Advanced Glycation End Product in Diabetic Rat Skeletal Muscle in vivo

Snow, Le Ann M.; Lynner, Christa B.; Nielsen, Erin M.; Neu, Hillari S.; Thompson, La Dora V.

doi:10.1159/000098210

Cited by 27 publications

(34 citation statements)

References 39 publications

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“…Negative controls were performed by completing the immunolabeling procedure, but with elimination of the primary antibody incubation step. The preparation and CML immunolabeling of the soleus muscle were performed in identical manner to that of the plantaris, which has been previously described [24] .…”

Section: Tissue Staining and Analysismentioning

confidence: 99%

“…AGEs have also been identified as markers of oxidative stress [17,19,20] . N -(carboxymethyl)-lysine (CML) is a non-cross-linking AGE that is present in vivo [15,21,22] and has been studied in animal models [23,24] .…”

Section: Introductionmentioning

confidence: 99%

“…Alt et al [23] determined that gastrocnemius muscle in diabetic rats showed increased amounts of CML accumulation in total muscle and in myofibrillar proteins. Snow et al [24] used immunohistochemistry to identify patterns of AGE accumulation in plantaris myofibers of rats with untreated diabetes. They showed that CML accumulated at sites in the cell interior as well as at the fiber periphery.…”

Section: Introductionmentioning

confidence: 99%

“…Secondary aims were (1) to evaluate the degree of atrophy in AGE-labeled fibers, as well as their fiber types, and (2) to compare AGE accumulation in soleus, as predominantly slow muscle, with plantaris, a predominantly fast muscle. The data for AGE accumulation in plantaris of diabetic rats has previously been published [24] . It was hypothesized that insulin administration would be associated with decreased CML accumulation in skeletal muscle, and that soleus, a predominantly slow muscle, would exhibit less CML accumulation than plantaris, a predominantly fast muscle.…”

Section: Introductionmentioning

confidence: 99%

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Influence of Insulin and Muscle Fiber Type in Nε-(Carboxymethyl)-Lysine Accumulation in Soleus Muscle of Rats with Streptozotocin-Induced Diabetes Mellitus

Snow¹,

Thompson²

2009

Pathobiology

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Background: Nε-(carboxymethyl)-lysine (CML) is an advanced glycation end product (AGE), the accumulation of which has been implicated in the etiology of diabetes complications. Skeletal muscle in diabetes demonstrates altered function, and increased accumulation of CML has been found in several fast-twitch muscles of diabetic animals. Objective: This study aims to explore the accumulation of CML in soleus (a slow muscle) in diabetic animals, with and without insulin therapy. Methods: Twenty-one rats were randomly divided into control and diabetes groups (DNI: diabetes without insulin; DI: diabetes with insulin; C: control). Diabetes was induced by intravenous administration of streptozotocin. At the end of the 12-week experimental period the soleus muscle was excised and snap frozen in liquid nitrogen. Muscle cross-sections were immunolabeled for CML. The number of CML-labeled muscle fibers was quantified; fibers were also evaluated for fiber types and cross-sectional areas. Results: The percentage of myofibers immunolabeling for CML was highest in the DNI group (13.8 ± 2.5%), lower in the DI group (5.4 ± 1.1%) and lowest in the C group (2.1 ± 0.6%). Statistical analysis revealed that AGE accumulation was significantly greater in the DNI group than in both C and DI groups (p = 0.0002). There was no significant difference between C and DI groups. In the DNI animals, AGE-positive myofibers showed a higher percentage of fast fiber types than did the AGE-negative fibers (49.5 ± 6.9 vs. 13.7 ± 1.5%, p = 0.002). No differences existed in cross-sectional areas between AGE-positive and AGE-negative fibers within any group. Conclusion: The greatest accumulation of AGE was in the soleus of the DNI group, and was significantly less in the DI group. These findings may be linked to disordered glucose metabolism, increased oxidative stress and/or fiber type transformation in these muscles.

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Section: Tissue Staining and Analysismentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Influence of Insulin and Muscle Fiber Type in Nε-(Carboxymethyl)-Lysine Accumulation in Soleus Muscle of Rats with Streptozotocin-Induced Diabetes Mellitus

Snow¹,

Thompson²

2009

Pathobiology

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“…Advanced glycation end products also accumulate in the skeletal muscle of diabetic animals (Snow et al, 2006). Although the levels of both SERCA2a and its inhibitor phospholamban decrease in diabetes, the phospholamban/SERCA2a ratio becomes higher Our results suggest that the SERCA2a protein level is an earlier marker than that of MyHC1 for muscle diabetes.…”

Section: Diabetic Modelmentioning

confidence: 56%

Uncoordinated expression of the main contractile and relaxation proteins in pathological skeletal muscles

Zsófia¹

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Autophagy signaling in hypertrophied muscles of diabetic and control rats

et al. 2023

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Autophagy plays a vital role in cell homeostasis by eliminating nonfunctional components and promoting cell survival. Here, we examined the levels of autophagy signaling proteins after 7 days of overload hypertrophy in the extensor digitorum longus (EDL) and soleus muscles of control and diabetic rats. We compared control and 3‐day streptozotocin‐induced diabetic rats, an experimental model for type 1 diabetes mellitus (T1DM). EDL muscles showed increased levels of basal autophagy signaling proteins. The diabetic state did not affect the extent of overload‐induced hypertrophy or the levels of autophagy signaling proteins (p‐ULK1, Beclin‐1, Atg5, Atg12‐5, Atg7, Atg3, LC3‐I and II, and p62) in either muscle. The p‐ULK‐1, Beclin‐1, and p62 protein expression levels were higher in the EDL muscle than in the soleus before the hypertrophic stimulus. On the contrary, the soleus muscle exhibited increased autophagic signaling after overload‐induced hypertrophy, with increases in Beclin‐1, Atg5, Atg12‐5, Atg7, Atg3, and LC3‐I expression in the control and diabetic groups, in addition to p‐ULK‐1 in the control groups. After hypertrophy, Beclin‐1 and Atg5 levels increased in the EDL muscle of both groups, while p‐ULK1 and LC3‐I increased in the control group. In conclusion, the baseline EDL muscle exhibited higher autophagy than the soleus muscle. Although TDM1 promotes skeletal muscle mass loss and strength reduction, it did not significantly alter the extent of overload‐induced hypertrophy and autophagy signaling proteins in EDL and soleus muscles, with the two groups exhibiting different patterns of autophagy activation.

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Advanced Glycation End Product in Diabetic Rat Skeletal Muscle in vivo

Cited by 27 publications

References 39 publications

Influence of Insulin and Muscle Fiber Type in Nε-(Carboxymethyl)-Lysine Accumulation in Soleus Muscle of Rats with Streptozotocin-Induced Diabetes Mellitus

Influence of Insulin and Muscle Fiber Type in Nε-(Carboxymethyl)-Lysine Accumulation in Soleus Muscle of Rats with Streptozotocin-Induced Diabetes Mellitus

Uncoordinated expression of the main contractile and relaxation proteins in pathological skeletal muscles

Autophagy signaling in hypertrophied muscles of diabetic and control rats

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