LIVIVO - Search results -

Search results

Result 1 - 10 of total 35

Search options

Article ; Online: Comment on "Fiber-type traps: revisiting common misconceptions about skeletal muscle fiber types with application to motor control, biomechanics, physiology, and biology".

Reggiani, Carlo / Murgia, Marta

Journal of applied physiology (Bethesda, Md. : 1985)

2024 Volume 136, Issue 2, Page(s) 437–438

MeSH term(s)	Biomechanical Phenomena ; Biology
Language	English
Publishing date	2024-02-14
Publishing country	United States
Document type	Letter
ZDB-ID	219139-8
ISSN	1522-1601 ; 0021-8987 ; 0161-7567 ; 8750-7587
ISSN (online)	1522-1601
ISSN	0021-8987 ; 0161-7567 ; 8750-7587
DOI	10.1152/japplphysiol.00008.2024
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Uc I Zs.249: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Order via subito

This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: MYH13, a superfast myosin expressed in extraocular, laryngeal and syringeal muscles.

Schiaffino, Stefano / Hughes, Simon M / Murgia, Marta / Reggiani, Carlo

The Journal of physiology

2023 Volume 602, Issue 3, Page(s) 427–443

Abstract: MYH13 is a unique type of sarcomeric myosin heavy chain (MYH) first detected in mammalian extraocular (EO) muscles and later also in vocal muscles, including laryngeal muscles of some mammals and syringeal muscles of songbirds. All these muscles are ... ...

Abstract	MYH13 is a unique type of sarcomeric myosin heavy chain (MYH) first detected in mammalian extraocular (EO) muscles and later also in vocal muscles, including laryngeal muscles of some mammals and syringeal muscles of songbirds. All these muscles are specialized in generating very fast contractions while producing relatively low force, a design appropriate for muscles acting against a much lower load than most skeletal muscles inserting into the skeleton. The definition of the physiological properties of muscle fibres containing MYH13 has been complicated by the mixed fibre type composition of EO muscles and the coexistence of different MYH types within the same fibre. A major advance in this area came from studies on isolated recombinant myosin motors and the demonstration that the affinity of actin-bound human MYH13 for ADP is much weaker than those of fast-type MYH1 (type 2X) and MYH2 (type 2A). This property is consistent with a very fast detachment of myosin from actin, a major determinant of shortening velocity. The MYH13 gene arose early during vertebrate evolution but was characterized only in mammals and birds and appears to have been lost in some teleost fish. The MYH13 gene is located at the 3' end of the mammalian fast/developmental gene cluster and in a similar position to the orthologous cluster in syntenic regions of the songbird genome. MYH13 gene regulation is controlled by a super-enhancer in the mammalian locus and deletion of the neighbouring fast MYH1 and MYH4 genes leads to abnormal MYH13 expression in mouse leg muscles.
MeSH term(s)	Animals ; Humans ; Mice ; Actins/metabolism ; Mammals/metabolism ; Myosin Heavy Chains/genetics ; Myosin Heavy Chains/metabolism ; Myosins/metabolism ; Oculomotor Muscles/metabolism
Chemical Substances	Actins ; Myosin Heavy Chains (EC 3.6.4.1) ; Myosins (EC 3.6.4.1) ; MYH13 protein, human
Language	English
Publishing date	2023-12-31
Publishing country	England
Document type	Journal Article
ZDB-ID	3115-x
ISSN	1469-7793 ; 0022-3751
ISSN (online)	1469-7793
ISSN	0022-3751
DOI	10.1113/JP285714
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Uc I Zs.65: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Muscle fiber phenotype: a culprit of abnormal metabolism and function in skeletal muscle of humans with obesity.

Serrano, Nathan / Hyatt, Jon-Philippe K / Houmard, Joseph A / Murgia, Marta / Katsanos, Christos S

American journal of physiology. Endocrinology and metabolism

2023 Volume 325, Issue 6, Page(s) E723–E733

Abstract: The proportion of the different types of fibers in a given skeletal muscle contributes to its overall metabolic and functional characteristics. Greater proportion of type I muscle fibers is associated with favorable oxidative metabolism and function of ... ...

Abstract	The proportion of the different types of fibers in a given skeletal muscle contributes to its overall metabolic and functional characteristics. Greater proportion of type I muscle fibers is associated with favorable oxidative metabolism and function of the muscle. Humans with obesity have a lower proportion of type I muscle fibers. We discuss how lower proportion of type I fibers in skeletal muscle of humans with obesity may explain metabolic and functional abnormalities reported in these individuals. These include lower muscle glucose disposal rate, mitochondrial content, protein synthesis, and quality/contractile function, as well as increased risk for heart disease, lower levels of physical activity, and propensity for weight gain/resistance to weight loss. We delineate future research directions and the need to examine hybrid muscle fiber populations, which are indicative of a transitory state of fiber phenotype within skeletal muscle. We also describe methodologies for precisely characterizing muscle fibers and gene expression at the single muscle fiber level to enhance our understanding of the regulation of muscle fiber phenotype in obesity. By contextualizing research in the field of muscle fiber type in obesity, we lay a foundation for future advancements and pave the way for translation of this knowledge to address impaired metabolism and function in obesity.
MeSH term(s)	Humans ; Muscle Fibers, Skeletal/metabolism ; Muscle, Skeletal/metabolism ; Obesity/metabolism ; Muscle Fibers, Slow-Twitch/metabolism ; Phenotype ; Myosin Heavy Chains/metabolism
Chemical Substances	Myosin Heavy Chains (EC 3.6.4.1)
Language	English
Publishing date	2023-10-25
Publishing country	United States
Document type	Journal Article ; Review ; Research Support, N.I.H., Extramural
ZDB-ID	603841-4
ISSN	1522-1555 ; 0193-1849
ISSN (online)	1522-1555
ISSN	0193-1849
DOI	10.1152/ajpendo.00190.2023
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Uc I Zs.89: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Multi-Omics Approach to Mitochondrial DNA Damage in Human Muscle Fibers.

Elstner, Matthias / Olszewski, Konrad / Prokisch, Holger / Klopstock, Thomas / Murgia, Marta

International journal of molecular sciences

2021 Volume 22, Issue 20

Abstract: Mitochondrial DNA deletions affect energy metabolism at tissue-specific and cell-specific threshold levels, but the pathophysiological mechanisms determining cell fate remain poorly understood. Chronic progressive external ophthalmoplegia (CPEO) is ... ...

Abstract	Mitochondrial DNA deletions affect energy metabolism at tissue-specific and cell-specific threshold levels, but the pathophysiological mechanisms determining cell fate remain poorly understood. Chronic progressive external ophthalmoplegia (CPEO) is caused by mtDNA deletions and characterized by a mosaic distribution of muscle fibers with defective cytochrome oxidase (COX) activity, interspersed among fibers with retained functional respiratory chain. We used diagnostic histochemistry to distinguish COX-negative from COX-positive fibers in nine muscle biopsies from CPEO patients and performed laser capture microdissection (LCM) coupled to genome-wide gene expression analysis. To gain molecular insight into the pathogenesis, we applied network and pathway analysis to highlight molecular differences of the COX-positive and COX-negative fiber transcriptome. We then integrated our results with proteomics data that we previously obtained comparing COX-positive and COX-negative fiber sections from three other patients. By virtue of the combination of LCM and a multi-omics approach, we here provide a comprehensive resource to tackle the pathogenic changes leading to progressive respiratory chain deficiency and disease in mitochondrial deletion syndromes. Our data show that COX-negative fibers upregulate transcripts involved in translational elongation and protein synthesis. Furthermore, based on functional annotation analysis, we find that mitochondrial transcripts are the most enriched among those with significantly different expression between COX-positive and COX-negative fibers, indicating that our unbiased large-scale approach resolves the core of the pathogenic changes. Further enrichments include transcripts encoding LIM domain proteins, ubiquitin ligases, proteins involved in RNA turnover, and, interestingly, cell cycle arrest and cell death. These pathways may thus have a functional association to the molecular pathogenesis of the disease. Overall, the transcriptome and proteome show a low degree of correlation in CPEO patients, suggesting a relevant contribution of post-transcriptional mechanisms in shaping this disease phenotype.
MeSH term(s)	DNA, Mitochondrial/genetics ; Electron Transport Complex IV/metabolism ; Female ; Gene Expression Profiling ; Gene Regulatory Networks ; Humans ; Laser Capture Microdissection ; Male ; Mitochondria, Muscle/genetics ; Mitochondria, Muscle/pathology ; Muscle Fibers, Skeletal/pathology ; NADPH Dehydrogenase/genetics ; NADPH Dehydrogenase/metabolism ; Ophthalmoplegia, Chronic Progressive External/genetics ; Ophthalmoplegia, Chronic Progressive External/pathology ; Proteomics/methods ; Succinate Dehydrogenase/metabolism
Chemical Substances	DNA, Mitochondrial ; NDUFA12 protein, human ; Succinate Dehydrogenase (EC 1.3.99.1) ; NADPH Dehydrogenase (EC 1.6.99.1) ; Electron Transport Complex IV (EC 1.9.3.1)
Language	English
Publishing date	2021-10-14
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms222011080
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: Genes Whose Gain or Loss of Function Changes Type 1, 2A, 2X, or 2B Muscle Fibre Proportions in Mice-A Systematic Review.

Kuhnen, Gabryela / Guedes Russomanno, Tiago / Murgia, Marta / Pillon, Nicolas J / Schönfelder, Martin / Wackerhage, Henning

International journal of molecular sciences

2022 Volume 23, Issue 21

Abstract: Adult skeletal muscle fibres are classified as type 1, 2A, 2X, and 2B. These classifications are based on the expression of the dominant myosin heavy chain isoform. Muscle fibre-specific gene expression and proportions of muscle fibre types change during ...

Abstract	Adult skeletal muscle fibres are classified as type 1, 2A, 2X, and 2B. These classifications are based on the expression of the dominant myosin heavy chain isoform. Muscle fibre-specific gene expression and proportions of muscle fibre types change during development and in response to exercise, chronic electrical stimulation, or inactivity. To identify genes whose gain or loss-of-function alters type 1, 2A, 2X, or 2B muscle fibre proportions in mice, we conducted a systematic review of transgenic mouse studies. The systematic review was conducted in accordance with the 2009 PRISMA guidelines and the PICO framework. We identified 25 "muscle fibre genes" (
MeSH term(s)	Adult ; Mice ; Animals ; Humans ; Muscle Fibers, Skeletal/metabolism ; Myosin Heavy Chains/genetics ; Myosin Heavy Chains/metabolism ; Protein Isoforms/metabolism ; Electric Stimulation ; Muscle, Skeletal/metabolism ; RNA-Binding Proteins/metabolism ; Forkhead Transcription Factors/metabolism ; Nuclear Receptor Co-Repressor 1/metabolism
Chemical Substances	Myosin Heavy Chains (EC 3.6.4.1) ; Protein Isoforms ; PPARGC1B protein, human ; RNA-Binding Proteins ; FoxJ3 protein, human ; Forkhead Transcription Factors ; Ncor1 protein, mouse ; Nuclear Receptor Co-Repressor 1
Language	English
Publishing date	2022-10-26
Publishing country	Switzerland
Document type	Systematic Review ; Journal Article ; Review
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms232112933
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: Fiber type diversity in skeletal muscle explored by mass spectrometry-based single fiber proteomics.

Schiaffino, Stefano / Reggiani, Carlo / Murgia, Marta

Histology and histopathology

2019 Volume 35, Issue 3, Page(s) 239–246

Abstract: Mammalian skeletal muscles are composed of a variety of muscle fibers with specialized functional properties. Slow fibers are suited for long lasting and low intensity contractile activity, while various subtypes of fast fibers are optimized to produce ... ...

Abstract	Mammalian skeletal muscles are composed of a variety of muscle fibers with specialized functional properties. Slow fibers are suited for long lasting and low intensity contractile activity, while various subtypes of fast fibers are optimized to produce high force and power even with a significant fatigue. The functional specialization of muscle fibers is based on selective gene expression regulation, which provides each fiber with a specific protein complement. The recent refinement of small-scale sample preparation, combined with the development of mass spectrometers characterized by high sensitivity, sequencing speed and mass accuracy, has allowed the characterization of the proteome of single muscle fibers with an unprecedented resolution. In the last few years, the first studies on the global proteomics of individual fibers of different types have been published. In this short review we discuss the methodological advancements which have opened the way to single fiber proteomics and the discovery power of this approach. We provide examples of how specific features of single fibers can be overlooked when whole muscle or multi-fiber samples are analyzed and can only be detected when a single fiber proteome is analyzed. Thus, novel subtype-specific metabolic features, most prominently mitochondrial specialization of fiber types have been revealed by single fiber proteomics. In the same way, specific adaptive responses of single fibers to aging or loss of neural input have been detected when single fibers were individually analyzed. We conclude that the fiber type-resolved proteomes represent a powerful tool which can be applied to a variety of physiological and pathological conditions.
MeSH term(s)	Animals ; Gene Expression Regulation ; Humans ; Mass Spectrometry ; Mice ; Mitochondria/metabolism ; Muscle Contraction ; Muscle Fibers, Skeletal/physiology ; Muscle Fibers, Slow-Twitch/physiology ; Muscle, Skeletal/physiology ; Myocardial Contraction ; Protein Isoforms ; Proteome/metabolism ; Proteomics
Chemical Substances	Protein Isoforms ; Proteome
Language	English
Publishing date	2019-10-15
Publishing country	Spain
Document type	Journal Article ; Review
ZDB-ID	83911-5
ISSN	1699-5848 ; 0213-3911
ISSN (online)	1699-5848
ISSN	0213-3911
DOI	10.14670/HH-18-170
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.B 3013: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Protein profile of fiber types in human skeletal muscle: a single-fiber proteomics study.

Murgia, Marta / Nogara, Leonardo / Baraldo, Martina / Reggiani, Carlo / Mann, Matthias / Schiaffino, Stefano

Skeletal muscle

2021 Volume 11, Issue 1, Page(s) 24

Abstract: Background: Human skeletal muscle is composed of three major fiber types, referred to as type 1, 2A, and 2X fibers. This heterogeneous cellular composition complicates the interpretation of studies based on whole skeletal muscle lysate. A single-fiber ... ...

Abstract	Background: Human skeletal muscle is composed of three major fiber types, referred to as type 1, 2A, and 2X fibers. This heterogeneous cellular composition complicates the interpretation of studies based on whole skeletal muscle lysate. A single-fiber proteomics approach is required to obtain a fiber-type resolved quantitative information on skeletal muscle pathophysiology. Methods: Single fibers were dissected from vastus lateralis muscle biopsies of young adult males and processed for mass spectrometry-based single-fiber proteomics. We provide and analyze a resource dataset based on relatively pure fibers, containing at least 80% of either MYH7 (marker of slow type 1 fibers), MYH2 (marker of fast 2A fibers), or MYH1 (marker of fast 2X fibers). Results: In a dataset of more than 3800 proteins detected by single-fiber proteomics, we selected 404 proteins showing a statistically significant difference among fiber types. We identified numerous type 1 or 2X fiber type-specific protein markers, defined as proteins present at 3-fold or higher levels in these compared to other fiber types. In contrast, we could detect only two 2A-specific protein markers in addition to MYH2. We observed three other major patterns: proteins showing a differential distribution according to the sequence 1 > 2A > 2X or 2X > 2A > 1 and type 2-specific proteins expressed in 2A and 2X fibers at levels 3 times greater than in type 1 fibers. In addition to precisely quantifying known fiber type-specific protein patterns, our study revealed several novel features of fiber type specificity, including the selective enrichment of components of the dystrophin and integrin complexes, as well as microtubular proteins, in type 2X fibers. The fiber type-specific distribution of some selected proteins revealed by proteomics was validated by immunofluorescence analyses with specific antibodies. Conclusion: We here show that numerous muscle proteins, including proteins whose function is unknown, are selectively enriched in specific fiber types, pointing to potential implications in muscle pathophysiology. This reinforces the notion that single-fiber proteomics, together with recently developed approaches to single-cell proteomics, will be instrumental to explore and quantify muscle cell heterogeneity.
MeSH term(s)	Humans ; Male ; Muscle Fibers, Skeletal ; Muscle Proteins ; Muscle, Skeletal ; Proteomics
Chemical Substances	Muscle Proteins
Language	English
Publishing date	2021-11-02
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2595637-1
ISSN	2044-5040 ; 2044-5040
ISSN (online)	2044-5040
ISSN	2044-5040
DOI	10.1186/s13395-021-00279-0
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article: Calsequestrins New Calcium Store Markers of Adult Zebrafish Cerebellum and Optic Tectum.

Furlan, Sandra / Campione, Marina / Murgia, Marta / Mosole, Simone / Argenton, Francesco / Volpe, Pompeo / Nori, Alessandra

Frontiers in neuroanatomy

2020 Volume 14, Page(s) 15

Abstract: Calcium stores in neurons are heterogeneous in compartmentalization and molecular composition. ...

Abstract	Calcium stores in neurons are heterogeneous in compartmentalization and molecular composition.
Language	English
Publishing date	2020-04-21
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2452969-2
ISSN	1662-5129
ISSN	1662-5129
DOI	10.3389/fnana.2020.00015
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: Molecular diversity and pleiotropic role of the mitochondrial calcium uniporter.

Murgia, Marta / Rizzuto, Rosario

Cell calcium

2014 Volume 58, Issue 1, Page(s) 11–17

Abstract: The long awaited molecular identification of the mitochondrial calcium uniporter (MCU) in 2011 has opened an exciting phase in the study of mitochondrial calcium homeostasis. On the one hand, MCU proved to be the core of a complex signaling system, ... ...

Abstract	The long awaited molecular identification of the mitochondrial calcium uniporter (MCU) in 2011 has opened an exciting phase in the study of mitochondrial calcium homeostasis. On the one hand, MCU proved to be the core of a complex signaling system, composed of a channel moiety (MCU itself and the related MCUb protein) and a family of essential regulators (the MICUs, MCUR, EMRE). On the other hand, the availability of molecular information and tools opened the possibility of directly altering mitochondrial calcium homeostasis in cell cultures or intact organisms, thus obtaining new insight into its role in physiological and pathological events. We will review here these exciting advancements, summarizing the current knowledge of the molecular composition of the MCU complex and of its role in shaping mitochondrial and cytosolic [Ca(2+)] signals.
MeSH term(s)	Calcium/metabolism ; Calcium Channels/chemistry ; Calcium Channels/genetics ; Calcium Channels/metabolism ; Calcium Signaling ; Humans ; Mitochondria/metabolism ; RNA Interference
Chemical Substances	Calcium Channels ; SMDT1 protein, human ; mitochondrial calcium uniporter ; Calcium (SY7Q814VUP)
Language	English
Publishing date	2014-11-13
Publishing country	Netherlands
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	757687-0
ISSN	1532-1991 ; 0143-4160
ISSN (online)	1532-1991
ISSN	0143-4160
DOI	10.1016/j.ceca.2014.11.001
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 1596: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (1.OG)
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article: Acyl-CoA thioesterase-2 facilitates β-oxidation in glycolytic skeletal muscle in a lipid supply dependent manner.

Bekeova, Carmen / Han, Ji In / Xu, Heli / Kerr, Evan / Blackburne, Brittney / Lynch, Shannon C / Mesaros, Clementina / Murgia, Marta / Vadigepalli, Rajanikanth / Beld, Joris / Leonardi, Roberta / Snyder, Nathaniel W / Seifert, Erin L

bioRxiv : the preprint server for biology

2023

Abstract: Acyl-Coenzyme A (acyl-CoA) thioesters are compartmentalized intermediates that participate in in multiple metabolic reactions within the mitochondrial matrix. The limited availability of free CoA (CoASH) in the matrix raises the question of how the local ...

Abstract	Acyl-Coenzyme A (acyl-CoA) thioesters are compartmentalized intermediates that participate in in multiple metabolic reactions within the mitochondrial matrix. The limited availability of free CoA (CoASH) in the matrix raises the question of how the local acyl-CoA concentration is regulated to prevent trapping of CoASH from overload of any specific substrate. Acyl-CoA thioesterase-2 (ACOT2) hydrolyzes long-chain acyl-CoAs to their constituent fatty acids and CoASH, and is the only mitochondrial matrix ACOT refractory to inhibition by CoASH. Thus, we reasoned that ACOT2 may constitutively regulate matrix acyl-CoA levels.
Language	English
Publishing date	2023-06-27
Publishing country	United States
Document type	Preprint
DOI	10.1101/2023.06.27.546724
Database	MEDical Literature Analysis and Retrieval System OnLINE

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Details ▾

To top

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

Order via subito

More links

Kategorien

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

Order via subito

More links

Kategorien

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

Inter-library loan at ZB MED