Proteins metabolism, Pituitary Neoplasms metabolism
- Abstract
SNAP-25 and Rab3A were originally identified as synaptic proteins involved in neuronal membrane traffic. Recently, both proteins have been detected in several mammalian endocrine cell types and have been proposed as essential components of the exocytotic pathway in neuroendocrine cells. In this study, the expression of SNAP-25 and Rab3A was analysed in biopsied human anterior pituitary tumours (21 cases) by immunocytochemical methods. No differences in Rab3A immunoreactivity were observed between tumour and normal pituitary cells. Strong SNAP-25 immunoreactivity was detected in tumour cells of prolactinomas (n = 3). Several growth hormone (GH)/prolactin (PRL) tumours also displayed intense SNAP-25 immunolabelling (n = 3), whereas the remaining GH-secreting adenomas (n = 4) exhibited moderate to weak SNAP-25 immunoreactivity. In contrast, SNAP-25 near-background immunostaining was observed in tumour cells of adrenocorticotrophic hormone (ACTH)-secreting tumours (n = 4) and non-secreting tumours (n = 7), as well as in normal pituitary cells. Since SNAP-25 and Rab3A have been shown to be involved in exocytotic events in rodent endocrine cells, overexpression of SNAP-25 protein in PRL and GH/PRL tumour cells might be implicated in the mechanism of exocytosis of the neoplastic human mammosomatotroph lineages.
- Published
- 1997
- Full Text
- View/download PDF
12. Expression of synaptosomal-associated protein SNAP-25 in endocrine anterior pituitary cells.
- Author
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Aguado F, Majó G, Ruiz-Montasell B, Canals JM, Casanova A, Marsal J, and Blasi J
- Subjects
- Animals, Botulinum Toxins pharmacology, Cells, Cultured, GTP-Binding Proteins metabolism, Immunoenzyme Techniques, Male, Membrane Proteins metabolism, Nerve Tissue Proteins genetics, Pituitary Gland, Anterior cytology, Qa-SNARE Proteins, R-SNARE Proteins, RNA, Messenger, Rats, Rats, Sprague-Dawley, Synaptosomal-Associated Protein 25, rab3 GTP-Binding Proteins, Nerve Tissue Proteins biosynthesis, Pituitary Gland, Anterior metabolism
- Abstract
A growing body of evidence indicates that the fundamental molecular mechanism of exocytosis in the secretory pathway may be structurally similar in all eukaryotic cells. The synaptosomal-associated protein of 25 kDa (SNAP-25) is a plasma membrane protein involved in regulated exocytosis in neurons. In order to compare exocytotic components in neurons and endocrine cells, we have analyzed the expression of SNAP-25 in the rat anterior pituitary. Western blotting analysis documented the presence of SNAP-25 in anterior pituitary homogenates and cultured anterior pituitary cells. In addition to SNAP-25, other neuronal proteins involved in exocytosis (syntaxin, VAMP/synaptobrevin and Rab3A) were also detected in the anterior pituitary. The specific expression of SNAP-25 mRNA in anterior pituitary cells was also corroborated by Northern analysis. SNAP-25 immunoreactivity was located at the plasma membrane of endocrine anterior pituitary cells. Characteristically, patches of fine punctate deposits exhibited intense SNAP-25 immunoreactivity. Double-labeling immunocytochemistry revealed that SNAP-25 was mainly associated with gonadotroph cell populations. Furthermore, we demonstrate that in the anterior pituitary, SNAP-25 is selectively cleaved by clostridial neurotoxins. In conclusion, our results establish the presence of SNAP-25 in secretory anterior pituitary cells and suggest a potential role of this protein in the secretion of adenohypophysial hormone.
- Published
- 1996
13. Cloning characterization and expression of the cDNA encoding a neuron-specific alpha-tubulin isoform highly represented in the electric lobe of Torpedo marmorata.
- Author
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Canals JM, Ruiz-Avila L, Aguado F, Majó G, and Marsal J
- Subjects
- Amino Acid Sequence, Animals, Base Sequence, Blotting, Southern, Brain Chemistry, DNA, Complementary genetics, Electric Organ innervation, Gene Expression, Gene Library, In Situ Hybridization, Molecular Sequence Data, Sequence Analysis, DNA, Sequence Homology, Amino Acid, Species Specificity, Tissue Distribution, Electric Organ chemistry, Nervous System chemistry, Neurons chemistry, Torpedo genetics, Tubulin genetics
- Abstract
A cDNA (alpha T6) encoding an alpha-tubulin from Torpedo marmorata (Tm) was isolated and sequenced. The deduced 451-amino-acid (aa) sequence codes for an alpha-tubulin of 50,161 Da. The aa sequence of alpha T6 of Tm showed a 70-99.6% identity to the other alpha-tubulins previously described. Moreover, the alpha T6 aa sequence was 95-99.6% identical to neural-specific tubulins of mouse, rat, human and siberian salmon. The corresponding mRNA is highly represented in the giant motoneurons of the electric lobe. All neuronal populations of the Tm brain exhibit variable levels of alpha T6 expression, with the highest levels in the long-axon-projecting neurons. These results suggest that this alpha-tubulin isoform may play an important role in the maintenance and/or remodeling of the neuronal cytoskeleton.
- Published
- 1995
- Full Text
- View/download PDF
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