Evolution of a Molluscan Cardioregulatory Neuropeptide
Evolution of a Molluscan Cardioregulatory Neuropeptide
复制标题
软体动物心脏调节神经肽的进化
DOI：
10.1093/icb/26.4.1007
复制
发表时间：
1986
影响因子：
2.6
通讯作者：
D. Price
中科院分区：
文献类型：
--
作者：
D. Price
概要。心脏兴奋性神经肽 FMRFamide 最初是从蛤中发现的，但现在已在其他几种软体动物中得到证实。尽管在某些物种中与相关肽共存，但它可能存在于整个软体动物门中。例如，我在这里报告了在中腹足类 Pomacea paludosa 中发现的肽苯丙氨酰-亮氨酰-精氨酰-苯丙氨酸酰胺 (FLRFamide)，它占 FMRFamide 样活性的 10-20%。该肽也可能是其他物种中 FMRFamide 样活性的次要成分。肺蜗牛具有几种密切相关的FLRFamide七肽类似物，这些是它们所独有的，例如从Helix aspersa中分离出的焦谷氨酰-天冬氨酰-脯氨酰-苯丙氨酰-亮氨酰-精氨酰-苯丙氨酸酰胺(pQDPFLRFamide)。已分离的另外两种肺七肽可能仅在 N 端氨基酸残基上与 pQDPFLRFamide 不同。七肽在其存在的物种中负责大部分 FMRFamide 样活性。
尽管四肽 FMRFamide 和 FLRFamide 对各种软体动物组织具有几乎相同的活性，但七肽对某些肺肌肉具有与四肽不同的活性。 1 试图通过假设导致现代肺动物的腹足动物系中存在基因重复来解释现代肺动物中发现的肽结构和功能多样性的进化。
SYNOPSIS. The cardioexcitatory neuropeptide FMRFamide was first identified from a clam, but has now been demonstrated in several other molluscs. It is probably present throughout the molluscan phylum though co-existing with related peptides in some species. For example, I report here the finding of the peptide phenylalanyl-leucyl-arginyl-phenylalanine amide (FLRFamide) in the mesogastropod Pomacea paludosa where it accounts for 10–20% of the total FMRFamide-like activity. This peptide may be a minor component of the FMRFamide-like activity in other species as well. The pulmonate snails have several, closely-related, heptapeptide analogs of FLRFamide that are unique to them, such as pyroglutamyl-aspartyl-prolyl-phenylalanyl-leucyl-arginyl-phenylalanine amide (pQDPFLRFamide) which was isolated from Helix aspersa . Two additional pulmonate heptapeptides that have been isolated probably differ from pQDPFLRFamide only in their N-terminal amino acid residues. The heptapeptides account for most of the FMRFamidelike activity in the species in which they occur.
Though the tetrapeptides FMRFamide and FLRFamide have virtually identical activities on various molluscan tissues, the heptapeptides have activity that is distinct from the tetrapeptides on some pulmonate muscles. 1 have attempted to explain the evolution of this diversity of peptide structure and function found in the modern pulmonates by postulating a gene duplication in the gastropod line leading to them.