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Soluble secretory Amyloid Beta-peptide (25-35) typically contain N-terminal signal sequences that direct them to the extracellular space. However, some proteins which do not contain signal sequence, including cytokines, growth factors, components of the extracellular matrix, and enzymes, were reported to be secreted via non-classical secretory pathway [23]. Non-classical secretory pathway is not mediated by a single transport mechanism, but has been suggested to consist of several distinct secretory machineries. Secreted proteins using alternative pathway have three features (1) the lack of N-terminal signal sequences, (2) the exclusion of the protein from classical secretory organelles such as ER, Golgi, and secretory granules, and (3) the resistance of these export process to Brefeldin A and Monensin, a classical inhibitor of ER–Golgi-dependent protein secretion [23].
As to the third feature, Brefeldin A and Monensin, which should inhibit ER–Golgi pathway, did not reduce visfatin release. These results indicated that visfatin release should not be mediated by ER–Golgi-dependent pathway.