NAMPT and NAPRT1: novel polymorphisms and distribution of variants between normal tissues and tumor samples

• Tipo: Artigo em Revista Científica Internacional
• Data: 2014

Autores

Sara Duarte Pereira (Autor) Outra; Sarah S Silva (Autor) Outra; Luisa Azevedo (Autor) FCUP; Luisa Castro (Autor) Outra; Antonio Amorim (Autor) FCUP; Raquel M Silva (Autor) Outra

Revista

Título: Scientific Reports

Vol. 4

Página Final: 6311

ISSN: 2045-2322

Editora: Springer Nature

Indexação

ISI Web of Knowledge - 22 Citações

Scopus - 21 Citações

Classificação Científica

FOS: Ciências exactas e naturais > Ciências biológicas

CORDIS: Ciências Naturais > Ciências biológicas

Outras Informações

ID Authenticus: P-009-TH1

DOI: 10.1038/srep06311

Abstract (EN): Nicotinamide phosphoribosyltransferase (NAMPT) and nicotinate phosphoribosyltransferase domain containing 1 (NAPRT1) are the main human NAD salvage enzymes. NAD regulates energy metabolism and cell signaling, and the enzymes that control NAD availability are linked to pathologies such as cancer and neurodegeneration. Here, we have screened normal and tumor samples from different tissues and populations of origin for mutations in human NAMPT and NAPRT1, and evaluated their potential pathogenicity. We have identified several novel polymorphisms and showed that NAPRT1 has a greater genetic diversity than NAMPT, where any alteration can have a greater functional impact. Some variants presented different frequencies between normal and tumor samples that were most likely related to their population of origin. The novel mutations described that affect protein structure or expression levels can be functionally relevant and should be considered in a disease context. Particularly, mutations that decrease NAPRT1 expression can predict the usefulness of Nicotinic Acid in tumor treatments with NAMPT inhibitors.

Idioma: Inglês

Tipo (Avaliação Docente): Científica