Induction of mammalian stress proteins by a triethylphosphine gold compound used in the therapy of rheumatoid arthritis

Caltabiano, Madelyn M.; Koestler, Thomas P.; Poste, George; Greig, Russell

doi:10.1016/s0006-291x(86)80391-6

Cited by 18 publications

(2 citation statements)

References 10 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In parallel, different groups identified a 32 kDa stress-responsive protein, whose expression was highly upregulated in different cell lines in response to challenges such as hyperthermia, heavy metals and oxidative stress. This protein, referred to as Heat-Shock Protein 32 (HSP-32) at that time [5][6][7][8][9][10], was later shown to be identical to HO-1 [11,12]. A third isoform, heme oxygenase-3 (HO-3), was characterized in 1997 in a number of different rat tissues, but displayed poor enzymatic activity [13] and its physiological role remains largely uncharacterized to this day.…”

Section: Introductionmentioning

confidence: 99%

Modulation of Inflammation and Immune Responses by Heme Oxygenase-1: Implications for Infection with Intracellular Pathogens

et al. 2020

View full text Add to dashboard Cite

Heme oxygenase-1 (HO-1) catalyzes the degradation of heme molecules releasing equimolar amounts of biliverdin, iron and carbon monoxide. Its expression is induced in response to stress signals such as reactive oxygen species and inflammatory mediators with antioxidant, anti-inflammatory and immunosuppressive consequences for the host. Interestingly, several intracellular pathogens responsible for major human diseases have been shown to be powerful inducers of HO-1 expression in both host cells and in vivo. Studies have shown that this HO-1 response can be either host detrimental by impairing pathogen control or host beneficial by limiting infection induced inflammation and tissue pathology. These properties make HO-1 an attractive target for host-directed therapy (HDT) of the diseases in question, many of which have been difficult to control using conventional antibiotic approaches. Here we review the mechanisms by which HO-1 expression is induced and how the enzyme regulates inflammatory and immune responses during infection with a number of different intracellular bacterial and protozoan pathogens highlighting mechanistic commonalities and differences with the goal of identifying targets for disease intervention.

show abstract

Section: Introductionmentioning

confidence: 99%

Modulation of Inflammation and Immune Responses by Heme Oxygenase-1: Implications for Infection with Intracellular Pathogens

et al. 2020

View full text Add to dashboard Cite

show abstract

“…The biochemical mechanism(s) responsible for this COmediated protection is not clearly understood, but it is thought to be associated with the ability of endogenous CO to suppress the production of proinflammatory cytokines, such as platelet-derived growth factor, endothelin and/or interleukin-1, and TNF-␣ (Platt and Nath 1998;Otterbein et al 2000), and to activate the Na ϩ ,K ϩ -ATPase for the maintenance of membrane potential (Nathanson et al 1995). Because of this, the anti-inflammatory potential of HO-1 expression is attractive for practical use, for example, in therapy for rheumatoid arthritis (Caltabiano et al 1986) and transplantation where rapid expression of HO-1 in cardiac xenografts can be essential to ensure long-term xenograft survival (Soares et al 1998). Although the end products of HO-1 may act as antistress agents, it may also be toxic to the lungs and other oxygen-sensitive tissues at elevated concentration (Forbes 1970).…”

Section: The Anti-inflammatory Properties Of Ho-1 and Its End Productsmentioning

confidence: 99%

Self-cytoprotection against stress: feedback regulation of heme-dependent metabolism

Schwartsburd

2001

Cell Stress Chaper

View full text Add to dashboard Cite

This minireview provides insight into feedback regulation of heme-dependent metabolism as a defensive cellular response against stress. Interactions among heme-, iron-, porphyrin-, and CO/NO-dependent metabolic pathways during the stress-induced response are emphasized in the context of feedback regulation. The hypothetical model of the latter interactions is presented as tightly controlled feedback cycles.

show abstract

The homology of a novel polypeptide with stress protein characteristics in embryonic mice brain and in the hypothalamus of caloric restricted rats as determined by ultramicro western blotting

et al. 1994

View full text Add to dashboard Cite

A novel protein (p34) was observed in polyacrylamide gel fluorographs of gestation day 13 embryonic mouse brain following retinoic acid dosing of dams. Another p34 polypeptide with identical gel migratory characteristics was seen in the hypothalamus of old caloric restricted rats after "food deprivation stress". Western blotting, employing an ultramicro trans-blot cell developed in our laboratory, detected identical immunochemical determinants between these proteins, verifying their homology. Peptide mapping and Western blotting further validated the uniqueness of p34 compared with other stress proteins including heme oxygenase.

show abstract

Induction of mammalian stress proteins by a triethylphosphine gold compound used in the therapy of rheumatoid arthritis

Cited by 18 publications

References 10 publications

Modulation of Inflammation and Immune Responses by Heme Oxygenase-1: Implications for Infection with Intracellular Pathogens

Modulation of Inflammation and Immune Responses by Heme Oxygenase-1: Implications for Infection with Intracellular Pathogens

Self-cytoprotection against stress: feedback regulation of heme-dependent metabolism

The homology of a novel polypeptide with stress protein characteristics in embryonic mice brain and in the hypothalamus of caloric restricted rats as determined by ultramicro western blotting

Contact Info

Product

Resources

About