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1.
Rev. venez. oncol ; 25(2): 109-112, abr.-jun. 2013.
Article in Spanish | LILACS | ID: lil-718944

ABSTRACT

La patología tumoral de las glándulas salivares representa el grupo más heterogéneo y complejo de los procesos tumorales de cabeza y cuello. Su prevalencia en la literatura mundial es descrita en un 5% de todas las neoplasias de cabeza y cuello. El tumor de glándula parótida es el más frecuente presentándose en un 75% de los tumores de glándula salivares. Su evolución es asintomática, descrito en la sexta década de la vida, manifestándose con aumento de volumen de la zona, siendo más frecuentes los tumores benignos. Se realiza estudio retrospectivo y descriptivo en base a historia clínica. La población correspondió a 6 individuos, 66,66% al sexo masculino y un 33,33% al femenino. El tumor se localizó en un 83,3% a nivel de la glándula parótida derecha. El resultado anatomopatológico concluyó en un 50% de frecuencia para adenoma pleomórfico, Un 33,3% para quiste benigno y un 16,6% para linfoma no Hodgkin. Fueron encontrados 6 casos compatibles con el diagnóstico clínico y anatomopatológico de tumor de glándula parótida con predisposición en el sexo masculino y pacientes menores de 40 años. Las técnicas quirúrgicas empleadas para la resección del tumor fueron la parotidectomía total y subtotal. Los hallazgos anatomopatológicos correspondieron en un 50% para el adenoma pleomórfico, 33,3% para el quiste benigno. Presentándose en un porcentaje elevado en relación a la literatura el linfoma no Hodgkin con 16,6%.


The tumor like pathology of the salivary glands represents the most heterogeneous and complex group of the tumor like processes of head and neck. Its prevalence in worldwide literature is described in a 5% of all the tumors of head and neck. The tumor of parotid gland is most frequent appearing in a 75% of the salivary gland tumors. Its evolution is asymptomatic, described in the sixth decade of the life, pronouncing itself with increase of volume of the zone, being more frequent the benign tumors. Retrospective and descriptive studyon the basis of clinical history is realized. The population corresponded to 6 individuals, 66.66% to male sex and 33.33% to female. The tumor located in 83.3% concerning the right parotid gland. The anatomical pathology result conclude in a 50% of frequency for pleomorphic adenoma, a 33.3% for benign cyst and 16.6% for lymphoma non Hodgkin. We was found 6 compatible cases with the clinical diagnosis and anatomical pathology of tumor of gland parotid with predisposition in masculine sex and patient minors of 40 years the used surgical techniques for the resection of the tumor were parotidectomy total and subtotal. The ended results of the biopsy findings corresponded in a 50% for the pleomorphic adenoma, 33.3% for the benign cyst. Appearing in a percentage lifted in relation to literature lymphoma non Hodgkin with a 16.6%.


Subject(s)
Humans , Male , Female , Adult , Middle Aged , Parotid Gland/abnormalities , Parotid Gland/surgery , Salivary Glands/abnormalities , Salivary Glands/surgery , Head and Neck Neoplasms/diagnosis , Head and Neck Neoplasms/therapy , Lymphoma , Medical Oncology
2.
J Mol Med (Berl) ; 88(1): 61-74, 2010 Jan.
Article in English | MEDLINE | ID: mdl-19768630

ABSTRACT

The Plasmodium falciparum P0 ribosomal phosphoprotein (PfP0) was identified for the first time by screening a cDNA expression library of P. falciparum parasites with sera from malaria-immune individuals. Due to its localization on the surface of different parasite life-cycle stages (merozoites and gametocytes) and its recognition by invasion-blocking antibodies, PfP0 has been considered a potential malaria-vaccine component. In this study, 16 20-mer-long synthetic peptides spanning the entire PfP0 sequence were evaluated by means of receptor-ligand assays with human red blood cells (RBCs) in order to determine the role played by these peptides in the invasion process. Four RBC high-activity binding peptides (HABPs), located mostly toward the N-terminal region, were identified: HABP 33898 ((1)MAKLSKQQKKQMYIEKLSSL(20)), HABP 33900 ((41)ASVRKSLRGKATILMGKNTRY(60)), HABP 33901 ((61)IRTALKKNLQAVPQIEKLLPY (80)), and HABP 33906 ((161)LIKQGEKVTASSATLLRKFNY(180)). The binding pattern of HABPs 33898 and 33906 to enzyme-treated RBCs suggests receptors of protein nature for these two HABPs, one of which could correspond to a common 58-kDa RBC membrane protein, as indicated by results of cross-linking assays. Both HABPs exhibited high content of alpha-helical features and prevented P. falciparum merozoite invasion to RBCs in vitro by up to 91%. The invasion-blocking ability reported here for these PfP0 HABPs supports their inclusion in immunological studies with the aim of assessing their potential as candidates for a vaccine against P. falciparum malaria.


Subject(s)
Erythrocytes/metabolism , Plasmodium falciparum/metabolism , Protozoan Proteins/chemistry , Protozoan Proteins/metabolism , Ribosomal Proteins/chemistry , Ribosomal Proteins/metabolism , Amino Acid Sequence , Humans , Molecular Sequence Data , Plasmodium falciparum/chemistry , Protein Binding
3.
Vaccine ; 27(49): 6877-86, 2009 Nov 16.
Article in English | MEDLINE | ID: mdl-19755146

ABSTRACT

Severe malaria pathology is directly associated with cytoadherence of infected red blood cells (iRBCs) to healthy RBCs and/or endothelial cells occurring during the intraerythrocytic development of Plasmodium falciparum. We synthesized, as 20-mer long peptides, the members of the ring exported (REX) protein family encoded in chromosome 9, as well as the early transcribed membrane proteins (E-TRAMP) 10.2 and 4, to identify specific RBC binding regions in these proteins. Twelve binding peptides were identified (designated as HABPs): three were identified in REX1, two in REX2, one in REX3, two in REX4 and four in E-TRAMP 10.2. The majority of these HABPs was conserved among different P. falciparum strains, according to sequence analysis. No HABPs were found in E-TRAMP 4. Bindings of HABPs were saturable and sensitive to the enzymatic treatment of RBCs and HABPs had different structural features, according to circular dichroism studies. Our results suggest that the REX and E-TRAMP families participate in relevant interactions with RBC membrane proteins, which highlight these proteins as potential targets for the development of fully effective immunoprophylactic methods.


Subject(s)
Erythrocytes/immunology , Peptides/immunology , Plasmodium falciparum/immunology , Protozoan Proteins/immunology , Amino Acid Sequence , DNA, Protozoan/genetics , Erythrocyte Membrane/immunology , Erythrocyte Membrane/metabolism , Erythrocytes/metabolism , Humans , Malaria Vaccines/immunology , Molecular Sequence Data , Peptides/chemistry , Plasmodium falciparum/genetics , Polymorphism, Genetic , Protein Binding , Protozoan Proteins/chemistry , Sensitivity and Specificity
4.
NOVA publ. cient ; 4(5): 14-26, jun. 2006. ilus, tab, graf
Article in Spanish | LILACS | ID: lil-474710

ABSTRACT

La única vacuna disponible contra la tuberculosis es la cepa Mycobacterium bovis BCG, que ofrece una eficacia protectiva variable (0/100-80/100), siendo urgente un nuevo agente profiláctico. Se han evaluado diversos candidatos a vacuna contra este patógeno, en los modelos animales de experimentación convencionales (murino, cobayo, conejo), obteniéndose información básica sobre el efecto de la vacuna en la carga bacterial frente a un reto infeccioso, así como también la reducción o prevención de la patología en los pulmones u otros órganos blanco; además de los aspectos relacionados con la respuesta inmune hacia el Mycobacterium tuberculosis. Los primates no humanos tienen ventajas sobre los modelos convencionales en la evaluación de vacunas, de hecho se ha verificado el comportamiento de agentes terapéuticos en humanos después de haber sido medida la capacidad protectiva de éstos en monos con tuberculosis inducida. Los primates mas estudiados en la infección por micobacterias son el cynomulgus, y el rhesus, observándose que estos animales mantienen la infección en un estado subclínico, muy similar a la tuberculosis humana donde el 90/100 de la población infectada mantiene la infección en un estado latente. Dado que el modelo animal debe semejar el comportamiento de las proteínas estudiadas en el ser humano, el mono Aotus puede representar ventajas en la investigación de tuberculosis por ser un primate con aproximadamente un 90/100 de similitud al humano en cuanto a las moléculas del sistema inmune estudiadas hasta hoy. La proteína ESAT-6 de (early secretory antigenic target 6 kD) de Mycobacterium tuberculosis es un componente minoritario del filtrado de cultivo de corto tiempo (CFP), ha sido genética y químicamente caracterizada e induce una potente respuestainmunogénica del tipo TH1. Este antígeno es secretado durante la fase inicial de crecimiento siendo fuertementereconocido por animales y humanos infectados por Mycobacterium tuberculosis...


Subject(s)
Mycobacterium tuberculosis , Tuberculosis , Vaccines
5.
Biol Chem ; 386(4): 361-7, 2005 Apr.
Article in English | MEDLINE | ID: mdl-15899698

ABSTRACT

Plasmodium falciparum histoaspartic protease (HAP) is an active enzyme involved in haemoglobin degradation. HAP is expressed as an inactive 51-kDa zymogen and is cleaved into an active 37-kDa enzyme. It has been proposed that this kind of protease might be implicated in the parasite's invasion of erythrocytes; however, this protein's role during invasion has still to be determined. Synthetic peptides derived from the HAP precursor (proHAP) were tested in erythrocyte binding assays to identify their possible function in the invasion process. Two proHAP high-activity binding peptides (HABPs) specifically bound to erythrocytes; these peptides were numbered 30609 (101LKNYIKESVKLFNKGLTKKS120) and 30610 (121YLGSEFDNVELKDLANVLSF140 ). The binding of these two peptides was saturable, presenting nanomolar affinity constants. These peptides interacted with 26- and 45-kDa proteins on the erythrocyte surface; the nature of these receptor sites was studied in peptide binding assays using enzyme-treated erythrocytes. The HABPs showed greater than 90% merozoite invasion inhibition in in vitro assays. Goat serum containing proHAP polymeric peptide antibodies inhibited parasite invasion in vitro .


Subject(s)
Aspartic Acid Endopeptidases/blood , Erythrocytes/enzymology , Peptide Fragments/metabolism , Plasmodium falciparum/enzymology , Amino Acid Sequence , Animals , Humans , Molecular Sequence Data , Molecular Weight , Plasmodium falciparum/pathogenicity , Protein Binding/physiology
6.
Peptides ; 24(7): 999-1006, 2003 Jul.
Article in English | MEDLINE | ID: mdl-14499278

ABSTRACT

Erythrocyte high activity binding peptides (HABPs) have been identified for the Plasmodium falciparum serine repeat antigen (SERA). HABP 6746, located in this protein's 50 kDa fragment had its critical binding residues replaced by amino acids having similar mass but different charge to change their immunologic properties. This peptide analogues were used to immunize Aotus monkeys that were challenged later on with a virulent P. falciparum strain to determine their protective efficacy. A shortening in alpha helix structure was found in the immunogenic and protective ones when their secondary structure was analyzed by NMR, to correlate their structure with their immunologic properties. These data, together with results from previous studies, suggest that this shortening in HABP helical configuration may lead to better fitting with immune system molecules, rendering them immunogenic and protective and therefore making them excellent candidates for consideration as components of a subunit based multicomponent synthetic vaccine against malaria.


Subject(s)
Antigens, Protozoan/immunology , Malaria Vaccines/immunology , Malaria, Falciparum/immunology , Vaccines, Subunit/immunology , Amino Acid Sequence , Animals , Antigens/immunology , Antigens, Protozoan/chemistry , Aotidae , Blotting, Western , Chromatography, High Pressure Liquid , Fluorescent Antibody Technique, Indirect , Magnetic Resonance Spectroscopy , Malaria Vaccines/chemistry , Malaria Vaccines/pharmacology , Models, Molecular , Molecular Sequence Data , Molecular Weight , Plasmodium falciparum/immunology , Polymers/chemistry , Polymers/pharmacology , Protein Structure, Secondary , Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization , Structure-Activity Relationship , Vaccination , Vaccines, Subunit/chemistry , Vaccines, Subunit/pharmacology , Vaccines, Synthetic/chemistry , Vaccines, Synthetic/immunology , Vaccines, Synthetic/pharmacology
7.
Biochem Biophys Res Commun ; 307(1): 148-56, 2003 Jul 18.
Article in English | MEDLINE | ID: mdl-12849994

ABSTRACT

Peptide 1585 (EVLYLKPLAGVYRSLKKQLE) has a highly conserved amino-acid sequence located in the Plasmodium falciparum main merozoite surface protein (MSP-1) C-terminal region, required for merozoite entry into human erythrocytes and therefore represents a vaccine candidate for P. falciparum malaria. Original sequence-specific binding to five HLA DRB1* alleles (0101, 0102, 0401, 0701, and 1101) revealed this peptide's specific HLA DRB1*0102 allele binding. This peptide's allele-specific binding to HLA DRB1*0102 took on broader specificity for the DRB1*0101, -0401, and -1101 alleles when lysine was replaced by glycine in position 17 (peptide 5198: EVLYLKPLAGVYRSLKG(17)QLE). Binding of the identified G(10)VYRSLKGQLE(20) C-terminal register to these alleles suggests that peptide promiscuous binding relied on fitting Y(12), L(15), and G(17) into P-1, P-4, and P-6, respectively. The implications of the findings and the future of this synthetic vaccine candidate are discussed.


Subject(s)
Alleles , Glycine/metabolism , Major Histocompatibility Complex/genetics , Merozoite Surface Protein 1/genetics , Peptides/metabolism , Plasmodium falciparum/metabolism , Amino Acid Sequence , Animals , HLA-DR Antigens/genetics , HLA-DR Antigens/immunology , HLA-DR Antigens/metabolism , HLA-DRB1 Chains , Humans , Major Histocompatibility Complex/physiology , Malaria Vaccines , Merozoite Surface Protein 1/metabolism , Molecular Sequence Data , Peptides/genetics , Peptides/immunology , Plasmodium falciparum/immunology , Protein Binding
8.
FEBS Lett ; 527(1-3): 95-100, 2002 Sep 11.
Article in English | MEDLINE | ID: mdl-12220641

ABSTRACT

One Plasmodium falciparum malaria antigen is an integral membrane protein called apical membrane antigen-1. High activity binding peptides to human red blood cells have been identified in this protein. 4337 is a conserved, non-immunogenic peptide with high activity red blood cell binding and its critical residues have already been identified. Peptide analogues (with amino acids having the same mass but different charge) were generated to change their immunogenic and protective characteristics. Three analogues having positive or negative immunological results were studied by nuclear magnetic resonance. The studied peptides all had an alpha-helix fragment, but in different peptide regions and extensions, except for randomly structured 4337. We show that altering a few amino acids induced immunogenicity and protectivity against experimental malaria and changed their three-dimensional structure, suggesting a better fit with immune system molecules and that modified peptides having better immunological properties can be included in the design of new malaria multi-component subunit-based vaccine.


Subject(s)
Antigens, Protozoan , Malaria, Falciparum/immunology , Membrane Proteins/chemistry , Membrane Proteins/immunology , Peptides/chemistry , Peptides/immunology , Protozoan Proteins/chemistry , Protozoan Proteins/immunology , Amino Acid Sequence , Animals , Haplorhini , Magnetic Resonance Spectroscopy , Malaria Vaccines/chemistry , Malaria Vaccines/pharmacology , Malaria, Falciparum/prevention & control , Membrane Proteins/pharmacology , Molecular Sequence Data , Peptides/pharmacology , Protein Conformation , Protozoan Proteins/pharmacology , Structure-Activity Relationship
9.
Vaccine ; 20(9-10): 1331-9, 2002 Jan 31.
Article in English | MEDLINE | ID: mdl-11818151

ABSTRACT

Plasmodium vivax merozoites have high preferential ability to interact with and invade reticulocytes, although these cells correspond to only 2% of the red blood cells (RBC) population. P. vivax merozoite surface protein-1 (Pv-MSP-1) is believed to have an important role in attachment and invasion process. Using 88 non-overlapping 20-mer peptides, covering the entire Pv-MSP-1 Belem strain sequence, RBC and reticulocyte binding assays were performed. Fourteen sequences were identified with high specific binding activity to reticulocytes, but only three had high specific binding activity to mature erythrocytes. These peptides showed affinity constant values between 20 and 150nM, indicating a strong interaction between these sequences and reticulocyte receptors. Critical residues in binding to reticulocytes for these peptides were determined by competition binding assays with glycine scanning analogues. All high binding peptides bind to reticulocyte surface proteins having a molecular mass of around 18-20kDa which are not present in mature RBC. Interestingly, some high activity binding peptides (HABPs) are located close to the hypothesised 42 and 19kDa fragment cleavage sites for this protein, suggesting that these sequences have an important role in target cell attachment and invasion process by Pv-MSP-1.HABPs may be clustered in two regions, with region I being located between amino acids 280-719, and region II between amino acids 1060-1599 with higher than 25% identity level. A P. falciparum MSP-1 antigenic domain binds to RBCs and inhibits parasite invasion. Peptides 1721 and 1724 bind with high activity to reticulocytes in homologous Pv-MSP-1, suggesting similar functions for these two sequences.


Subject(s)
Merozoite Surface Protein 1/metabolism , Plasmodium vivax/immunology , Reticulocytes/metabolism , Amino Acid Sequence , Animals , Binding Sites , Carrier Proteins/metabolism , Humans , Merozoite Surface Protein 1/chemistry , Molecular Sequence Data
10.
Rev. ABO nac ; 6(1): 14-6, fev.-mar. 1998. ilus
Article in Portuguese | LILACS, BBO - Dentistry | ID: biblio-872234

ABSTRACT

Duas cabeças pensam melhor do que uma. Ortodontistas já pedem avaliação fonoaudiológica de seus pacientes antes de iniciar o tratamento. Distúrbios afetam o aprendizado na infância e trazem problemas de saúde também aos adultos


Subject(s)
Child , Adult , Orthodontics , Speech Therapy
11.
Med. UIS ; 8(1): 2-5, ene.-mar. 1994. tab
Article in Spanish | LILACS | ID: lil-232149

ABSTRACT

Con la técnica de Kinyoun para Cryptosporodium se estudiaron 1988 muestras de materia fecal llevadas para estudio a diez laboratorios del área metropolitana de Bucaramanga, Colombia. Correspondían a 103 lactantes, 113 preescolares, 201 escolares, 1162 adultos jóvenes, 322 adultos mayores y 87 ancianos; 55.48 por ciento eran mujeres y el 97.94 por ciento vivían en zona urbana. Un 13.93 por ciento pertenecían a personas con diarrea. Se encontraron tres muestras positivas, todas en menores de dos años y con diarrea: 2.91 por ciento de los lactantes y el 4.69 por cientode los lactantes con diarrea. Con esto se confirma la presencia del parásito en el Nororiente colombiano, con una prevalencia similar a la encontrada en otras partes del país


Subject(s)
Humans , Cryptosporidiosis/diagnosis , Cryptosporidiosis/drug therapy , Cryptosporidiosis/pathology , Cryptosporidiosis/physiopathology , Cryptosporidiosis/prevention & control
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