Talk:Heat shock protein

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Article issues

BROKEN LINK: the link to the faculty member's website is broken...

This page is merged-from Heat-shock protein. See its history in the redirect, if you wish.

The two pages had different POV's. Both assume the cells survive the heat shock.

The current lead page paragraph has the idea that genetic factors influence the expression of the HSPs. Thus there is a molecular slant to the POV. The transcriptional genetics POV needs some references to disentangle whether there is an actual molecular process which creates the HSPs. If that is so, then HSP production could be performed via the recombinant DNA technology. Need references.

The H-SP page had the idea that structural factors (or regulatory factors) influence cellular and organ development. Thus there is the concept that heat stress somehow banks the H-SPs, in larger and larger amounts, without destroying the cell itself, which is a factor in the cellular or organ survival. If an HSP is like a hormone, then we need references to show the influence/quantity needed for development of some cellular or organ structure. If the growth in amount of H-SP shows grains or chains of H-SP in the cell itself, then that would be an argument for a simple manufacturing process (due to the stress) within the cell, without recourse to RNA or DNA mechanisms. Again, we need references. -Problems and criticism- I need to return to this page to somehow integrate the two separate streams of thought. It helps to have them on the same page. Ancheta Wis 08:49, 13 Jan 2005 (UTC)

Original contributors: please respond.

Response

Hi,

The heat shock proteins are indeed regulated at the transcriptional level. The specific transcription factor has been identified; in humans the key one is HSF1. A specific heat shock promoter region has also been identified, to which HSF1 binds. The heat shock promoter is located just upstream of all the heat shock protein genes. In response to stress, HSF1 is phosphorylated and trimerizes; the kinase that phosphorylates it is unknown, as is the particular signal that starts the process. That the heat shock response is transcriptionally regulated is also supported by the time it takes to see an increase in heat shock protein levels following cellular stress--more than half an hour, and increasing over the course of several hours.

Heat shock proteins don't seem to be toxic in most cells, even at relatively high levels. They actually tend to have antiapoptotic effects, both by acting as chaperones for the protein folding process, and by sequestering pro-apoptotic factors. Malignant cells often constitutively express high levels of some heat shock proteins (including at least Hsp70 and Hsp27; possibly others), possibly because a) it helps them to survive in the unpleasant tumour microenvironment, and b) it staves off any residual apoptotic machinery that they have remaining.

Note that heat shock proteins outside of cells can act as inflammatory signals. (The mechanism by which the inflammatory response is activated here is not well understood.) In general, HSPs are intracellular proteins only; their presence in the extracellular space is the likely result of necrosis or cell lysis and acts as a signal for that reason.

Actually, some function extracellulary related to platelet aggregation, cellular wound healing, and modulating immune responses GetAgrippa 04:59, 2 September 2006 (UTC)[reply]

Several members of the HSP family are regularly produced in the lab using conventional recombinant techniques. Stressgen Bioreagents sells them commercially for research purposes. [[1]]

There's a bit of a start, anyway. I must be off to work.... --TenOfAllTrades 13:50, 13 Jan 2005 (UTC)

Criticisms

I think the Researcher section is anectdotal and borders on advertisment. There are numerous researchers pursuing this subject. I find it offensive to the vast majority who are not mentioned.GetAgrippa 12:44, 31 August 2006 (UTC)[reply]

I agree that they should be removed unless there is solid proof that these are the world's biggest experts on HSPs. JFW | T@lk 21:36, 31 August 2006 (UTC)[reply]

Jfdwolff, Does this sort of thing fall into vanity guidelines clause??GetAgrippa 04:44, 2 September 2006 (UTC)[reply]

Perhaps a history secton and mention notable names in various fields. Dr. Lundquist is a recognizable name, but others come immediately to my mind (that is subjective admittedly).GetAgrippa 11:47, 1 September 2006 (UTC)[reply]

The heat shock proteins have been linked to development, immunology, cancer, cardiovascular, and numerous other fields. This topic needs major expansion.GetAgrippa 12:44, 31 August 2006 (UTC)[reply]

Since the heat shocks are ancient molecules that are highly convserved ,perhaps it should be introduced with Groel and its chaperonin function. Then build on the theme with mammalian heat shock proteins and their role in numerous areas. The heat shock induction is of interest, but the endogeneous pool that serves in homeostasis perhaps is more significant.GetAgrippa 13:41, 31 August 2006 (UTC)[reply]

I just noticed the chaperonin link. Maybe start with brief histoy in bacteria and link to chaperonin, and then develop from there?GetAgrippa 11:49, 1 September 2006 (UTC)[reply]

I suppose the chaperone table to be re-structured. It is somehow not clearly laid out. A list of all chaperones with links to the appropriate protein pages would also add more clarity. Tirkfl 08:22, 13 April 2007 (UTC)[reply]

Heat shock proteins encompass several structurally and evolutionarily distinct classes of proteins. This article needs to be amended (or split) to reflect that fact.

Cardiovasculature Roles

I will organize and reference this section. Perhaps we should have sections for Cardiovascular, Immunology, Development, Cancer, etc. and link them to other articles?GetAgrippa 11:47, 1 September 2006 (UTC)[reply]

Silkworm

The section on heat shock protein in silkworm (wandering into other topics) deals with an interesting specialised topic but is a very long way from the right style and format for an encyclopedia article. The section is still in need of major editing by someone who has knowledge of the article as a whole and correct Wikipedia style. Specific problems include the very long title (which still fails to cover the scope of the section), and the numbered list of things that need to be done at the end. Also, references are needed, as always.82.1.151.34 (talk) 17:50, 20 September 2008 (UTC)[reply]

I suspect that this section (specifically this version) is a copyright violation, but without a source this can not be definitively determined. If this article can be shown to be a copyright infringement, please list the article on Wikipedia:Copyright problems. If you are certain that the article is not a copyright violation, you should give evidence below. Please do not remove this tag without discussion.

69.140.152.55 (talk) 02:34, 15 November 2008 (UTC)[reply]

Using Google, the material in the silk worm section does not appear to be plagiarized. However I do agree that this section has multiple issues and it doesn't really fit in with the rest of the article. Therefore I have deleted the section. If someone would like to rescue the section (and if so, I strongly suggest that this topic be split out into a new article), the original version of this section may be found in the edit history. Boghog2 (talk) 08:34, 15 November 2008 (UTC)[reply]

Kidney failure

I remember a case when it was said that a person had so much stress proteins that it resulted in kidney failure, as the stress proteins in the plama clogged up the nephrons of the kidneys. Was this possible? 86.147.244.1 (talk) 21:24, 29 December 2008 (UTC)[reply]

Outdated Clinical Trials

I noticed that the citations for the current clinical trials are outdated. For example, the HSPgp96 citation links to a clinical trial that was withdrawn before it began, due to lack of participants^[1]. Also, the HSP90 inhibitor, 17-AAG, is mentioned as a current trial, but the citation is for a paper from 2006, which is more than 10 years old now. If there are more current trials in session, I think it would be worth updating this information. BioKnitter (talk) 20:26, 26 January 2017 (UTC)[reply]

References

^ "Immune Response and Safety of HS110 Vaccine in Combination With Erlotinib in Patients With Non-Small Cell Lung Cancer". Retrieved 26 January 2017.

Covid-19

Heat shock protein 70 has been implicated in Covid-19 as being one of several molecules whose levels are particularly raised in sufferers of the disease. Inflammation Profiling of Critically Ill Coronavirus Disease 2019 Patients 92.25.47.124 (talk) 00:01, 26 June 2020 (UTC)[reply]

Wiki Education assignment: Molecular Genetics

This article was the subject of a Wiki Education Foundation-supported course assignment, between 22 August 2022 and 9 December 2022. Further details are available on the course page. Student editor(s): ConnerButcher16 (article contribs).

— Assignment last updated by ConnerButcher16 (talk) 19:16, 29 August 2022 (UTC)[reply]

Eye lens crystallin proteins

The eye lens crystallins found in mammallian eye lenses are closely related to the heat shock proteins. I do not have sufficient time at the moment to improve upon the lens section, but far more animals have been studied than Zebrafish. Additionally, while alpha crystallin is the most closely related to the HSP's, there are other similarly related crystallins. Specifically, there should be more mention of other lens proteins. Maybe a geneticist should write something here, I'm a physicist and the genetics aspects are out of my wheelhouse. Malnu (talk) 19:34, 11 January 2024 (UTC)[reply]

[1] "Immune Response and Safety of HS110 Vaccine in Combination With Erlotinib in Patients With Non-Small Cell Lung Cancer". Retrieved 26 January 2017.

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