Molecular cloning of a functional allatostatin gut/brain receptor and an allatostatin preprohormone from the silkworm Bombyx mori.

Thomas Secher; C Lenz; G Cazzamali; Gunnar Sørensen; M Williamson; G N Hansen; P Svane; C J Grimmelikhuijzen

doi:10.1074/jbc.M106675200

Molecular cloning of a functional allatostatin gut/brain receptor and an allatostatin preprohormone from the silkworm Bombyx mori.

Thomas Secher, C Lenz, G Cazzamali, Gunnar Sørensen, M Williamson, G N Hansen, P Svane, C J Grimmelikhuijzen

70 Citations (Scopus)

Abstract

The cockroach-type or A-type allatostatins are inhibitory insect neuropeptides with the C-terminal sequence Tyr/Phe-X-Phe-Gly-Leu-NH(2). Here, we have cloned an A-type allatostatin receptor from the silkworm Bombyx mori (BAR). BAR is 361 amino acid residues long, has seven transmembrane domains, shows 60% amino acid residue identity with the first Drosophila allatostatin receptor (DAR-1), and 48% identity with the second Drosophila allatostatin receptor (DAR-2). The BAR gene has two introns and three exons. These two introns coincide with and have the same intron phasing as two introns in the DAR-1 and DAR-2 genes, showing that the three receptors are not only structurally but also evolutionarily related. Furthermore, we have cloned a Bombyx allatostatin preprohormone that contains eight different A-type allatostatins. Chinese hamster ovary cells permanently transfected with BAR DNA react on the addition of 4 x 10(-9)M Bombyx A-type allatostatins with a second messenger cascade (measured as bioluminescence), showing that BAR is a functional A-type allatostatin receptor. Southern blots suggest that Bombyx has at least one other BAR-related gene in addition to the BAR gene described in this paper. Northern blots and quantitative reverse transcriptase-polymerase chain reaction of different larval tissues show that BAR mRNA is mainly expressed in the gut and to a much lesser extent in the brain. To our knowledge, this is the first report on the molecular cloning and functional expression of an insect gut/brain peptide hormone receptor.

Original language	English
Journal	Journal of Biological Chemistry
Volume	276
Issue number	50
Pages (from-to)	47052-60
Number of pages	8
ISSN	0021-9258
DOIs	https://doi.org/10.1074/jbc.M106675200
Publication status	Published - 2001

Access to Document

10.1074/jbc.M106675200

Cite this

@article{14edfba0ec2811dcbee902004c4f4f50,

title = "Molecular cloning of a functional allatostatin gut/brain receptor and an allatostatin preprohormone from the silkworm Bombyx mori.",

abstract = "The cockroach-type or A-type allatostatins are inhibitory insect neuropeptides with the C-terminal sequence Tyr/Phe-X-Phe-Gly-Leu-NH(2). Here, we have cloned an A-type allatostatin receptor from the silkworm Bombyx mori (BAR). BAR is 361 amino acid residues long, has seven transmembrane domains, shows 60% amino acid residue identity with the first Drosophila allatostatin receptor (DAR-1), and 48% identity with the second Drosophila allatostatin receptor (DAR-2). The BAR gene has two introns and three exons. These two introns coincide with and have the same intron phasing as two introns in the DAR-1 and DAR-2 genes, showing that the three receptors are not only structurally but also evolutionarily related. Furthermore, we have cloned a Bombyx allatostatin preprohormone that contains eight different A-type allatostatins. Chinese hamster ovary cells permanently transfected with BAR DNA react on the addition of 4 x 10(-9)M Bombyx A-type allatostatins with a second messenger cascade (measured as bioluminescence), showing that BAR is a functional A-type allatostatin receptor. Southern blots suggest that Bombyx has at least one other BAR-related gene in addition to the BAR gene described in this paper. Northern blots and quantitative reverse transcriptase-polymerase chain reaction of different larval tissues show that BAR mRNA is mainly expressed in the gut and to a much lesser extent in the brain. To our knowledge, this is the first report on the molecular cloning and functional expression of an insect gut/brain peptide hormone receptor.",

author = "Thomas Secher and C Lenz and G Cazzamali and Gunnar S{\o}rensen and M Williamson and Hansen, {G N} and P Svane and Grimmelikhuijzen, {C J}",

note = "Keywords: Amino Acid Sequence; Animals; Blotting, Northern; Blotting, Southern; Bombyx; Brain; CHO Cells; Cloning, Molecular; Cricetinae; DNA, Complementary; Digestive System; Dose-Response Relationship, Drug; Drosophila; Drosophila Proteins; Evolution, Molecular; Exons; Hormones; Insect Proteins; Introns; Kinetics; Molecular Sequence Data; Neuropeptides; Phylogeny; Protein Precursors; RNA, Messenger; Receptors, Cell Surface; Receptors, G-Protein-Coupled; Receptors, Neuropeptide; Reverse Transcriptase Polymerase Chain Reaction; Sequence Homology, Amino Acid; Signal Transduction; Tissue Distribution; Transfection",

year = "2001",

doi = "10.1074/jbc.M106675200",

language = "English",

volume = "276",

pages = "47052--60",

journal = "Journal of Biological Chemistry",

issn = "0021-9258",

publisher = "American Society for Biochemistry and Molecular Biology, Inc.",

number = "50",

}

TY - JOUR

T1 - Molecular cloning of a functional allatostatin gut/brain receptor and an allatostatin preprohormone from the silkworm Bombyx mori.

AU - Secher, Thomas

AU - Lenz, C

AU - Cazzamali, G

AU - Sørensen, Gunnar

AU - Williamson, M

AU - Hansen, G N

AU - Svane, P

AU - Grimmelikhuijzen, C J

N1 - Keywords: Amino Acid Sequence; Animals; Blotting, Northern; Blotting, Southern; Bombyx; Brain; CHO Cells; Cloning, Molecular; Cricetinae; DNA, Complementary; Digestive System; Dose-Response Relationship, Drug; Drosophila; Drosophila Proteins; Evolution, Molecular; Exons; Hormones; Insect Proteins; Introns; Kinetics; Molecular Sequence Data; Neuropeptides; Phylogeny; Protein Precursors; RNA, Messenger; Receptors, Cell Surface; Receptors, G-Protein-Coupled; Receptors, Neuropeptide; Reverse Transcriptase Polymerase Chain Reaction; Sequence Homology, Amino Acid; Signal Transduction; Tissue Distribution; Transfection

PY - 2001

Y1 - 2001

N2 - The cockroach-type or A-type allatostatins are inhibitory insect neuropeptides with the C-terminal sequence Tyr/Phe-X-Phe-Gly-Leu-NH(2). Here, we have cloned an A-type allatostatin receptor from the silkworm Bombyx mori (BAR). BAR is 361 amino acid residues long, has seven transmembrane domains, shows 60% amino acid residue identity with the first Drosophila allatostatin receptor (DAR-1), and 48% identity with the second Drosophila allatostatin receptor (DAR-2). The BAR gene has two introns and three exons. These two introns coincide with and have the same intron phasing as two introns in the DAR-1 and DAR-2 genes, showing that the three receptors are not only structurally but also evolutionarily related. Furthermore, we have cloned a Bombyx allatostatin preprohormone that contains eight different A-type allatostatins. Chinese hamster ovary cells permanently transfected with BAR DNA react on the addition of 4 x 10(-9)M Bombyx A-type allatostatins with a second messenger cascade (measured as bioluminescence), showing that BAR is a functional A-type allatostatin receptor. Southern blots suggest that Bombyx has at least one other BAR-related gene in addition to the BAR gene described in this paper. Northern blots and quantitative reverse transcriptase-polymerase chain reaction of different larval tissues show that BAR mRNA is mainly expressed in the gut and to a much lesser extent in the brain. To our knowledge, this is the first report on the molecular cloning and functional expression of an insect gut/brain peptide hormone receptor.

AB - The cockroach-type or A-type allatostatins are inhibitory insect neuropeptides with the C-terminal sequence Tyr/Phe-X-Phe-Gly-Leu-NH(2). Here, we have cloned an A-type allatostatin receptor from the silkworm Bombyx mori (BAR). BAR is 361 amino acid residues long, has seven transmembrane domains, shows 60% amino acid residue identity with the first Drosophila allatostatin receptor (DAR-1), and 48% identity with the second Drosophila allatostatin receptor (DAR-2). The BAR gene has two introns and three exons. These two introns coincide with and have the same intron phasing as two introns in the DAR-1 and DAR-2 genes, showing that the three receptors are not only structurally but also evolutionarily related. Furthermore, we have cloned a Bombyx allatostatin preprohormone that contains eight different A-type allatostatins. Chinese hamster ovary cells permanently transfected with BAR DNA react on the addition of 4 x 10(-9)M Bombyx A-type allatostatins with a second messenger cascade (measured as bioluminescence), showing that BAR is a functional A-type allatostatin receptor. Southern blots suggest that Bombyx has at least one other BAR-related gene in addition to the BAR gene described in this paper. Northern blots and quantitative reverse transcriptase-polymerase chain reaction of different larval tissues show that BAR mRNA is mainly expressed in the gut and to a much lesser extent in the brain. To our knowledge, this is the first report on the molecular cloning and functional expression of an insect gut/brain peptide hormone receptor.

U2 - 10.1074/jbc.M106675200

DO - 10.1074/jbc.M106675200

M3 - Journal article

C2 - 11590150

SN - 0021-9258

VL - 276

SP - 47052

EP - 47060

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

IS - 50

ER -

Molecular cloning of a functional allatostatin gut/brain receptor and an allatostatin preprohormone from the silkworm Bombyx mori.

Abstract

Access to Document

Fingerprint

Cite this