Role of the Post-translational Modifications of HSP60 in Disease

Baron, Byron

doi:10.1007/978-3-030-23154-5_6

Cited by 3 publications

(2 citation statements)

References 188 publications

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“…Pathogenic chaperones with aberrant PTMs associated with NCPs, other than those described above, have not been reported. Most of the naturally occurring or induced PTMs in Hsp60 (HSPD1) with a pathogenic role have been implicated in carcinogenesis [154][155][156][157], apoptosis signaling regulation [158,159], and immune system regulation [160], but none has been associated with NCPs [25,161]. However, an involvement of Hsp60 (HSPD1) in AD and PD is under scrutiny.…”

Section: Discussionmentioning

confidence: 99%

The Neurochaperonopathies: Anomalies of the Chaperone System with Pathogenic Effects in Neurodegenerative and Neuromuscular Disorders

et al. 2021

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The chaperone (or chaperoning) system (CS) constitutes molecular chaperones, co-chaperones, and chaperone co-factors, interactors and receptors, and its canonical role is protein quality control. A malfunction of the CS may cause diseases, known as the chaperonopathies. These are caused by qualitatively and/or quantitatively abnormal molecular chaperones. Since the CS is ubiquitous, chaperonopathies are systemic, affecting various tissues and organs, playing an etiologic-pathogenic role in diverse conditions. In this review, we focus on chaperonopathies involved in the pathogenic mechanisms of diseases of the central and peripheral nervous systems: the neurochaperonopathies (NCPs). Genetic NCPs are linked to pathogenic variants of chaperone genes encoding, for example, the small Hsp, Hsp10, Hsp40, Hsp60, and CCT-BBS (chaperonin-containing TCP-1- Bardet–Biedl syndrome) chaperones. Instead, the acquired NCPs are associated with malfunctional chaperones, such as Hsp70, Hsp90, and VCP/p97 with aberrant post-translational modifications. Awareness of the chaperonopathies as the underlying primary or secondary causes of disease will improve diagnosis and patient management and open the possibility of investigating and developing chaperonotherapy, namely treatment with the abnormal chaperone as the main target. Positive chaperonotherapy would apply in chaperonopathies by defect, i.e., chaperone insufficiency, and consist of chaperone replacement or boosting, whereas negative chaperonotherapy would be pertinent when a chaperone actively participates in the initiation and progression of the disease and must be blocked and eliminated.

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Section: Discussionmentioning

confidence: 99%

The Neurochaperonopathies: Anomalies of the Chaperone System with Pathogenic Effects in Neurodegenerative and Neuromuscular Disorders

et al. 2021

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“…e.g., certain tumor types, autoimmune conditions, prion disease [65] Acquired chaperonopathies can be caused by aberrant post-translational modifications (PTMs) that have an impact on the structure/function of the chaperone molecule. The Hsp60 amino acid sequence contains various critical sites that can be affected by PTMs [67]. Possible PTMs are phosphorylation, O-GlcNAcylation, nitration, acetylation, S-nitrosylation, citrullination, methylation, oxidation, biotinylation, and ubiquitination [51].…”

Section: Mistake or Collaborationismmentioning

confidence: 99%

The Challenging Riddle about the Janus-Type Role of Hsp60 and Related Extracellular Vesicles and miRNAs in Carcinogenesis and the Promises of Its Solution

et al. 2021

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Hsp60 is one of the most ancient and evolutionarily conserved members of the chaperoning system. It typically resides within mitochondria, in which it contributes to maintaining the organelle’s proteome integrity and homeostasis. In the last few years, it has been shown that Hsp60 also occurs in other locations, intracellularly and extracellularly, including cytosol, plasma-cell membrane, and extracellular vesicles (EVs). Consequently, non-canonical functions and interacting partners of Hsp60 have been identified and it has been realized that it is a hub molecule in diverse networks and pathways and that it is implicated, directly or indirectly, in the development of various pathological conditions, the Hsp60 chaperonopathies. In this review, we will focus on the multi-faceted role of this chaperonin in human cancers, showing the contribution of intra- and extracellular Hsp60 in cancer development and progression, as well as the impact of miRNA-mediated regulation of Hsp60 in carcinogenesis. There are still various aspects of this intricate biological scenario that are poorly understood but ongoing research is steadily providing new insights and we will direct attention to them. For instance, we will highlight the possible applications of the Hsp60 involvement in carcinogenesis not only in diagnosis, but also in the development of specific anti-cancer therapies centered on the use of the chaperonin as therapeutic target or agent and depending on its role, pro- or anti-tumor.

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Lysine acetylation plays a role in the allograft-induced stress response of the pearl oyster (Pinctada fucata martensii)

Fang²,

Liang³

et al. 2022

Fish & Shellfish Immunology

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Role of the Post-translational Modifications of HSP60 in Disease

Cited by 3 publications

References 188 publications

The Neurochaperonopathies: Anomalies of the Chaperone System with Pathogenic Effects in Neurodegenerative and Neuromuscular Disorders

The Neurochaperonopathies: Anomalies of the Chaperone System with Pathogenic Effects in Neurodegenerative and Neuromuscular Disorders

The Challenging Riddle about the Janus-Type Role of Hsp60 and Related Extracellular Vesicles and miRNAs in Carcinogenesis and the Promises of Its Solution

Lysine acetylation plays a role in the allograft-induced stress response of the pearl oyster (Pinctada fucata martensii)

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