@article{MTMT:2715592,
	title = {The complex function of hsp70 in metastatic cancer.},
	url = {https://m2.mtmt.hu/api/publication/2715592},
	author = {Juhász, Kata and Lipp, AM and Nimmervoll, B and Sonnleitner, A and Hesse, J and Haselgruebler, T and Balogi, Zsolt},
	doi = {10.3390/cancers6010042},
	journal-iso = {CANCERS},
	journal = {CANCERS},
	volume = {6},
	unique-id = {2715592},
	abstract = {Elevated expression of the inducible heat shock protein 70 (Hsp70) is known to correlate with poor prognosis in many cancers. Hsp70 confers survival advantage as well as resistance to chemotherapeutic agents, and promotes tumor cell invasion. At the same time, tumor-derived extracellular Hsp70 has been recognized as a "chaperokine", activating antitumor immunity. In this review we discuss localization dependent functions of Hsp70 in the context of invasive cancer. Understanding the molecular principles of metastasis formation steps, as well as interactions of the tumor cells with the microenvironment and the immune system is essential for fighting metastatic cancer. Although Hsp70 has been implicated in different steps of the metastatic process, the exact mechanisms of its action remain to be explored. Known and potential functions of Hsp70 in controlling or modulating of invasion and metastasis are discussed.},
	year = {2014},
	eissn = {2072-6694},
	pages = {42-66}
}

@article{MTMT:2020268,
	title = {Discrimination of clinical stages in non-small cell lung cancer patients by serum HSP27 and HSP70: a multi-institutional case-control study},
	url = {https://m2.mtmt.hu/api/publication/2020268},
	author = {Zimmermann, M and Nickl, S and Lambers, C and Hacker, S and Mitterbauer, A and Hoetzenecker, K and Horváth-Rózsás, Anita and Ostoros, Gyula and Laszlo, Viktoria and Hofbauer, H and Rényi-Vámos, Ferenc István and Klepetko, W and Döme, Balázs and Ankersmit, HJ},
	doi = {10.1016/j.cca.2012.03.008},
	journal-iso = {CLIN CHIM ACTA},
	journal = {CLINICA CHIMICA ACTA},
	volume = {413},
	unique-id = {2020268},
	issn = {0009-8981},
	abstract = {Introduction: Lung cancer represents a major healthcare problem. Accordingly, there is an urgent need to identify serum biomarkers for early diagnosis of lung pathology. We have recently described that patients with manifest COPD evidence elevated levels of heat shock proteins (HSPs). Based on these data, we speculated whether HSPs are also increased in patients with diagnosed lung cancer.
		
		Methods: Serum levels of HSP27, phospho-HSP27 (pHSP27) and HSP70 in patients with non-small cell lung cancer (NSCLC) diagnosed at an early (stages I-II, n=37) or advanced (stages IIIA-IV, n=72) stage were determined by using ELISA. Healthy smokers (n=24). healthy never-smoker volunteers (n=33) and COPD patients (n=34) according to COLD classification served as control population.
		
		Results: Serum levels of HSP27 were elevated in patients with NSCLC diagnosed at an early or advanced stage when compared with both healthy control groups (P<0.005 and P<0.0001 respectively). Statistically significant differences were furthermore found between the groups of patient; with early vs. advanced stage NSCLC (P=0.0021). Serum levels of HSP70 were also significantly elevated in patients with NSCLC diagnosed at an early or at an advanced stage when compared with either healthy control,groups (P=0.0028 and P<0.0001 respectively). In univariate logistic regression models including healthy subjects and patients with NSCLC. HSP70 had an area under the curve (AUC) of 0.779 (P<0.0001) and HSP27 showed an AUC of 0.870 (P<0.0001).
		
		Conclusion: Our data suggest that serum HSP27 levels might serve as a possible tool to discriminate between early and advanced stages NSCLC. (C) 2012 Elsevier B.V. All rights reserved.},
	year = {2012},
	eissn = {1873-3492},
	pages = {1115-1120},
	orcid-numbers = {Rényi-Vámos, Ferenc István/0000-0002-0555-2096; Döme, Balázs/0000-0001-8799-8624}
}

@article{MTMT:1921579,
	title = {Targeting membrane heat-shock protein 70 (Hsp70) on tumors by cmHsp70.1 antibody},
	url = {https://m2.mtmt.hu/api/publication/1921579},
	author = {Stangl, S and Gehrmann, M and Riegger, J and Kuhs, K and Riederer, I and Sievert, W and Hube, K and Mocikat, R and Dressel, R and Kremmer, E and Pockley, AG and Friedrich, L and Vigh, László and Skerra, A and Multhoff, G},
	doi = {10.1073/pnas.1016065108},
	journal-iso = {P NATL ACAD SCI USA},
	journal = {PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA},
	volume = {108},
	unique-id = {1921579},
	issn = {0027-8424},
	abstract = {Immunization of mice with a 14-mer peptide TKDNNLLGRFELSG, termed "TKD," comprising amino acids 450-461 (aa(450-461)) in the C terminus of inducible Hsp70, resulted in the generation of an IgG1 mouse mAb cmHsp70.1. The epitope recognized by cmHsp70.1 mAb, which has been confirmed to be located in the TKD sequence by SPOT analysis, is frequently detectable on the cell surface of human and mouse tumors, but not on isogenic cells and normal tissues, and membrane Hsp70 might thus serve as a tumor-specific target structure. As shown for human tumors, Hsp70 is associated with cholesterol-rich microdomains in the plasma membrane of mouse tumors. Herein, we show that the cmHsp70.1 mAb can selectively induce antibody-dependent cellular cytotoxicity (ADCC) of membrane Hsp70(+) mouse tumor cells by unstimulated mouse spleen cells. Tumor killing could be further enhanced by activating the effector cells with TKD and IL-2. Three consecutive injections of the cmHsp70.1 mAb into mice bearing CT26 tumors significantly inhibited tumor growth and enhanced the overall survival. These effects were associated with infiltrations of NK cells, macrophages, and granulocytes. The Hsp70 specificity of the ADCC response was confirmed by preventing the antitumor response in tumor-bearing mice by coinjecting the cognate TKD peptide with the cmHsp70.1 mAb, and by blocking the binding of cmHsp70.1 mAb to CT26 tumor cells using either TKD peptide or the C-terminal substrate-binding domain of Hsp70.},
	year = {2011},
	eissn = {1091-6490},
	pages = {733-738}
}