Agonist-induced desensitization and down-regulation of delta opioid receptors alter the levels of their 125I-beta-endorphin cross-linked products in subcellular fractions from NG108-15 cells

Biochemistry
M M BelchevaC J Coscia

Abstract

The delta opioid binding sites in subcellular fractions from NG108-15 cells were characterized with respect to their relative molecular size and levels under conditions of receptor adaptation. 125I-beta-Endorphin was cross-linked to preparations enriched in plasma membranes (P20), nuclear membranes or nuclear matrices. Five cross-linked bands appear in all subcellular fractions. The largest molecular size reaction product in nuclear matrix preparations (approximately 72 kDa) differed from that in the other two fractions-(approximately 83 kDa). Immunoblot analyses with an antibody to the delta opioid receptor gave a P20 band pattern similar to that for the corresponding cross-linked products. To determine which cross-linked products in P20 are glycoproteins, labeled membranes were solubilized and purified by wheat germ agglutinin chromatography. The absence of a approximately 36 kDa band after purification suggests that this product is not a glycoprotein. The remaining four bands were present in N-acetyl-D-glucosamine eluates, although their % distribution changes in favor of the largest molecular size band (approximately 83 kDa). Immunoblotting of the eluate gave a single diffuse band at approximately 73 kDa, suggesting the nat...Continue Reading

Citations

Nov 7, 1998·Brain Research. Developmental Brain Research·M M BelchevaC J Coscia
Jun 19, 2008·Zhong xi yi jie he xue bao = Journal of Chinese integrative medicine·Xue-song TianJing-chun Guo
Oct 19, 2001·Oncogene·J P O'BryanC E Oldham

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