Complement C1q Binding Protein (C1QBP): Physiological Functions, Mutation-Associated Mitochondrial Cardiomyopathy and Current Disease Models

Wang, Jie; Huang, Christopher L.‐H.; Zhang, Yanmin

doi:10.3389/fcvm.2022.843853

Cited by 12 publications

(9 citation statements)

References 54 publications

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“…In mice, C3 signaling initiates the recruitment of monocytes or macrophages to the site of injury and is critical to stimulating muscle regeneration 61 . Lastly, CFH prevents complement activation against resident host cells by blocking the alternative pathway and assembly of the membrane attack complex, which includes C9, and C1QBP inhibits C1 activation 62,63 . These findings, coupled with previous research, suggest that a persistent and likely polarized immune response toward M2 healing inflammation promotes regrowth and may protect new tissues by maintaining self‐recognition or survival 64,65 (He et al.…”

Section: Resultsmentioning

confidence: 76%

“…61 Lastly, CFH prevents complement activation against resident host cells by blocking the alternative pathway and assembly of the membrane attack complex, which includes C9, and C1QBP inhibits C1 activation. 62,63 These findings, coupled F I G U R E 5 Biological processes enriched to the regenerating tail tip are summarized into major functional categories as a treemap. Each rectangle shows a single, representative GO term where size is determined by the absolute log10 p-values of related, enriched biological processes within each group.…”

Section: Enrichment and Pathway Analysis Of Proteins Expressed Throug...mentioning

confidence: 99%

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Comparative proteomic analysis of tail regeneration in the green anole lizard, Anolis carolinensis

Xu,

Hutchins,

Eckalbar

et al. 2023

Natural Sciences

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As amniote vertebrates, lizards are the most closely related organisms to humans capable of appendage regeneration. Lizards can autotomize, or release their tails as a means of predator evasion, and subsequently regenerate a functional replacement. Green anoles (Anolis carolinensis) can regenerate their tails through a process that involves differential expression of hundreds of genes, which has previously been analyzed by transcriptomic and microRNA analysis. To investigate protein expression in regenerating tissue, we performed a whole proteomic analysis of regenerating tail tip and base. This is the first proteomic data set available for any anole lizard. We identified a total of 2646 proteins—976 proteins only in the regenerating tail base, 796 only in the tail tip, and 874 in both tip and base. For over 90% of these proteins in these tissues, we were able to assign a clear orthology to gene models in either the Ensembl or NCBI databases. For 13 proteins in the tail base, 9 proteins in the tail tip, and 10 proteins in both regions, the gene model in Ensembl and NCBI matched an uncharacterized protein, confirming that these predictions are present in the proteome. Ontology and pathways analysis of proteins expressed in the regenerating tail base identified categories, including actin filament‐based process, ncRNA metabolism, regulation of phosphatase activity, small GTPase‐mediated signal transduction, and cellular component organization or biogenesis. Analysis of proteins expressed in the tail tip identified categories, including regulation of organelle organization, regulation of protein localization, ubiquitin‐dependent protein catabolism, small GTPase‐mediated signal transduction, morphogenesis of epithelium, and regulation of biological quality. These proteomic findings confirm pathways and gene families activated in tail regeneration in the green anole as well as identify uncharacterized proteins whose role in regrowth remains to be revealed. This study demonstrates the insights that are possible from the integration of proteomic and transcriptomic data in tail regrowth in the green anole, with potentially broader application to studies in other regenerative models.KEY POINTSThis research is highly interdisciplinary, combining our previous analyses with these most recent findings: Appendage regeneration is a conserved trait among vertebrates and has been characterized in animals ranging from teleost fish (zebrafish), urodele amphibians (axolotl), anuran amphibians (Xenopus frog), squamate reptiles (various species of lizards), and even crocodilians (American alligator). Comparative genomic and proteomic analysis of this process allows us to identify the genetic pathways and cellular processes under evolutionary selection for this regrowth capacity. Activating these conserved genetic pathways and cellular processes will be critical to developing regenerative medical therapies in humans. The identification of proteins expressed in regeneration extends analyses based only on predicted proteins from transcriptomic analysis, and permits integration with protein‐expression studies of regrowing nervous and musculoskeletal structures.

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Section: Resultsmentioning

confidence: 76%

Section: Enrichment and Pathway Analysis Of Proteins Expressed Throug...mentioning

confidence: 99%

Comparative proteomic analysis of tail regeneration in the green anole lizard, Anolis carolinensis

Xu,

Hutchins,

Eckalbar

et al. 2023

Natural Sciences

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“…Complement C1q binding protein (C1QBP) was upregulated in the ECM-enriched ovary with age. C1QBP is a mitochondrial protein that regulates mitochondrial oxidative phosphorylation [ 68 ]. Given that mitochondrial function is compromised in the aging ovary, increased C1QBP protein expression may be a compensatory mechanism.…”

Section: Discussionmentioning

confidence: 99%

Proteomic quantification of native and ECM-enriched mouse ovaries reveals an age-dependent fibro-inflammatory signature

Dipali,

King,

Rose

et al. 2023

Aging

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The ovarian microenvironment becomes fibrotic and stiff with age, in part due to increased collagen and decreased hyaluronan. However, the extracellular matrix (ECM) is a complex network of hundreds of proteins, glycoproteins, and glycans which are highly tissue specific and undergo pronounced changes with age. To obtain an unbiased and comprehensive profile of age-associated alterations to the murine ovarian proteome and ECM, we used a label-free quantitative proteomic methodology. We validated conditions to enrich for the ECM prior to proteomic analysis. Following analysis by data-independent acquisition (DIA) and quantitative data processing, we observed that both native and ECM-enriched ovaries clustered separately based on age, indicating distinct age-dependent proteomic signatures. We identified a total of 4,721 proteins from both native and ECM-enriched ovaries, of which 383 proteins were significantly altered with advanced age, including 58 ECM proteins. Several ECM proteins upregulated with age have been associated with fibrosis in other organs, but to date their roles in ovarian fibrosis are unknown. Pathways regulating DNA metabolism and translation were downregulated with age, whereas pathways involved in ECM remodeling and immune response were upregulated. Interestingly, immune-related pathways were upregulated with age even in ECM-enriched ovaries, suggesting a novel interplay between the ECM and the immune system. Moreover, we identified putative markers of unique immune cell populations present in the ovary with age. These findings provide evidence from a proteomic perspective that the aging ovary provides a fibroinflammatory milieu, and our study suggests target proteins which may drive these age-associated phenotypes for future investigation.

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“…??? [145][146][147][148][149] Abbreviations: FACT Complex, facilitates chromatin transcription complex; ASF1, anti-silencing function 1; APLF, aprataxin and polynucleotide kinase-like factor; NPM1, nucleophosmin; CHAF1A, chromatin assembly factor 1 subunit A; CHAF1B, chromatin assembly factor 1 subunit B; HIRA, histone cell cycle regulator; NAP1, nucleosome assembly protein 1; SPT6, transcription elongation factor; DAXX, death domain-associated protein; C1QBP, complement 1 Q subcomponent-binding protein; ?? ?, unknown.…”

Section: Introductionmentioning

confidence: 99%

Comparative Review on Cancer Pathology from Aberrant Histone Chaperone Activity

Lee,

Bao

2024

IJMS

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Histone chaperones are integral to chromatin dynamics, facilitating the assembly and disassembly of nucleosomes, thereby playing a crucial role in regulating gene expression and maintaining genomic stability. Moreover, they prevent aberrant histone interactions prior to chromatin assembly. Disruption in histone chaperone function may result in genomic instability, which is implicated in pathogenesis. This review aims to elucidate the role of histone chaperones in cancer pathologies and explore their potential as therapeutic targets. Histone chaperones have been found to be dysregulated in various cancers, with alterations in expression levels, mutations, or aberrant interactions leading to tumorigenesis and cancer progression. In addition, this review intends to highlight the molecular mechanisms of interactions between histone chaperones and oncogenic factors, underscoring their roles in cancer cell survival and proliferation. The dysregulation of histone chaperones is significantly correlated with cancer development, establishing them as active contributors to cancer pathology and viable targets for therapeutic intervention. This review advocates for continued research into histone chaperone-targeted therapies, which hold potential for precision medicine in oncology. Future advancements in understanding chaperone functions and interactions are anticipated to lead to novel cancer treatments, enhancing patient care and outcomes.

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Complement C1q Binding Protein (C1QBP): Physiological Functions, Mutation-Associated Mitochondrial Cardiomyopathy and Current Disease Models

Cited by 12 publications

References 54 publications

Comparative proteomic analysis of tail regeneration in the green anole lizard, Anolis carolinensis

Comparative proteomic analysis of tail regeneration in the green anole lizard, Anolis carolinensis

Proteomic quantification of native and ECM-enriched mouse ovaries reveals an age-dependent fibro-inflammatory signature

Comparative Review on Cancer Pathology from Aberrant Histone Chaperone Activity

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