Danielle Resende Camisasca1, Lorena da Rós Gonçalves2, Márcia Regina Soares3, Vanessa Sandim4, Fábio César Sousa Nogueira5, Carlos Henrique Saraiva Garcia6, Rodrigo Santana7, Silvia Paula de Oliveira8, Luisa Aguirre Buexm9, Paulo Antônio Silvestre de Faria10, Fernando Luiz Dias11, Denise de Abreu Pereira12, Russolina B Zingali13, Gilda Alves14, Simone Queiroz Chaves Lourenço15. 1. Oral Pathology, Federal Fluminense University (UFF), R. Marques de Paraná, 303/4° andar (Hospital Universitário Antônio Pedro), Centro Niterói, Brazil, CEP: 24033-900. Electronic address: daniellecamisasca@yahoo.com.br. 2. Serviço de Hematologia, Laboratório de Genética Aplicada, Brazilian National Cancer Institute (INCA), Hospital do Câncer I, Praça da Cruz Vermelha, 23 - 6° andar, Rio de Janeiro, RJ, Brazil, CEP: 20230-130. Electronic address: lorena.da@terra.com.br. 3. Departamento de Bioquímica, Instituto de Química, Universidade Federal do Rio de Janeiro (UFRJ), Av. Athos daSilveira, 149/541, Cidade Universitária, Rio deJaneiro, RJ, Brazil, CEP: 21941-909. Electronic address: marcia@iq.ufrj.br. 4. Serviço de Hematologia, Laboratório de Genética Aplicada, Brazilian National Cancer Institute (INCA), Hospital do Câncer I, Praça da Cruz Vermelha, 23 - 6° andar, Rio de Janeiro, RJ, Brazil, CEP: 20230-130; Laboratório de Hemostase e Venenos e Unidade de Espectrometria de Massas e Proteômica, Instituto de Bioquímica Médica, Programa de Biologia Estrutural, Universidade Federal do Rio de Janeiro (UFRJ), Av. Carlos Chagas Filho, 373, CCS Bloco H2 sala 04, Cidade Universitária, Rio de Janeiro, RJ, Brazil, CEP 21941-902. Electronic address: nessasandim@gmail.com. 5. Departamento de Bioquímica, Instituto de Química, Universidade Federal do Rio de Janeiro (UFRJ), Av. Athos daSilveira, 149/541, Cidade Universitária, Rio deJaneiro, RJ, Brazil, CEP: 21941-909. Electronic address: fabiocsn@gmail.com. 6. Departamento de Bioquímica, Instituto de Química, Universidade Federal do Rio de Janeiro (UFRJ), Av. Athos daSilveira, 149/541, Cidade Universitária, Rio deJaneiro, RJ, Brazil, CEP: 21941-909. Electronic address: scarlogarcia@gmail.com. 7. Serviço de Hematologia, Laboratório de Genética Aplicada, Brazilian National Cancer Institute (INCA), Hospital do Câncer I, Praça da Cruz Vermelha, 23 - 6° andar, Rio de Janeiro, RJ, Brazil, CEP: 20230-130. Electronic address: chokus05@hotmail.com. 8. Odontoclínica Central do Exército (OCEX), Praça da República, 123 - Centro, Rio de Janeiro, RJ, Brazil, CEP: 20211-340. Electronic address: silviaoliv@hotmail.com. 9. Oncology Graduate Program, Molecular Carcinogenesis Program, Research Center, Brazilian National Cancer Institute, Rua André Cavalcanti, 37, 6° andar, Centro, 20231-050 Rio de Janeiro, RJ, Brazil. Electronic address: labuexm@hotmail.com. 10. Pathology Division (Divisão de Patologia), Brazilian National Cancer Institute (INCA), Rua Cordeiro da Graça, 156, Rio de Janeiro, RJ, Brazil, CEP:20220-400. Electronic address: pauloafaria@gmail.com. 11. Head and Neck Surgery Department, Brazilian National Cancer Institute (INCA), Hospital do Câncer I, Praça da Cruz Vermelha, 23 - 6°andar, Rio de Janeiro, RJ, Brazil, CEP:20230-130. Electronic address: fdias@inca.gov.br. 12. Serviço de Hematologia, Laboratório de Genética Aplicada, Brazilian National Cancer Institute (INCA), Hospital do Câncer I, Praça da Cruz Vermelha, 23 - 6° andar, Rio de Janeiro, RJ, Brazil, CEP: 20230-130. Electronic address: deniseap@inca.gov.br. 13. Rede Proteômica do Rio de Janeiro, Rio de Janeiro, Brazil; Laboratório de Hemostase e Venenos e Unidade de Espectrometria de Massas e Proteômica, Instituto de Bioquímica Médica, Programa de Biologia Estrutural, Universidade Federal do Rio de Janeiro (UFRJ), Av. Carlos Chagas Filho, 373, CCS Bloco H2 sala 04, Cidade Universitária, Rio de Janeiro, RJ, Brazil, CEP 21941-902. Electronic address: lzingali@bioqmed.ufrj.br. 14. Serviço de Hematologia, Laboratório de Genética Aplicada, Brazilian National Cancer Institute (INCA), Hospital do Câncer I, Praça da Cruz Vermelha, 23 - 6° andar, Rio de Janeiro, RJ, Brazil, CEP: 20230-130. Electronic address: galvesbrown@gmail.com. 15. Oral Pathology, Federal Fluminense University (UFF), R. Marques de Paraná, 303/4° andar (Hospital Universitário Antônio Pedro), Centro Niterói, Brazil, CEP: 24033-900. Electronic address: silourenco2015@gmail.com.
Abstract
BACKGROUND: Oral leukoplakia is the most common potentially malignant disorder in the oral cavity and can precede carcinoma. This study aimed to identify possible oral leukoplakia salivary biomarkers. METHODS: Unstimulated saliva was collected from participants and protein concentration was determined. Proteins were then precipitated with cold acetone and separated using 2DE over a pH range of 3-10. Spot demarcation and matching were performed and protein identification was done through MS analysis. Oral leukoplakia tissues were submitted to immunohistochemistry analysis for keratin 10 (CK10). A complementary analysis of oral leukoplakias that were not included previously was performed in addition. RESULTS: 226±10 spots were identified in oral leukoplakia 2DE gels, and 262±12 spots were identified in volunteers. Twenty-two spots were highly abundant in oral leukoplakias or not detected in the control group, such as apolipoprotein A1, alpha amylase, cystatins, keratin 10, and lysozyme precursor. All were identified. All oral leukoplakia cases were immunopositive for CK10, mainly in the superficial epithelial layers. CONCLUSIONS: The 2DE salivary protein profiles of individuals with and without oral leukoplakia were observably different. CK10 appears to be an interesting protein and should be further studied in oral carcinogenesis. SIGNIFICANCE: MS-based proteomics enables large-scale analysis of proteins. Proteomics can provide detailed descriptions of proteomes of cells and tissues, including body fluids, and appears as a powerful tool to study human disorders. Saliva is readily accessible through non invasive collection and can mirror diverse disease states. Saliva from both diseased and healthy subjects can be analyzed through 2DE and differences between groups could be found. Routine immunohistochemistry analysis confirmed one of these findings, with CK10 being positive tissues from individuals with oral leukoplakia. Therefore, the present study allows insights into development of an important potential oral cancer precursor, named oral leukoplakia. However, the results can be extrapolated and tested in other precancer states, such as proliferative verrucous leukoplakia, patients at risk of oral cancer due to lifestyle behavior and/or cancer history in the family or even those who are under surveillance after a treated primary oral cancer.
BACKGROUND:Oral leukoplakia is the most common potentially malignant disorder in the oral cavity and can precede carcinoma. This study aimed to identify possible oral leukoplakia salivary biomarkers. METHODS: Unstimulated saliva was collected from participants and protein concentration was determined. Proteins were then precipitated with cold acetone and separated using 2DE over a pH range of 3-10. Spot demarcation and matching were performed and protein identification was done through MS analysis. Oral leukoplakia tissues were submitted to immunohistochemistry analysis for keratin 10 (CK10). A complementary analysis of oral leukoplakias that were not included previously was performed in addition. RESULTS: 226±10 spots were identified in oral leukoplakia2DE gels, and 262±12 spots were identified in volunteers. Twenty-two spots were highly abundant in oral leukoplakias or not detected in the control group, such as apolipoprotein A1, alpha amylase, cystatins, keratin 10, and lysozyme precursor. All were identified. All oral leukoplakia cases were immunopositive for CK10, mainly in the superficial epithelial layers. CONCLUSIONS: The 2DE salivary protein profiles of individuals with and without oral leukoplakia were observably different. CK10 appears to be an interesting protein and should be further studied in oral carcinogenesis. SIGNIFICANCE: MS-based proteomics enables large-scale analysis of proteins. Proteomics can provide detailed descriptions of proteomes of cells and tissues, including body fluids, and appears as a powerful tool to study human disorders. Saliva is readily accessible through non invasive collection and can mirror diverse disease states. Saliva from both diseased and healthy subjects can be analyzed through 2DE and differences between groups could be found. Routine immunohistochemistry analysis confirmed one of these findings, with CK10 being positive tissues from individuals with oral leukoplakia. Therefore, the present study allows insights into development of an important potential oral cancer precursor, named oral leukoplakia. However, the results can be extrapolated and tested in other precancer states, such as proliferative verrucous leukoplakia, patients at risk of oral cancer due to lifestyle behavior and/or cancer history in the family or even those who are under surveillance after a treated primary oral cancer.
Authors: Sheila M F Torres; Eva Furrow; Clarissa P Souza; Jennifer L Granick; Ebbing P de Jong; Timothy J Griffin; Xiong Wang Journal: PLoS One Date: 2018-01-12 Impact factor: 3.240
Authors: Ha Ra Cho; Han Sol Kim; Jun Seo Park; Seung Cheol Park; Kwang Pyo Kim; Troy D Wood; Yong Seok Choi Journal: PLoS One Date: 2017-07-24 Impact factor: 3.240
Authors: Alejandro I Lorenzo-Pouso; Mario Pérez-Sayáns; Susana B Bravo; Pía López-Jornet; María García-Vence; Manuela Alonso-Sampedro; Javier Carballo; Abel García-García Journal: Dis Markers Date: 2018-11-07 Impact factor: 3.434
Authors: Alessandra Vidotto; Giovana M Polachini; Marina de Paula-Silva; Sonia M Oliani; Tiago Henrique; Rossana V M López; Patrícia M Cury; Fabio D Nunes; José F Góis-Filho; Marcos B de Carvalho; Andréia M Leopoldino; Eloiza H Tajara Journal: BMC Med Genomics Date: 2018-08-29 Impact factor: 3.063
Authors: M Castagnola; E Scarano; G C Passali; I Messana; T Cabras; F Iavarone; G Di Cintio; A Fiorita; E De Corso; G Paludetti Journal: Acta Otorhinolaryngol Ital Date: 2017-04 Impact factor: 2.124