13 aa and NT8-13 were synthesized using standard fmoc amino acids and purified >90-100% by hplc.
Neurotensin (NT) is an endogenous tridecapeptide neurotransmitter (pGlu-Leu-Tyr-Glu-Asn-Lys-Pro-Arg-Arg-pro-Tyr-Ile-Leu-OH) that was originally isolated from bovine hypothalamus. NT influences distinct central and peripheral physiological functions in mammals. Central administration of NT modulates dopaminergic transmission and triggers hypothermic and naloxone-insensitive analgesic responses, whereas peripheral effects include hypotension, decrease gastric acid release, potentiation of lipid digestion. NT causes contraction of smooth muscle. NT is widely distributed throughout the CNS. It has been localized to catecholamine-containing neurons. NT gene (human chromosome 12q21) produces both NT and neuromedin N (NN). In the rat, the NT precursor consists of a 169-aa polypeptide. The signal peptide (1-22 aa) is removed to produce a peptide that is further processed to produce NN (142-147 aa) and NT (150-162 aa). NT sequence is completely conserved in mouse, rat, human, canine, bovine etc. NT initiates its biological action by interacting with two distinct G-protein coupled receptors (NTR1 and NTR2). Recently, a third receptor NTR3 has been identified that is identical to gp95/sortilin and it is not coupled via the G-proteins. All three receptors bind NT through its C-terminal hexapeptide sequence (8 RRPYIL 13). Biologically active NT (NT8-13) has also been shown to interact with the extracellular domain 3 (between TM6-7) of NTR1.
