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Fast oxidation of α-melanocyte-stimulating hormone and derived peptides under laboratory conditions causes irreproducible results-Insights from studies of prolylcarboxypeptidase in human cell types.
Pigment Cell & Melanoma Research ( IF 3.9 ) Pub Date : 2019-12-25 , DOI: 10.1111/pcmr.12852
Malte Bayer 1 , Nino Tsiskarishvili 2 , Agatha Stegemann 2 , Markus Böhm 2 , Simone König 1
Affiliation  

α‐melanocyte stimulating hormone (α‐MSH, AcSYSMEHFRWGKPVNH2; Singh & Mukhopadhyay, 2014, D’Agostino & Diano, 2010) has a variety of biological effects in the skin such as the regulation of pigment formation and the modulation of inflammatory and immune reactions (Böhm et al., 2006; Brzoska et al., 2009). In contrast to a plethora of reports investigating the signal transduction pathways of α‐MSH, especially in melanocytes, little is known about the enzymatic degradation of this peptide. Recently, prolylcarboxypeptidase (PRCP), has been shown to serve as an endogenous regulator of the central melanocortin system by degrading α‐MSH (Wallingford et al., 2009). PRCP inactivates α‐MSH by the removal of the N‐terminal valine residue.

中文翻译:

在实验室条件下,α-黑素细胞刺激激素和衍生肽的快速氧化导致无法再现的结果-人类细胞中脯氨酰羧肽酶研究的见解。

α-黑素细胞刺激激素(α-MSH,Ac SYSMEHFRWGKPV NH2; Singh和Mukhopadhyay,2014年,D'Agostino和Diano,2010年)在皮肤中具有多种生物学效应,例如调节色素形成,调节炎症和免疫反应(Böhm等,2006; Brzoska等,2009)。与大量研究α-MSH的信号转导途径的报告相反,尤其是在黑素细胞中,对该肽的酶促降解了解甚少。最近,脯氨酰羧肽酶(PRCP)已被证明可通过降解α-MSH来作为中枢黑皮质素系统的内源性调节剂(Wallingford et al。,2009)。PRCP通过去除N末端缬氨酸残基使α-MSH失活。
更新日期:2019-12-17
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