Proximal skeletal muscle alterations in streptozotocin‐diabetic rats: A histochemical and morphometric analysis

Medina-Sánchez, M; Rodriguez-Sanchez, Carmen; Vega-Álvarez, José Antonio; Menéndez-Peláez, Armando; Pérez-Casas, A

doi:10.1002/aja.1001910105

Cited by 31 publications

(31 citation statements)

References 35 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The results of this study support previous observations that fast myofibers are affected first in the course of muscle atrophy (43), leading to the prevalence of slower fiber types. However, some of the proteins studied may also be involved in neuropathy-induced changes (e.g., MLP, myf-6, Ank3) in which neuropathy increases the expression of fast MHC, changing fiber type composition in a faster direction (52).…”

Section: Discussionsupporting

confidence: 82%

“…Our preliminary results from the quadriceps femoris muscle of these mice show a transition from MHC IIb toward MHC IIa in D25 and DT25 (Touvra A, Silvennoinen M, Kivelä R, Lehti TM, Komulainen J, Kontro H, Vihko V, Kainulainen H, unpublished results). The decrease in MyoD mRNA level and the transition in MHC toward slower type myofibers are consistent with the findings of previous studies (43). myf-6 is important in the maintenance of both mature myogenic and neuromuscular-specific gene expression (40).…”

Section: Z-discsupporting

confidence: 80%

“…The increase in MLP transcription may be a consequence of change in prevalent myofiber type to slower fibers (43) or diabetesinduced neuropathy (52). The ability of exercise to prevent diabetes-induced changes in MLP mRNA expression in DT1 and DT3 may indicate deceleration in the transition to the slower fiber type or in the development of neuropathy.…”

Section: Z-discmentioning

confidence: 99%

See 2 more Smart Citations

Effects of streptozotocin-induced diabetes and physical training on gene expression of titin-based stretch-sensing complexes in mouse striated muscle

Lehti¹,

Silvennoinen²,

Kivelä³

et al. 2007

American Journal of Physiology-Endocrinology and Metabolism

View full text Add to dashboard Cite

Lehti TM, Silvennoinen M, Kivelä R, Kainulainen H, Komulainen J. Effects of streptozotocin-induced diabetes and physical training on gene expression of titin-based stretch-sensing complexes in mouse striated muscle. Am J Physiol Endocrinol Metab 292: E533-E542, 2007. First published September 26, 2006; doi:10.1152/ajpendo.00229.2006.-In striated muscle, a sarcomeric noncontractile protein, titin, is proposed to form the backbone of the stress-and strain-sensing structures. We investigated the effects of diabetes, physical training, and their combination on the gene expression of proteins of putative titin stretch-sensing complexes in skeletal and cardiac muscle. Mice were divided into control (C), training (T), streptozotocininduced diabetic (D), and diabetic training (DT) groups. Training groups performed for 1, 3, or 5 wk of endurance training on a motor-driven treadmill. Muscle samples from T and DT groups together with respective controls were collected 24 h after the last training session. Gene expression of calf muscles (soleus, gastrocnemius, and plantaris) and cardiac muscle were analyzed using microarray and quantitative PCR. Diabetes induced changes in mRNA expression of the proteins of titin stretch-sensing complexes in Z-disc (MLP, myostatin), I-band (CARP, Ankrd2), and M-line (titin kinase signaling). Training alleviated diabetes-induced changes in most affected mRNA levels in skeletal muscle but only one change in cardiac muscle. In conclusion, we showed diabetes-induced changes in mRNA levels of several fiber-type-biased proteins (MLP, myostatin, Ankrd2) in skeletal muscle. These results are consistent with previous observations of diabetes-induced atrophy leading to slower fiber type composition. The ability of exercise to alleviate diabetes-induced changes may indicate slower transition of fiber type. skeletal muscle; cardiac muscle; microarray; muscle LIM protein; myostatin IN SKELETAL AND CARDIAC MUSCLE, a sarcomeric noncontractile protein, titin, forms a spring from the Z-disc to the A-band. Titin is the only molecule that extends over half a sarcomere. It maintains the temporal and spatial assembly of the contractile filaments (32, 54). On the basis of its location and interactions with several structural and signaling proteins, titin is thought to be the backbone of the stress-and strain-sensing structure in striated muscle (45). Interestingly, gene expression of some of these proteins is affected by diabetes or insulin resistance (21,42,53).At the Z-disc, titin interacts with telethonin (or T-cap), small ankyrin-1 (sAnk1), and obscurin (32). Telethonin is a linking protein for several signaling and structural proteins, e.g., muscle LIM protein (MLP) and myostatin (16). Interaction of the MLP with myogenic regulatory factors (MRFs) in the nucleus and its effect on expression of brain natriuretic peptide (BNP) and atrial natriuretic factor (ANF) make MLP a possible stretch-regulatory protein (16).The central I-band of titin contains an N2A region and a cardiac-specific N2B region. N2A intera...

show abstract

Section: Discussionsupporting

confidence: 82%

Section: Z-discsupporting

confidence: 80%

Section: Z-discmentioning

confidence: 99%

See 1 more Smart Citation

Effects of streptozotocin-induced diabetes and physical training on gene expression of titin-based stretch-sensing complexes in mouse striated muscle

Lehti¹,

Silvennoinen²,

Kivelä³

et al. 2007

American Journal of Physiology-Endocrinology and Metabolism

View full text Add to dashboard Cite

show abstract

“…The body weight data are consistent with other reports, with the diabetic animals weighing less than controls [18,19] . These data are indicative of the effect of insulin as an inhibitor of protein degradation [20,21] .…”

Section: Muscle Weights and General Mhc Fiber Typessupporting

confidence: 82%

Advanced Glycation End Product in Diabetic Rat Skeletal Muscle in vivo

et al. 2006

View full text Add to dashboard Cite

Background: Advanced glycation end products (AGEs) are implicated in the etiology of diabetic complications in the kidney, nerve and eye. Skeletal muscle contractile parameters have also been found to be altered in diabetes. Glycation has not been extensively studied in skeletal muscle, but AGE-modified proteins may influence contractility. Objective and Methods: The aim of this study was to use immunohistochemistry to identify distribution patterns of the AGE NΕ-(carboxymethyl)-lysine in plantaris muscle of diabetic rats. Results: Results revealed the presence of NΕ-(carboxymethyl)-lysine intracellularly and also at sites along the myofiber periphery. The number of myofibers immunolabeling for AGE in animals with diabetes was more than 4-fold greater than in control animals. Additionally, there was a greater proportion of slow + fast myosin heavy chain coexpression in the AGE-positive cells from diabetic animals than in AGE-positive fibers from control animals. No significant difference was present between cross-sectional areas of AGE-positive fibers and AGE-negative fibers within the respective experimental groups. Conclusions: AGE accumulation is greater in skeletal muscle in vivo from diabetic animals than in control animals. This AGE accumulation appears to be associated with fiber-type transformation rather than with myofiber size. Further study is needed to determine the identity of these AGE-modified proteins and to determine how they influence skeletal muscle function in diabetes.

show abstract

“…Consistent with previous results [8,9,33,34], our muscle fibre analysis showed that sedentary behaviour in diabetic rats results in a fibre type-specific reduction in cross-sectional area, with the type IIb/d fibres being most compromised. In addition, although effective in attenuating muscle fibre area loss in all fibre types, we show that regular voluntary physical activity in diabetic animal models largely protects these same glycolytic muscle fibres.…”

Section: Discussionsupporting

confidence: 79%

Voluntary physical activity and leucine correct impairments in muscle protein synthesis in partially pancreatectomised rats

et al. 2011

View full text Add to dashboard Cite

Aims/hypothesis Poorly controlled type 1 diabetes mellitus can cause reduced skeletal muscle mass and weakness during adolescence, which may affect long-term management of the disease. The aim of this study was to determine whether regular voluntary physical activity and leucine feeding restore rates of protein synthesis and deficits in skeletal muscle mass in a young, hypoinsulinaemic/hyperglycaemic rat model of diabetes. Methods Four-week-old male Sprague-Dawley rats were partially pancreatectomised (Px) to induce hypoinsulinaemia/hyperglycaemia and housed with/without access to running wheels for 3 weeks (n=12-14/group). Sham surgery rats (shams) served as sedentary controls (n=18). Protein synthesis and markers of protein anabolism were assessed in the fasted state and following leucine gavage.Fibre type and cross-sectional areas of the gastrocnemius muscle were measured using a metachromatic ATPase stain. Results Compared with sedentary behaviour, regular activity lowered fasting glycaemia and reduced fed hyperglycaemia in Px rats. Active-Px rats, which ran 2.2±0.71 km/night, displayed greater muscle mass and fibre areas similar to shams, while sedentary-Px rats displayed a 20-30% loss in muscle fibre areas. Muscle protein synthesis (basal and in response to leucine gavage) was impaired in sedentary-Px (by~65%), but not in active-Px rats, when compared with shams. Following leucine gavage, the phosphorylation status of eIF4E binding protein 1 (4E-BP1) and ribosomal S6 kinase 1 (S6K1), markers of mammalian target of rapamycin complex 1 (mTORC1) signalling, increased in shams (by two-and ninefold, respectively) and in active-Px (1.5-and fourfold, respectively) rats, but not in sedentary-Px rats. Conclusion/interpretation Moderate physical activity in young Px rats normalises impairments in skeletal muscle growth and protein synthesis. These findings illustrate the critical compensatory role that modest physical activity and targeted nutrition can have on skeletal muscle growth during periods of hypoinsulinaemia in adolescent diabetes.

show abstract

Proximal skeletal muscle alterations in streptozotocin‐diabetic rats: A histochemical and morphometric analysis

Cited by 31 publications

References 35 publications

Effects of streptozotocin-induced diabetes and physical training on gene expression of titin-based stretch-sensing complexes in mouse striated muscle

Effects of streptozotocin-induced diabetes and physical training on gene expression of titin-based stretch-sensing complexes in mouse striated muscle

Advanced Glycation End Product in Diabetic Rat Skeletal Muscle in vivo

Voluntary physical activity and leucine correct impairments in muscle protein synthesis in partially pancreatectomised rats

Contact Info

Product

Resources

About