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LymnaDFamides, a new family of neuropeptides from the pond snail, Lymnaea stagnalis. Clue to cholecystokinin immunoreactivity in invertebrates?

作者信息

Johnsen A H, Rehfeld J F

机构信息

Department of Clinical Biochemistry, Rigshospitalet University of Copenhagen, Denmark.

出版信息

Eur J Biochem. 1993 Apr 15;213(2):875-9. doi: 10.1111/j.1432-1033.1993.tb17831.x.

DOI:10.1111/j.1432-1033.1993.tb17831.x
PMID:8477756
Abstract

Five tridecapeptides have been identified from the central nervous system of the pond snail, Lymnaea stagnalis. The sequences are Pro-Xaa-Asp-Arg-Ile-Ser-Yaa-Ser-Ala-Phe-Ser-Asp-Phe. NH2, where Xaa is either Tyr or Phe and Yaa either Asn, Ser or Gly. The peptides are named lymnaDFamides to acknowledge identity with the C-terminal dipeptide of the mammalian neuropeptides, cholecystokinin (CCK) and gastrin. They were detected by an antiserum that recognizes the biologically active C-termini of cholecystokinin and gastrin. LymnaDFamide-1 (Xaa = Tyr and Yaa = Asn) had no effect on trout gallbladder, which responds equally to CCK and gastrin. We propose that the lymnaDFamides belong to an Asp-Phe-amide superfamily, which includes CCK and gastrin, and suggest that the widespread CCK/gastrin immunoreactivity in invertebrates is due to peptides belonging to such a superfamily.

摘要

相似文献

1
LymnaDFamides, a new family of neuropeptides from the pond snail, Lymnaea stagnalis. Clue to cholecystokinin immunoreactivity in invertebrates?
Eur J Biochem. 1993 Apr 15;213(2):875-9. doi: 10.1111/j.1432-1033.1993.tb17831.x.
2
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Ann N Y Acad Sci. 1994 Mar 23;713:404-6. doi: 10.1111/j.1749-6632.1994.tb44108.x.
3
Is invertebrate CCK-like immunoreactivity caused by Asp-Phe-amides similar to the lymnaDFamides (a new family of molluscan neuropeptides)?
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Phylogeny of the cholecystokinin/gastrin family.胆囊收缩素/胃泌素家族的系统发育。
Front Neuroendocrinol. 1998 Apr;19(2):73-99. doi: 10.1006/frne.1997.0163.
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Conformational analysis of possible biologically active (receptor-bound) conformations of peptides derived from cholecystokinin, cerulein and little gastrin and the opiate peptide, Met-enkephalin.对源自胆囊收缩素、雨蛙肽和小胃泌素的肽以及阿片肽甲硫氨酸脑啡肽的可能生物活性(受体结合)构象的构象分析。
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Structure-activity relationships for myotropic activity of the gastrin/cholecystokinin-like insect sulfakinins.促胃泌素/缩胆囊素样昆虫速激肽的肌动活性的构效关系。
Pept Res. 1989 Mar-Apr;2(2):171-7.
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Cionin, a protochordean hybrid of cholecystokinin and gastrin: biological activity in mammalian systems.西奥宁,一种胆囊收缩素与胃泌素的原索动物杂交体:在哺乳动物系统中的生物活性。
Am J Physiol. 1991 Jun;260(6 Pt 1):G976-82. doi: 10.1152/ajpgi.1991.260.6.G977.
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Role of CCK in gallbladder function.胆囊收缩素在胆囊功能中的作用。
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Neuropeptides Gly-Asp-Pro-Phe-Leu-Arg-Phe-amide (GDPFLRFamide) and Ser-Asp-Pro-Phe-Leu-Arg-Phe-amide (SDPFLRFamide) are encoded by an exon 3' to Phe-Met-Arg-Phe-NH2 (FMRFamide) in the snail Lymnaea stagnalis.神经肽甘氨酸-天冬氨酸-脯氨酸-苯丙氨酸-亮氨酸-精氨酸-苯丙氨酸酰胺(GDPFLRFamide)和丝氨酸-天冬氨酸-脯氨酸-苯丙氨酸-亮氨酸-精氨酸-苯丙氨酸酰胺(SDPFLRFamide)由椎实螺(Lymnaea stagnalis)中位于苯丙氨酸-甲硫氨酸-精氨酸-苯丙氨酸-氨基(FMRFamide)下游3'的一个外显子编码。
J Neurosci. 1991 Mar;11(3):740-5. doi: 10.1523/JNEUROSCI.11-03-00740.1991.

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Cell Mol Life Sci. 2022 Mar 14;79(3):188. doi: 10.1007/s00018-022-04214-4.
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Localisation of sulfakinin neuronal pathways in the blowfly Calliphora vomitoria.
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Cell Tissue Res. 1994 Jan;275(1):177-86. doi: 10.1007/BF00305385.