Abstract
The D-galactose (D-gal)-induced animal model, generated by repeated subcutaneous D-gal injections over approximately 6 weeks, has been frequently used for diabetes and aging research. However, little research has investigated the direct correlation between D-gal and autoantibody formation despite several reports on diabetes-and aging-related autoantibodies. The purpose of this study was to determine whether repetitive injection of D-gal can induce autoantibody production in mice. First, we used Bovine Serum Albumin (BSA) and Advanced Glycation End products (AGE)-BSA as the test antigens. The immunoreactivity of serum samples from mice treated with D-gal for 6 weeks was evaluated using Enzyme-Linked Immunosorbent Assay (ELISA). We found that serum samples of D-gal-treated mice had significantly high antibody titers against both BSA and AGE-BSA. Furthermore, the result showed that aminoguanidine treatment, an AGE inhibitor tended to decrease this immunoreactivity. The results of competitive inhibition ELISA using BSA and AGE-BSA as the competitors suggested that the serum samples from D-gal-treated mice contained antibodies not only against BSA but also specific to AGE-BSA. To assess whether the immunoreactivity against BSA is comparable to that against Mouse Serum Albumin (MSA), we examined the reactivity of D-gal-induced antibodies against MSA. Unexpectedly, D-gal-induced antibodies did not react with MSA. This suggests that the production of antibodies by D-gal is in response to an unknown antigen(s), aside from MSA, in mice and that this unknown antigen(s) may share similar sequences or three-dimensional structures with BSA.
Highlights
(carboxymethyl) Lysine (CML) and pentosidine have been found to accumulate on proteins of the skin and Advanced Glycation End products (AGEs) are lens at accelerated rates in diabetic and aged tissues formed in vivo by the Maillard reaction, a non-enzymatic (Dyer et al, 1993; Handa et al, 1999)
Additional tests showed the antibodies did not react against Mouse Serum Albumin (MSA). These results suggest that the production of antibodies by repetitive injection of D-gal is due to unknown mouse protein(s), aside from MSA and the neo-epitopes of the unknown mouse protein(s) may share identical sequence(s) or three-dimensional structure(s) with Bovine Serum Albumin (BSA)
These results showed that antibodies were produced against BSA and AGE-BSA in the serum of D-gal-treated mice and that the production of antibodies may be due to the formation of AGEs
Summary
(carboxymethyl) Lysine (CML) and pentosidine have been found to accumulate on proteins of the skin and Advanced Glycation End products (AGEs) are lens at accelerated rates in diabetic and aged tissues formed in vivo by the Maillard reaction, a non-enzymatic (Dyer et al, 1993; Handa et al, 1999). Ji-Hun Park and Tae-Saeng Choi / American Journal of Immunology 10 (1): 3-9, 2014 liver and blood cells (Lei et al, 2008; Xie and Ling, 2008; Aydin et al, 2012; Hsia et al, 2012; Wu et al, 2012) more recently, we found phenotypes of Polycystic Ovary Syndrome (PCOS) in this model (Park and Choi, 2012) These induced phenotypes may be the result of excessive formation of Reactive Oxygen Species (ROS) and D-gal-induced accumulation of AGEs (Song et al, 1999). Previous studies have demonstrated antibody production in response to CML-BSA in diabetic human patients (Shibayama et al, 1999) as well as higher antigenicity of AGE-IgG than IgG (Rasheed et al, 2009)
Sign-in/Register to view highlights & summary 
Published Version (
Free)
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
