原代大鼠雪旺细胞上α-促黑素细胞激素受体的增溶部分特性分析

Solubilisation partial characterisation of the alpha-MSH receptor on primary rat Schwann cells.

作者信息

Dyer J K, Ahmed A R, Oliver G W, Poulton C W, Haynes L W

机构信息

Department of Zoology, School of Biological Sciences, University of Bristol, UK.

出版信息

FEBS Lett. 1993 Dec 20;336(1):103-6. doi: 10.1016/0014-5793(93)81619-b.

DOI:10.1016/0014-5793(93)81619-b

PMID:8262190

Abstract

The ACTH/MSH melanocortin core peptide sequence possesses neurotrophic properties in peripheral nerve. During functional neuroanatomical recovery after damage to peripheral nerves, Schwann cells play a significant role in facilitating regeneration. Here we employ a modified super-potent alpha-MSH analogue to solubilise alpha-MSH receptor proteins from cultured primary rat Schwann cells. [125I-Tyr2,Nle4,D-Phe7,ATB-Lys11]-alpha-MSH photoaffinity labelled proteins from Schwann cells were analyzed by SDS-PAGE followed by autoradiography. The results indicate that the alpha-MSH receptor proteins labelled have a molecular weight of 42-45 kDa. These data are the first to demonstrate solubilisation and characterisation of alpha-MSH receptors from non-melanoma cells.

摘要

促肾上腺皮质激素/促黑素细胞激素（ACTH/MSH）黑素皮质素核心肽序列在外周神经中具有神经营养特性。在外周神经损伤后的功能性神经解剖学恢复过程中，雪旺细胞在促进再生方面发挥着重要作用。在此，我们使用一种经过修饰的超强α-MSH类似物来溶解培养的原代大鼠雪旺细胞中的α-MSH受体蛋白。通过SDS-PAGE和放射自显影分析了[125I-Tyr2,Nle4,D-Phe7,ATB-Lys11]-α-MSH对雪旺细胞蛋白的光亲和标记。结果表明，被标记的α-MSH受体蛋白分子量为42 - 45 kDa。这些数据首次证明了从非黑素瘤细胞中溶解并鉴定α-MSH受体。