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1.
Food Chem ; 308: 125601, 2020 Mar 05.
Artigo em Inglês | MEDLINE | ID: mdl-31670190

RESUMO

The aim of this work was to analyse the hypotensive effect of amaranth protein/peptides on spontaneously hypertensive rats (SHR). The mechanism of action of these peptides was studied in vivo and ex vivo. We also tested the effect of protection against gastrointestinal digestion (GID) exerted by an O:W emulsion on the integrity of the antihypertensive peptides. All samples tested produced a decrease in blood pressure (SBP). The animals treated with emulsion (GE) and emulsion + peptide (GE+VIKP) showed the most significant reduction in the SBP (42 ±â€¯2 mmHg and 35 ±â€¯2 mmHg, respectively). The results presented suggest that after GID, a variety of peptides with biological activities were released or were resistant to this process. These peptides play a role in the regulation of the SBP by acting on plasma ACE, plasma renin and the vascular system. These results support the use of amaranth protein/peptides in the elaboration of functional foods for hypertensive individuals.


Assuntos
Amaranthus/química , Anti-Hipertensivos/farmacologia , Hipertensão/tratamento farmacológico , Peptídeos/farmacologia , Sistema Renina-Angiotensina/efeitos dos fármacos , Animais , Anti-Hipertensivos/uso terapêutico , Pressão Sanguínea/efeitos dos fármacos , Masculino , Peptídeos/uso terapêutico , Proteínas de Plantas/farmacologia , Proteínas de Plantas/uso terapêutico , Ratos , Ratos Endogâmicos SHR
2.
Plant Foods Hum Nutr ; 74(3): 405-413, 2019 Sep.
Artigo em Inglês | MEDLINE | ID: mdl-31273642

RESUMO

The aim of this work was to evaluate the ability of broken rice, an underutilized industrial by-product, as a potential functional and health promoting ingredient. With this purpose, the ability to inhibit the angiotensin converting enzyme and renin of a rice protein hydrolyzate (RPH) obtained from a high-protein variety of broken rice (var. Nutriar FCAyF) was analyzed (IC50 = 0.87 and 2.7 mg/mL, respectively). RPH was separated by gel permeation chromatography and in a second purification step by RP-HPLC. The sequence of antihypertensive peptides presented in two RP-HPLC fractions was analyzed. Peptides capable of interacting with the active sites of both enzymes were identified. In this study, we demonstrate that the hydrolysis treatment improves functional and biological properties of rice proteins. Protein preparations obtained from a by-product of rice industry, such as broken rice, are a promising ingredient with potentially good biological properties.


Assuntos
Inibidores da Enzima Conversora de Angiotensina/farmacologia , Anti-Hipertensivos/isolamento & purificação , Oryza/química , Peptídeos/isolamento & purificação , Renina/antagonistas & inibidores , Anti-Hipertensivos/farmacologia , Cromatografia Líquida de Alta Pressão , Promoção da Saúde , Hidrólise , Simulação de Acoplamento Molecular , Peptídeos/farmacologia , Peptidil Dipeptidase A/metabolismo , Proteínas de Plantas/antagonistas & inibidores , Proteínas de Plantas/metabolismo , Renina/metabolismo
3.
Glia ; 66(1): 47-61, 2018 01.
Artigo em Inglês | MEDLINE | ID: mdl-28795439

RESUMO

We show that the G protein-coupled receptor GPR37-like 1 (GPR37L1) is expressed in most astrocytes and some oligodendrocyte precursors in the mouse central nervous system. This contrasts with GPR37, which is mainly in mature oligodendrocytes. Comparison of wild type and Gpr37l1-/- mice showed that loss of GPR37L1 did not affect the input resistance or resting potential of astrocytes or neurons in the hippocampus. However, GPR37L1-mediated signalling inhibited astrocyte glutamate transporters and - surprisingly, given its lack of expression in neurons - reduced neuronal NMDA receptor (NMDAR) activity during prolonged activation of the receptors as occurs in ischemia. This effect on NMDAR signalling was not mediated by a change in the release of D-serine or TNF-α, two astrocyte-derived agents known to modulate NMDAR function. After middle cerebral artery occlusion, Gpr37l1 expression was increased around the lesion. Neuronal death was increased by ∼40% in Gpr37l1-/- brain compared to wild type in an in vitro model of ischemia. Thus, GPR37L1 protects neurons during ischemia, presumably by modulating extracellular glutamate concentration and NMDAR activation.


Assuntos
Sistema X-AG de Transporte de Aminoácidos/metabolismo , Astrócitos/metabolismo , Infarto da Artéria Cerebral Média/terapia , Neurônios/metabolismo , Receptores Acoplados a Proteínas-G/metabolismo , Receptores de N-Metil-D-Aspartato/metabolismo , Potenciais de Ação/genética , Animais , Animais Recém-Nascidos , Ácido Aspártico/farmacologia , Astrócitos/efeitos dos fármacos , Encéfalo/patologia , Modelos Animais de Doenças , Comportamento Exploratório/fisiologia , Regulação da Expressão Gênica no Desenvolvimento/genética , Hipocampo/citologia , Infarto da Artéria Cerebral Média/patologia , Infarto da Artéria Cerebral Média/fisiopatologia , Camundongos , Camundongos Endogâmicos C57BL , Camundongos Transgênicos , Mutação/genética , N-Metilaspartato/farmacologia , Neurônios/fisiologia , Receptores Acoplados a Proteínas-G/genética , /fisiologia
4.
J Agric Food Chem ; 65(34): 7415-7423, 2017 Aug 30.
Artigo em Inglês | MEDLINE | ID: mdl-28805378

RESUMO

Among the factors affecting the development of cardiovascular diseases, hypertension is one of the most important. Research done on amaranth proteins has demonstrated their hypotensive capacity in vivo and in vitro; nevertheless, the mechanism underlying this effect remains unclear. The aim of this study was to analyze in vitro the inhibition of peptides derived from an amaranth hydrolysate (AHH) on other RAS enzymes other than ACE. The chymase and renin activities were studied. AHH was not able to inhibit chymase activity, although a dose-response effect was found on renin activity (IC50 0.6 mg/mL). To provide an approach to the renin inhibition mechanism, we analyzed AHH renin inhibition kinetics and performed a structural characterization of the peptides involved in the effect in terms of molecular size and hydrophobicity. Results suggest that amaranth peptides exhibit renin competitive inhibition behavior. Renin inhibition potency was directly related to peptide hydrophobicity. RP-HPLC separation of AHH and subsequent analysis of the peptide sequences showed 6 peptides belonging to 11S globulin (that can be grouped into 3 families) that would be responsible for renin inhibition. These results demonstrate that Amaranthus hypochondriacus seeds are an adequate source of peptides with renin inhibitory properties that could be used in functional food formulations.


Assuntos
Amaranthus/química , Inibidores da Enzima Conversora de Angiotensina/química , Anti-Hipertensivos/química , Peptídeos/química , Proteínas de Plantas/química , Sistema Renina-Angiotensina/efeitos dos fármacos , Amaranthus/genética , Sequência de Aminoácidos , Inibidores da Enzima Conversora de Angiotensina/farmacologia , Anti-Hipertensivos/farmacologia , Humanos , Cinética , Peptídeos/genética , Peptídeos/farmacologia , Proteínas de Plantas/genética , Proteínas de Plantas/farmacologia
5.
Proteomics ; 17(15-16)2017 Aug.
Artigo em Inglês | MEDLINE | ID: mdl-28643898

RESUMO

Exposure to cow's milk constitutes one of the most common causes of food allergy. In addition, exposure to soy proteins has become relevant in a restricted proportion of milk allergic pediatric patients treated with soy formulae as a dairy substitute, because of the cross-allergenicity described between soy and milk proteins. We have previously identified several cross-reactive allergens between milk and soy that may explain this intolerance. The purpose of the present work was to identify epitopes in the purified αS1-casein and the recombinant soy allergen Gly m 5.0101 (Gly m 5) using an α-casein-specific monoclonal antibody (1D5 mAb) through two different approaches for epitope mapping, to understand cross-reactivity between milk and soy. The 1D5 mAb was immobilized onto magnetic beads, incubated with the peptide mixture previously obtained by enzymatic digestion of the allergens, and the captured peptides were identified by MALDI-TOF MS analysis. On a second approach, the peptide mixture was resolved by RP-HPLC and immunodominant peptides were identified by dot blot with the mAb. Finally, recognized peptides were sequenced by MALDI-TOF MS. This novel MS based approach led us to identify and characterize four peptides on α-casein and three peptides on Gly m 5 with a common core motif. Information obtained from these cross-reactive epitopes allows us to gain valuable insight into the molecular mechanisms of cross-reactivity, to further develop new and more effective vaccines for food allergy.


Assuntos
Alérgenos/imunologia , Reações Cruzadas , Mapeamento de Epitopos/métodos , Epitopos de Linfócito B/imunologia , Leite/química , Soja/química , Espectrometria de Massas por Ionização e Dessorção a Laser Assistida por Matriz/métodos , Sequência de Aminoácidos , Animais , Caseínas/análise , Bovinos , Epitopos de Linfócito B/análise , Feminino , Humanos , Lactente , Proteínas do Leite/análise , Proteínas do Leite/imunologia , Fragmentos de Peptídeos/análise , Fragmentos de Peptídeos/imunologia , Proteínas de Soja/análise
6.
Comp Immunol Microbiol Infect Dis ; 50: 110-115, 2017 Feb.
Artigo em Inglês | MEDLINE | ID: mdl-28131371

RESUMO

Swine farms provide a dynamic environment for the evolution of influenza A viruses (IAVs). The present report shows the results of a surveillance effort of IAV infection in one commercial swine farm in Argentina. Two cross-sectional serological and virological studies (n=480) were carried out in 2011 and 2012. Virus shedding was detected in nasal samples from pigs from ages 7, 21 and 42-days old. More than 90% of sows and gilts but less than 40% of 21-days old piglets had antibodies against IAV. In addition, IAV was detected in 8/17 nasal swabs and 10/15 lung samples taken from necropsied pigs. A subset of these samples was further processed for virus isolation resulting in 6 viruses of the H1N2 subtype (δ2 cluster). Pathological studies revealed an association between suppurative bronchopneumonia and necrotizing bronchiolitis with IAV positive samples. Statistical analyses showed that the degree of lesions in bronchi, bronchiole, and alveoli was higher in lungs positive to IAV. The results of this study depict the relevance of continuing long-term active surveillance of IAV in swine populations to establish IAV evolution relevant to swine and humans.


Assuntos
Broncopneumonia/veterinária , Monitoramento Epidemiológico , Vírus da Influenza A Subtipo H1N1 , Infecções por Orthomyxoviridae/veterinária , Doenças dos Suínos/epidemiologia , Animais , Anticorpos Antivirais/sangue , Argentina/epidemiologia , Broncopneumonia/epidemiologia , Broncopneumonia/virologia , Estudos Transversais , Humanos , Vírus da Influenza A Subtipo H1N1/classificação , Vírus da Influenza A Subtipo H1N1/imunologia , Vírus da Influenza A Subtipo H1N1/isolamento & purificação , Vírus da Influenza A Subtipo H1N2/isolamento & purificação , Influenza Humana , Pulmão/patologia , Pulmão/virologia , Nariz/virologia , Infecções por Orthomyxoviridae/epidemiologia , Infecções por Orthomyxoviridae/fisiopatologia , Infecções por Orthomyxoviridae/virologia , Sus scrofa , Suínos , Doenças dos Suínos/virologia , Eliminação de Partículas Virais
7.
Dev Neurobiol ; 75(5): 522-38, 2015 May.
Artigo em Inglês | MEDLINE | ID: mdl-25363628

RESUMO

The basic organization of somatosensory circuits in the spinal cord is already setup during the initial patterning of the dorsal neural tube. Extrinsic signals, such as Wnt and TGF-ß pathways, activate combinatorial codes of transcription factors that are responsible for generating a pattern of discrete domains of dorsal progenitors (dp). These progenitors will give rise to distinct dorsal interneurons (dI). The Wnt/ ßcatenin signaling pathway controls specification of dp/dI1-3 progenitors and interneurons. According to the current model in the field, Wnt/ßcatenin activity seems to act in a graded fashion in the spinal cord, as different relative levels determine the identity of adjacent progenitors. However, it is not clear how this activity gradient is controlled and how the identities of dI1-3 are differentially regulated by Wnt signalling. We have determined that two SoxD transcription factors, Sox5 and Sox6, are expressed in restricted domains of dorsal progenitors in the neural tube. Using gain- and loss-of function approaches in chicken embryos, we have established that Sox5 controls cell fate specification of dp2 and dp3 progenitors and, as a result, controls the correct number of the corresponding dorsal interneurons (dI2 and dI3). Furthermore, Sox5 exerts its function by restricting dorsally Wnt signaling activity via direct transcriptional induction of the negative Wnt pathway regulator Axin2. By that way, Sox5 acts as a Wnt pathway modulator that contributes to sharpen the dorsal gradient of Wnt/ßcatenin activity to control the distinction of two functionally distinct types of interneurons, dI2 and dI3 involved in the somatosensory relay.


Assuntos
Proteínas Aviárias/metabolismo , Regulação da Expressão Gênica no Desenvolvimento/fisiologia , Interneurônios/citologia , Fatores de Transcrição SOXD/metabolismo , Medula Espinal/metabolismo , Células-Tronco/citologia , Animais , Proteínas Aviárias/genética , Diferenciação Celular/fisiologia , Embrião de Galinha , Galinhas , Fatores de Transcrição SOXD/genética , Transdução de Sinais/genética , Medula Espinal/embriologia , Proteínas Wnt/metabolismo
8.
J Sci Food Agric ; 92(2): 397-403, 2012 Jan 30.
Artigo em Inglês | MEDLINE | ID: mdl-21834100

RESUMO

BACKGROUND: Amaranth 7S globulin is a minor globulin component and its impact on the properties of an amaranth protein ingredient depends on its proportion in the variety of amaranth being considered. Some physicochemical, functional and angiotesin I-converting enzyme (ACE) inhibitory properties of amaranth vicilin were studied in this work and compared with the 11S globulin. RESULTS: Fluorescence spectroscopy results indicated that 7S globulin tryptophans were more exposed to the solvent and, by calorimetry, the 7S globulin denaturation temperature (T(d) ) was found lower than the 11S globulin T(d) , suggesting a more flexible structure. The 7S globulin surface hydrophobicity was higher than that of the 11S globulin, which is in agreement with the better emulsifying properties of the 7S globulin. The solubility in neutral buffer of the 7S globulin (851 ± 25 g kg(-1) ) was also higher than that of the 11S globulin (195 ± 6 g kg(-1) ). Bioinformatic analyses showed the presence of ACE inhibitory peptides encrypted in 7S tryptic sequences and peptides released after in vitro gastrointestinal digestion showed a high ACE-inhibitory capacity (IC(50) = 0.17 g L(-1) ), similar to that of 11S globulin peptides. CONCLUSION: Compared with the 11S globulin, the 7S globulin presents similar ACE inhibitory activity and some functional advantages, better solubility and emulsifying activity, which suits some food requirements. The functional behavior has been related with the structural properties.


Assuntos
Amaranthus/metabolismo , Inibidores da Enzima Conversora de Angiotensina/farmacologia , Globulinas/farmacologia , Proteínas de Plantas/farmacologia , Amaranthus/química , Amaranthus/genética , Inibidores da Enzima Conversora de Angiotensina/química , Regulação da Expressão Gênica de Plantas/fisiologia , Globulinas/genética , Globulinas/metabolismo , Interações Hidrofóbicas e Hidrofílicas , Proteínas de Plantas/química , Proteínas de Plantas/metabolismo , Espectrometria de Fluorescência
9.
J Cell Biol ; 194(3): 489-503, 2011 Aug 08.
Artigo em Inglês | MEDLINE | ID: mdl-21807879

RESUMO

Coordination between functionally related adjacent tissues is essential during development. For example, formation of trunk neural crest cells (NCCs) is highly influenced by the adjacent mesoderm, but the molecular mechanism involved is not well understood. As part of this mechanism, fibroblast growth factor (FGF) and retinoic acid (RA) mesodermal gradients control the onset of neurogenesis in the extending neural tube. In this paper, using gain- and loss-of-function experiments, we show that caudal FGF signaling prevents premature specification of NCCs and, consequently, premature epithelial-mesenchymal transition (EMT) to allow cell emigration. In contrast, rostrally generated RA promotes EMT of NCCs at somitic levels. Furthermore, we show that FGF and RA signaling control EMT in part through the modulation of elements of the bone morphogenetic protein and Wnt signaling pathways. These data establish a clear role for opposition of FGF and RA signaling in control of the timing of NCC EMT and emigration and, consequently, coordination of the development of the central and peripheral nervous system during vertebrate trunk elongation.


Assuntos
Transição Epitelial-Mesenquimal , Fatores de Crescimento de Fibroblastos/metabolismo , Crista Neural/citologia , Tretinoína/metabolismo , Animais , Proteínas Morfogenéticas Ósseas/metabolismo , Proteínas Morfogenéticas Ósseas/fisiologia , Ciclo Celular , Movimento Celular , Sistema Nervoso Central/embriologia , Embrião de Galinha , Eletroporação , Transição Epitelial-Mesenquimal/genética , Regulação da Expressão Gênica no Desenvolvimento , Sistema de Sinalização das MAP Quinases , Proteínas Quinases Ativadas por Mitógeno/metabolismo , Crista Neural/metabolismo , Crista Neural/fisiologia , Sistema Nervoso Periférico/embriologia , Reação em Cadeia da Polimerase , Transdução de Sinais , Fatores de Transcrição/biossíntese , Proteínas Wnt/metabolismo
10.
J Agric Food Chem ; 58(24): 12957-63, 2010 Dec 22.
Artigo em Inglês | MEDLINE | ID: mdl-21117690

RESUMO

The 7S-globulin fraction is a minor component of the amaranth storage proteins. The present work provides new information about this protein. The amaranth 7S-globulin or vicilin presented a sedimentation coefficient of 8.6 ± 0.6 S and was composed of main subunits of 66, 52, 38, and 16 kDa. On the basis of mass spectrometry (MS) analysis of tryptic fragments, the 52, 38, and 16 kDa subunits presented sequence homology with sesame vicilin, whereas the 66 kDa subunit showed sequence similarity with a putative vicilin. Several characteristics of the 66 kDa subunit were similar to members of the convicilin family. Results support the hypothesis that the 7S-globulin molecules are composed of subunits coming from at least two gene families with primary products of 66 and 52 kDa, respectively. According to the present information, amaranth vicilin may be classified into the vicilin group that includes pea, broad bean, and sesame vicilins, among others.


Assuntos
Amaranthus/química , Subunidades Proteicas/química , Proteínas de Armazenamento de Sementes/química , Sequência de Aminoácidos , Dados de Sequência Molecular , Peso Molecular , Mapeamento de Peptídeos , Alinhamento de Sequência
11.
EMBO Rep ; 11(6): 466-72, 2010 Jun.
Artigo em Inglês | MEDLINE | ID: mdl-20448664

RESUMO

Genes of the SOX family of high-mobility group transcription factors are essential during nervous system development. In this study, we show that SOX5 is expressed by neural progenitors in the chick spinal cord and is turned off as differentiation proceeds. The overexpression of SOX5 in neural progenitors causes premature cell cycle exit and prevents terminal differentiation. Conversely, knocking down SOX5 protein extends the proliferative period of neural progenitors and causes marked cell death in a dorsal interneuron (dI3) population. Furthermore, SOX5 reduces WNT-beta-catenin signalling, thereby triggering the expression of the negative regulator of the pathway axin2. We propose that SOX5 regulates the timing of cell cycle exit by opposing WNT-beta-catenin activity on cell cycle progression.


Assuntos
Ciclo Celular , Neurônios/citologia , Fatores de Transcrição SOXD/metabolismo , Transdução de Sinais , Células-Tronco/metabolismo , Proteínas Wnt/metabolismo , beta Catenina/metabolismo , Animais , Ciclo Celular/genética , Diferenciação Celular/genética , Embrião de Galinha , Regulação para Baixo/genética , Regulação da Expressão Gênica no Desenvolvimento , Interneurônios/citologia , Interneurônios/metabolismo , Fatores de Transcrição SOXD/genética , Medula Espinal/citologia , Medula Espinal/embriologia , Medula Espinal/metabolismo , Células-Tronco/citologia , Fatores de Tempo , beta Catenina/genética
12.
Protein J ; 28(9-10): 457-67, 2009 Dec.
Artigo em Inglês | MEDLINE | ID: mdl-19921410

RESUMO

Amaranth is an ancient crop with a high content of good quality proteins. Globulins are some of the most abundant storage proteins of amaranth grain. They contain two fractions distinguishable according to their different solubility: the salt-soluble 7S and 11S-globulins and the globulin-p soluble in mild-alkaline, low-ionic-strength solutions. As part of the amaranth proteins characterization, in this work we investigated the structural characteristics responsible for the different physicochemical properties of these globulins. We studied certain conformational parameters of the purified aggregates (AMGp) and individual molecules (IMGp) of globulin-p and of the partially purified globulin (ppGb) and compared the AMGp polypeptide sequences with the sequence of the 11S-globulin propolypeptide from Amaranthus (gi|122726601). The results indicated that the AMGp aggregates are responsible for the different solubility of globulin-p. Subtle conformational differences as determined by fluorescence spectroscopy and urea sensitivity were found between the molecules studied: The AMGp showed some surface differences from the IMGp and the ppGb; the AMGp also had a lower affinity for the hydrophobic fluorescent probe 1,8-aniline-naphthalene-sulfonate and a higher ionic charge than the ppGb and the IMGp, characteristics that might cause their lower solubility. In addition, we have demonstrated differences between the AMGp polypeptide sequences and that reported for amaranth 11S-globulin. These differences suggest that the globulin-p and 11S-globulin are two 11S-globulin isoforms comprised of polypeptides coming from different legumin-gene subfamilies.


Assuntos
Amaranthus/química , Globulinas/química , Proteínas de Armazenamento de Sementes/química , Conformação Proteica , Isoformas de Proteínas/química
13.
Protein J ; 26(5): 327-33, 2007 Aug.
Artigo em Inglês | MEDLINE | ID: mdl-17503166

RESUMO

The polypeptides integrating amaranth globulin-p and 11S-globulin were characterized by two-dimensional electrophoresis, ion-exchange chromatography and RP-HPLC. All polypeptides exhibited charge and hydrophobic heterogeneity. Almost all acid (A, pI 5-7) and basic (B, pI 9-10) polypeptides were present in both globulins, and the same happened with the unprocessed M polypeptides with pI in the range of 7-7.5 which fits well with a sequence containing both the A and B polypeptides. There were other polypeptides only present in 11S-globulin, like some of 41 and 16 kDa, which might come from another precursor or be the products of a different processing of the propolypeptide. These results suggested that, although amaranth subunits from different subfamilies are interchangeable in different oligomers, some structural differences between them might affect the assembly of globulin molecules. Structural differences arising from this behavior could account for the different physicochemical properties of globulin molecules.


Assuntos
Amaranthus/química , Globulinas/química , Proteínas de Plantas/química , Sementes/química , Eletroforese em Gel Bidimensional , Ponto Isoelétrico , Peso Molecular , Relação Estrutura-Atividade
14.
Am J Primatol ; 61(2): 53-60, 2003 Oct.
Artigo em Inglês | MEDLINE | ID: mdl-14582127

RESUMO

The large human populations in cities are an important source of demand for wildlife pets, including primates, and not much is known about the primate species involved in terms of their general origin, the length of time they are kept as pets, and some of the maintenance problems encountered with their use as pets. We report the results of a survey conducted in Mexico City among primate pet owners, which was aimed at providing some of the above information. We used an ethnographic approach, and pet owners were treated as informants to gain their trust so that we could enter their homes and learn about the life of their primate pets. We surveyed 179 owners of primate pets, which included 12 primate species. Of these, three were native species (Ateles geoffroyi, Alouatta pigra, and A. palliata). The rest were other neotropical primate species not native to Mexico, and some paleotropical species. Spider monkeys and two species of howler monkeys native to Mexico accounted for 67% and 15%, respectively, of the primate cases investigated. The most expensive primate pets were those imported from abroad, while the least expensive were the Mexican species. About 45% of the native primate pets were obtained by their owners in a large market in Mexico City, and the rest were obtained in southern Mexico. Although they can provide companionship for children and adults, primate pets are subject to a number of hazards, some of which put their lives at risk. The demand by city dwellers for primate pets, along with habitat destruction and fragmentation, exerts a significant pressure on wild populations in southern Mexico.


Assuntos
Animais Domésticos , Primatas , Acidentes , Adulto , Envelhecimento , Alouatta , Animais , Causas de Morte , Cebidae , Custos e Análise de Custo , Dieta , Feminino , Humanos , Masculino , México , Pessoa de Meia-Idade , Doenças dos Primatas/epidemiologia , Doenças dos Primatas/mortalidade , População Urbana
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