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2.
G Ital Dermatol Venereol ; 145(2): 313-5, 2010 Apr.
Artículo en Inglés | MEDLINE | ID: mdl-20467404

RESUMEN

Kerion Celsi is a parasitic fungal skin infection that tends to occur mainly on the back of the neck, scalp or beard. It is caused by animal fungi. Sometimes the condition resolves itself in a matter of weeks but hair loss in the affected area may be permanent. We report a case of a young woman with Kerion Celsi favored by the use of a tretinoin+minoxidil+betametasone valerate lotion.


Asunto(s)
Betametasona/efectos adversos , Minoxidil/efectos adversos , Tiña del Cuero Cabelludo/inducido químicamente , Tretinoina/efectos adversos , Adulto , Alopecia Areata/tratamiento farmacológico , Betametasona/administración & dosificación , Quimioterapia Combinada , Femenino , Humanos , Minoxidil/administración & dosificación , Tretinoina/administración & dosificación
3.
Dermatol Ther ; 22 Suppl 1: S27-9, 2009 Nov.
Artículo en Inglés | MEDLINE | ID: mdl-19891689

RESUMEN

Leishmaniasis is a human disease produced by a parasite of the Leishmania genus transmitted by prick of an infected female sandfly. The disease occurs clinically with either cutaneous, mucocutaneous or visceral form, depending on the infective species and the immune status of the patient. Antimonial drugs are the current treatment of choice for all clinical forms. We report a case of cutaneous Leishmaniasis in a young girl successfully treated with itraconazole.


Asunto(s)
Antiprotozoarios/uso terapéutico , Itraconazol/uso terapéutico , Leishmaniasis Cutánea/tratamiento farmacológico , Adolescente , Femenino , Humanos , Leishmaniasis Cutánea/patología
5.
Anticancer Res ; 24(3b): 1897-900, 2004.
Artículo en Inglés | MEDLINE | ID: mdl-15274372

RESUMEN

Kaposi's sarcoma (KS) of the tongue is extremely rare in immunocompetent patients. We report a case of KS of the tongue associated with a median rhomboid glossitis. The main clinical, pathological and immunohistochemical features allowed the differential diagnosis.


Asunto(s)
Glositis/patología , Sarcoma de Kaposi/patología , Neoplasias de la Lengua/patología , Anciano , Diagnóstico Diferencial , Glositis/complicaciones , Glositis/diagnóstico , Humanos , Inmunohistoquímica , Masculino , Sarcoma de Kaposi/complicaciones , Sarcoma de Kaposi/diagnóstico , Neoplasias de la Lengua/complicaciones , Neoplasias de la Lengua/diagnóstico
6.
Mol Microbiol ; 50(4): 1257-69, 2003 Nov.
Artículo en Inglés | MEDLINE | ID: mdl-14622413

RESUMEN

The malate-aspartate NADH shuttle in mammalian cells requires the activity of the mitochondrial aspartate-glutamate carrier (AGC). Recently, we identified in man two AGC isoforms, aralar1 and citrin, which are regulated by calcium on the external face of the inner mitochondrial membrane. We have now identified Agc1p as the yeast counterpart of the human AGC. The corresponding gene was overexpressed in bacteria and yeast mitochondria, and the protein was reconstituted in liposomes where it was identified as an aspartate-glutamate transporter from its transport properties. Furthermore, yeast cells lacking Agc1p were unable to grow on acetate and oleic acid, and had reduced levels of valine, ornithine and citrulline; in contrast they grew on ethanol. Expression of the human AGC isoforms can replace the function of Agc1p. However, unlike its human orthologues, yeast Agc1p catalyses both aspartate-glutamate exchange and substrate uniport activities. We conclude that Agc1p performs two metabolic roles in Saccharomyces cerevisiae. On the one hand, it functions as a uniporter to supply the mitochondria with glutamate for nitrogen metabolism and ornithine synthesis. On the other, the Agc1p, as an aspartate-glutamate exchanger, plays a role within the malate-aspartate NADH shuttle which is critical for the growth of yeast on acetate and fatty acids as carbon sources. These results provide strong evidence of the existence of a malate-aspartate NADH shuttle in yeast.


Asunto(s)
Sistemas de Transporte de Aminoácidos Acídicos/metabolismo , Antiportadores/metabolismo , Mitocondrias/metabolismo , Proteínas de Saccharomyces cerevisiae/metabolismo , Saccharomyces cerevisiae/metabolismo , Acetatos/metabolismo , Sistemas de Transporte de Aminoácidos Acídicos/genética , Animales , Antiportadores/genética , Ácido Aspártico/metabolismo , Dióxido de Carbono/metabolismo , Ácido Glutámico/metabolismo , Humanos , Liposomas/química , Liposomas/metabolismo , Malatos/metabolismo , Potenciales de la Membrana , Ornitina/metabolismo , Isoformas de Proteínas/genética , Isoformas de Proteínas/metabolismo , Proteínas Recombinantes/genética , Proteínas Recombinantes/metabolismo , Proteínas de Saccharomyces cerevisiae/genética
7.
J Eur Acad Dermatol Venereol ; 17(2): 204-5, 2003 Mar.
Artículo en Inglés | MEDLINE | ID: mdl-12705753

RESUMEN

The authors report a case of congenital rubella in a 7-month-old female infant presenting a Blueberry Muffin Rash. Blueberry Muffin Syndrome is a cutaneous manifestation characterized by widespread maculo papular lesions of a reddish-blue or magenta colour, due to persistent dermal erythropoiesis in patients with congenital viral infections.


Asunto(s)
Eritropoyesis , Trastornos de la Pigmentación/etiología , Rubéola (Sarampión Alemán)/congénito , Enfermedades de la Piel/etiología , Femenino , Humanos , Lactante
8.
J Eur Acad Dermatol Venereol ; 17(1): 37-41, 2003 Jan.
Artículo en Inglés | MEDLINE | ID: mdl-12602966

RESUMEN

BACKGROUND: Cancer might be envisaged as the result of a genetic process causing the unregulated proliferation of a given cell as well as its inability to undergo differentiation and/or apoptosis. Alterations of genes regulating cell division cycle appear to play a key role in the development of human cancer. OBJECTIVE: On the bases of the above considerations, we decided to establish new cell lines from human melanoma specimens, in order to analyse the molecular alterations in primary preparations of malignant cells. RESULTS: The present paper describes two new established cell lines and their genetic and biochemical features. Both the melanoma cell lines show inactivation of the cyclin-dependent kinase inhibitor gene, CDKN2A/p16INK4A, thus demostrating that this alteration occurs in primary human melanomas. No other alterations were observable when we investigated several different cell cycle genes including those encoding cyclins, cyclin-dependent kinases and cyclin-dependent kinase inhibitors. Analyses at protein level by means of immunoblotting confirmed the results obtained at the genetic level. Moreover, the inducibility of a pivotal cyclin-dependent kinase inhibitor gene, namely p21CIP1 gene, was obtained by treating the cells with histone deacetylase inhibitors, namely butyrate and phenylbutyrate. CONCLUSIONS: Our results suggest a primary role of cyclin-dependent kinase inhibitor genes inactivation in the origin of human melanoma and allow the proposal of new therapeutic strategies based on the transcriptional activation of p21CIP1 gene.


Asunto(s)
Quinasas Ciclina-Dependientes/antagonistas & inhibidores , Melanoma/genética , Neoplasias Cutáneas/genética , División Celular , Inhibidor p21 de las Quinasas Dependientes de la Ciclina , Ciclinas/genética , Inhibidores Enzimáticos , Genes p16 , Humanos , Immunoblotting , Melanoma/patología , Reacción en Cadena de la Polimerasa de Transcriptasa Inversa , Neoplasias Cutáneas/patología , Células Tumorales Cultivadas
9.
EMBO J ; 21(21): 5653-61, 2002 Nov 01.
Artículo en Inglés | MEDLINE | ID: mdl-12411483

RESUMEN

The genome of Saccharomyces cerevisiae contains 35 members of a family of transport proteins that, with a single exception, are found in the inner membranes of mitochondria. The transport functions of the 15 biochemically identified mitochondrial carriers are concerned with shuttling substrates, biosynthetic intermediates and cofactors across the inner membrane. Here the identification of the mitochondrial carrier for the essential cofactor thiamine pyrophosphate (ThPP) is described. The protein has been overexpressed in bacteria, reconstituted into phospholipid vesicles and identified by its transport properties. In confirmation of its identity, cells lacking the gene for this carrier had reduced levels of ThPP in their mitochondria, and decreased activity of acetolactate synthase, a ThPP-requiring enzyme found in the organellar matrix. They also required thiamine for growth on fermentative carbon sources.


Asunto(s)
Mitocondrias/metabolismo , Saccharomyces cerevisiae/metabolismo , Tiamina Pirofosfato/metabolismo , Carbono/metabolismo , Fermentación , Membranas Intracelulares/metabolismo , Cinética , Proteínas Recombinantes/metabolismo , Tiamina/metabolismo
13.
Minerva Ginecol ; 53(1 Suppl 1): 75-7, 2001 Feb.
Artículo en Inglés | MEDLINE | ID: mdl-11526727

RESUMEN

BACKGROUND: This study was performed to evaluate, in women suffering from Systemic Lupus Erythematosus (SLE), the relationship between the assumption of oral contraceptives and the evolution of the disease. METHODS: In the Institute of Obstetrics and Gynaecology in collaboration with the Institute of Dermosyphilopathical Clinic of Second University of Studies of Naples, 20 women in fertile age suffering from SLE with specific cutaneous manifestations were studied for the year 1999. All the patients requested to take, at contraceptive purpose, low-dosage estroprogestagens. The contraceptives we prescribed have, as active substance, the gestodene at the dose of 0.075 mg and the etinilestrdiol at the dose of 0.02 mg per day. Patients' group in object was compared for a year with a similar control group of women suffering from SLE not subjected to any pharmacological therapy. RESULTS: Only 5 patients out 20 have had to suspend therapy after 4 or 5 months, because a relapse of the illness was experienced while the others 15 patients did not lament a relapse of the illness. In the control group a more or less similar percentage of patients, during the months of the observation, spontaneously had episodes of relapse of the illness. CONCLUSIONS: The results of our brief study have shown that the administration of hormonal contraceptives in reality doesn't constantly produce immediate and remarkable exacerbations of the illness in women suffering from SLE. In our opinion the contraception with the latest estroprogestagens can comfortably be effected under strict medical control, probably because the medicines at low dosage are quickly metabolized and in the majority of the cases they don't have capacity to influence the course of such chronic connectivitis.


Asunto(s)
Anticonceptivos Hormonales Orales/efectos adversos , Lupus Eritematoso Sistémico/complicaciones , Adulto , Femenino , Humanos , Recurrencia
14.
J Eur Acad Dermatol Venereol ; 15(5): 427-9, 2001 Sep.
Artículo en Inglés | MEDLINE | ID: mdl-11763383

RESUMEN

Dermatofibrosarcoma is a rare, low-grade malignant skin tumour that can be considered the equivalent of malignant non-cutaneous soft tissue fibrohistiocytoma. The high rate of recurrence of this tumour is correlated with poor surgical management because lesions, often smaller than 2 cm in diameter, may be confused with dermatofibroma or keloid. Our findings confirm the importance of accurate diagnosis of primary lesions and the need for aggressive surgical treatment (excision of 5 cm of surrounding tissue) to lower the incidence of local relapse.


Asunto(s)
Dermatofibrosarcoma/diagnóstico , Dermatofibrosarcoma/cirugía , Neoplasias Cutáneas/diagnóstico , Neoplasias Cutáneas/cirugía , Adulto , Biopsia con Aguja , Femenino , Estudios de Seguimiento , Humanos , Masculino , Persona de Mediana Edad , Índice de Severidad de la Enfermedad , Resultado del Tratamiento
15.
Biochim Biophys Acta ; 1459(2-3): 363-9, 2000 Aug 15.
Artículo en Inglés | MEDLINE | ID: mdl-11004452

RESUMEN

The genome of Saccharomyces cerevisiae encodes 35 putative members of the mitochondrial carrier family. Known members of this family transport substrates and products across the inner membranes of mitochondria. We are attempting to identify the functions of the yeast mitochondrial transporters via high-yield expression in Escherichia coli and/or S. cerevisiae, purification and reconstitution of their protein products into liposomes, where their transport properties are investigated. With this strategy, we have already identified the functions of seven S. cerevisiae gene products, whose structural and functional properties assigned them to the mitochondrial carrier family. The functional information obtained in the reconstituted system and the use of knock-out yeast strains can be usefully exploited for the investigation of the physiological role of individual transporters. Furthermore, the yeast carrier sequences can be used to identify the orthologous proteins in other organisms, including man.


Asunto(s)
Proteínas Portadoras/metabolismo , Proteínas de Escherichia coli , Proteínas de Transporte de Membrana , Saccharomyces cerevisiae/metabolismo , Sistemas de Transporte de Aminoácidos Básicos , Animales , Antiportadores/química , Antiportadores/metabolismo , Proteínas Bacterianas/química , Proteínas Bacterianas/metabolismo , Caenorhabditis elegans/genética , Caenorhabditis elegans/metabolismo , Carnitina Aciltransferasas/química , Carnitina Aciltransferasas/metabolismo , Proteínas Portadoras/química , Proteínas Portadoras/genética , Clonación Molecular , Transportadores de Ácidos Dicarboxílicos , Escherichia coli/genética , Escherichia coli/metabolismo , Humanos , Membranas Intracelulares/metabolismo , Proteínas de la Membrana/química , Proteínas de la Membrana/metabolismo , Mitocondrias/metabolismo , Saccharomyces cerevisiae/genética
16.
J Biol Chem ; 274(32): 22184-90, 1999 Aug 06.
Artículo en Inglés | MEDLINE | ID: mdl-10428783

RESUMEN

Saccharomyces cerevisiae encodes 35 members of the mitochondrial carrier family, including the OAC protein. The transport specificities of some family members are known, but most are not. The function of the OAC has been revealed by overproduction in Escherichia coli, reconstitution into liposomes, and demonstration that the proteoliposomes transport malonate, oxaloacetate, sulfate, and thiosulfate. Reconstituted OAC catalyzes both unidirectional transport and exchange of substrates. In S. cerevisiae, OAC is in inner mitochondrial membranes, and deletion of its gene greatly reduces transport of oxaloacetate sulfate, thiosulfate, and malonate. Mitochondria from wild-type cells swelled in isoosmotic solutions of ammonium salts of oxaloacetate, sulfate, thiosulfate, and malonate, indicating that these anions are cotransported with protons. Overexpression of OAC in the deletion strain increased greatly the [(35)S]sulfate/sulfate and [(35)S]sulfate/oxaloacetate exchanges in proteoliposomes reconstituted with digitonin extracts of mitochondria. The main physiological role of OAC appears to be to use the proton-motive force to take up into mitochondria oxaloacetate produced from pyruvate by cytoplasmic pyruvate carboxylase.


Asunto(s)
Proteínas de Transporte de Anión , Proteínas Portadoras/metabolismo , Mitocondrias/metabolismo , Ácido Oxaloacético/metabolismo , Proteínas de Saccharomyces cerevisiae , Saccharomyces cerevisiae/metabolismo , Sulfatos/metabolismo , Transporte Biológico , Proteínas Portadoras/genética , Escherichia coli/genética , Proteínas Fúngicas/genética , Proteínas Fúngicas/metabolismo , Cinética , Malonatos/metabolismo , Datos de Secuencia Molecular , Mutación , Proteolípidos , Fuerza Protón-Motriz , Proteínas Recombinantes/metabolismo , Saccharomyces cerevisiae/genética , Eliminación de Secuencia , Tiosulfatos/metabolismo
17.
Mol Microbiol ; 31(2): 569-77, 1999 Jan.
Artículo en Inglés | MEDLINE | ID: mdl-10027973

RESUMEN

The dicarboxylate carrier (DIC) is an integral membrane protein that catalyses a dicarboxylate-phosphate exchange across the inner mitochondrial membrane. We generated a yeast mutant lacking the gene for the DIC. The deletion mutant failed to grow on acetate or ethanol as sole carbon source but was viable on glucose, galactose, pyruvate, lactate and glycerol. The growth on ethanol or acetate was largely restored by the addition of low concentrations of aspartate, glutamate, fumarate, citrate, oxoglutarate, oxaloacetate and glucose, but not of succinate, leucine and lysine. The expression of the DIC gene in wild-type yeast was repressed in media containing ethanol or acetate with or without glycerol. These results indicate that the primary function of DIC is to transport cytoplasmic dicarboxylates into the mitochondrial matrix rather than to direct carbon flux to gluconeogenesis by exporting malate from the mitochondria. The delta DIC mutant may serve as a convenient host for overexpression of DIC and for the demonstration of its correct targeting and assembly.


Asunto(s)
Proteínas Portadoras/fisiología , Ácidos Dicarboxílicos/metabolismo , Acetatos , Carbono , Proteínas Portadoras/genética , Medios de Cultivo , Transportadores de Ácidos Dicarboxílicos , Etanol , Regulación Fúngica de la Expresión Génica , Membranas Intracelulares/metabolismo , Malatos/metabolismo , Mitocondrias/metabolismo , Fosfatos/metabolismo , Saccharomyces cerevisiae/crecimiento & desarrollo
18.
Biochem J ; 333 ( Pt 1): 151-8, 1998 Jul 01.
Artículo en Inglés | MEDLINE | ID: mdl-9639574

RESUMEN

We have studied the targeting and assembly of the 2-oxoglutarate carrier (OGC), an integral inner-membrane protein of mitochondria. The precursor of OGC, synthesized without a cleavable presequence, is transported into mitochondria in an ATP- and membrane potential-dependent manner. Import of the mammalian OGC occurs efficiently into both mammalian and yeast mitochondria. Targeting of OGC reveals a clear dependence on the mitochondrial surface receptor Tom70 (the 70 kDa subunit of the translocase of the outer mitochondrial membrane), whereas a cleavable preprotein depends on Tom20 (the 20 kDa subunit), supporting a model of specificity differences of the receptors and the existence of distinct targeting pathways to mitochondria. The assembly of minute amounts of OGC imported in vitro to the dimeric form can be monitored by blue native electrophoresis of digitonin-lysed mitochondria. The assembly of mammalian OGC and fungal ADP/ATP carrier occurs with high efficiency in both mammalian and yeast mitochondria. These findings indicate a dynamic behaviour of the carrier dimers in the mitochondrial inner membrane and suggest a high conservation of the assembly reactions from mammals to fungi.


Asunto(s)
Proteínas Portadoras/metabolismo , Membranas Intracelulares/metabolismo , Ácidos Cetoglutáricos/metabolismo , Proteínas de Transporte de Membrana , Mitocondrias/metabolismo , Animales , Transporte Biológico/fisiología , Proteínas Portadoras/química , Dimerización , Electroforesis en Gel de Poliacrilamida , Mitocondrias/ultraestructura , Mitocondrias Hepáticas/metabolismo , Translocasas Mitocondriales de ADP y ATP/metabolismo , Ratas , Saccharomyces cerevisiae/metabolismo , Saccharomyces cerevisiae/ultraestructura
19.
Mol Cell Biol ; 16(11): 6524-31, 1996 Nov.
Artículo en Inglés | MEDLINE | ID: mdl-8887681

RESUMEN

Two different functions have been proposed for the phosphate carrier protein/p32 of Saccharomyces cerevisiae mitochondria: transport of phosphate and requirement for import of precursor proteins into mitochondria. We characterized a yeast mutant lacking the gene for the phosphate carrier/p32 and found both a block in the import of phosphate and a strong reduction in the import of preproteins transported to the mitochondrial inner membrane and matrix. Binding of preproteins to the surface of mutant mitochondria and import of outer membrane proteins were not inhibited, indicating that the inhibition of protein import occurred after the recognition step at the outer membrane. The membrane potential across the inner membrane of the mutant mitochondria was strongly reduced. Restoration of the membrane potential restored preprotein import but did not affect the block of phosphate transport of the mutant mitochondria. We conclude that the inhibition of protein import into mitochondria lacking the phosphate carrier/p32 is indirectly caused by a reduction of the mitochondrial membrane potential (delta(gamma)), and we propose a model that the reduction of delta(psi) is due to the defective phosphate import, suggesting that phosphate transport is the primary function of the phosphate carrier/p32.


Asunto(s)
Proteínas Portadoras/metabolismo , Mitocondrias/fisiología , Fosfatos/metabolismo , Saccharomyces cerevisiae/fisiología , Adenosina Trifosfato/metabolismo , Sitios de Unión , Proteínas Portadoras/genética , Endopeptidasa K , Etilmaleimida/farmacología , Membranas Intracelulares/efectos de los fármacos , Membranas Intracelulares/fisiología , Cinética , Potenciales de la Membrana , Mersalil/farmacología , Dilatación Mitocondrial , Proteínas de Unión a Fosfato , Precursores de Proteínas/metabolismo , Saccharomyces cerevisiae/genética
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