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Review ArticleReview

The Tachykinin Peptide Family

Cinzia Severini, Giovanna Improta, Giuliana Falconieri-Erspamer, Severo Salvadori and Vittorio Erspamer
Pharmacological Reviews June 2002, 54 (2) 285-322; DOI: https://doi.org/10.1124/pr.54.2.285
Cinzia Severini
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Giovanna Improta
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Giuliana Falconieri-Erspamer
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Severo Salvadori
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Vittorio Erspamer
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Abstract

The tachykinin peptide family certainly represents one of the largest peptide families described in the animal organism. So far, more than 40 tachykinins have been isolated from invertebrate (insects, worms, and molluscs), protochordate, and vertebrate (skin, gastrointestinal tract, peripheral and central nervous system) tissues. Substance P (SP), first identified by bioassay as early as 1931 but sequenced only in 1971, several years after the elucidation of the structure of eledoisin from molluscan tissues and of physalaemin from amphibian skin, may be considered as a prototype of the tachykinins. Hitherto, as many as 19 tachykinins have been isolated from amphibian integument, and eight additional peptides have been isolated from amphibian gut and brain. Counterparts of skin tachykinins in mammalian tissues are SP, neurokinin A, and neurokinin B. Three main receptor subtypes for the tachykinins have been identified (NK1, NK2, and NK3), but their number is probably destined to increase. It is obvious that the peripheral and central effects of the tachykinins may substantially vary depending on the activation of different receptor subtypes. Matters are further complicated by the frequent capacity of the single tachykinins to bind, although with different affinity, to more receptors. It has been recognized that tachykinins have a variety of effects in physiological and pathological conditions, and there is evidence suggesting intrinsic neuroprotective and neurodegenerative properties of these neuropeptides. This review provides an update on the current body of knowledge regarding tachykinin occurrence and distribution in the animal kingdom, from the lowest invertebrates to man, and the physiological and pharmacological actions of tachykinins outlining the pregnant importance of this large peptide family.

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Pharmacological Reviews: 54 (2)
Pharmacological Reviews
Vol. 54, Issue 2
1 Jun 2002
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Review ArticleReview

The Tachykinin Peptide Family

Cinzia Severini, Giovanna Improta, Giuliana Falconieri-Erspamer, Severo Salvadori and Vittorio Erspamer
Pharmacological Reviews June 1, 2002, 54 (2) 285-322; DOI: https://doi.org/10.1124/pr.54.2.285

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Review ArticleReview

The Tachykinin Peptide Family

Cinzia Severini, Giovanna Improta, Giuliana Falconieri-Erspamer, Severo Salvadori and Vittorio Erspamer
Pharmacological Reviews June 1, 2002, 54 (2) 285-322; DOI: https://doi.org/10.1124/pr.54.2.285
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  • Article
    • Abstract
    • I. Introduction
    • II. Occurrence and Species Distribution of Tachykinin-Like Peptides
    • III. Localization of Tachykinin-Like Peptides
    • IV. Relationships between Structure/Activity Receptor Selectivity
    • V. Tachykinin-Like Peptides: Pharmacological Actions
    • VI. Tachykinins in Human Diseases and Therapeutics
    • VII. General Conclusions
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    • References
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