Abstract
Introduction HSP90 is known as a stabilizer of the proteome and is required for many newly synthesized proteins and introducing damaged proteins back into the refolding chaperone cycle. Due to its key position and interaction with several hundreds of proteins in a cell, it is a target for noxious cells and a responsive sensitive biomarker for cellular stress. Cellular stress is when unfolded proteins are formed by, e.g. mutational events, changes in the osmolality, or redox status. One challenge is to monitor and discriminate the cellular answers to relevant and reliable signals. The aim of this narrative review is to provide an overview of currently available microarray applications using HSP90 as the target.
Methods Pubmed search was performed for available studies on microarray-oriented techniques.
Results Different strategies have been used to measure the presence of HSP90, e.g., immunologically, by turnover, or binding activities. Protein microarrays have a broad application range. As a highly miniaturized assay system they are used to study protein-ligand or protein-protein interaction and used to measure the presence of a target as a diagnostic tool. Q-Dots have interesting electrical and optical properties. The exploitation of its optoelectronic properties for sensing plays a momentous role in the biomolecular diagnostic assay for HSP90.
Conclusions Target-oriented trawling of natural product compound libraries can help to identify novel compounds that inactivate the HSP90 function or increase the affinity for the natural ligand or client or help to restore the activity. HSP90 is a biomarker used in future as a stress marker for disease treatments, observing endurance status of athlete or life style management.
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Abbreviations
- 17-AAG:
-
17-N-allylamino-17-demethoxygeldanamycin
- Aarsd1:
-
muscle specific cochaperone (alanyl-tRNA synthetase domain-containing 1)
- AIF:
-
apopotosis inducing factor
- Apaf1:
-
apoptotic protease activating factor 1
- CdSe:
-
cadmium selenide
- CgA:
-
chromogranin A
- CTD:
-
c-terminal domain
- Cy5:
-
Cyanin 5
- IgA:
-
Immunoglobulin A
- MD:
-
middle domain
- NTD:
-
N-terminal domain
- PMA:
-
protein microarray
- PPI:
-
protein-protein interaction
- PU-H71:
-
6-amino-8-[(6-iodo-1,3-benzodioxol-5-yl)thio]-N-(1-methylethyl)-9H-purine-9-propanamine
- Q-dots:
-
quantum dots
- SPR:
-
surface plasma resonance
- ZnS:
-
zinc sulfide
References
Angenendt P, Glökler J, Murphy D et al (2002) Toward optimized antibody microarrays: a comparison of current microarray support materials. Anal Biochem 309:253–260
Arruda DL, Wilson WC, Nguyen C (2009) Microelectrical sensors as emerging platforms for protein biomarker detection in point-of-care diagnostics. Expert Rev Mol Diagn 9:749–755
Arya H (2005) Quantum dots in bio-imaging: revolution by the small. Biochem Biophys Res Commun 329:1173–1177
Belaya I, Suwa M, Chen T (2018) Long-term exercise protects against cellular stresses in aged mice. Oxidative Med Cell Longev 2018:2894247
Bilan R, Fleury F, Nabiev I et al (2015) Quantum dot surface chemistry and functionalization for cell targeting and imaging. Bioconjug Chem 26:609–624
Bilan R, Nabiev I, Sukhanova A (2016) Quantum dot-based nanotools for bioimaging, diagnostics, and drug delivery. Chembiochem 17:2103–2114
Campanella C, Pace A, Caruso BC et al (2018) Heat shock proteins in Alzheimer’s disease: role and targeting. Int J Mol Sci 19:pii: E2603
Chen B, Feder ME, Kang L (2018) Evolution of heat-shock protein expression underlying adaptive responses to environmental stress. Mol Ecol 27:3040–3054
Cretich M, Damin F, Chiari M (2014) Protein microarray technology: how far off is routine diagnostics? Analyst 139:528–542
Delmotte P, Delmotte-Plaque J (1953) A new antifungal substance of fungal origin. Nature 171:344
Echeverría PC, Bernthaler A, Dupuis P (2011) An interaction network predicted from public data as a discovery tool: application to the Hsp90 molecular chaperone machine. PLoS One 6:e26044
Echeverría PC, Briand PA, Picard D (2016) A remodeled Hsp90 molecular chaperone ensemble with the novel cochaperone Aarsd1 is required for muscle differentiation. Mol Cell Biol 36:1310–1321
Franke J, Eichner S, Zeilinger C et al (2013) Targeting heat-shock-protein 90 (Hsp90) by natural products: geldanamycin, a show case in cancer therapy. Nat Prod Rep 30:1299–1323
Fu Y, Xu X, Huang D et al (2017) Plasma heat shock protein 90 alpha as a biomarker for the diagnosis of liver cancer: an official, large-scale, and multicenter clinical trial. EBioMedicine 24:56–63
Geller R, Pechmann S, Acevedo A et al (2018) Hsp90 shapes protein and RNA evolution to balance trade-offs between protein stability and aggregation. Nat Commun 9:1781
Grenert JP, Sullivan WP, Fadden P et al (1997) The amino-terminal domain of heat shock protein 90 (hsp90) that binds geldanamycin is an ATP/ADP switch domain that regulates hsp90 conformation. J Biol Chem 272:23843–23850
Gupta S, Manubhai KP, Kulkarni V et al (2016) An overview of innovations and industrial solutions in Protein Microarray Technology. Proteomics 16:1297–1308
Holt LJ, Büssow K, Walter G et al (2000) By-passing selection: direct screening for antibody-antigen interactions using protein arrays. Nucleic Acids Res 28:E72
Hu S, Xie Z, Qian J et al (2011) Functional protein microarray technology. Wiley Interdiscip Rev Syst Biol Med:1–19
Jäättelä M, Wissing D, Bauer PA (1992) Major heat shock protein HSP70 protects tumor cells from tumor necrosis factor cytotoxicity. EMBO J 11:3507–3512
Jäättelä M, Wissing D, Kokholm K (1998) Hsp70 exerts its anti-apoptotic function downstream of caspase-3-like proteases. EMBO J 17:6124–6134
Jego G, Hazoumé A, Seigneuric R, Garrido C (2013) Targeting heat shock proteins in cancer. Cancer Lett 332:275–285
Joshi S, Wang T, Araujo TLS et al (2018) Adapting to stress – chaperome networks in cancer. Nat Rev Cancer 18:562–575
Kampinga HH, Hageman J, Vos MJ et al (2009) Guidelines for the nomenclature of the human heat shock proteins. Cell Stress Chaperones 14:105–111
Karagöz GE, Rüdiger SG (2015) Hsp90 interaction with clients. Trends Biochem Sci 40:117–125
Kellmann M, Bertollo M, Bosquet L et al (2018) Recovery and performance in sport: consensus statement. Int J Sports Physiol Perform 13:240–245
Khandelwal A, Kent CN, Balch M et al (2018) Structure-guided design of an Hsp90β N-terminal isoform-selective inhibitor. Nat Commun 9:425
Kim Y, Khalil AA, Kabapy NF et al (2011) Heat shock proteins in oncology: diagnostic biomarkers or therapeutic targets? Biochim Biophys Acta Rev Cancer 1816:89–104
Kinfe HH (2019) Versatility of glycals in synthetic organic chemistry: coupling reactions, diversity oriented synthesis and natural product synthesis. Org Biomol Chem 17:4153–4182
Klein HU, McCabe C, Gjoneska E et al (2019) Epigenome-wide study uncovers large-scale changes in histone acetylation driven by tau pathology in aging and Alzheimer’s human brains. Nat Neurosci 22:37–46
Lang BJ, Guerrero-Giménez ME, Prince TL et al (2019) Heat shock proteins are essential components in transformation and tumor progression: cancer cell intrinsic pathways and beyond. Int J Mol Sci 20:pii: E4507
Lee EC, Fragala MS, Kavouras SA et al (2017) Biomarkers in sports and exercise: tracking health, performance, and recovery in athletes. J Strength Cond Res 31:2920–2937
Li L, Wang L, You QD et al (2019) Heat shock protein 90 inhibitors: an update on achievements, challenges, and future directions. J Med Chem 12. (in press)
Lindquist S (2009) Protein folding sculpting evolutionary change. Cold Spring Harb Symp Quant Biol 74:103–108
Lueking A, Cahill DJ, Müllner S (2005) Protein biochips: a new and versatile platform technology for molecular medicine. Drug Discov Today 10:789–794
Mattoussi H, Mauro M, Goldman ER et al (2000) Self-assembly of CdSe−ZnS quantum dot bioconjugates using an engineered recombinant protein. J Am Chem Soc 122(49):12142–12150
Millson SH, Chua CS, Roe SM et al (2011) Features of the Streptomyces hygroscopicus HtpG reveal how partial geldanamycin resistance can arise with mutation to the ATP binding pocket of a eukaryotic Hsp90. FASEB J 25:3828–3837
Mishra P, Flynn JM, Starr TN et al (2016) Systematic mutant analyses elucidate general and client-specific aspects of HSP90 function. Cell Rep 15:588–598
Mohammadi Ostad-Kalayeh S, Hrupins V, Helmsen S et al (2017) Development of a microarray-based assay for efficient testing of new HSP70/DnaK inhibitors. Bioorg Med Chem 25:6345–6352
Mohammadi-Ostad-Kalayeh S, Stahl F, Scheper T et al (2018) Heat shock proteins revisited: using a mutasynthetically generated reblastatin library to compare the inhibition of human and leishmania Hsp90s. Chembiochem 19:562–574
Murillo-Solano C, Dong C, Sanchez CG et al (2017) Identification and characterization of the antiplasmodial activity of Hsp90 inhibitors. Malar J 16:292
Neckers L, Blagg B, Haystead T et al (2018) Methods to validate Hsp90 inhibitor specificity, to identify off-target effects, and to rethink approaches for further clinical development. Cell Stress Chaperones 23:467–482
Nimse SB, Sonawane MD, Song KS et al (2016) Biomarker detection technologies and future directions. Analyst 141:740–755
Palma LC, Ferreira LFGR, Petersen ALOA et al (2019) A docking-based structural analysis of geldanamycin-derived inhibitor binding to human or Leishmania Hsp90. Sci Rep 9:4756
Park YH, Seo JH, Park JH et al (2017) Hsp70 acetylation prevents caspase-dependent/independent apoptosis and autophagic cell death in cancer cells. Int J Oncol 51:573–578
Peng ZA, Peng X (2001) Formation of high-quality CdTe, CdSe, and CdS nanocrystals using CdO as precursor. J Am Chem Soc 123:183–184
Pflegerl K, Hahn R, Schallaun E et al (2001) Quantification of plasma-derived blood coagulation factor VIII by real-time biosensor measurements. J Chromatogr B Biomed Sci Appl 752:335–347
Picard D, Khursheed B, Garabedian MJ et al (1990) Reduced levels of Hsp90 compromise steroid receptor action in vivo. Nature 348:166–168
Piper PW, Millson SH (2012) Spotlight on the microbes that produce heat shock protein 90-targeting antibiotics. Open Biol 2:120138
Posfai D, Eubanks AL, Keim AI et al (2018) Identification of Hsp90 inhibitors with anti-plasmodium activity. Antimicrob Agents Chemother 62:e01799–e01717
Qin C, Tao L, Phang YH et al (2015) The assessment of the readiness of molecular biomarker-based mobile health technologies for healthcare applications. Sci Rep 5:17854
Radli M, Rüdiger SGD (2018) Dancing with the Diva: Hsp90-client interactions. J Mol Biol 430:3029–3040
Raman S, Singh M, Tatu U et al (2015) First structural view of a peptide interacting with the nucleotide binding domain of heat shock protein 90. Sci Rep 5:17015
Rodina A, Wang T, Yan P et al (2016) The epichaperome is an integrated chaperome network that facilitates tumour survival. Nature 538:397–401
Rosenzweig R, Nillegoda NB, Mayer MP et al (2019) The Hsp70 chaperone network. Nat Rev Mol Cell Biol 20:665–680
Rutherford SL, Lindquist S (1998) Hsp90 as a capacitor for morphological evolution. Nature 396:336–342
Sang Q, Liu X, Wang L et al (2018) Curcumin protects an SH-SY5Y cell model of Parkinson’s disease against toxic injury by regulating HSP90. Cell Physiol Biochem 51:681–691
Schax E, Walter JG, Märzhäuser H et al (2014) Microarray-based screening of heat shock protein inhibitors. J Biotechnol 180:1–9
Schinn SM, Broadbent A, Bradley WT et al (2016) Protein synthesis directly from PCR: progress and applications of cell-free protein synthesis with linear DNA. New Biotechnol 33:480–487
Schopf FH, Biebl MM, Buchner J (2017) The HSP90 chaperone machinery. Nat Rev Mol Cell Biol 18:345–360
Sharma R, Mohammadi-Ostad-Kalayeh S, Stahl F et al (2017) Two new labdane diterpenoids and one new β lactam compound from the aerial part of Roylea cinerea. Phytochem Lett 19:101–107
Starr TN, Flynn JM, Mishra P et al (2018) Pervasive contingency and entrenchment in a billion years of HSP90 evolution. Proc Natl Acad Sci U S A 115:4453–4458
Takatsu T, Ohtsuki M, Muramatsu A et al (2000) Enokita R, Kurakata SI. Reblastatin, a novel benzenoid ansamycin-type cell cycle inhibitor. J Antibiot (Tokyo) 53:1310–1312
Tassone G, Mangani S, Botta M et al (2018) Probing the role of Arg97 in Heat shock protein 90 N-terminal domain from the parasite Leishmania braziliensis through site-directed mutagenesis on the human counterpart. Biochim Biophys Acta, Proteins Proteomics 1866:1190–1198
Thorpe RT, Atkinson G, Drust B et al (2017) Monitoring fatigue status in elite team-sport athletes: implications for practice. Int J Sports Physiol Perform 12:S227–S234
Torres Acosta JA, Michlmayr H, Shams M et al (2019) Zearalenone and ß-Zearalenol but not their glucosides inhibit heat shock protein 90 ATPase activity. Front Pharmacol 10:1160
Tuck MK, Chan DW, Chia D et al (2009) Standard operating procedures for serum and plasma collection: early detection research network consensus statement standard operating procedure integration working group. J Proteome Res 8:113–117
Turbyville TJ, Wijeratne EM, Liu MX et al (2006) Search for Hsp90 inhibitors with potential anticancer activity: isolation and SAR studies of radicicol and monocillin I from two plant-associated fungi of the Sonoran desert. J Nat Prod 69:178–184
Ueda T, Tamura T, Hamachi I (2019) Development of a cell-based ligand-screening system for identifying Hsp90 inhibitors. Biochemistry 59:179–182
Verba KA, Wang RY, Arakawa A et al (2016) Atomic structure of Hsp90-Cdc37-Cdk4 reveals that Hsp90 traps and stabilizes an unfolded kinase. Science 352:1542–1547
Wade M, Li YC, Wahl GM (2013) Protein microarray technology. Nat Rev Cancer 13:83–96
Wang S, Xu Y, Maine EA et al (2008) Functional characterization of the biosynthesis of radicicol, an Hsp90 inhibitor resorcylic acid lactone from Chaetomium chiversii. Chem Biol 15:1328–1338
Wang T, Rodina A, Dunphy MP et al (2019) Chaperome heterogeneity and its implications for cancer study and treatment. J Biol Chem 294:2162–2179
Wu J, Liu T, Rios Z et al (2017) Heat shock proteins and cancer. Trends Pharmacol Sci 38:226–256
Wuest F, Bouvet V, Mai B et al (2012) Fluorine- and rhenium-containing geldanamycin derivatives as leads for the development of molecular probes for imaging Hsp90. Org Biomol Chem 10:6724–6731
Xu Y, Wallace MA, Fitzgerald MC (2016) Thermodynamic analysis of the geldanamycin-Hsp90 interaction in a whole cell lysate using a mass spectrometry-based proteomics approach. J Am Soc Mass Spectrom:1670–1676
Yelleswarapu V, Buser JR, Haber M et al (2019) Mobile platform for rapid sub-picogram-per-milliliter, multiplexed, digital droplet detection of proteins. Proc Natl Acad Sci U S A 116:4489–4495
Yin M, Jiang M, Ren Z et al (2017) The complete genome sequence of Streptomyces autolyticus CGMCC 0516, the producer of geldanamycin, autolytimycin, reblastatin and elaiophylin. J Biotechnol 252:27–31
Yue Q, Stahl F, Plettenburg O et al (2018) The noncompetitive effect of gambogic acid displaces fluorescence-labeled ATP but requires ATP for binding to Hsp90/HtpG. Biochemistry 57:2601–2605
Acknowlegements
Funding: AK financed by Exposè scholarship from the Graduate Academy Leibniz University Hannover.
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Kishore, A., Zeilinger, C. (2020). Threading Microarrays into Novel Applications. In: Asea, A.A.A., Kaur, P. (eds) Heat Shock Proteins in Human Diseases. Heat Shock Proteins, vol 21. Springer, Cham. https://doi.org/10.1007/7515_2020_7
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