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Updated: May 30, 2026
06:31
Identification and Dissection of Diverse Mouse Adipose Depots
Published on: July 11, 2019
N-linked glycosylation of mouse adiponectin
M Tanaka1, A Fukuhara, I Shimomura
1Department of Metabolic Medicine, Graduate School of Medicine, Osaka University, Osaka , Japan. mas_tanaka@research.otsuka.co.jp
Hormone and Metabolic Research = Hormon- Und Stoffwechselforschung = Hormones Et Metabolisme
|July 20, 2011
Summary
This study reveals that mouse adiponectin undergoes N-linked glycosylation, a posttranslational modification. Specifically, N-glycosylation occurs at asparagine 53, affecting adiponectin
Area of Science:
- Biochemistry
- Molecular Biology
- Endocrinology
Background:
- Adiponectin is a key adipokine with insulin-sensitizing, anti-diabetic, anti-atherogenic, anti-inflammatory, and cardioprotective functions.
- Previous research has indicated various posttranslational modifications of adiponectin.
Purpose of the Study:
- To investigate the posttranslational modifications of mouse adiponectin.
- To identify the specific type and site of glycosylation on mouse adiponectin.
Main Methods:
- Analysis of mouse adiponectin migration patterns on SDS-PAGE.
- Treatment with PNGase (N-glycosidase) to assess the effect on adiponectin mobility.
- Inhibition of N-glycosylation using tunicamycin in 3T3-L1 adipocytes.
- Site-directed mutagenesis of potential N-glycosylation sites in adiponectin.
Main Results:
- Mouse adiponectin exhibited two distinct bands on SDS-PAGE, with the slower band sensitive to PNGase treatment, suggesting N-glycosylation.
- Tunicamycin treatment reduced the proportion of the slower migrating band in cultured 3T3-L1 adipocytes.
- Mutant adiponectin lacking glycosylation at asparagine 53 or threonine 55 failed to produce the slower migrating band.
Conclusions:
- A portion of mouse adiponectin is modified by N-linked glycosylation.
- The N-glycosylation site is identified as asparagine 53.
- This finding clarifies a specific posttranslational modification of adiponectin.
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