Tachykinin‐like Peptides and Their Receptors: A Review

Abstract

Tachykinin-like peptides have been identified in many vertebrate and invertebrate species. On the basis of the data reviewed in this paper, these peptides can be classified into two distinct subfamilies, which are recognized by their respective sequence characteristics. All known vertebrate tachykinins and a few invertebrate ones share a common C-terminal sequence motif, -FXGLMa. The insect tachykinins, which have a common -GFX1GX2Ra C-terminus, display about 30% of sequence homology with the first group. Tachykinins are multifunctional brain/gut peptides. In mammals and insects, various isoforms play an important neuromodulatory role in the central nervous system. They are involved in the processing of sensory information and in the control of motor activities. In addition, members of both subfamilies elicit stimulatory responses on a variety of visceral muscles. The receptors for mammalian and insect tachykinins show a high degree of sequence conservation and their functional characteristics are very similar. In both mammals and insects, angiotensin-converting enzyme (ACE) plays a prominent role in tachykinin peptide metabolism.

Peptidergic control of food intake and digestion in insects1This review is part of a virtual symposium on recent advances in understanding a variety of complex regulatory processes in insect physiology and endocrinology, including development, metabolism, cold hardiness, food intake and digestion, and diuresis, through the use of omics technologies in the postgenomic era.

“…First described and studied in vertebrate species, they were found to exert a variety of biological functions in both the central and the peripheral nervous system, as well as in several other tissues. Insect members of this family are also referred to as "tachykinin-related peptides" (TRPs) or "insectatachykinins" (TK) (Nässel 1999;Vanden Broeck et al 1999). In insects they have, among other roles, been associated with the regulation of food intake and processing (reviewed by Audsley and Weaver 2009).…”

Identification and characterization of a tachykinin-containing neuroendocrine organ in the commissural ganglion of the crabCancer productus

“…Homologous structures in other decapods are hypothesized to function similarly. 3304 1999; Nässel, 1999;Vanden Broeck et al, 1999;Severini et al, 2002). For example, 10 TRPs have been isolated from the cockroach Leucophea maderae Nässel, 1996, 1997), seven from the honeybee Apis mellifera (Takeuchi et al, 2003), five from the locust Locusta migratoria (Schoofs et al, 1990a(Schoofs et al, ,b, 1993, five from the fruit fly Drosophila melanogaster (Siviter et al, 2000) and three from the mosquito Culex salinarius (Meola et al, 1998).…”

“…Like all vertebrate tachykinins, and a few invertebrate isoforms sequenced from salivary tissues (e.g. eledoisin), these two peptides contain the carboxy (C)-terminal amino acid motif -FXGLMamide, where X represents a variable amino acid (Nachman et al, 1999;Nässel, 1999;Vanden Broeck et al, 1999;Severini et al, 2002). In invertebrates, a plethora of peptides containing the C-terminal amino acid motif -FX I GX II Ramide have been identified and collectively termed tachykinin-related peptides or TRPs (Nachman et al, 1999;Nässel, 1999;Vanden Broeck et al, 1999).…”

“…eledoisin), these two peptides contain the carboxy (C)-terminal amino acid motif -FXGLMamide, where X represents a variable amino acid (Nachman et al, 1999;Nässel, 1999;Vanden Broeck et al, 1999;Severini et al, 2002). In invertebrates, a plethora of peptides containing the C-terminal amino acid motif -FX I GX II Ramide have been identified and collectively termed tachykinin-related peptides or TRPs (Nachman et al, 1999;Nässel, 1999;Vanden Broeck et al, 1999). Comparisons of sequence homology, tissue distribution, chemical/ conformational requirements for receptor interaction and physiological function suggest a common evolutionary origin for both the vertebrate-and invertebrate-type peptides (Nachman et al, 1999;Nässel, 1999;Vanden Broeck et al, 1999;Severini et al, 2002).…”

Cutting Edge: Hemokinin Has Substance P-Like Function and Expression in Inflammation

“…Another recently discovered molecule belonging to the tachykinin family of neuropeptides called hemokinin (HK) 1 derives from a protein named preprotachykinin (PPT) C (21)(22)(23). It is a product of a gene (Tac4) distinct from that of SP.…”