PMID- 30919448
OWN - NLM
STAT- MEDLINE
DCOM- 20200727
LR  - 20240421
IS  - 1469-7793 (Electronic)
IS  - 0022-3751 (Print)
IS  - 0022-3751 (Linking)
VI  - 597
IP  - 10
DP  - 2019 May
TI  - Protein composition of the muscle mitochondrial reticulum during postnatal 
      development.
PG  - 2707-2727
LID - 10.1113/JP277579 [doi]
AB  - KEY POINTS: Muscle mitochondrial networks changed from a longitudinal, fibre 
      parallel orientation to a perpendicular configuration during postnatal 
      development. Mitochondrial dynamics, mitophagy and calcium uptake proteins were 
      abundant during early postnatal development. Mitochondrial biogenesis and 
      oxidative phosphorylation proteins were upregulated throughout muscle 
      development. Postnatal muscle mitochondrial network formation is accompanied by a 
      change in protein expression profile from mitochondria designed for co-ordinated 
      cellular assembly to mitochondria highly specialized for cellular energy 
      metabolism. ABSTRACT: Striated muscle mitochondria form connected networks 
      capable of rapid cellular energy distribution. However, the mitochondrial 
      reticulum is not formed at birth and the mechanisms driving network development 
      remain unclear. In the present study, we aimed to establish the network formation 
      timecourse and protein expression profile during postnatal development of the 
      murine muscle mitochondrial reticulum. Two-photon microscopy was used to observe 
      mitochondrial network orientation in tibialis anterior (TA) muscles of live mice 
      at postnatal days (P) 1, 7, 14, 21 and 42, respectively. All muscle fibres 
      maintained a longitudinal, fibre parallel mitochondrial network orientation early 
      in development (P1-7). Mixed networks were most common at P14 but, by P21, almost 
      all fibres had developed the perpendicular mitochondrial orientation observed in 
      mature, glycolytic fibres. Tandem mass tag proteomics were then applied to 
      examine changes in 6869 protein abundances in developing TA muscles. 
      Mitochondrial proteins increased by 32% from P1 to P42. In addition, both 
      nuclear- and mitochondrial-DNA encoded oxidative phosphorylation (OxPhos) 
      components were increased during development, whereas OxPhos assembly factors 
      decreased. Although mitochondrial dynamics and mitophagy were induced at P1-7, 
      mitochondrial biogenesis was enhanced after P14. Moreover, calcium signalling 
      proteins and the mitochondrial calcium uniporter had the highest expression early 
      in postnatal development. In conclusion, mitochondrial networks transform from a 
      fibre parallel to perpendicular orientation during the second and third weeks 
      after birth in murine glycolytic skeletal muscle. This structural transition is 
      accompanied by a change in protein expression profile from mitochondria designed 
      for co-ordinated cellular assembly to mitochondria highly specialized for 
      cellular energy metabolism.
CI  - Published 2019. This article is a U.S. Government work and is in the public 
      domain in the USA.
FAU - Kim, Yuho
AU  - Kim Y
AD  - National Heart, Lung, and Blood Institute National Institutes of Health, 
      Bethesda, MD, USA.
FAU - Yang, Daniel S
AU  - Yang DS
AD  - National Heart, Lung, and Blood Institute National Institutes of Health, 
      Bethesda, MD, USA.
FAU - Katti, Prasanna
AU  - Katti P
AD  - National Heart, Lung, and Blood Institute National Institutes of Health, 
      Bethesda, MD, USA.
FAU - Glancy, Brian
AU  - Glancy B
AUID- ORCID: 0000-0002-8571-244X
AD  - National Heart, Lung, and Blood Institute National Institutes of Health, 
      Bethesda, MD, USA.
AD  - National Institute of Arthritis and Musculoskeletal and Skin Diseases, National 
      Institutes of Health, Bethesda, MD, USA.
LA  - eng
GR  - ZIA HL006221/ImNIH/Intramural NIH HHS/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
PT  - Research Support, N.I.H., Intramural
DEP - 20190408
PL  - England
TA  - J Physiol
JT  - The Journal of physiology
JID - 0266262
RN  - 0 (Calmodulin)
RN  - EC 3.1.3.16 (Calcineurin)
RN  - EC 3.4.22.- (Calpain)
RN  - SY7Q814VUP (Calcium)
SB  - IM
CIN - J Physiol. 2019 May;597(10):2619-2620. PMID: 30980403
MH  - Aging
MH  - Animals
MH  - Animals, Newborn
MH  - Calcineurin/metabolism
MH  - Calcium/metabolism
MH  - Calcium Signaling
MH  - Calmodulin/genetics/metabolism
MH  - Calpain/genetics/metabolism
MH  - Female
MH  - Gene Expression Regulation, Developmental
MH  - Male
MH  - Mice
MH  - Mice, Inbred C57BL
MH  - Mitochondria, Muscle/*physiology
MH  - Mitochondrial Dynamics/*physiology
MH  - Muscle Development/*physiology
MH  - Muscle, Skeletal/*growth & development
MH  - Oxidative Phosphorylation
MH  - Up-Regulation
PMC - PMC6826232
OTO - NOTNLM
OT  - mitochondrial development
OT  - postnatal muscle development
OT  - proteomics
EDAT- 2019/03/29 06:00
MHDA- 2020/07/28 06:00
PMCR- 2020/05/15
CRDT- 2019/03/29 06:00
PHST- 2018/12/14 00:00 [received]
PHST- 2019/03/11 00:00 [accepted]
PHST- 2019/03/29 06:00 [pubmed]
PHST- 2020/07/28 06:00 [medline]
PHST- 2019/03/29 06:00 [entrez]
PHST- 2020/05/15 00:00 [pmc-release]
AID - TJP13497 [pii]
AID - 10.1113/JP277579 [doi]
PST - ppublish
SO  - J Physiol. 2019 May;597(10):2707-2727. doi: 10.1113/JP277579. Epub 2019 Apr 8.