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鲑鱼促黑素细胞激素的化学和生物学特性

Chemical and biological characterization of salmon melanocyte-stimulating hormones.

作者信息

Kawauchi H, Kawazoe I, Adachi Y, Buckley D I, Ramachandran J

出版信息

Gen Comp Endocrinol. 1984 Jan;53(1):37-48. doi: 10.1016/0016-6480(84)90222-3.

DOI:10.1016/0016-6480(84)90222-3
PMID:6325292
Abstract

Ten peptides related to melanocyto-stimulating hormone (MSH) have been identified in an acid acetone extract of the chum salmon pituitary. All these peptides are related to the alpha-MSH and beta-MSH families, but no peptide related to gamma-MSH has been found. This result is in accordance with the finding that the gamma-MSH segment is deleted from the N-terminal peptide of salmon pro-opiocortin (NPP I). Based on the structures of newly isolated peptides, the maturation process of MSH is discussed. The major components of salmon MSH were tested for biological activities. In the lipolytic assay with rabbit fat cells, alpha-MSH I and alpha-MSH II were equipotent, but beta-MSH I and NPP I exhibited very low or no activity. On the other hand, the des-acetyl-alpha-MSH I was found to be four times as potent as alpha-MSH I in this assay. The steroidogenic activities of alpha-MSH I and N-des-acetyl-alpha-MSH I were approximately 0.05% of the potency of ovine ACTH. All other peptides exhibited less than 0.01% potency. Salmon alpha-MSHs were found to be somewhat more potent melanophore-stimulating agents than the beta-MSHs.

摘要

在大麻哈鱼垂体的酸性丙酮提取物中已鉴定出十种与促黑素细胞激素(MSH)相关的肽。所有这些肽都与α-MSH和β-MSH家族相关,但未发现与γ-MSH相关的肽。这一结果与鲑鱼阿黑皮素原(NPP I)的N端肽中γ-MSH片段缺失的发现一致。基于新分离肽的结构,讨论了MSH的成熟过程。对大麻哈鱼MSH的主要成分进行了生物活性测试。在兔脂肪细胞的脂解试验中,α-MSH I和α-MSH II活性相当,但β-MSH I和NPP I活性极低或无活性。另一方面,在该试验中发现去乙酰-α-MSH I的活性是α-MSH I的四倍。α-MSH I和N-去乙酰-α-MSH I的类固醇生成活性约为绵羊促肾上腺皮质激素活性的0.05%。所有其他肽的活性均低于0.01%。发现大麻哈鱼α-MSH作为黑素细胞刺激剂比β-MSH稍有效。

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