Secreted nucleobindin-2 inhibits 3T3-L1 adipocyte differentiation.

Abstract:

:Nucleobindin-2 is a 420 amino acid EF-hand Ca²⁺ binding protein that can be further processed to generate an 82 amino terminal peptide termed Nesfatin-1. To examine the function of secreted Nucleobindin-2 in adipocyte differentiation, cultured 3T3-L1 cells were incubated with either 0 or 100 nM of GST, GST-Nucleobindin-2, prior to and during the initiation of adipocyte differentiation. Nucleobindin-2 treatment decreased neutral lipid accumulation (Oil-Red O staining) and expression of several marker genes for adipocyte differentiation (PPARγ, aP2, and adipsin). When Nucleobindin- 2 was constitutively secreted into cultured medium, cAMP content and insulin stimulated CREB phosphorylation were significantly reduced. On the other hand, intracellularly overexpressed Nucleobindin-2 failed to affect cAMP content and CREB phosphorylation. Taken together, these data indicate that secreted Nucleobindin-2 is a suppressor of adipocyte differentiation through inhibition of cAMP production and insulin signal.

journal_name

Protein Pept Lett

authors

Tagaya Y,Osaki A,Miura A,Okada S,Ohshima K,Hashimoto K,Yamada M,Satoh T,Shimizu H,Mori M

doi

10.2174/092986612802084546

subject

Has Abstract

pub_date

2012-09-01 00:00:00

pages

997-1004

issue

9

eissn

0929-8665

issn

1875-5305

pii

PPL-EPUB-20120405-007

journal_volume

19

pub_type

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