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1.
Medicina (Kaunas) ; 58(10)2022 Oct 11.
Artigo em Inglês | MEDLINE | ID: mdl-36295596

RESUMO

Background and Objectives: Perilipins 1-5 (PLIN) are lipid droplet-associated proteins that participate in regulating lipid storage and metabolism, and the PLIN5 isoform is known to form a nuclear complex with peroxisome proliferator-activated receptor-gamma coactivator 1-alpha (PGC-1α) to regulate lipid metabolism gene expression. However, the changes in PLIN isoforms' expression in response to pregnancy-induced cardiac hypertrophy are not thoroughly studied. The aim of this study was to quantify the mRNA expression of PLIN isoforms and PGC-1α along with total triacylglycerol (TAG) and cholesterol levels during late pregnancy and the postpartum period in the rat left ventricle. Materials and Methods: Female Sprague-Dawley rats were divided into three groups: non-pregnant, late pregnancy, and postpartum. The mRNA and protein levels were evaluated using quantitative RT-PCR and Western blotting, respectively. TAG and total cholesterol content were evaluated using commercial colorimetric methods. Results: The expression of mRNAs for PLIN1, 2, and 5 increased during pregnancy and the postpartum period. PGC-1α mRNA and protein expression increased during pregnancy and the postpartum period. Moreover, TAG and total cholesterol increased during pregnancy and returned to basal levels after pregnancy. Conclusions: Our results demonstrate that pregnancy upregulates differentially the expression of PLIN isoforms along with PGC-1α, suggesting that together they might be involved in the regulation of the lipid metabolic shift induced by pregnancy.


Assuntos
Receptores Ativados por Proliferador de Peroxissomo , Fatores de Transcrição , Ratos , Feminino , Animais , Gravidez , Perilipina-1 , Fatores de Transcrição/genética , Fatores de Transcrição/metabolismo , Receptores Ativados por Proliferador de Peroxissomo/metabolismo , Ratos Sprague-Dawley , Coativador 1-alfa do Receptor gama Ativado por Proliferador de Peroxissomo/genética , Coativador 1-alfa do Receptor gama Ativado por Proliferador de Peroxissomo/metabolismo , Cardiomegalia/genética , Cardiomegalia/metabolismo , Isoformas de Proteínas/genética , Isoformas de Proteínas/metabolismo , RNA Mensageiro/genética , RNA Mensageiro/metabolismo , Triglicerídeos , Colesterol
2.
Rev. chil. nutr ; 49(5)oct. 2022.
Artigo em Espanhol | LILACS-Express | LILACS | ID: biblio-1407844

RESUMO

RESUMEN La sucralosa es un edulcorante no calórico de amplio consumo a nivel mundial, es considerado como un aditivo seguro, debido a que es eliminado en periodos cortos de tiempo. Recientemente se evidenció su bioacumulación en tejido adiposo, donde se encuentran inmersos macrófagos, células del sistema inmune involucradas en el desarrollo de la inflamación sistémica de bajo grado. A la fecha, no se cuenta con suficiente información para demostrar si los edulcorantes potencian los procesos inflamatorios alterando la función de células presentes en tejido y/o contribuyen en el desarrollo de patologías metabólicas. Por lo anterior, en nuestro trabajo se evaluó el efecto de la sucralosa en la viabilidad de los macrófagos diferenciados de la línea celular monocítica THP-1, por azul de tripán y ensayos de MTT, así como su efecto en la polarización M1/M2 por PCR según la expresión de IRF4, IRF5, STAT1, STAT6, perfil de expresión de IL-6, IL-12, TNF-α, TGF-β, IL-10 y SOCS3 por qPCR, y la cuantificación de la quimiocina IP-10 por ELISA. Los resultados indicaron que la sucralosa no tiene efectos citotóxicos, pero disminuye el número de células viables metabólicamente activas determinadas por MTT de manera dependiente de la concentración. La sucralosa incrementa la concentración de la quimiocina IP-10 y la expresión génica del factor de transcripción IRF5 y disminuye la expresión de IRF4 y STAT6, favoreciendo la polarización hacia poblaciones M1. La bioacumulación de sucralosa en tejido adiposo, y su interacción con macrófagos, podría inducir su polarización a M1.


ABSTRACT Sucralose is a non-nutritive sweetener widely consumed worldwide; it is considered a safe additive because it is eliminated quickly. Recently its bioaccumulation in adipose tissue was evidenced, where macrophages, cells of the immune system involved in developing low-grade systemic inflammation, are found. To date, there is a paucity of information regarding whether sweeteners potentiate inflammatory processes by altering the function of cells present in tissue and/or contribute to the development of metabolic pathologies. We evaluate the effect of sucralose on the viability of differentiated macrophages of the monocytic cell line THP-1, by trypan blue and MTT assays, respectively, as well as its effect on M1/ M2 by PCR according to the expression of IRF4, IRF5, STAT1, STAT6, expression profile of IL6, IL-12, TNF-α, TGF-β, IL-10 and SOCS3 by qPCR, and the quantification of the chemokine IP-10 by ELISE. The results indicated that sucralose has no cytotoxic effects but decreases the number of metabolically active viable cells determined by MTT of macrophages in a concentration-dependent manner. Sucralose increased the concentration of the chemokine IP-10 and the gene expression of the transcription factors IRF5 and decreased the expression of IRF4 and STAT 6 gene expression, favoring polarization towards M1 populations. The bioaccumulation of sucralose in adipose tissue, and its interaction with macrophages, could induce its polarization to M1.

3.
Genes (Basel) ; 13(5)2022 05 20.
Artigo em Inglês | MEDLINE | ID: mdl-35627302

RESUMO

The major histocompatibility complex (MHC) enables vertebrates to cope with pathogens and maintain healthy populations, thus making it a unique set of loci for addressing ecology and evolutionary biology questions. The aim of our study was to examine the variability of Heermann's Gull MHC class II (MHCIIB) and compare these loci with other Charadriiformes. Fifty-nine MHCIIB haplotypes were recovered from sixty-eight Heermann's Gulls by cloning, of them, twelve were identified as putative true alleles, forty-five as unique alleles, and two as pseudogenes. Intra and interspecific relationships indicated at least two loci in Heermann's Gull MHCIIB and trans-species polymorphism among Charadriiformes (coinciding with the documented evidence of two ancient avian MHCIIB lineages, except in the Charadriidae family). Additionally, sites under diversifying selection revealed a better match with peptide-binding sites inferred in birds than those described in humans. Despite the negative anthropogenic activity reported on Isla Rasa, Heermann's Gull showed MHCIIB variability consistent with population expansion, possibly due to a sudden growth following conservation efforts. Duplication must play an essential role in shaping Charadriiformes MHCIIB variability, buffering selective pressures through balancing selection. These findings suggest that MHC copy number and protected islands can contribute to seabird conservation.


Assuntos
Charadriiformes , Animais , Aves/genética , Charadriiformes/genética , Genes MHC da Classe II/genética , Antígenos de Histocompatibilidade Classe II/genética , Humanos , Filogenia , Seleção Genética
4.
Life Sci ; 285: 119943, 2021 Nov 15.
Artigo em Inglês | MEDLINE | ID: mdl-34516992

RESUMO

Glycine betaine (N, N, N-trimethyl amine) is an osmolyte accumulated in cells that is key for cell volume and turgor regulation, is the principal methyl donor in the methionine cycle and is a DNA and proteins stabilizer. In humans, glycine betaine is synthesized from choline and can be obtained from some foods. Glycine betaine (GB) roles are illustrated in chemical, metabolic, agriculture, and clinical medical studies due to its chemical and physiological properties. Several studies have extensively described GB role and accumulation related to specific pathologies, focusing mainly on analyzing its positive and negative role in these pathologies. However, it is necessary to explain the relationship between glycine betaine and different pathologies concerning its role as an antioxidant, ability to methylate DNA, interact with transcription factors and cell receptors, and participate in the control of homocysteine concentration in liver, kidney and brain. This review summarizes the most important findings and integrates GB role in neurodegenerative, cardiovascular, hepatic, and renal diseases. Furthermore, we discuss GB impact on other dysfunctions as inflammation, oxidative stress, and glucose metabolism, to understand their cross-talks and provide reliable data to establish a base for further investigations.


Assuntos
Betaína/metabolismo , Doenças Cardiovasculares/metabolismo , Nefropatias/metabolismo , Hepatopatias/metabolismo , Doenças Neurodegenerativas/metabolismo , Tamanho Celular , Humanos , Hiper-Homocisteinemia/metabolismo , Concentração Osmolar , S-Adenosilmetionina/metabolismo
5.
Luminescence ; 36(7): 1733-1742, 2021 Nov.
Artigo em Inglês | MEDLINE | ID: mdl-34213071

RESUMO

Glycine betaine is the main osmolyte synthesized and accumulated in mammalian renal cells. Glycine betaine synthesis is catalyzed by the enzyme betaine aldehyde dehydrogenase (BADH) using NAD+ as the coenzyme. Previous studies have shown that porcine kidney betaine aldehyde dehydrogenase (pkBADH) binds NAD+ with different affinities at each active site and that the binding is K+ dependent. The objective of this work was to analyze the changes in the pkBADH secondary and tertiary structure resulting from variable concentrations of NAD+ and the role played by K+ . Intrinsic fluorescence studies were carried out at fixed-variable concentrations of K+ and titrating the enzyme with varying concentrations of NAD+ . Fluorescence analysis showed a shift of the maximum emission towards red as the concentration of K+ was increased. Changes in the exposure of tryptophan located near the NAD+ binding site were found when the enzyme was titrated with NAD+ in the presence of potassium. Fluorescence data analysis showed that the K+ presence promoted static quenching that facilitated the pkBADH-NAD+ complex formation. DC data analysis showed that binding of K+ to the enzyme caused changes in the α-helix content of 4% and 12% in the presence of 25 mM and 100 mM K+ , respectively. The presence of K+ during NAD+ binding to pkBADH increased the thermal stability of the complex. These results indicated that K+ facilitated the pkBADH-NAD+ complex formation and suggested that K+ caused small changes in secondary and tertiary structures that could influence the active site conformation.


Assuntos
Betaína-Aldeído Desidrogenase , Potássio , Animais , Betaína-Aldeído Desidrogenase/metabolismo , Sítios de Ligação , Coenzimas , Cinética , Conformação Molecular , Suínos
6.
J Bioenerg Biomembr ; 52(2): 61-70, 2020 04.
Artigo em Inglês | MEDLINE | ID: mdl-32128683

RESUMO

Betaine aldehyde dehydrogenase (BADH) catalyzes the oxidation of betaine aldehyde to glycine betaine using NAD+ as a coenzyme. Studies in porcine kidney BADH (pkBADH) suggested that the enzyme exhibits heterogeneity of active sites and undergoes potassium-induced conformational changes. This study aimed to analyze if potassium concentration plays a role in the heterogeneity of pkBADH active sites through changes in NAD+ affinity constants, in its secondary structure content and stability. The enzyme was titrated with NAD+ 1 mM at fixed-variable KCl concentration, and the interaction measured by Isothermal Titration Calorimetry (ITC) and Circular Dichroism (CD). ITC data showed that K+ increased the first active site affinity in a manner dependent on its concentration; KD values to the first site were 14.4, 13.1, and 10.4 µM, at 25, 50, and 75 mM KCl. ΔG values showed that the coenzyme binding is a spontaneous reaction without changes between active sites or depending on KCl concentration. ΔH and TΔSb values showed that NAD+ binding to the active site is an endothermic process and is carried out at the expense of changes in entropy. α-Helix content increased as KCl increased, enzyme (Tm)app values were 2.6 °C and 3.3 °C higher at 20 mM and 200 mM K+. PkBADH molecular model showed three different interaction K+ sites. Results suggested K+ can interact with pkBADH and cause changes in the secondary structure, it provokes changes in the enzyme affinity by the coenzyme, and in the thermostability.


Assuntos
Betaína-Aldeído Desidrogenase/metabolismo , NAD/metabolismo , Potássio/metabolismo , Sítios de Ligação , Modelos Moleculares
7.
Artigo em Inglês | MEDLINE | ID: mdl-31790808

RESUMO

In marine animals, glycine betaine is one of the main osmolytes accumulated under osmotic stress conditions; nevertheless, in penaeids, shrimps little is known about the pathways involved in glycine betaine biosynthesis. In animal cells, glycine betaine is synthesized by the enzyme betaine aldehyde dehydrogenase (BADH). We herein investigated the salinity effect on the synthesis and concentration of glycine betaine on white shrimp Litopenaeus vannamei. Shrimps were subjected to 10, 20, 35, 40, 50, and 60 ppt salinity conditions for seven days. BADH activity increased in hepatopancreas and gills of shrimps subjected to salinities above 35 ppt salinity. In muscle, the BADH activity decreased at 35 ppt salinity. In hepatopancreas from shrimps subjected to 50 and 60 ppt salinities, BADH activity increased 1.1 and 1.7-fold. At 60 ppt salinity, BADH activity increased 1.5-fold respect to 35 ppt in gills. Glycine betaine concentration increased in hepatopancreas, gills, muscle, and hemolymph in shrimps subjected to salinities above 35 ppt. Glycine betaine concentration also increased at 20 ppt salinity, while at 10 ppt, not detected significant differences. The catch of glycine betaine from hemolymph by the cell likely is carried out to avoid protein denaturalization. Ammonia concentration in the aquarium's water only increased at salinities of 20 ppt and 10 ppt (1.1-fold relative to 35 ppt). Our data demonstrated that in L. vannamei, salinity regulates BADH activity and glycine betaine content in a tissue-specific manner.


Assuntos
Betaína-Aldeído Desidrogenase/metabolismo , Betaína/metabolismo , Osmorregulação , Pressão Osmótica , Penaeidae/metabolismo , Salinidade , Animais , Hemolinfa/metabolismo , Hepatopâncreas/metabolismo , Penaeidae/efeitos dos fármacos
8.
Artigo em Inglês | MEDLINE | ID: mdl-30041062

RESUMO

Hypoxia inducible factor-1 (HIF-1) is a transcriptional factor that induces genes involved in glucose metabolism. HIF-1 is formed by a regulatory α-subunit (HIF-1α) and a constitutive ß-subunit (HIF-1ß). The white spot syndrome virus (WSSV) induces a shift in glucose metabolism and oxidative stress. HIF-1α is associated with the induction of metabolic changes in tissues of WSSV-infected shrimp. However, the contributions of HIF-1 to viral load and antioxidant responses in WSSV-infected shrimp have been not examined. In this study, the effect of HIF-1 silencing on viral load and the expression and activity of antioxidant enzymes (superoxide dismutase-SOD, glutathione S-transferase-GST, and catalase) along with oxidative damage (lipid peroxidation and protein carbonyl) in tissues of white shrimp infected with the WSSV were studied. The viral load increased in hepatopancreas and muscle after WSSV infection, and the accumulative mortality was of 100% at 72 h post-infection. The expression and activity of SOD, catalase, and GST decreased in each tissue evaluated after WSSV infection. Protein carbonyl concentrations increased in each tissue after WSSV infection, while lipid peroxidation increased in hepatopancreas, but not in muscle. Silencing of HIF-1α decreased the WSSV viral load in hepatopancreas and muscle of infected shrimp along with shrimp mortality. Silencing of HIF-1α ameliorated the antioxidant response in a tissue-specific manner, which translated to a decrease in oxidative damage. These results suggest that HIF-1 is essential for restoring the antioxidant response, which counters the oxidative injury associated with WSSV infection.


Assuntos
Regulação da Expressão Gênica no Desenvolvimento , Subunidade alfa do Fator 1 Induzível por Hipóxia/antagonistas & inibidores , Penaeidae/virologia , Vírus da Síndrome da Mancha Branca 1/patogenicidade , Animais , Aquicultura , DNA Viral/isolamento & purificação , Inativação Gênica , Hepatopâncreas/crescimento & desenvolvimento , Hepatopâncreas/metabolismo , Hepatopâncreas/virologia , Subunidade alfa do Fator 1 Induzível por Hipóxia/genética , Subunidade alfa do Fator 1 Induzível por Hipóxia/metabolismo , Injeções Intramusculares , Peroxidação de Lipídeos , México , Músculos/metabolismo , Músculos/virologia , Especificidade de Órgãos , Estresse Oxidativo , Oxirredutases/genética , Oxirredutases/metabolismo , Penaeidae/crescimento & desenvolvimento , Penaeidae/metabolismo , Carbonilação Proteica , Interferência de RNA , RNA de Cadeia Dupla/administração & dosagem , RNA de Cadeia Dupla/metabolismo , Carga Viral , Vírus da Síndrome da Mancha Branca 1/isolamento & purificação , Vírus da Síndrome da Mancha Branca 1/fisiologia
9.
Chem Biol Interact ; 276: 65-74, 2017 Oct 01.
Artigo em Inglês | MEDLINE | ID: mdl-28212821

RESUMO

The enzyme betaine aldehyde dehydrogenase (BADH) catalyzes the irreversible oxidation of betaine aldehyde to glycine betaine (GB), a very efficient osmolyte accumulated during osmotic stress. In this study, we determined the nucleotide sequence of the cDNA for the BADH from the white shrimp Litopenaeus vannamei (LvBADH). The cDNA was 1882 bp long, with a complete open reading frame of 1524 bp, encoding 507 amino acids with a predicted molecular mass of 54.15 kDa and a pI of 5.4. The predicted LvBADH amino acid sequence shares a high degree of identity with marine invertebrate BADHs. Catalytic residues (C-298, E-264 and N-167) and the decapeptide VTLELGGKSP involved in nucleotide binding and highly conserved in BADHs were identified in the amino acid sequence. Phylogenetic analyses classified LvBADH in a clade that includes ALDH9 sequences from marine invertebrates. Molecular modeling of LvBADH revealed that the protein has amino acid residues and sequence motifs essential for the function of the ALDH9 family of enzymes. LvBADH modeling showed three potential monovalent cation binding sites, one site is located in an intra-subunit cavity; other in an inter-subunit cavity and a third in a central-cavity of the protein. The results show that LvBADH shares a high degree of identity with BADH sequences from marine invertebrates and enzymes that belong to the ALDH9 family. Our findings suggest that the LvBADH has molecular mechanisms of regulation similar to those of other BADHs belonging to the ALDH9 family, and that BADH might be playing a role in the osmoregulation capacity of L. vannamei.


Assuntos
Betaína-Aldeído Desidrogenase/metabolismo , Betaína/metabolismo , Modelos Moleculares , Penaeidae/enzimologia , Motivos de Aminoácidos , Sequência de Aminoácidos , Animais , Betaína-Aldeído Desidrogenase/classificação , Betaína-Aldeído Desidrogenase/genética , Sítios de Ligação , Biocatálise , Clonagem Molecular , Humanos , Dados de Sequência Molecular , Filogenia , Estrutura Terciária de Proteína , Proteínas Recombinantes/biossíntese , Proteínas Recombinantes/química , Proteínas Recombinantes/isolamento & purificação , Alinhamento de Sequência
10.
Artigo em Inglês | MEDLINE | ID: mdl-26219579

RESUMO

Crustaceans overcome osmotic disturbances by regulating their intracellular concentration of ions and osmolytes. Glycine betaine (GB), an osmolyte accumulated in response to hyperosmotic stress, is synthesized by betaine aldehyde dehydrogenase (BADH EC 1.2.1.8) through the oxidation of betaine aldehyde. A partial BADH cDNA sequence from the white shrimp Litopenaeus vannamei was obtained and its organ-specific expression during osmotic stress (low and high salinity) was evaluated. The partial BADH cDNA sequence (LvBADH) is 1103bp long and encodes an open reading frame for 217 protein residues. The amino acid sequence of LvBADH is related to that of other BADHs, TMABA-DH and ALDH9 from invertebrate and vertebrate homologues, and includes the essential domains of their function and regulation. LvBADH activity and mRNA expression were detected in the gills, hepatopancreas and muscle with the highest levels in the hepatopancreas. LvBADH mRNA expression increased 2-3-fold in the hepatopancreas and gills after 7days of osmotic variation (25 and 40ppt). In contrast, LvBADH mRNA expression in muscle decreased 4-fold and 15-fold after 7days at low and high salinity, respectively. The results indicate that LvBADH is ubiquitously expressed, but its levels are organ-specific and regulated by osmotic stress, and that LvBADH is involved in the cellular response of crustaceans to variations in environmental salinity.


Assuntos
Betaína-Aldeído Desidrogenase/genética , Betaína-Aldeído Desidrogenase/metabolismo , Decápodes/genética , Sequência de Aminoácidos , Animais , Sequência de Bases , Betaína-Aldeído Desidrogenase/química , DNA Complementar/química , DNA Complementar/genética , Decápodes/enzimologia , Decápodes/metabolismo , Dados de Sequência Molecular , Especificidade de Órgãos , Pressão Osmótica , RNA Mensageiro/metabolismo
11.
Chem Biol Interact ; 191(1-3): 159-64, 2011 May 30.
Artigo em Inglês | MEDLINE | ID: mdl-21296058

RESUMO

Concentrated urine formation in the kidney is accompanied by conditions that favor the accumulation of reactive oxygen species (ROS). Under hyperosmotic conditions, medulla cells accumulate glycine betaine, which is an osmolyte synthesized by betaine aldehyde dehydrogenase (BADH, EC 1.2.1.8). All BADHs identified to date have a highly reactive cysteine residue at the active site, and this cysteine is susceptible to oxidation by hydrogen peroxide. Porcine kidney BADH incubated with H(2)O(2) (0-500 µM) lost 25% of its activity. However, pkBADH inactivation by hydrogen peroxide was limited, even after 120 min of incubation. The presence of coenzyme NAD(+) (10-50 µM) increased the extent of inactivation (60%) at 120 min of reaction, but the ligands betaine aldehyde (50 and 500 µM) and glycine betaine (100 mM) did not change the rate or extent of inactivation as compared to the reaction without ligand. 2-Mercaptoethanol and dithiothreitol, but not reduced glutathione, were able to restore enzyme activity. Mass spectrometry analysis of hydrogen peroxide inactivated BADH revealed oxidation of M278, M243, M241 and H335 in the absence and oxidation of M94, M327 and M278 in the presence of NAD(+). Molecular modeling of BADH revealed that the oxidized methionine and histidine residues are near the NAD(+) binding site. In the presence of the coenzyme, these oxidized residues are proximal to the betaine aldehyde binding site. None of the oxidized amino acid residues participates directly in catalysis. We suggest that pkBADH inactivation by hydrogen peroxide occurs via disulfide bond formation between vicinal catalytic cysteines (C288 and C289).


Assuntos
Betaína-Aldeído Desidrogenase/metabolismo , Peróxido de Hidrogênio/farmacologia , Rim/enzimologia , Animais , Betaína-Aldeído Desidrogenase/química , Ativação Enzimática/efeitos dos fármacos , Reativadores Enzimáticos/farmacologia , Estabilidade Enzimática/efeitos dos fármacos , Cinética , Ligantes , Modelos Moleculares , Conformação Proteica , Suínos
12.
P R Health Sci J ; 29(3): 305-11, 2010 Sep.
Artigo em Inglês | MEDLINE | ID: mdl-20799520

RESUMO

Diagnosing cancer using microarray analysis to study differential gene expression has been a recent focus of intense research Although several very sophisticated analysis tools have been developed with this aim in mind, it still remains a challenge to keep these methods free of parametric adjustments as well as maintain their transparency for the final user. Nonparametric methods in general have been associated with these last two characteristics, thus becoming attractive tools for microarray analysis in cancer research. In particular, diagnosing cancer via microarray analysis is an exercise whereby tissue is characterized according to its differential gene expression levels. In this manuscript, two novel nonparametric methods for cancer diagnosis using microarray data are described and their performance assessed against a baseline approach that utilizes the Mann-Whitney test for median differences. Both methods show promising results in terms of their potential use in making diagnoses.


Assuntos
Neoplasias/diagnóstico , Humanos , Análise em Microsséries/métodos , Análise em Microsséries/estatística & dados numéricos , Neoplasias/genética , Estatísticas não Paramétricas
13.
Rev. cienc. med. Pinar Rio ; 13(2): 255-261, abr.-jun. 2009.
Artigo em Espanhol | LILACS | ID: lil-739306

RESUMO

Antecedentes. Esta rara hamartomatosis melanocítica de la piel y leptomeninges fue descrita por Vichow en 1859 y nombrada como Melanosis Neurocutanea por Von Bogaert en 1948. Puede reconocerse clínicamente por la presencia en la piel de nevus pigmentados de color oscuro, gruesos y pilosos, repartidos en forma "de Baño de asiento" (hipogastrio, nalgas y parte superior de los muslos) con manifestaciones neurológicas expresadas por hidrocefalia, convulsiones y retraso mental. Existe elevado riesgo de malignización de los nevus. La mayoría de los casos son esporádicos, aunque se ha sugerido un patrón de herencia autosómico dominante con expresividad variable (MIM: 249400). Presentación de caso. Paciente femenina de 6 meses de edad, producto de cuarta gestación, a término, normopeso, padres jóvenes no consanguíneos e historia familiar negativo de defecto congénitos. En la exploración física se comprobaron múltiples nevus pigmentados con al distribución y característica de una Melanosis Neurocutánea; a partir de los dos meses se comprobaron fontanela anterior tensa y rápido crecimiento del perímetro cefálico confirmado por TAC una hidrocefalia obstructiva con marcada dilatación de III y IV ventrículo motivo por el cual le fue realizada por Neurocirugía una derivación de LCR ventrículo-peritoneal. Evoluciona con un marcado retraso en el desarrollo psicomotor. Fallece a la edad de 13 meses. Conclusión. Melanosis Neurocutánea asociada a Hidrocefalia obstructiva por Melanosis difusa del S.N.C.


Background: This rare melonocytic hamartoma of the skin and leptomeninges was first described by Vichow in 1859 and named Neurocutaneous Melanosis by Von Bogaert in 1948. Clinically, it is recognised due to the presence in the skin of dark pigmented, thick and pilose nevi spread like a "seat bath" (hypogastric region, buttocks, the upper part of the thighs), having neurological disorders which are expressed by hydrocephaly, seizures and mental retardation. The risk of malignancy in the nevi is observed. The majority of the cases are sporadic, though a pattern of autosomal dominant heredity with a variable expression (MIM: 249400) is suggested. Case Report: A six-months female patient, born from the fourth pregnancy, in term, normal weight and having young no consanguineous parents and a negative familial history of genetic defects was treated in the neurosurgical consultation. In the physical examination multiple pigmented nevi were observed with a distribution and features which matched with a Neurocutaneous Melanosis; starting from the two months of age, the anterior fontanel was tense and a sudden growing of the cephalic perimeter was observed; confirming with CAT-scan an obstructive hydrocephaly which showed a marked dilatation of the 3rd and 4th ventricles of the brain; this was the reason, to perform by means of a neurosurgery a CSF ventriculoperitoneal shunt. A marked retardation of the psychomotor development was observed, dying at 13 months of age. Conclusion: Neurocutaneous Melanosis associated with an Obstructive Hydrocephaly due to a Diffuse Melanosis of the Central Nervous System (CNS).

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