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Article ; Online: Signaling roles of platelets in skeletal muscle regeneration

Graca, Flavia A. / Minden‐Birkenmaier, Benjamin A. / Stephan, Anna / Demontis, Fabio / Labelle, Myriam

BioEssays. 2023 Dec., v. 45, no. 12 p.e2300134-

2023

Abstract: Platelets have important hemostatic functions in repairing blood vessels upon tissue injury. Cytokines, growth factors, and metabolites stored in platelet α‐granules and dense granules are released upon platelet activation and clotting. Emerging evidence ...

Abstract	Platelets have important hemostatic functions in repairing blood vessels upon tissue injury. Cytokines, growth factors, and metabolites stored in platelet α‐granules and dense granules are released upon platelet activation and clotting. Emerging evidence indicates that such platelet‐derived signaling factors are instrumental in guiding tissue regeneration. Here, we discuss the important roles of platelet‐secreted signaling factors in skeletal muscle regeneration. Chemokines secreted by platelets in the early phase after injury are needed to recruit neutrophils to injured muscles, and impeding this early step of muscle regeneration exacerbates inflammation at later stages, compromises neo‐angiogenesis and the growth of newly formed myofibers, and reduces post‐injury muscle force production. Platelets also contribute to the recruitment of pro‐regenerative stromal cells from the adipose tissue, and the platelet releasate may also regulate the metabolism and proliferation of muscle satellite cells, which sustain myogenesis. Therefore, harnessing the signaling functions of platelets and the platelet secretome may provide new avenues for promoting skeletal muscle regeneration in health and disease.
Keywords	adipose tissue ; angiogenesis ; chemokines ; inflammation ; metabolism ; metabolites ; muscle development ; muscles ; neutrophils ; platelet activation ; skeletal muscle ; tissue repair
Language	English
Dates of publication	2023-12
Publishing place	John Wiley & Sons, Ltd
Document type	Article ; Online
Note	JOURNAL ARTICLE
ZDB-ID	50140-2
ISSN	1521-1878 ; 0265-9247
ISSN (online)	1521-1878
ISSN	0265-9247
DOI	10.1002/bies.202300134
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: Electroporation of Small Interfering RNAs into Tibialis Anterior Muscles of Mice.

Stephan, Anna / Graca, Flavia A / Hunt, Liam C / Demontis, Fabio

Bio-protocol

2022 Volume 12, Issue 11

Abstract: Aging and wasting of skeletal muscle reduce organismal fitness. Regrettably, only limited interventions are currently available to address this unmet medical need. Many methods have been developed to study this condition, including the intramuscular ... ...

Abstract	Aging and wasting of skeletal muscle reduce organismal fitness. Regrettably, only limited interventions are currently available to address this unmet medical need. Many methods have been developed to study this condition, including the intramuscular electroporation of DNA plasmids. However, this technique requires surgery and high electrical fields, which cause tissue damage. Here, we report an optimized protocol for the electroporation of small interfering RNAs (siRNAs) into the tibialis anterior muscle of mice. This protocol does not require surgery and, because of the small siRNA size, mild electroporation conditions are utilized. By inducing target mRNA knockdown, this method can be used to interrogate gene function in muscles of mice from different strains, genotypes, and ages. Moreover, a complementary method for siRNA transfection into differentiated myotubes can be used for testing siRNA efficacy before
Language	English
Publishing date	2022-06-05
Publishing country	United States
Document type	Journal Article
ZDB-ID	2833269-6
ISSN	2331-8325 ; 2331-8325
ISSN (online)	2331-8325
ISSN	2331-8325
DOI	10.21769/BioProtoc.4428
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Signaling roles of platelets in skeletal muscle regeneration.

Graca, Flavia A / Minden-Birkenmaier, Benjamin A / Stephan, Anna / Demontis, Fabio / Labelle, Myriam

BioEssays : news and reviews in molecular, cellular and developmental biology

2023 Volume 45, Issue 12, Page(s) e2300134

Abstract: Platelets have important hemostatic functions in repairing blood vessels upon tissue injury. Cytokines, growth factors, and metabolites stored in platelet α-granules and dense granules are released upon platelet activation and clotting. Emerging evidence ...

Abstract	Platelets have important hemostatic functions in repairing blood vessels upon tissue injury. Cytokines, growth factors, and metabolites stored in platelet α-granules and dense granules are released upon platelet activation and clotting. Emerging evidence indicates that such platelet-derived signaling factors are instrumental in guiding tissue regeneration. Here, we discuss the important roles of platelet-secreted signaling factors in skeletal muscle regeneration. Chemokines secreted by platelets in the early phase after injury are needed to recruit neutrophils to injured muscles, and impeding this early step of muscle regeneration exacerbates inflammation at later stages, compromises neo-angiogenesis and the growth of newly formed myofibers, and reduces post-injury muscle force production. Platelets also contribute to the recruitment of pro-regenerative stromal cells from the adipose tissue, and the platelet releasate may also regulate the metabolism and proliferation of muscle satellite cells, which sustain myogenesis. Therefore, harnessing the signaling functions of platelets and the platelet secretome may provide new avenues for promoting skeletal muscle regeneration in health and disease.
MeSH term(s)	Blood Platelets/metabolism ; Muscle, Skeletal/physiology ; Signal Transduction ; Wound Healing ; Cytokines/metabolism
Chemical Substances	Cytokines
Language	English
Publishing date	2023-09-15
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
ZDB-ID	50140-2
ISSN	1521-1878 ; 0265-9247
ISSN (online)	1521-1878
ISSN	0265-9247
DOI	10.1002/bies.202300134
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Platelet-derived chemokines promote skeletal muscle regeneration by guiding neutrophil recruitment to injured muscles.

Graca, Flavia A / Stephan, Anna / Minden-Birkenmaier, Benjamin A / Shirinifard, Abbas / Wang, Yong-Dong / Demontis, Fabio / Labelle, Myriam

Nature communications

2023 Volume 14, Issue 1, Page(s) 2900

Abstract: Skeletal muscle regeneration involves coordinated interactions between different cell types. Injection of platelet-rich plasma is circumstantially considered an aid to muscle repair but whether platelets promote regeneration beyond their role in ... ...

Abstract	Skeletal muscle regeneration involves coordinated interactions between different cell types. Injection of platelet-rich plasma is circumstantially considered an aid to muscle repair but whether platelets promote regeneration beyond their role in hemostasis remains unexplored. Here, we find that signaling via platelet-released chemokines is an early event necessary for muscle repair in mice. Platelet depletion reduces the levels of the platelet-secreted neutrophil chemoattractants CXCL5 and CXCL7/PPBP. Consequently, early-phase neutrophil infiltration to injured muscles is impaired whereas later inflammation is exacerbated. Consistent with this model, neutrophil infiltration to injured muscles is compromised in male mice with Cxcl7-knockout platelets. Moreover, neo-angiogenesis and the re-establishment of myofiber size and muscle strength occurs optimally in control mice post-injury but not in Cxcl7ko mice and in neutrophil-depleted mice. Altogether, these findings indicate that platelet-secreted CXCL7 promotes regeneration by recruiting neutrophils to injured muscles, and that this signaling axis could be utilized therapeutically to boost muscle regeneration.
MeSH term(s)	Mice ; Male ; Animals ; Neutrophil Infiltration ; Chemokines ; Muscle, Skeletal/physiology ; Inflammation ; Neutrophils/physiology
Chemical Substances	Chemokines
Language	English
Publishing date	2023-05-22
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/s41467-023-38624-0
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Modulation of protease expression by the transcription factor Ptx1/PITX regulates protein quality control during aging.

Jiao, Jianqin / Curley, Michelle / Graca, Flavia A / Robles-Murguia, Maricela / Shirinifard, Abbas / Finkelstein, David / Xu, Beisi / Fan, Yiping / Demontis, Fabio

Cell reports

2023 Volume 42, Issue 1, Page(s) 111970

Abstract: Protein quality control is important for healthy aging and is dysregulated in age-related diseases. The autophagy-lysosome and ubiquitin-proteasome are key for proteostasis, but it remains largely unknown whether other proteolytic systems also contribute ...

Abstract	Protein quality control is important for healthy aging and is dysregulated in age-related diseases. The autophagy-lysosome and ubiquitin-proteasome are key for proteostasis, but it remains largely unknown whether other proteolytic systems also contribute to maintain proteostasis during aging. Here, we find that expression of proteolytic enzymes (proteases/peptidases) distinct from the autophagy-lysosome and ubiquitin-proteasome systems declines during skeletal muscle aging in Drosophila. Age-dependent protease downregulation undermines proteostasis, as demonstrated by the increase in detergent-insoluble poly-ubiquitinated proteins and pathogenic huntingtin-polyQ levels in response to protease knockdown. Computational analyses identify the transcription factor Ptx1 (homologous to human PITX1/2/3) as a regulator of protease expression. Consistent with this model, Ptx1 protein levels increase with aging, and Ptx1 RNAi counteracts the age-associated downregulation of protease expression. Moreover, Ptx1 RNAi improves muscle protein quality control in a protease-dependent manner and extends lifespan. These findings indicate that proteases and their transcriptional modulator Ptx1 ensure proteostasis during aging.
MeSH term(s)	Humans ; Aging/metabolism ; Endopeptidases/metabolism ; Proteasome Endopeptidase Complex/metabolism ; Proteolysis ; Transcription Factors/metabolism ; Ubiquitins/metabolism ; Animals ; Drosophila
Chemical Substances	Endopeptidases (EC 3.4.-) ; Proteasome Endopeptidase Complex (EC 3.4.25.1) ; Transcription Factors ; Ubiquitins ; Ptx1 protein, Drosophila
Language	English
Publishing date	2023-01-10
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2649101-1
ISSN	2211-1247 ; 2211-1247
ISSN (online)	2211-1247
ISSN	2211-1247
DOI	10.1016/j.celrep.2022.111970
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: A large-scale transgenic RNAi screen identifies transcription factors that modulate myofiber size in Drosophila.

Graca, Flavia A / Sheffield, Natalie / Puppa, Melissa / Finkelstein, David / Hunt, Liam C / Demontis, Fabio

PLoS genetics

2021 Volume 17, Issue 11, Page(s) e1009926

Abstract: Myofiber atrophy occurs with aging and in many diseases but the underlying mechanisms are incompletely understood. Here, we have used >1,100 muscle-targeted RNAi interventions to comprehensively assess the function of 447 transcription factors in the ... ...

Abstract	Myofiber atrophy occurs with aging and in many diseases but the underlying mechanisms are incompletely understood. Here, we have used >1,100 muscle-targeted RNAi interventions to comprehensively assess the function of 447 transcription factors in the developmental growth of body wall skeletal muscles in Drosophila. This screen identifies new regulators of myofiber atrophy and hypertrophy, including the transcription factor Deaf1. Deaf1 RNAi increases myofiber size whereas Deaf1 overexpression induces atrophy. Consistent with its annotation as a Gsk3 phosphorylation substrate, Deaf1 and Gsk3 induce largely overlapping transcriptional changes that are opposed by Deaf1 RNAi. The top category of Deaf1-regulated genes consists of glycolytic enzymes, which are suppressed by Deaf1 and Gsk3 but are upregulated by Deaf1 RNAi. Similar to Deaf1 and Gsk3 overexpression, RNAi for glycolytic enzymes reduces myofiber growth. Altogether, this study defines the repertoire of transcription factors that regulate developmental myofiber growth and the role of Gsk3/Deaf1/glycolysis in this process.
MeSH term(s)	Animals ; Animals, Genetically Modified/genetics ; DNA-Binding Proteins/genetics ; Disease Models, Animal ; Drosophila Proteins/genetics ; Drosophila melanogaster/genetics ; Embryonic Development/genetics ; Glycogen Synthase Kinase 3/genetics ; Glycolysis/genetics ; Humans ; Muscle, Skeletal/growth & development ; Muscle, Skeletal/metabolism ; Muscular Atrophy/genetics ; Muscular Atrophy/pathology ; Myofibrils/genetics ; Myofibrils/metabolism ; RNA Interference ; Transcription Factors/genetics
Chemical Substances	DNA-Binding Proteins ; Deaf1 protein, Drosophila ; Drosophila Proteins ; Transcription Factors ; Glycogen Synthase Kinase 3 (EC 2.7.11.26)
Language	English
Publishing date	2021-11-15
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2186725-2
ISSN	1553-7404 ; 1553-7390
ISSN (online)	1553-7404
ISSN	1553-7390
DOI	10.1371/journal.pgen.1009926
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Progressive development of melanoma-induced cachexia differentially impacts organ systems in mice.

Graca, Flavia A / Stephan, Anna / Wang, Yong-Dong / Shirinifard, Abbas / Jiao, Jianqin / Vogel, Peter / Labelle, Myriam / Demontis, Fabio

Cell reports

2022 Volume 42, Issue 1, Page(s) 111934

Abstract: Cachexia is a systemic wasting syndrome that increases cancer-associated mortality. How cachexia progressively and differentially impacts distinct tissues is largely unknown. Here, we find that the heart and skeletal muscle undergo wasting at early ... ...

Abstract	Cachexia is a systemic wasting syndrome that increases cancer-associated mortality. How cachexia progressively and differentially impacts distinct tissues is largely unknown. Here, we find that the heart and skeletal muscle undergo wasting at early stages and are the tissues transcriptionally most impacted by cachexia. We also identify general and organ-specific transcriptional changes that indicate functional derangement by cachexia even in tissues that do not undergo wasting, such as the brain. Secreted factors constitute a top category of cancer-regulated genes in host tissues, and these changes include upregulation of the angiotensin-converting enzyme (ACE). ACE inhibition with the drug lisinopril improves muscle force and partially impedes cachexia-induced transcriptional changes, although wasting is not prevented, suggesting that cancer-induced host-secreted factors can regulate tissue function during cachexia. Altogether, by defining prevalent and temporal and tissue-specific responses to cachexia, this resource highlights biomarkers and possible targets for general and tissue-tailored anti-cachexia therapies.
MeSH term(s)	Mice ; Animals ; Cachexia ; Neoplasms/pathology ; Muscle, Skeletal/pathology ; Wasting Syndrome/complications ; Melanoma/pathology ; Muscular Atrophy/pathology
Language	English
Publishing date	2022-12-29
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2649101-1
ISSN	2211-1247 ; 2211-1247
ISSN (online)	2211-1247
ISSN	2211-1247
DOI	10.1016/j.celrep.2022.111934
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Analysis of proteostasis during aging with western blot of detergent-soluble and insoluble protein fractions.

Rai, Mamta / Curley, Michelle / Coleman, Zane / Nityanandam, Anjana / Jiao, Jianqin / Graca, Flavia A / Hunt, Liam C / Demontis, Fabio

STAR protocols

2021 Volume 2, Issue 3, Page(s) 100628

Abstract: Defects in protein quality control are the underlying cause of age-related diseases. The western blot analysis of detergent-soluble and insoluble protein fractions has proven useful in identifying interventions that regulate proteostasis. Here, we ... ...

Abstract	Defects in protein quality control are the underlying cause of age-related diseases. The western blot analysis of detergent-soluble and insoluble protein fractions has proven useful in identifying interventions that regulate proteostasis. Here, we describe the protocol for such analyses in
MeSH term(s)	Animals ; Blotting, Western/methods ; Detergents/chemistry ; Electrophoresis, Polyacrylamide Gel ; HEK293 Cells ; Humans ; Mice ; Proteins/chemistry ; Proteins/metabolism ; Proteostasis ; Solubility ; Ubiquitination
Chemical Substances	Detergents ; Proteins
Language	English
Publishing date	2021-06-23
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ISSN	2666-1667
ISSN (online)	2666-1667
DOI	10.1016/j.xpro.2021.100628
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: An adaptive stress response that confers cellular resilience to decreased ubiquitination.

Hunt, Liam C / Pagala, Vishwajeeth / Stephan, Anna / Xie, Boer / Kodali, Kiran / Kavdia, Kanisha / Wang, Yong-Dong / Shirinifard, Abbas / Curley, Michelle / Graca, Flavia A / Fu, Yingxue / Poudel, Suresh / Li, Yuxin / Wang, Xusheng / Tan, Haiyan / Peng, Junmin / Demontis, Fabio

Nature communications

2023 Volume 14, Issue 1, Page(s) 7348

Abstract: Ubiquitination is a post-translational modification initiated by the E1 enzyme UBA1, which transfers ubiquitin to ~35 E2 ubiquitin-conjugating enzymes. While UBA1 loss is cell lethal, it remains unknown how partial reduction in UBA1 activity is endured. ... ...

Abstract	Ubiquitination is a post-translational modification initiated by the E1 enzyme UBA1, which transfers ubiquitin to ~35 E2 ubiquitin-conjugating enzymes. While UBA1 loss is cell lethal, it remains unknown how partial reduction in UBA1 activity is endured. Here, we utilize deep-coverage mass spectrometry to define the E1-E2 interactome and to determine the proteins that are modulated by knockdown of UBA1 and of each E2 in human cells. These analyses define the UBA1/E2-sensitive proteome and the E2 specificity in protein modulation. Interestingly, profound adaptations in peroxisomes and other organelles are triggered by decreased ubiquitination. While the cargo receptor PEX5 depends on its mono-ubiquitination for binding to peroxisomal proteins and importing them into peroxisomes, we find that UBA1/E2 knockdown induces the compensatory upregulation of other PEX proteins necessary for PEX5 docking to the peroxisomal membrane. Altogether, this study defines a homeostatic mechanism that sustains peroxisomal protein import in cells with decreased ubiquitination capacity.
MeSH term(s)	Humans ; Ubiquitination ; Ubiquitin/metabolism ; Protein Transport/physiology ; Peroxisomes/metabolism ; Intracellular Membranes/metabolism
Chemical Substances	Ubiquitin
Language	English
Publishing date	2023-11-14
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/s41467-023-43262-7
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Resveratrol directly suppresses proteolysis possibly via PKA/CREB signaling in denervated rat skeletal muscle.

I S Júnior, Ivanildo / Zanetti, Gustavo O / Vieira, Tales S / Albuquerque, Flávia P / Gomes, Dayane A / Paula-Gomes, Silva / Valentim, Rafael R / Graça, Flavia A / Kettlhut, Isis C / Navegantes, Luiz C C / Gonçalves, Dawit A P / Lira, Eduardo C

Anais da Academia Brasileira de Ciencias

2023 Volume 95, Issue suppl 2, Page(s) e20220877

Abstract: Although there are reports that polyphenol resveratrol (Rsv) may cause muscle hypertrophy in basal conditions and attenuate muscle wasting in catabolic situations, its mechanism of action is still unclear. Our study evaluated the ex vivo effects of Rsv ... ...

Abstract	Although there are reports that polyphenol resveratrol (Rsv) may cause muscle hypertrophy in basal conditions and attenuate muscle wasting in catabolic situations, its mechanism of action is still unclear. Our study evaluated the ex vivo effects of Rsv on protein metabolism and intracellular signaling in innervated (sham-operated; Sham) and 3-day sciatic denervated (Den) rat skeletal muscles. Rsv (10-4 M) reduced total proteolysis (40%) in sham muscles. Den increased total proteolysis (~40%) in muscle, which was accompanied by an increase in the activities of ubiquitin-proteasome (~3-fold) and lysosomal (100%) proteolytic systems. Rsv reduced total proteolysis (59%) in Den muscles by inhibiting the hyperactivation of ubiquitin-proteasome (50%) and lysosomal (~70%) systems. Neither Rsv nor Den altered calcium-dependent proteolysis in muscles. Mechanistically, Rsv stimulated PKA/CREB signaling in Den muscles, and PKA blockage by H89 (50μM) abolished the antiproteolytic action of the polyphenol. Rsv reduced FoxO4 phosphorylation (~60%) in both Sham and Den muscles and Akt phosphorylation (36%) in Den muscles. Rsv also caused a homeostatic effect in Den muscles by returning their protein synthesis rates to levels similar to Sham muscles. These data indicate that Rsv directly inhibits the proteolytic activity of lysosomal and ubiquitin-proteasome systems, mainly in Den muscles through, at least in part, the activation of PKA/CREB signaling.
MeSH term(s)	Rats ; Animals ; Proteolysis ; Proteasome Endopeptidase Complex/metabolism ; Proteasome Endopeptidase Complex/pharmacology ; Resveratrol/pharmacology ; Muscle, Skeletal/metabolism ; Rats, Wistar ; Ubiquitins/metabolism ; Ubiquitins/pharmacology
Chemical Substances	Proteasome Endopeptidase Complex (EC 3.4.25.1) ; Resveratrol (Q369O8926L) ; Ubiquitins
Language	English
Publishing date	2023-12-01
Publishing country	Brazil
Document type	Journal Article
ZDB-ID	2046885-4
ISSN	1678-2690 ; 0001-3765
ISSN (online)	1678-2690
ISSN	0001-3765
DOI	10.1590/0001-3765202320220877
Database	MEDical Literature Analysis and Retrieval System OnLINE

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