Characterizing the binding of dopamine D1–D2 receptors invitro and in temporal and frontal lobe tissue total protein

FEBS Letters

article

Deborah L. Heyl¹  Margaret Champion¹  Robert Muterspaugh¹  Megan Connolly¹  Adam Baraka¹  Pouya Khazaei¹  Briana Moe¹  Zeinab Al-Sheemary¹  Nael Jaber¹  Hedeel Guy-Evans¹ 

[1] Chemistry Department, Eastern Michigan University

关键词: binding;    brain lobe;    dopamine receptor;    kinetics;    peptide;   

DOI  :  10.1002/1873-3468.13351

来源: John Wiley & Sons Ltd.

【 摘 要 】

Dysfunction of the dopaminergic pathway is linked to numerous diseases of the nervous system. The D1–D2 receptor heteromer is known to play a role in certain neuropsychiatric disorders, such as depression. Here, we synthesized an eight amino acid residue peptide, EAARRAQE, derived from the third intracellular loop of the D2 receptor and show that the peptide binds to the D1 receptor with comparable efficiency as that of the full-length D2 receptor protein. Moreover, immunoprecipitation studies show the existence of a heteromeric complex formed both in vitro and in total protein derived from temporal and frontal lobe tissue from normal and depressed subjects. The efficiency of the peptide to block the D1–D2 heteromeric complex was comparable in all the samples tested.

【 授权许可】

Unknown