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Bombesin Receptor Antagonists: Different Classes and Cellular Basis of Action

  • Chapter
Book cover Peptides in Oncology II

Part of the book series: Recent Results in Cancer Research ((RECENTCANCER,volume 129))

Abstract

The naturally occurring bombesin (Bn)-related peptides can be divided structurally into three different groups based on chemical structure (Erspamer 1988; Erspamer and Melchiorri 1977; Minamino et al. 1983, 1984). The amphibian peptide Bn resembles other amphibian peptides such as alytesin and the mammalian peptide gastrin-releasing peptide (GRP) (Anastasia et al. 1971; Erspamer 1988; Erspamer and Melchiorri 1977; McDonald et al. 1979) in possessing a carboxy terminal Gly-His-Leu-Met-amide (Fig. 1). The second class includes the amphibian peptides ranatensin and litorin, which resemble the mammalian peptide neuromedin B (Erspamer 1988; Erspamer and Melchiorri 1977; Minamino et al. 1983, 1984) in possessing a COOH terminal Gly-His-Phe-Met-amide (Table 1). The third group, comprised of the amphibian peptide phyllolitorin and other structurally related amphibian peptides, have at present no mammalian counterpart and are characterized by having a COOH terminal Gly-Ser-Phe-Met-amide or Gly-Ser-Leu-Met-amide (Erspamer 1988) (Table 1).

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  1. National Institutes of Health, Building 10, Room 9C-103, Bethesda, MD, 20892, USA

    R. T. Jensen, J. E. Mrozinski Jr. & D. H. Coy

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  1. Klinik für Innere Medizin II: Onkologie — Hämatologie — Endokrinologie — Stoffwechselerkrankungen, Klinikum der Friedrich-Schiller-Universität Jena, Erlanger Allee 101, O-6902, Jena-Lobeda, Germany

    K. Höffken

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Jensen, R.T., Mrozinski, J.E., Coy, D.H. (1993). Bombesin Receptor Antagonists: Different Classes and Cellular Basis of Action. In: Höffken, K. (eds) Peptides in Oncology II. Recent Results in Cancer Research, vol 129. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-84956-5_8

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