Single Muscle Fiber Proteomics Reveals Fiber-Type-Specific Features of Human Muscle Aging
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Single Muscle Fiber Proteomics Reveals Fiber-Type-Specific Features of Human Muscle Aging. / Murgia, Marta; Toniolo, Luana; Nagaraj, Nagarjuna; Ciciliot, Stefano; Vindigni, Vincenzo; Schiaffino, Stefano; Reggiani, Carlo; Mann, Matthias.
In: Cell Reports, Vol. 19, No. 11, 13.06.2017, p. 2396-2409.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - Single Muscle Fiber Proteomics Reveals Fiber-Type-Specific Features of Human Muscle Aging
AU - Murgia, Marta
AU - Toniolo, Luana
AU - Nagaraj, Nagarjuna
AU - Ciciliot, Stefano
AU - Vindigni, Vincenzo
AU - Schiaffino, Stefano
AU - Reggiani, Carlo
AU - Mann, Matthias
N1 - Copyright © 2017 The Author(s). Published by Elsevier Inc. All rights reserved.
PY - 2017/6/13
Y1 - 2017/6/13
N2 - Skeletal muscle is a key tissue in human aging, which affects different muscle fiber types unequally. We developed a highly sensitive single muscle fiber proteomics workflow to study human aging and show that the senescence of slow and fast muscle fibers is characterized by diverging metabolic and protein quality control adaptations. Whereas mitochondrial content declines with aging in both fiber types, glycolysis and glycogen metabolism are upregulated in slow but downregulated in fast muscle fibers. Aging mitochondria decrease expression of the redox enzyme monoamine oxidase A. Slow fibers upregulate a subset of actin and myosin chaperones, whereas an opposite change happens in fast fibers. These changes in metabolism and sarcomere quality control may be related to the ability of slow, but not fast, muscle fibers to maintain their mass during aging. We conclude that single muscle fiber analysis by proteomics can elucidate pathophysiology in a sub-type-specific manner.
AB - Skeletal muscle is a key tissue in human aging, which affects different muscle fiber types unequally. We developed a highly sensitive single muscle fiber proteomics workflow to study human aging and show that the senescence of slow and fast muscle fibers is characterized by diverging metabolic and protein quality control adaptations. Whereas mitochondrial content declines with aging in both fiber types, glycolysis and glycogen metabolism are upregulated in slow but downregulated in fast muscle fibers. Aging mitochondria decrease expression of the redox enzyme monoamine oxidase A. Slow fibers upregulate a subset of actin and myosin chaperones, whereas an opposite change happens in fast fibers. These changes in metabolism and sarcomere quality control may be related to the ability of slow, but not fast, muscle fibers to maintain their mass during aging. We conclude that single muscle fiber analysis by proteomics can elucidate pathophysiology in a sub-type-specific manner.
KW - Journal Article
U2 - 10.1016/j.celrep.2017.05.054
DO - 10.1016/j.celrep.2017.05.054
M3 - Journal article
C2 - 28614723
VL - 19
SP - 2396
EP - 2409
JO - Cell Reports
JF - Cell Reports
SN - 2211-1247
IS - 11
ER -
ID: 184292069