Immunohistochemistry of Human Hsp60 in Health and Disease: Recent Advances in Immunomorphology and Methods for Assessing the Chaperonin in Extracellular Vesicles.
Cancer
Chaperone system
Confocal microscopy
Double immunofluorescence
Extracellular vesicles
Hsp60
Immunofluorescence
Immunohistochemistry
Immunomorphology
Transmission electron microscopy
microRNA
Journal
Methods in molecular biology (Clifton, N.J.)
ISSN: 1940-6029
Titre abrégé: Methods Mol Biol
Pays: United States
ID NLM: 9214969
Informations de publication
Date de publication:
2023
2023
Historique:
medline:
7
8
2023
pubmed:
4
8
2023
entrez:
4
8
2023
Statut:
ppublish
Résumé
The subject matter of this chapter is defined by the title of its two previous editions, "Immunohistochemistry of human Hsp60 in health and disease: From autoimmunity to cancer," the latest of which appeared in 2018. Since then, considerable advances have been made in the fields of autoimmunity and cancer and some of them are closely linked to progress in the understanding of the chaperone system (CS). This is a physiological system composed of molecular chaperones, co-chaperones, chaperone cofactors, and chaperone interactors and receptors. The molecular chaperones are the chief members of the CS, and here we focus on one of them, Hsp60. Since extracellular vesicles (EVs) have also emerged as key factors in the functioning of the CS and in carcinogenesis, we have incorporated a detailed section about them. This chapter explains how to assess Hsp60 in tissues and in EVs for application in diagnosis, prognostication, and patient monitoring and, eventually, for developing methods using them as therapeutic targets and tools. We describe immunohistochemical techniques, immunofluorescence and double immunofluorescence-confocal microscopy, and methods for collecting and isolating EVs from blood plasma and for assessing their contents in Hsp60 and related microRNAs (miRNAs). All these procedures have proven to be reliable and useful in the study and management of various types of cancer and inflammatory and autoimmune conditions.
Identifiants
pubmed: 37540441
doi: 10.1007/978-1-0716-3342-7_20
doi:
Substances chimiques
Molecular Chaperones
0
Chaperonins
EC 3.6.1.-
Chaperonin 60
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
263-279Informations de copyright
© 2023. The Author(s), under exclusive license to Springer Science+Business Media, LLC, part of Springer Nature.
Références
Macario AJL, Conway de Macario E, Cappello F (2013) The Chaperonopathies. Diseases with defective molecular chaperones. Springer, Dordrecht/Heidelberg/New York/London
doi: 10.1007/978-94-007-4667-1
Bross P, Fernandez-Guerra P (2016) Front Mol Biosci 3:49. https://doi.org/10.3389/fmolb.2016.00049
doi: 10.3389/fmolb.2016.00049
pubmed: 27630992
pmcid: 5006179
Gomez-Llorente Y, Jebara F, Patra M et al (2020) Structural basis for active single and double ring complexes in human mitochondrial Hsp60-Hsp10 chaperonin. Nat Commun 11:1916. https://doi.org/10.1038/s41467-020-15698-8
doi: 10.1038/s41467-020-15698-8
pubmed: 32317635
pmcid: 7174398
Macario AJL, Conway de Macario E (2023) The chaperone system in autoimmunity, inflammation, and virus-induced diseases: role of chaperonins. In: Fink G (ed) Stress: immunology and inflammation. Handbook of stress series, vol 5. Chapter 13. Elsevier/Academic, San Diego, USA
Cappello F, Conway de Macario E, Zummo G, Macario AJL (2011) Immunohistochemistry of human Hsp60 in health and disease: from autoimmunity to cancer. Methods Mol Biol 787:245–254. https://doi.org/10.1007/978-1-61779-295-3_18
doi: 10.1007/978-1-61779-295-3_18
pubmed: 21898240
Cappello F, Conway de Macario E, Rappa F et al (2018) Immunohistochemistry of human Hsp60 in health and disease: from autoimmunity to cancer. Methods Mol Biol 1709:293–305. https://doi.org/10.1007/978-1-4939-7477-1_21
doi: 10.1007/978-1-4939-7477-1_21
pubmed: 29177667
Caruso Bavisotto C, Alberti G, Vitale AM et al (2020) Hsp60 post-translational modifications: functional and pathological consequences. Front Mol Biosci 7:95. https://doi.org/10.3389/fmolb.2020.00095
doi: 10.3389/fmolb.2020.00095
pubmed: 32582761
pmcid: 7289027
Vitale AM, Conway de Macario E, Alessandro R et al (2020) Missense mutations of human Hsp60: a computational analysis to unveil their pathological significance. Front Genet 11:969. https://doi.org/10.3389/fgene.2020.00969 . Section Genetics of Common and Rare Diseases
doi: 10.3389/fgene.2020.00969
pubmed: 33014020
pmcid: 7461820
Basset CA, Rappa F, Lentini VL et al (2021) Hsp27 and Hsp60 in human submandibular salivary gland: quantitative patterns in healthy and cancerous tissues with potential implications for differential diagnosis and carcinogenesis. Acta Histochem 123:151771. https://doi.org/10.1016/j.acthis.2021.151771
doi: 10.1016/j.acthis.2021.151771
pubmed: 34419757
Alberti G, Vergilio G, Paladino L et al (2022) The chaperone system in breast cancer: roles and therapeutic prospects of the molecular chaperones Hsp27, Hsp60, Hsp70, and Hsp90. Int J Mol Sci 23:7792
doi: 10.3390/ijms23147792
pubmed: 35887137
pmcid: 9324353
Sun B, Li G, Yu Q et al (2021) HSP60 in cancer: a promising biomarker for diagnosis and a potentially useful target for treatment. J Drug Target 30:31–45. https://doi.org/10.1080/1061186X.2021.1920025
doi: 10.1080/1061186X.2021.1920025
pubmed: 33939586
Tang Y, Zhou Y, Fan S et al (2022) The multiple roles and therapeutic potential of HSP60 in cancer. Biochem Pharmacol 201:115096. https://doi.org/10.1016/j.bcp.2022.115096
doi: 10.1016/j.bcp.2022.115096
pubmed: 35609646
Tikhomirova TS, Matyunin MA, Lobanov MY et al (2022) In-depth analysis of amino acid and nucleotide sequences of Hsp60: how conserved is this protein? Proteins 90:1119–1141. https://doi.org/10.1002/prot.26294
doi: 10.1002/prot.26294
pubmed: 34964171
Caruso Bavisotto C, Scalia F, Marino Gammazza A et al (2020) Extracellular vesicle-mediated cell-cell communication in the nervous system: focus on neurological diseases. Int J Mol Sci 20:pii: E434. https://doi.org/10.3390/ijms20020434
doi: 10.3390/ijms20020434
David S, Vitale AM, Fucarino F et al (2021) The challenging riddle about the Janus-type role of Hsp60 and related extracellular vesicles and miRNAs in carcinogenesis and the promises of its solution. Appl Sci 11:1175. https://doi.org/10.3390/app11031175
doi: 10.3390/app11031175
Graziano F, Iacopino DG, Cammarata G, Scalia G, Campanella C, Giannone AG et al (2021) The triad Hsp60-miRNAs-extracellular vesicles in brain tumors: assessing its components for understanding tumorigenesis and monitoring patients. Appl Sci 11:2867. https://doi.org/10.3390/app11062867
doi: 10.3390/app11062867
Rappa F, Pitruzzella A, Marino Gammazza A et al (2016) Quantitative patterns of Hsps in tubular adenoma compared with normal and tumor tissues reveal the value of Hsp10 and Hsp60 in early diagnosis of large bowel cancer. Cell Stress Chaperones 21:927–933. https://doi.org/10.1007/s12192-016-0721-5
doi: 10.1007/s12192-016-0721-5
pubmed: 27491302
pmcid: 5003810
McKee C, Sigala B, Soeda J et al (2015) Amphiregulin activates human hepatic stellate cells and is upregulated in non-alcoholic steatohepatitis. Sci Rep 5:8812. https://doi.org/10.1038/srep08812
doi: 10.1038/srep08812
pubmed: 25744849
pmcid: 4351520
Rappa F, Sciume C, Bello M et al (2014) Comparative analysis of hsp10 and hsp90 expression in healthy mucosa and adenocarcinoma of the large bowel. Anticancer Res 34:4153–4159
pubmed: 25075042
Alberti G, Campanella C, Paladino L et al (2022) The chaperone system in glioblastoma multiforme and derived cell lines: diagnostic and mechanistic implications. Front Biosci (Landmark Ed) 27. https://doi.org/10.31083/j.fbl2703097
Mishra A, Mirzaei H, Guidi N et al (2021) Fasting-mimicking diet prevents high-fat diet effect on cardiometabolic risk and lifespan. Nat Metab 3:1342–1356. https://doi.org/10.1038/s42255-021-00469-6
doi: 10.1038/s42255-021-00469-6
pubmed: 34650272
Barone R, Marino Gammazza A, Paladino L et al (2021) Morphological alterations and stress protein variations in lung biopsies obtained from autopsies of COVID-19 subjects. Cell 10:3136. https://doi.org/10.3390/cells10113136
doi: 10.3390/cells10113136
Théry C, Witwer KW, Aikawa E et al (2018) Minimal information for studies of extracellular vesicles 2018 (MISEV2018): a position statement of the International Society for Extracellular Vesicles and update of the MISEV2014 guidelines. J Extracell Vesicles 7:1535750. https://doi.org/10.1080/20013078.2018.1535750
doi: 10.1080/20013078.2018.1535750
pubmed: 30637094
pmcid: 6322352
Théry C, Clayton A, Amigorena S et al (2006) Isolation and characterization of exosomes from cell culture supernatants. Chapter 3. Unit 3.22. https://doi.org/10.1002/0471143030.cb0322s30
Campanella C, Rappa F, Sciumè C et al (2015) Heat shock protein 60 levels in tissue and circulating exosomes in human large bowel cancer before and after ablative surgery. Cancer 121:3230–3239. https://doi.org/10.1002/cncr.29499
doi: 10.1002/cncr.29499
pubmed: 26060090
Caruso Bavisotto C, Cipolla C, Graceffa G et al (2019) Immunomorphological pattern of molecular chaperones in normal and pathological thyroid tissues and circulating exosomes: potential use in clinics. Int J Mol Sci 20:4496. https://doi.org/10.3390/ijms20184496
doi: 10.3390/ijms20184496
pubmed: 31514388
pmcid: 6770414