O-GlcNAcylation, an original modulator of contractile activity in striated muscle

被引:19
作者
Cieniewski-Bernard, C. [1 ,2 ]
Montel, V. [1 ,2 ]
Stevens, L. [1 ,2 ]
Bastide, B. [1 ,2 ]
机构
[1] Univ Lille 1, EA3608, IFR114, F-59650 Villeneuve Dascq, France
[2] Univ Lille Nord France, F-59000 Lille, France
关键词
O-GlcNAC; O-GlcNacylation; Post-translational modifications; Contractile activity; Calcium activation parameters; Diabetes; Contractile proteins; LINKED N-ACETYLGLUCOSAMINE; PROTECTS NEONATAL CARDIOMYOCYTES; ISCHEMIA-REPERFUSION INJURY; LIGHT-CHAIN KINASE; SKELETAL-MUSCLE; GLCNAC MODIFICATION; HEART-FAILURE; ACETYL-GLUCOSAMINE; INSULIN-RESISTANCE; DYNAMIC INTERPLAY;
D O I
10.1007/s10974-010-9201-1
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
There is growing evidence that O-linked N-acetyl-D-glucosaminylation, more simply termed O-Glc-NAcylation or O-GlcNAc, is a post-translational modification involved in many cellular processes from transcription to modulation of protein properties. O-GlcNAc is a dynamic and reversible glycosylation and therefore quite similar to the phosphorylation/dephosphorylation process, with which O-GlcNAc can interplay. Since O-GlcNAc serves as a glucose sensor by the way of hexosamine biosynthesis pathway, this glycosylation is often associated with glucose toxicity and development of insulin resistance. In this way, O-GlcNAc could be involved in muscle pathological consequences of diabetes. Nevertheless, in regards of several studies performed in healthy striated muscles, O-GlcNAc seems to exert protective effects against different types of injuries. Recent new insights suggest a key implication of O-GlcNAc in skeletal and cardiac muscles contractile activity, in particular by O-GlcNAc modification of motor as well as regulating contractile proteins. While evidence linked O-GlcNAc to the regulation of calcium activation properties, its exact role remains to be defined as well as the existence of potential interference with phosphorylation. The better understanding of the exact function of OGlcNAc in this physiological process could contribute to the determination of newly markers of skeletal dysfunctions.
引用
收藏
页码:281 / 287
页数:7
相关论文
共 65 条
[1]   Relationship between protein O-linked glycosylation and insulin-stimulated glucose transport in rat skeletal muscle following calorie restriction or exposure to O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate [J].
Arias, EB ;
Cartee, GD .
ACTA PHYSIOLOGICA SCANDINAVICA, 2005, 183 (03) :281-289
[2]   Heart failure-associated alterations in troponin I phosphorylation impair ventricular relaxation-afterload and force-frequency responses and systolic function [J].
Bilchick, Kenneth C. ;
Duncan, Jennifer G. ;
Ravi, Rajashree ;
Takimoto, Eiki ;
Champion, Hunter C. ;
Gao, Wei Dong ;
Stull, Linda B. ;
Kass, David A. ;
Murphy, Anne M. .
AMERICAN JOURNAL OF PHYSIOLOGY-HEART AND CIRCULATORY PHYSIOLOGY, 2007, 292 (01) :H318-H325
[3]   ACTIVATION OF SKELETAL-MUSCLE MYOSIN LIGHT CHAIN KINASE BY CALCIUM(2+) AND CALMODULIN [J].
BLUMENTHAL, DK ;
STULL, JT .
BIOCHEMISTRY, 1980, 19 (24) :5608-5614
[4]   The cellular fate of glucose and its relevance in type 2 diabetes [J].
Bouché, C ;
Serdy, S ;
Kahn, CR ;
Goldfine, AB .
ENDOCRINE REVIEWS, 2004, 25 (05) :807-830
[5]  
Butkinaree C., 2009, BIOCH BIOPHYS ACTA
[6]   Glucosamine protects neonatal cardiomyocytes from ischemia-reperfusion injury via increased protein O-GlcNAc and increased mitochondrial Bcl-2 [J].
Champattanachai, Voraratt ;
Marchase, Richard B. ;
Chatham, John C. .
AMERICAN JOURNAL OF PHYSIOLOGY-CELL PHYSIOLOGY, 2008, 294 (06) :C1509-C1520
[7]   Glucosamine protects neonatal cardiomyocytes from ischemia-reperfusion injury via increased protein-associated O-GlcNAc [J].
Champattanachai, Voraratt ;
Marchase, Richard B. ;
Chatham, John C. .
AMERICAN JOURNAL OF PHYSIOLOGY-CELL PHYSIOLOGY, 2007, 292 (01) :C178-C187
[8]  
Chou TY, 2001, ADV EXP MED BIOL, V491, P413
[9]   O-GlcNAc level variations are associated with the development of skeletal muscle atrophy [J].
Cieniewski-Bernard, C ;
Mounier, Y ;
Michalski, JC ;
Bastide, B .
JOURNAL OF APPLIED PHYSIOLOGY, 2006, 100 (05) :1499-1505
[10]   Identification of O-linked N-acetylglucosamine proteins in rat skeletal muscle using two-dimensional gel electrophoresis and mass spectrometry [J].
Cieniewski-Bernard, C ;
Bastide, B ;
Lefebvre, T ;
Lemoine, J ;
Mounier, Y ;
Michalski, JC .
MOLECULAR & CELLULAR PROTEOMICS, 2004, 3 (06) :577-585