Concepts in Characterization of Tachykinin Receptorsa

Different Subtypes of Tachykinin NK1 Receptor Binding Sites Are Present in the Rat Brain

“…There is also evidence for a release of NKA and NPK in the brain (Diez‐Guerra et al, 1988), and even when used in rather low concentration, these peptides as well as NPγ were shown to induce different central biological responses. These peptides act on NK 2 receptors in peripheral tissues (Burcher et al, 1991), and this seems also to be the case for some central NKA or NPγ‐evoked responses that were selectively antagonized by the NK 2 receptor antagonist SR 48968 (Martini‐Luccarini et al., 1996; Picard and Couture, 1996; Steinberg et al, 1998). Direct evidence for the presence of these receptors in brain tissues has recently been reported, but these receptors were observed in only limited density in the septal area (Steinberg et al, 1998).…”

Substance P: Structure, Function, and Therapeutics

“…[39][40][41][42][43][44]. Maggi and Schwartz [45] have investigated the limited selectivity of ligands such as SP, NKA, NKB for a particular NK receptor.…”

Creation and functional screening of a multi-usepeptide library.

“…The utility of a MUPL was explored by constructing one based on the sequence of bombesin- (8)(9)(10)(11)(12)(13)(14). Bombesin and related peptides such as gastrin-releasing peptide actuate a wide range of biological processes, including smooth muscle contraction, release of gastrointestinal hormones, and enzyme secretion from the pancreas (26)(27)(28)(29)(30).…”

“…The minimum amino acid sequence required to elicit biological activity of the bombesin receptor encompasses residues 8-14, YAVGHLM-amide (35,36). It has been suggested that Trp2l, analogous to Trp8 in bombesin or Trpl in bombesin- (8)(9)(10)(11)(12)(13)(14), plays an important role in binding of GRP to the bombesin receptor. To investigate the importance of tryptophan and alanine as the first two and methionine as the final amino acid for peptide-mediated receptor activation, a 1444-member MUPL was constructed based on this sequence in which the first two positions were -filled by all possible combinations of nineteen L amino acids while four L amino acids were incorporated at position 7 (Fig.…”

“…This would enable the peptides to interact with receptors free of interferences from other peptide species and would also make both their amino and carboxyl termini available. There are numerous examples in which the ends of peptides are critically important for interactions with and activation of transmembrane receptors such as GCRs (6)(7)(8)(9).…”