perisulfakinin and leucosulfakinin

perisulfakinin has been researched along with leucosulfakinin* in 2 studies

Other Studies

2 other study(ies) available for perisulfakinin and leucosulfakinin

Article	Year
In vitro release of digestive enzymes by FMRF amide related neuropeptides and analogues in the lepidopteran insect Opisina arenosella (Walk.). Peptides, 2002, Volume: 23, Issue:10 The insect neuropeptides FMRF amide, leucomyosupressin (LMS) and neuropeptide analogues leucosulfakinins (FLSK and LSK II Ser (SO(3)H)), perisulfakinin (PSK), proleucosulfakinin (PLSK), 14A[phi1]WP-I, 542phi1, and 378A[5b]WP-I were assayed for their effects on the release of amylase and protease from the midgut tissue of larvae of Opisina arenosella. In the bioassay, empty midgut tubes ligated at both ends using hair were incubated with insect saline containing neuropeptides/analogues in a bioassay apparatus at 37 degrees C for 30 min. After incubation the contents of the midgut preparations were analyzed for amylase and protease activity. In control experiments, the midgut preparations were incubated in insect saline without neuropeptides. The results of the study reveal that for stimulating amylase release from midgut tissue, the peptides require an FXRF amide (X may be methionine or leucine) sequence at the C-terminal. The presence of HMRF amide at C-terminal of peptides may inhibit the release of amylase. Meanwhile, peptides with both FMRF and HMRF amide sequence at the C-terminal are found to be effective in stimulating protease release. The tetrapeptide segment at the C-terminal probably represent the active core of the neuropeptide. Topics: Amino Acid Sequence; Amylases; Animals; Digestive System; Endopeptidases; FMRFamide; In Vitro Techniques; Insect Hormones; Larva; Lepidoptera; Leucine; Methionine; Molecular Sequence Data; Neuropeptides	2002
Isolation and structure of two gastrin/CCK-like neuropeptides from the American cockroach homologous to the leucosulfakinins. Neuropeptides, 1989, Volume: 14, Issue:3 Perisulfakinin, a peptide with sequence similarity to gastrin and cholecystokinin, was isolated from the corpora cardiaca of the American cockroach. Its sequence was determined to be Glu-Gln-Phe H-Asp-Asp-Tyr(SO3H)-Gly-His-Met-Arg-Phe-amide. The peptide induced hindgut contractions in the same species at concentrations as low as 250 pM. A related non-sulfated peptide was also isolated and sequenced; it was found to be identical with non-sulfated leucosulfakinin II (pGlu-Ser-Asp-Asp-Tyr-Gly-His-Met-Arg-Phe-amide). This peptide did not stimulate hindgut contractions. The structures of the cockroach peptides of the leucosulfakinin family are thus much more conserved than the cockroach hypertrehalosemic hormones. Topics: Amino Acid Sequence; Animals; Cholecystokinin; Cockroaches; Gastrins; Molecular Sequence Data; Neuropeptides; Sequence Homology, Nucleic Acid	1989

Article

Year

In vitro release of digestive enzymes by FMRF amide related neuropeptides and analogues in the lepidopteran insect Opisina arenosella (Walk.).

Peptides, 2002, Volume: 23, Issue:10

The insect neuropeptides FMRF amide, leucomyosupressin (LMS) and neuropeptide analogues leucosulfakinins (FLSK and LSK II Ser (SO(3)H)), perisulfakinin (PSK), proleucosulfakinin (PLSK), 14A[phi1]WP-I, 542phi1, and 378A[5b]WP-I were assayed for their effects on the release of amylase and protease from the midgut tissue of larvae of Opisina arenosella. In the bioassay, empty midgut tubes ligated at both ends using hair were incubated with insect saline containing neuropeptides/analogues in a bioassay apparatus at 37 degrees C for 30 min. After incubation the contents of the midgut preparations were analyzed for amylase and protease activity. In control experiments, the midgut preparations were incubated in insect saline without neuropeptides. The results of the study reveal that for stimulating amylase release from midgut tissue, the peptides require an FXRF amide (X may be methionine or leucine) sequence at the C-terminal. The presence of HMRF amide at C-terminal of peptides may inhibit the release of amylase. Meanwhile, peptides with both FMRF and HMRF amide sequence at the C-terminal are found to be effective in stimulating protease release. The tetrapeptide segment at the C-terminal probably represent the active core of the neuropeptide.

Topics: Amino Acid Sequence; Amylases; Animals; Digestive System; Endopeptidases; FMRFamide; In Vitro Techniques; Insect Hormones; Larva; Lepidoptera; Leucine; Methionine; Molecular Sequence Data; Neuropeptides

2002

Isolation and structure of two gastrin/CCK-like neuropeptides from the American cockroach homologous to the leucosulfakinins.

Neuropeptides, 1989, Volume: 14, Issue:3

Perisulfakinin, a peptide with sequence similarity to gastrin and cholecystokinin, was isolated from the corpora cardiaca of the American cockroach. Its sequence was determined to be Glu-Gln-Phe H-Asp-Asp-Tyr(SO3H)-Gly-His-Met-Arg-Phe-amide. The peptide induced hindgut contractions in the same species at concentrations as low as 250 pM. A related non-sulfated peptide was also isolated and sequenced; it was found to be identical with non-sulfated leucosulfakinin II (pGlu-Ser-Asp-Asp-Tyr-Gly-His-Met-Arg-Phe-amide). This peptide did not stimulate hindgut contractions. The structures of the cockroach peptides of the leucosulfakinin family are thus much more conserved than the cockroach hypertrehalosemic hormones.

Topics: Amino Acid Sequence; Animals; Cholecystokinin; Cockroaches; Gastrins; Molecular Sequence Data; Neuropeptides; Sequence Homology, Nucleic Acid

1989