Isolation and primary structure of a novel pheromonotropic neuropeptide structurally related to leucopyrokinin from the armyworm larvae, Pseudaletia separata

Matsumoto, Shogo; Fónagy, Adrien; Kurihara, Masaaki; Uchiumi, Kyoichi; Nagamine, Toshihiro; Chijimatsu, Masao; Mitsui, Takashi

doi:10.1016/0006-291x(92)91765-i

Cited by 97 publications

(26 citation statements)

References 15 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Third, our analysis of amplification products derived from genomic templates (Table 1) indicates that the preprohormone coding region shown in Fig. 1 is discontinuous (36).…”

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Structural organization of the Helicoverpa zea gene encoding the precursor protein for pheromone biosynthesis-activating neuropeptide and other neuropeptides.

Peter

Knipple

Roelofs

1994

Proc. Natl. Acad. Sci. U.S.A.

125

View full text Add to dashboard Cite

show abstract

“…Third, our analysis of amplification products derived from genomic templates (Table 1) indicates that the preprohormone coding region shown in Fig. 1 is discontinuous (36).…”

Section: Discussionmentioning

confidence: 99%

“…3 (Fig. 3), shows homology to apheromonotropin isolated from larvae of the armyworm Pseudaletia separata (36). A second peptide, Asn2k-Leu47 (Fig.…”

Section: Discussionmentioning

confidence: 99%

Structural organization of the Helicoverpa zea gene encoding the precursor protein for pheromone biosynthesis-activating neuropeptide and other neuropeptides.

Peter

Knipple

Roelofs

1994

Proc. Natl. Acad. Sci. U.S.A.

125

View full text Add to dashboard Cite

show abstract

“…Widely distributed across numerous insect species, the FXPRLamides include melanization peptides (Matsumoto et al, 1992), pheromone biosynthesis activating neuropeptides (PBANs; Iglesias et al, 2002) and egg diapause induction peptides (Nachman et al, 1993). FXPRLamides also include peptides that affect visceral muscle function.…”

Section: Classification Of Tegpgmwfgprla (Mas-pk-1)mentioning

confidence: 99%

Sequence and expression of theCAPA/CAP2bgene in the tobacco hawkmoth,Manduca sexta

Loi

Tublitz

2004

Journal of Experimental Biology

View full text Add to dashboard Cite

SUMMARY The gene coding for cardioacceleratory peptide 2b (CAP2b; pELYAFPRV) has been isolated and sequenced from the moth Manduca sexta (GenBank accession #AY649544). Because of its significant homology to the CAPAgene in Drosophila melanogaster, this gene is called the Manduca CAPA gene. The Manduca CAPA gene is 958 nucleotides long with 29 untranslated nucleotides from the beginning of the sequence to the putative start initiation site. The CAPA gene has a single open reading frame,441 nucleotides long, that codes for a predicted precursor protein of 147 amino acids. The predicted prepropeptide encodes a single copy of each of three deduced propeptides, a CAP2b propeptide, with a Q substituted for an E at the N-terminus (QLYAFPRVa), and two novel CAP2b-related propeptides(DGVLNLYPFPRVa and TEGPGMWFGPRLa). To reduce confusion and to adopt a more standardized nomenclature, we rename pELYAFPRVa as Mas-CAPA-1 and assign the names of Mas-CAPA-2 to DGVLNLYPFPRVa and Mas-PK-1 (Pyrokinin-1) to TEGPGMWFGPRLa. The spatial and temporal expression pattern of the CAPA gene in the Manduca central nervous system (CNS) was determined in all major post-embryonic stages using in situ hybridization techniques. The CAPA gene is expressed in a total of 27 pairs of neurons in the post-embryonic Manduca CNS. A total of 16 pairs of cells is observed in the brain, two pairs in the sub-esophageal ganglion (SEG), one pair in the third thoracic ganglion (T3), one pair in each unfused abdominal ganglion(A1–A6) and two pairs in the fused terminal ganglion. The mRNA from the CAPA gene is present in nearly every ganglion in each post-embryonic stage. The number of cells expressing the CAPA gene varies during post-embryonic life, starting at 54 cells in first-instar larvae and declining to a minimum of 14 cells midway through adult development.

show abstract

“…In addition, it has been found that this C-terminal pentapeptide (where Xxx ϭ Ser, Gly, Thr, Val) is homologous with the C-terminal pentapeptide sequence of other families of insect neuropeptides: the pyrokinins (PK) and the myotropins (MT) (myotropic peptides isolated from Leucophaea maderae and Locusta migratoria) (32)(33)(34)(35)(36)(37)(38)(39), and also with the C-terminal region of Pseudaletia separata pheromonotropin (Pss-PT) (40) and Bombyx mori diapause hormone (Bom-DH) (41).…”

mentioning

confidence: 99%

Backbone Cyclic Peptide Antagonists, Derived from the Insect Pheromone Biosynthesis Activating Neuropeptide, Inhibit Sex Pheromone Biosynthesis in Moths

Altstein¹,

Ben-Aziz²,

Daniel³

et al. 1999

Journal of Biological Chemistry

View full text Add to dashboard Cite

We describe an application of the backbone cyclization and cycloscan concept for the design and synthesis of pheromone biosynthesis activating neuropeptide (PBAN) antagonists capable of inhibiting sex pheromone biosynthesis in Heliothis peltigera female moths. Two backbone cyclic (BBC) sub-libraries were designed and synthesized. The structure of the first sub-library ([Arg 27 ]PBAN27-33NH 2 , termed the Ser sub-library) was based on the active C-terminal hexapeptide sequence (Tyr-Phe-Ser-Pro-Arg-Leu-NH 2 ) of PBAN1-33NH 2 , which was found to comprise its active core. It is well established that the activation of multiple receptors by the same peptide arises from the ability of a given peptide to exist in different interchangeable bioactive conformations (1). To attain receptor selectivity it is, therefore, essential to restrict the conformational space of a peptide so it can attain one bioactive conformation.Cyclization is an important and attractive way to restrict the conformational space of peptidic structures (1). Conformationally restricted peptides containing medium and long range cyclizations have been mainly prepared following the same modes of cyclization of naturally occurring peptides. These include end-to-end, side-chain-to-side-chain, and side-chain-toend (2). These modes of cyclization involve modifications of side chains and ends which in many cases are essential for bioactivity, and therefore their modification causes loss of activity. Also, these modes of cyclization are not sufficient to screen effectively the conformational space available for a linear peptide with a given sequence. To overcome these limitations, we have introduced two methods called backbone cyclization (2) and cycloscan (3).Backbone cyclization is a general method by which a conformational constraint is imposed on peptides through the connection of the N ␣ and/or C ␣ atoms in the peptide backbone to each other or to side chains or to the carboxyl and amino ends (2). Thus, the cyclization can be performed while retaining the functionality and the activity of the side chains. Backbone cyclization allows nine new modes of cyclization in addition to the four modes in naturally occurring peptides. Preparation of backbone cyclic (BBC) 1 peptides involves the use of a large variety of orthogonally protected N ␣ and C ␣ (-amino-, -carboxy-, and -thio-alkyl) amino acids building units (4 -6). Synthetic procedures have been developed to incorporate these building units into peptides using the solid phase methodology (7,8).The advantages of backbone cyclization over the naturally occurring modes of cyclization are because of the immense variability of spatial orientation of the constitute residues which result from the multiple anchoring points within a chain or between chains. This allows us to screen the conformational space of a given peptide in an extremely efficient manner. Furthermore, most of the modes of backbone cyclization do not involve chemical modifications of side chains which are essential for biological activity. Ba...

show abstract

Isolation and primary structure of a novel pheromonotropic neuropeptide structurally related to leucopyrokinin from the armyworm larvae, Pseudaletia separata

Cited by 97 publications

References 15 publications

Structural organization of the Helicoverpa zea gene encoding the precursor protein for pheromone biosynthesis-activating neuropeptide and other neuropeptides.

Structural organization of the Helicoverpa zea gene encoding the precursor protein for pheromone biosynthesis-activating neuropeptide and other neuropeptides.

Sequence and expression of theCAPA/CAP2bgene in the tobacco hawkmoth,Manduca sexta

Backbone Cyclic Peptide Antagonists, Derived from the Insect Pheromone Biosynthesis Activating Neuropeptide, Inhibit Sex Pheromone Biosynthesis in Moths

Contact Info

Product

Resources

About