[7] Activation of TAAR1 by T1AM results in the production of large amounts of cyclic adenosine monophosphate (cAMP).

[8] Wu et al. have pointed out that this relationship is not typical of the endocrine system, indicating that TAAR1 activity may not be coupled to G proteins in some tissues, or that T1AM may interact with other receptor subtypes.

[9] T1AM has been found to produce TAAR1-dependent tyrosine hydroxylase (TH) phosphorylation in mouse dorsal striatum slices.

[10][6] Accordingly, higher rates of L-DOPA accumulation were observed after administration of T1AM in mice treated with a DOPA decarboxylase inhibitor.

[6] In contrast to T1AM, the trace amines β-phenethylamine and tyramine reduced TH phosphorylation, which was independent of the TAAR1, and hence do not appear to augment TH functional activity.