Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Annexin A2 causes motor incoordination via muscle-cerebellum axis in sarcopenia

ABSTRACT: Annexin A2 causes motor incoordination via muscle-cerebellum axis in sarcopenia

ORGANISM(S): Mus Musculus

SUBMITTER: Dongyun Gu

PROVIDER: PXD068704 | iProX | Mon Sep 22 00:00:00 GMT+01:00 2025

REPOSITORIES: iProX

ACCESS DATA

Json Xml

Publications

Annexin A2 Causes Motor Incoordination via Muscle-Cerebellum Axis in Sarcopenia.

Jiao Xin X Wang Zengguang Z Chang Hanwen H Li Yongjin Y Wang Binbin B Shao Xinfa X Zhang Yuxin Y Lin Yixuan Y Jia Xinlin X Zhou Xianhao X Li Wentao W Luo Dinghao D Deng Tanjun T Lin Xingzuan X Xu Chen C Gan Yaokai Y Gu Dongyun D

Journal of cachexia, sarcopenia and muscle 20260201 1

<h4>Background</h4>Sarcopenia is a prevalent age-related disorder characterized by progressive muscle atrophy. Impaired balance is one of its most critical clinical consequences, often leading to falling and even bone fractures. As the cerebellum plays a central role in regulating motor coordination, elucidating the molecular mechanisms underlying imbalance in sarcopenia, particularly those mediated by the muscle-cerebellum axis, remains an important yet unresolved question.<h4>Methods</h4>4D la ...[more]

PMID: 41588637

Similar Datasets

Role of annexin A2 in muscle repair

Project description:Repair of injured muscle involves repair of injured myofibers through the involvement of dysferlin and its interacting partners, including annexin. Studies with mice and patients have established that dysferlin deficit leads to chronic inflammation and adipogenic replacement of the diseased muscle. However, longitudinal analysis of annexin deficit on muscle pathology and function is lacking. Here we show that unlike annexin A1, but similar to dysferlin, lack of annexin A2 (AnxA2) causes poor myofiber repair and progressive weakening with age. However, unlike dysferlin-deficient muscle, AnxA2-deficient muscles do not exhibit chronic inflammation or adipogenic replacement. Deletion of AnxA2 in dysferlin deficient mice reduces inflammation, adipogenic replacement, and loss in muscle function caused by dysferlin deficit. These results show that: a) AnxA2 facilitates myofiber repair, b) chronic inflammation and adipogenic replacement of dysferlinopathic muscle requires AnxA2, and c) inhibiting AnxA2-mediated inflammation is a novel therapeutic avenue for dysferlinopathy.

2016-10-04 | GSE87557 | GEO

Excess muscle plasma membrane leak disrupts extracellular matrix content and shifts macrophage-mediated muscle repair

Project description:Plasma membrane repair is critical for tissue integrity, especially for elongated contractile muscle cells. Genetically-mediated defects in plasma membrane resealing produce persistent leak, leading to a disordered extracellular matrix. Loss of the membrane repair protein dysferlin slows sarcolemmal resealing and promotes excess leak. Annexin A6 is also implicated in sarcolemmal repair, forming repair caps at the site of membrane disruption. On its own, deletion of the gene for annexin A6, Anxa6, had little effect on muscle health. In contrast, combined loss of dysferlin and annexin A6 (DysfA6) generated muscle fibers with profoundly defective membrane leak. Strikingly, Anxa6 deletion in the context of loss of dystrophin (mdxA6) did not exacerbate muscle defects. The persistent membrane leak in DysfA6 muscle resulted in marked macrophage infiltration with disordered macrophage polarization. Injured muscle fibers were targets of macrophage efferocytosis. Loss of Anxa6 was associated with increased expression of annexins A1 and A2, both of which were heavily deposited into the extracellular matrix. In vitro, macrophages exposed to annexins A1 and A2 expressed increased Csf1, consistent with a model where excess leak results in annexins A1 and A2 in the extracellular matrix, where this protein composition elicits macrophage proliferation and efferocytosis.

2026-06-15 | GSE328583 | GEO

Excess muscle plasma membrane leak disrupts extracellular matrix content and shifts macrophage-mediated muscle repair [scRNA-Seq]

2026-06-15 | GSE328601 | GEO

Excess muscle plasma membrane leak disrupts extracellular matrix content and shifts macrophage-mediated muscle repair

2026-06-15 | PXD077779 | Pride

Mus musculus

Project description:Role of annexin A2 in muscle repair

| PRJNA345192 | ENA

Human skeletal muscle fibroblasts and stem cells cultured with rat motor neuron cells

Project description:The study was designed to compare whether and how muscle fibroblasts (FIB) and muscle stem cells (MYO) interact with motor neurons. Moreover, we aimed to investigate whether muscle cells, isolated from lifelong exercisers, exerted a protective and supportive effect on motor neurons. These objectives were investigated in vitro using primary muscle cells from human donors and primary motor neurons from rat embryos and were analyzed by immunocytochemistry and species-specific RNA sequencing. A short period (24 hours) of co-culture was chosen for the RNA seq experiment, as differences on the gene expression level were expected to be greater initially. This accession contains the counts from the human RNA sequences.

2026-02-21 | E-MTAB-14395 | biostudies-arrayexpress

Human skeletal muscle fibroblasts and stem cells cultured with rat motor neuron cells

2026-02-21 | E-MTAB-14397 | biostudies-arrayexpress

Expression data of J3T-1, J3T-2, J3T-1shA, J3T-2A glioma

Project description:We have previously established two sibling glioma subclones, J3T-1 and J3T-2, showing distinct invasive and angiogenic phenotypes. J3T-1, expressing high annexin A2, demonstrates robust angiogenesis and tumor invasion around neovasculature. J3T-2, expressing low annexin A2, demonstrates diffuse invasion along white matter tracts. Knockdown of annexin A2 in J3T-1 (J3T-1shA) resulted in diffuse invasion pattern, and overexpression of annexin A2 in J3T-2 (J3T-2A) showed prominent angiogenesis. We used microarrays to identify genes which promote the phenotypic transition regulated by annexin A2.

2020-04-20 | GSE138374 | GEO

The Bap1-SMN axis in Dpp4+ skeletal muscle mesenchymal cells regulates survival of motor neurons

Project description:Spinal muscular atrophy (SMA) is a neuromuscular disease caused by mutations in the survival of motor neuron (SMN) gene. Although the primary manifestation of SMA is degeneration of motor neurons in a dying-back manner, deficient SMN intrinsic to motor neurons does not cause severe motor neuron loss, as is the case in SMA mouse models. Thus, the involvement of non-neuronal cells in the pathogenesis of SMA has been suggested. Here, we report that a novel subset of fibro-adipogenic progenitors expressing Dpp4 (Dpp4+ FAPs) is required for the survival of motor neurons, in which BRCA1-associating protein 1 (Bap1) is crucial for the stabilization of SMN by preventing its ubiquitination-dependent degradation. Inactivation of Bap1 in FAPs decreased SMN levels and accompanied degeneration of the neuromuscular junction, leading to dying-back loss of motor neurons and muscle atrophy, reminiscent of SMA pathogenesis. Overexpression of ubiquitination-resistant SMN variant, SMNK186R, in Bap1-null FAPs completely prevented neuromuscular degenerations. In addition, transplantation of Dpp4+ FAPs, but not Dpp4- FAPs, completely rescued neuromuscular defects in the mutant mice. Our data revealed that Bap1-mediated stabilization of SMN in Dpp4+ FAPs is crucial for the survival of motor neurons and provided a new therapeutic approach to treat SMA.

2022-06-30 | GSE190426 | GEO

Effects of human skeletal muscle fibroblast and stem cell media on cultured rat motor neuron cells

Project description:The study was designed to compare whether and how muscle fibroblasts (FIB) and muscle stem cells (MYO) interact with motor neurons. Moreover, we aimed to investigate whether muscle cells, isolated from lifelong exercisers, exerted a protective and supportive effect on motor neurons. These objectives were investigated in vitro using primary muscle cells from human donors and primary motor neurons from rat embryos and were analyzed by immunocytochemistry and species-specific RNA sequencing. Rat neuron cells were treated for 24 hours with conditioned media from human skeletal muscle fibroblasts and myoblasts.

2026-02-21 | E-MTAB-14399 | biostudies-arrayexpress

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

Tweets

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data