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1.
Biochimie ; 208: 100-116, 2023 May.
Article in English | MEDLINE | ID: mdl-36586566

ABSTRACT

Poor lifestyle choices and genetic predisposition are factors that increase the number of cancer cases, one example being breast cancer, the third most diagnosed type of malignancy. Currently, there is a demand for the development of new strategies to ensure early detection and treatment options that could contribute to the complete remission of breast tumors, which could lead to increased overall survival rates. In this context, the glycans observed at the surface of cancer cells are presented as efficient tumor cell markers. These carbohydrate structures can be recognized by lectins which can act as decoders of the glycocode. The application of plant lectins as tools for diagnosis/treatment of breast cancer encompasses the detection and sorting of glycans found in healthy and malignant cells. Here, we present an overview of the most recent studies in this field, demonstrating the potential of lectins as: mapping agents to detect differentially expressed glycans in breast cancer, as histochemistry/cytochemistry analysis agents, in lectin arrays, immobilized in chromatographic matrices, in drug delivery, and as biosensing agents. In addition, we describe lectins that present antiproliferative effects by themselves and/or in conjunction with other drugs in a synergistic effect.


Subject(s)
Breast Neoplasms , Fabaceae , Humans , Female , Lectins/chemistry , Breast Neoplasms/diagnosis , Breast Neoplasms/drug therapy , Polysaccharides/chemistry , Plant Lectins , Vegetables , Biomarkers, Tumor
2.
Int J Biol Macromol ; 199: 243-251, 2022 Feb 28.
Article in English | MEDLINE | ID: mdl-35016969

ABSTRACT

The lack of specific pharmacological therapy for Autistic Spectrum Disorder (ASD) and its clinical heterogeneity demand efforts directed toward the identification of biomarkers to aid in diagnosis. Proteomics offers a new perspective for studying the altered proteins associated with autism spectrum disorders (ASD) and we have saliva as an easy-to-collect biological fluid with important biomolecules for investigating biomarkers in various diseases. In this sense, saliva could be used to identify potential biomarkers of ASD. In the current work, saliva samples were collected from children with different degrees of ASD and healthy children and proteomics approaches were applied to generate data on differentially expressed proteins between groups which will serve as a basis for future validation studies as protein markers. Data are available via ProteomeXchange with identifier PXD030065. As results, 132 proteins were present in 80% of the saliva pools of all analyzed groups. Twenty-five proteins were identified as overexpressed in the group of severe and mild/moderate ASD carriers, among which, eight were identified as potential biomarkers for ASD.


Subject(s)
Autism Spectrum Disorder , Proteomics , Autism Spectrum Disorder/diagnosis , Autism Spectrum Disorder/metabolism , Biomarkers/metabolism , Child , Humans , Saliva/metabolism
3.
Int J Biol Macromol ; 190: 543-553, 2021 Nov 01.
Article in English | MEDLINE | ID: mdl-34508719

ABSTRACT

Environmental factors, as well as genetic factors, contribute to the increase in prostate cancer cases (PCa), the second leading cause of cancer death in men. This fact calls for the development of more reliable, quick and low-cost early detection tests to distinguish between malignant and benign cases. Abnormal cell glycosylation pattern is a promising PCa marker for this purpose. Proteins, such as lectins can decode the information contained in the glycosylation patterns. Several studies have reported on applications of plant lectins as diagnostic tools for PCa considering the ability to differentiate it from benign cases. In addition, they can be used to detect, separate and differentiate the glycosylation patterns of cells or proteins present in serum, urine and semen. Herein, we present an overview of these studies, showing the lectins that map glycans differentially expressed in PCa, as well as benign hyperplasia (BPH). We further review their applications in biosensors, histochemical tests, immunoassays, chromatography, arrays and, finally, their therapeutic potential. This is the first study to review vegetable lectins applied specifically to PCa.


Subject(s)
Lectins/therapeutic use , Prostatic Hyperplasia/diagnosis , Prostatic Hyperplasia/therapy , Prostatic Neoplasms/diagnosis , Prostatic Neoplasms/therapy , Animals , Glycosylation , Humans , Lectins/chemistry , Male , Models, Biological , Polysaccharides/metabolism
4.
J. Health Biol. Sci. (Online) ; 5(4): 306-310, out-dez/2017. ilus
Article in English | LILACS | ID: biblio-868025

ABSTRACT

Background: The vasorelaxant effect of lectins from leguminous plants (Diocleinae subtribe) is well described. However, this effect has been little explored for lectins isolated from Dalbergieae tribe, except for that of Vatairea guianensis, that induces vasorelaxation involving nitric oxide and the lectin domain. Objective: To evaluate the vasorelaxant effect of a lectin isolated from Lonchocarpus araripensis (LAL), Dalbergieae tribe, and the involvement of the lectin domain and endothelium derived relaxing factors. Methods: Aortic rings of Wistar rats (250 - 300 g) were mounted in organ bath and mantained in physiological conditions (CEUA No. 10130208-8/40). LAL (0.1­100 µg/ml) was added to phenylephrine (0.1 µM)-contracted tissues with either endothelium intact or denuded. In order to investigate the mechanisms of LAL relaxation, inhibitors of NOS (L-NAME: 100 µM), cyclooxygenase (indomethacin: 10 µM), or potassium channels (TEA: 5 mM) were added to endothelized tissues 30 min before contraction. The involvement of lectin domain was assessed by previous incubation of LAL (30 µg/ml) with GlcNAc (0.1 M). Results: LAL (0.1-100 µg/ml) induced relaxation only in endothelized aorta, being maximal at 100 µg/ml (62.57 ± 7.8%). The relaxant effect induced by LAL at 30 µg/ml (52.49 ± 10.32%) was abolished by previous incubation with GlcNAc. LAL relaxant effect (IC50 9.75 ± 7.1) was partially reversed by indomethacin (IC50 LAL + indomethacin: 30.47 ± 10.93) and was abolished by L-NAME or TEA. Conclusion: LAL exhibits vasorelaxant activity in contracted endothelized aorta of rats, involving the lectin domain, muscarinic receptor of acetylcholine and endothelial derived relaxing factors. (AU)


Introdução: O efeito vasorrelaxante de lectinas de plantas leguminosas (Subtribo Diocleinae) já é bem descrito, embora pouco explorado para lectinas isoladas da tribo Dalbergieae, com exceção da lectina de Vatairea guianensis, que induz relaxamento com envolvimento de óxido nítrico e do domínio lectínico. Objetivo: Avaliar o efeito vasorrelaxante da lectina isolada de Lonchocarpus araripensis (LAL), tribo Dalbergieae, e o envolvimento do domínio lectínico e de fatores relaxantes derivados do endotélio (EDRF). Métodos: Anéis de aorta de ratos Wistar (250-300 g) foram montados em banho de órgãos em condições fisiológicas (Tyrode, 37 ° C, 95% de O2 e 5% de CO2, pH = 7,4) (CEUA No. 10130208-8/40). LAL (0,1-100 µg/ml) foi adicionada a tecidos pré-contraídos com fenilefrina (0,1 µM) com ou sem endotélio. Para investigar os mecanismos de relaxamento, foram adicionados inibidores de NOS (L-NAME: 100 µM), guanilato ciclase (ODQ: 10 µM), receptor muscarínico (atropina: 1 µM), ciclooxigenase (indometacina: 10 µM) ou canais de potássio (TEA: 5 mM) aos tecidos endotelizados 30 minutos antes da contração. O envolvimento do domínio lectínico foi avaliado por incubação prévia da LAL (30 µg/ml) com GlcNAc (0,1 M). Resultados: LAL (0,1-100 µg/ml) relaxou apenas anéis de aorta endotelizadas, com efeito máximo na dose de 100 µg/ml (62,57 ± 7,8%). O efeito relaxante da LAL a 30 µg/ml (52,49 ± 10,32%) foi abolido por incubação prévia com GlcNAc, atropina ou ODQ. O relaxamento da LAL (IC50 9,75 ± 7,1) a 10, 30 e 100 µg/ml foi parcialmente revertido por indometacina (IC50 LAL + indometacina: 30,47 ± 10,93) e abolido por L-NAME e TEA. Conclusão: A LAL exibe atividade vasorrelaxante em aorta endotelizada de ratos, no estado contraído, envolvendo o domínio lectínico, receptor muscarínico e fatores relaxantes derivados do endotélio. (AU)


Subject(s)
Plant Lectins
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