Ghrelin-like peptide with fatty acid modification and O-glycosylation in the red stingray, Dasyatis akajei.

Ghrelin-like peptide with fatty acid modification and O-glycosylation in the red stingray, Dasyatis akajei.
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DOI:
10.1186/1471-2091-10-30
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发表时间:
2009-12-14
期刊:
影响因子:
--
通讯作者:
Kangawa K
Kangawa K
中科院分区:
生物4区
文献类型:
--
作者:
Kaiya H;Kodama S;Ishiguro K;Matsuda K;Uchiyama M;Miyazato M;Kangawa K

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Ghrelin(GRLN)是一种刺激食欲和释放生长激素(GH)的肽,主要由从鱼类到哺乳动物的各种脊椎动物的胃合成和分泌。在这里,我们报告的GRLN样肽(GRLN-LP)的软骨鱼,红黄貂鱼,Dasyatis akajei。纯化的肽含有16个氨基酸(GVSFHPQPRS 10 TSKPSA),并且在位置3处的丝氨酸残基被正辛酸修饰。这种修改是GRLN的特点。N-末端的6个氨基酸残基(GVSFHP)与最近鉴定的另一种板鳃鲨GRLN-LP相同,但与其他GRLN肽的同一性较低。因此,我们将这种肽命名为黄貂鱼GRLN-LP。独特的是,黄貂鱼GRLN-LP是O-糖基化的粘蛋白型聚糖链[N-乙酰基己糖胺(HexNAc)3己糖(Hex)2]在位置11的苏氨酸(Thr-11)或位置10的丝氨酸(Ser-10)和Thr-11。用大鼠GHS-R1 a表达细胞系测定细胞内Ca 2+浓度,结果表明,O-聚糖酶对糖链结构的去除使黄貂鱼GRLN-LP的体外活性降低,提示糖链结构对黄貂鱼GRLN-LP的活性维持起着重要作用。本研究揭示了GRLN和GRLN-LP在脊椎动物中的结构多样性。
Ghrelin (GRLN) is now known to be an appetite-stimulating and growth hormone (GH)-releasing peptide that is predominantly synthesized and secreted from the stomachs of various vertebrate species from fish to mammals. Here, we report a GRLN-like peptide (GRLN-LP) in a cartilaginous fish, the red stingray, Dasyatis akajei. The purified peptide contains 16 amino acids (GVSFHPQPRS10TSKPSA), and the serine residue at position 3 is modified by n-octanoic acid. The modification is the characteristic of GRLN. The six N-terminal amino acid residues (GVSFHP) were identical to another elasmobranch shark GRLN-LP that was recently identified although it had low identity with other GRLN peptides. Therefore, we designated this peptide stingray GRLN-LP. Uniquely, stingray GRLN-LP was O-glycosylated with mucin-type glycan chains [N-acetyl hexosamine (HexNAc)3 hexose(Hex)2] at threonine at position 11 (Thr-11) or both serine at position 10 (Ser-10) and Thr-11. Removal of the glycan structure by O-glycanase made the in vitro activity of stingray GRLN-LP decreased when it was evaluated by the increase in intracellular Ca2+ concentrations using a rat GHS-R1a-expressing cell line, suggesting that the glycan structure plays an important role for maintaining the activity of stingray GRLN-LP. This study reveals the structural diversity of GRLN and GRLN-LP in vertebrates.
DOI: 10.1016/s0303-7207(96)03945-7
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影响因子: 11.1
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