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Printable Handouts
Navigable Slide Index
- Introduction
- Scope
- Contents
- The chaperoning system, the chaperonopathies
- Molecular chaperones/Hsps: cell life and survival
- Disruption of Hsp function = Chaperonopathies
- The chaperonopathies
- Hsp60: structure, location, function
- Human Hsp60 amino acid sequence
- The chaperonin Hsp60
- Hsp60 assists protein folding in mitochondria
- Hsp60 resides and works inside mitochondria
- Hsp60 in cells: light microscopy and EM
- Hsp60: genetic chaperonopathies
- Hsp60 gene, protein and mutations
- Hsp60 and cancer
- Hsp60 in carcinogenesis of four tissues/organs
- Uterine exocervix
- Carcinogenic steps in uterine exocervix
- Hsp60 increases in exocervical carcinogenesis
- Large bowel
- Carcinogenic steps in large bowel
- Hsp60 increases in large bowel carcinogenesis
- Hsp60 immunopositivity detects dysplastic cells
- Hsp60 in neural and vasal infiltration in cancer
- Prostate
- Carcinogenic steps in prostate
- Hsp60 increases during prostate carcinogenesis
- Hsp60 in distant metastasis of prostate cancer
- Airways
- Carcinogenic steps of airways
- Hsp60 decrease during airways carcinogenesis
- Hsp60 can increase or decrease in carcinogenesis
- Studies showed increase, decrease or no change
- Examples of Hsp60 levels in tumors (1)
- Examples of Hsp60 levels in tumors (2)
- Hsp60 levels in tumors predicting prognosis
- Hsp60 secretion by cancer cells
- Hsp60 present in exosomes from cancer cells
- Inhibitors confirmed Hsp60 secretion
- Experiments with secretion inhibitors
- Conclusions and perspectives (1)
- Conclusions and perspectives (2)
- Conclusions and perspectives (3)
- Conclusions and perspectives (4)
- Conclusions and perspectives (5)
- Bibliography (1)
- Bibliography (2)
Topics Covered
- Chaperonology
- The chaperoning system
- Chaperonopathies
- Hsp60
- Genetic Hsp60 chaperonopathies
- Hsp60 in cancer
- Update talk: Chaperonin system
- Update talk: Maintenance of protein homeostasis
- Update talk: Interaction with immune system
- Update talk: Chaperone Hsp60
- Update talk: Chaperonopathies
- Update talk: Examples of Hsp60 aberrant PTM and their impact on function
- Update talk: Doxorubicin
- Update talk: Missense variants and pathogenicity
Links
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External Links
Talk Citation
Cappello, F. and Macario, A.J.L. (2021, July 29). Mitochondrial chaperonin Hsp60: locations, functions and pathology [Video file]. In The Biomedical & Life Sciences Collection, Henry Stewart Talks. Retrieved September 1, 2024, from https://doi.org/10.69645/PWRO3251.Export Citation (RIS)
Publication History
Financial Disclosures
- Prof. Francesco Cappello has not informed HSTalks of any commercial/financial relationship that it is appropriate to disclose.
- Prof. Alberto J. L. Macario has not informed HSTalks of any commercial/financial relationship that it is appropriate to disclose.
Update Available
The speaker addresses developments since the publication of the original talk. We recommend listening to the associated update as well as the lecture.
- Full lecture Duration: 25:38 min
- Update Duration: 4:23 min
Mitochondrial chaperonin Hsp60: locations, functions and pathology
A selection of talks on Oncology
Transcript
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0:00
The topic of this talk belongs to chaperonology,
the scientific discipline dealing with molecular chaperones,
normal and abnormal in physiology and pathology.
The subfield of chaperonology encompasses chaperonopathies,
the diseases in which chaperones play a role in pathogenesis and/or are
biomarkers useful for diagnosis and assessing prognosis and response to treatment.
This talk focuses on one among the many chaperones; HSP60,
traditionally known as in mitochondrial chaperonin, CPN 60,
that as the name suggests,
has a molecular weight of about 60 kiloDalton.
0:46
HSP60 plays a variety of roles inside and outside cells,
including not only improving quality control, folding,
refolding, translocation degradation, but also in other functions more or
less unrelated to its task of assisting polypeptide maturation.
Furthermore, HSP60 is associated with many pathological processes.
Because of this and because its
chaperonin can occur in any cellular or extracellular compartment,
its malfunction can be predicted to have wider spread and probably serious consequences.
It is impossible to cover all aspects of HSP60 physiology and pathology in one talk,
therefore, in this talk,
we have concentrated on some aspects of
genetic HSP60 chaperonopathies and on work pertaining to HSP60 and cancer.