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  • 1
    Electronic Resource
    Electronic Resource
    The folliculostatins of two dipteran insect species, their relation to matrix proteins and prospects for practical applications (1995)
    Springer
    Entomologia experimentalis et applicata 77 (1995), S. 1-9 
    Details
    ISSN: 1570-7458
    Keywords: insect endocrinology ; ecdysone ; juvenile hormone ; reproduction ; growth ; inhibin ; oostatin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The first insect folliculostatic peptide was isolated from vitellogenic ovaries of the mosquitoAedes aegypti. This decapeptide directly inhibits trypsin biosynthesis in the gut, and indirectly ovarian development. The factor was named Trypsin Modulating Oostatic Factor or TMOF by its discoverers. From the fleshfly Neobellieria bullata 2 folliculostatins have been isolated, the hexapeptide Neb-TMOF and the 19-mer Neb-colloostatin. The available data suggest that at least 2 of the 3 folliculostatins originate from matrix (like) proteins present in the ovary, a hitherto unknown source of hormones. Furthermore, one of the folliculostatins (Neb-TMOF) is a potent inhibitor of ecdysone biosynthesis by larval ring glands of fleshflies. The discovery of the dipteran folliculostatins, which do not show any resemblance to inhibins of vertebrates, may significantly contribute to a better understanding of the hormonal control of growth in insects and perhaps, in other animals as well. None of the 3 folliculostatins is blocked at its N- or C-terminus. This, in combination with the pleiotropy of their effects and the narrow species specificity make such peptides prime candidates for, testing their potential in insect pest control by means of molecular biological methods.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02383011
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Insect Trypsin Modulating Oostatic Factor (Neb-TMOF) and Its Analogs: Preliminary Structure/Biological Function Relationship Studies (1998)
    Springer
    International journal of peptide research and therapeutics 5 (1998), S. 391-393 
    Details
    ISSN: 1573-3904
    Keywords: insect oostatic factor ; Neb-TMOF and analogs ; trypsin modulating oostatic factor ; trypsin modulating peptide
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Neb-TMOF, the trypsin modulating oostatic factor of gray fleshfly Neobellieria bullata, is a hexapeptide with the following sequence: H-Asn-Pro-Thr-Asn-Leu-His-OH. It has been isolated from vitellogenic ovaries in 1994. TMOF, the newly discovered insect peptide, inhibits trypsin biosynthesis in the gut, lowers yolk polypeptide concentration in the hemolymph and strongly inhibits ecdysone biosynthesis by larval ring glands. It is interesting that this short non-protected peptide contains in its molecule two Asn residues at positions 1 and 4 and His at its C-terminus. To obtain information about the role of the His-6 and Asn-4 residues we synthesised two series of Neb-TMOF analogs, modified: (1) in position 6 by D-His (I), His(Bzl) (II) and Phe(p-X) derivatives, where X = NH2 (III), NO2 (IV), OEt (V) and OH (VI) and (2) in position 4 by such amino acid residues as Ser (VII), Thr (VIII), Gly (IX), Asp (X), Glu (XI) and D-Asn (XII). The influence of these peptides on trypsin biosynthesis in N. bullata was determined in vivo. In preliminary investigations, we found that Neb-TMOF, [Phe(NH2)6], and [Phe(NO2)6]-Neb-TMOF inhibited trypsin biosynthesis, whereas [D-His)6]- and [D-His(Bzl)6]-Neb-TMOF were inactive. In further biological studies performed in vitro on heart of Tenebrio molitor we found that Neb-TMOF and [Phe(p-NH2)6-Neb-TMOF showed weak cardioexcitatory activity, about 30% of the cardioexcitatory activity of proctolin, an insect neuromodulating peptide.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1008895612705
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Insect trypsin modulating oostatic factor (Neb-TMOF) and its analogs: Preliminary structure/biological function relationship studies (1998)
    Springer
    International journal of peptide research and therapeutics 5 (1998), S. 391-393 
    Details
    ISSN: 1573-3904
    Keywords: insect oostatic factor ; Neb-TMOF and analogs ; trypsin modulating oostatic factor ; trypsin modulating peptide
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Summary Neb-TMOF, the trypsin modulating oostatic factor of gray fleshflyNeobellieria bullata, is a hexapeptide with the following sequence: H-Asn-Pro-Thr-Asn-Leu-His-OH. It has been isolated from vitellogenic ovaries in 1994. TMOF, the newly discovered insect peptide, inhibits trypsin biosynthesis in the gut, lowers yolk polypeptide concentration in the hemolymph and strongly inhibits ecdysone biosynthesis by larval ring glands. It is interesting that this short non-protected peptide contains in its molecule two Asn residues at positions 1 and 4 and His at its C-terminus. To obtain information about the role of the His-6 and Asn-4 residues we synthesised two series of Neb-TMOF analogs, modified: (1) in position 6 byd-His (I), His(Bzl) (II) and Phe(p-X) derivatives, where X=NH2 (III), NO2 (IV), OEt (V) and OH (VI) and (2) in position 4 by such amino acid residues as Ser (VII), Thr (VIII), Gly (IX), Asp (X), Glu (XI) andd-Asn (XII). The influence of these peptides on trypsin biosynthesis inN. bullata was determinedin vivo. In preliminary investigations, we found that Neb-TMOF, [Phe(NH2)6], and [Phe(NO2)6]-Neb-TMOF inhibited trypsin biosynthesis, whereas [d-His)6]- and [d-His(Bzl)6]-Neb-TMOF were inactive. In further biological studies performedin vitro on heart ofTenebrio molitor were found that-TMOF and [Phe(p-NH2)6]-Neb-TMOF showed weak cardioexcitatory activity, about 30% of the cardioexcitatory activity of proctolin, an insect neuromodulating peptide.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02443493
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    Paper (German National Licenses)
    Fulltext
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