Increases in glycogenin and glycogenin mRNA accompany glycogen resynthesis in human skeletal muscle

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Increases in glycogenin and glycogenin mRNA accompany glycogen resynthesis in human skeletal muscle. / Shearer, Jane; Wilson, Rhonda J.; Battram, Danielle S.; Richter, Erik A.; Robinson, Deborah L.; Bakovic, Marica; Graham, Terry E.

I: American Journal of Physiology: Endocrinology and Metabolism, Bind 289, Nr. 3, 2005, s. E508-E514.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Harvard

Shearer, J, Wilson, RJ, Battram, DS, Richter, EA, Robinson, DL, Bakovic, M & Graham, TE 2005, 'Increases in glycogenin and glycogenin mRNA accompany glycogen resynthesis in human skeletal muscle', American Journal of Physiology: Endocrinology and Metabolism, bind 289, nr. 3, s. E508-E514. https://doi.org/10.1152/ajpendo.00100.2005

APA

Shearer, J., Wilson, R. J., Battram, D. S., Richter, E. A., Robinson, D. L., Bakovic, M., & Graham, T. E. (2005). Increases in glycogenin and glycogenin mRNA accompany glycogen resynthesis in human skeletal muscle. American Journal of Physiology: Endocrinology and Metabolism, 289(3), E508-E514. https://doi.org/10.1152/ajpendo.00100.2005

Vancouver

Shearer J, Wilson RJ, Battram DS, Richter EA, Robinson DL, Bakovic M o.a. Increases in glycogenin and glycogenin mRNA accompany glycogen resynthesis in human skeletal muscle. American Journal of Physiology: Endocrinology and Metabolism. 2005;289(3):E508-E514. https://doi.org/10.1152/ajpendo.00100.2005

Author

Shearer, Jane ; Wilson, Rhonda J. ; Battram, Danielle S. ; Richter, Erik A. ; Robinson, Deborah L. ; Bakovic, Marica ; Graham, Terry E. / Increases in glycogenin and glycogenin mRNA accompany glycogen resynthesis in human skeletal muscle. I: American Journal of Physiology: Endocrinology and Metabolism. 2005 ; Bind 289, Nr. 3. s. E508-E514.

Bibtex

@article{e61e9b50a23a11dbbee902004c4f4f50,
title = "Increases in glycogenin and glycogenin mRNA accompany glycogen resynthesis in human skeletal muscle",
abstract = "Glycogenin is the self-glycosylating protein primer that initiates glycogen granule formation. To examine the role of this protein during glycogen resynthesis, eight male subjects exercised to exhaustion on a cycle ergometer at 75% VO2 max followed by five 30-s sprints at maximal capacity to further deplete glycogen stores. During recovery, carbohydrate (75 g/h) was supplied to promote rapid glycogen repletion, and muscle biopsies were obtained from the vastus lateralis at 0, 30, 120, and 300 min postexercise. At time 0, no free (deglycosylated) glycogenin was detected in muscle, indicating that all glycogenin was complexed to carbohydrate. Glycogenin activity, a measure of the glycosylating ability of the protein, increased at 30 min and remained elevated for the remainder of the study. Quantitative RT-PCR showed elevated glycogenin mRNA at 120 min followed by increases in protein levels at 300 min. Glycogenin specific activity (glycogenin activity/relative protein content) was also elevated at 120 min. Proglycogen increased at all time points, with the highest rate of resynthesis occurring between 0 and 30 min. In comparison, macroglycogen levels did not significantly increase until 300 min postexercise. Together, these results show that, during recovery from prolonged exhaustive exercise, glycogenin mRNA and protein content and activity increase in muscle. This may facilitate rapid glycogen resynthesis by providing the glycogenin backbone of proglycogen, the major component of glycogen synthesized in early recovery. ",
author = "Jane Shearer and Wilson, {Rhonda J.} and Battram, {Danielle S.} and Richter, {Erik A.} and Robinson, {Deborah L.} and Marica Bakovic and Graham, {Terry E.}",
note = "PUF 2005 5200 008",
year = "2005",
doi = "10.1152/ajpendo.00100.2005",
language = "English",
volume = "289",
pages = "E508--E514",
journal = "American Journal of Physiology: Endocrinology and Metabolism",
issn = "0193-1849",
publisher = "American Physiological Society",
number = "3",

}

RIS

TY - JOUR

T1 - Increases in glycogenin and glycogenin mRNA accompany glycogen resynthesis in human skeletal muscle

AU - Shearer, Jane

AU - Wilson, Rhonda J.

AU - Battram, Danielle S.

AU - Richter, Erik A.

AU - Robinson, Deborah L.

AU - Bakovic, Marica

AU - Graham, Terry E.

N1 - PUF 2005 5200 008

PY - 2005

Y1 - 2005

N2 - Glycogenin is the self-glycosylating protein primer that initiates glycogen granule formation. To examine the role of this protein during glycogen resynthesis, eight male subjects exercised to exhaustion on a cycle ergometer at 75% VO2 max followed by five 30-s sprints at maximal capacity to further deplete glycogen stores. During recovery, carbohydrate (75 g/h) was supplied to promote rapid glycogen repletion, and muscle biopsies were obtained from the vastus lateralis at 0, 30, 120, and 300 min postexercise. At time 0, no free (deglycosylated) glycogenin was detected in muscle, indicating that all glycogenin was complexed to carbohydrate. Glycogenin activity, a measure of the glycosylating ability of the protein, increased at 30 min and remained elevated for the remainder of the study. Quantitative RT-PCR showed elevated glycogenin mRNA at 120 min followed by increases in protein levels at 300 min. Glycogenin specific activity (glycogenin activity/relative protein content) was also elevated at 120 min. Proglycogen increased at all time points, with the highest rate of resynthesis occurring between 0 and 30 min. In comparison, macroglycogen levels did not significantly increase until 300 min postexercise. Together, these results show that, during recovery from prolonged exhaustive exercise, glycogenin mRNA and protein content and activity increase in muscle. This may facilitate rapid glycogen resynthesis by providing the glycogenin backbone of proglycogen, the major component of glycogen synthesized in early recovery.

AB - Glycogenin is the self-glycosylating protein primer that initiates glycogen granule formation. To examine the role of this protein during glycogen resynthesis, eight male subjects exercised to exhaustion on a cycle ergometer at 75% VO2 max followed by five 30-s sprints at maximal capacity to further deplete glycogen stores. During recovery, carbohydrate (75 g/h) was supplied to promote rapid glycogen repletion, and muscle biopsies were obtained from the vastus lateralis at 0, 30, 120, and 300 min postexercise. At time 0, no free (deglycosylated) glycogenin was detected in muscle, indicating that all glycogenin was complexed to carbohydrate. Glycogenin activity, a measure of the glycosylating ability of the protein, increased at 30 min and remained elevated for the remainder of the study. Quantitative RT-PCR showed elevated glycogenin mRNA at 120 min followed by increases in protein levels at 300 min. Glycogenin specific activity (glycogenin activity/relative protein content) was also elevated at 120 min. Proglycogen increased at all time points, with the highest rate of resynthesis occurring between 0 and 30 min. In comparison, macroglycogen levels did not significantly increase until 300 min postexercise. Together, these results show that, during recovery from prolonged exhaustive exercise, glycogenin mRNA and protein content and activity increase in muscle. This may facilitate rapid glycogen resynthesis by providing the glycogenin backbone of proglycogen, the major component of glycogen synthesized in early recovery.

U2 - 10.1152/ajpendo.00100.2005

DO - 10.1152/ajpendo.00100.2005

M3 - Journal article

C2 - 15870102

VL - 289

SP - E508-E514

JO - American Journal of Physiology: Endocrinology and Metabolism

JF - American Journal of Physiology: Endocrinology and Metabolism

SN - 0193-1849

IS - 3

ER -

ID: 92594