Kitano, Eduardo S.
Serrano, Solange M. T.
Número total de Autores: 6
Afiliação do(s) autor(es):
 Fed Univ Sao Paulo ICT UNIFESP, Dept Sci & Technol, Funct Prote Lab, Sao Jose Dos Campos, SP - Brazil
 Inst Butantan, Ctr Toxins Immune Response & Cell Signaling CeTIC, Lab Especial Toxinol Aplicada, Sao Paulo - Brazil
 Inst Butantan, Ctr Excellence New Target Discovery CENTD, Sao Paulo - Brazil
 Univ Sao Paulo, Fac Med, Inst Canc Estado Sao Paulo, Sao Paulo - Brazil
Número total de Afiliações: 4
Tipo de documento:
JOURNAL OF PROTEOMICS;
FEB 10 2019.
Citações Web of Science:
The comprehensive profiling of the repertoire of secreted proteins from cancer cells samples provides information on the signaling events in oncogenesis as well as on the cross-talk between normal and tumoral cells. Moreover, the analysis of post-translational modifications in secreted proteins may unravel biological circuits regulated by irreversible modifications such as proteolytic processing. In this context, we used Terminal Amine Isotopic Labeling of Substrates (TAILS) to perform a system-wide investigation on the N-terminome of the secretomes derived from a paired set of mouse cell lines: Melan-a (a normal melanocyte) and Tm1 (its transformed phenotype). Evaluation of the amino acid identities at the scissile bond in internal peptides revealed significant differences, suggesting distinct proteolytic processes acting in the normal and tumoral secretomes. The mapping and annotation of cleavage sites in the tumoral secretome suggested functional roles of active proteases in central biological processes related to oncogenesis, such as the processing of growth factors, cleavage of extracellular matrix proteins and the shedding of ectopic domains from the cell surface, some of which may represent novel processed forms of the corresponding proteins. In the context of the tumor microenvironment, these results suggest important biological roles of proteolytic processing in murine melanoma secreted proteins. (AU)