Heat Shock Proteins: Stimulators of Innate and Acquired Immunity

Colaço, Camilo; Bailey, Christopher R.; Walker, K. Barry; Keeble, James

doi:10.1155/2013/461230

Cited by 81 publications

(70 citation statements)

References 111 publications

(195 reference statements)

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“…Heat shock proteins (HSPs) are a superfamily of highly conserved molecular chaperones which are induced in plant, yeast, bacterial, and mammalian cells in response to sublethal physiological and environmental stresses [15,16]. Their key role is to protect cells from stress by assisting in protein folding and stabilisation.…”

Section: Introductionmentioning

confidence: 99%

Leukocyte integrin α4β7 associates with heat shock protein 70

et al. 2015

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The leukocyte integrin cell adhesion molecules α4β7 and αEβ7 mediate the homing and retention of lymphocytes to the gut, and sites of inflammation. Here we have identified heat shock protein 70 (HSP70) as a major protein that associates with the cytoplasmic domain of the integrin β7 subunit. HSPs are molecular chaperones that protect cells from stress but more recently have been reported to also regulate cell adhesion and invasion via modulation of β1, β2, and β3 integrins and integrin-associated signalling molecules. Several HSP70 isoforms including HSP70-3, HSP70-1L, HSP70-8, and HSP70-9 were specifically precipitated from T cells by a bead-conjugated β7 subunit cytoplasmic domain peptide and subsequently identified by high-resolution liquid chromatography-tandem mass spectrometry. In confirmation, the β7 subunit was co-immunoprecipitated from a T cell lysate by an anti-HSP70 antibody. Further, recombinant human HSP70-1a was precipitated by β7 cytoplasmic domain-coupled beads. The HSP70 inhibitor KNK437 decreased the expression of HSP70 without affecting the expression of the β7 integrin. It significantly inhibited α4β7-mediated adhesion of T cells to mucosal addressin cell adhesion molecule 1 (MAdCAM-1), suggesting HSP70 is critical for maintaining β7 integrin signalling function. The functional implications of the association of β7 integrins with the different isoforms of HSP70 warrants further investigation.

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Section: Introductionmentioning

confidence: 99%

Leukocyte integrin α4β7 associates with heat shock protein 70

et al. 2015

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“…Induction of tolerance against heat shock proteins (HSPs) has been also achieved using LAB. HSPs participate in the control of autoimmunity and in the cellular response to stress and are overexpressed in diseases involving inflammation and autoimmunity mechanisms, such as atherosclerosis and encephalomyelitis [18]. Oral administration of L. lactis strains secreting different forms of HSP-65 exerted a protective effect against endothelial damage and against the formation of atherosclerotic lesions in a low-density lipoprotein receptor-deficient (LDL-RD) mouse model [19].…”

Section: Engineered Bacteria Against Inflammatory and Autoimmune Disomentioning

confidence: 99%

Engineered bacteria as therapeutic agents

Piñero-Lambea

Ruano-Gallego

Fernández

2015

Current Opinion in Biotechnology

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Although bacteria are generally regarded as the causative agents of infectious diseases, most bacteria inhabiting the human body are non-pathogenic and some of them can be turned, after proper engineering, into 'smart' living therapeutics of defined properties for the treatment of different illnesses. This review focuses on recent developments to engineer bacteria for the treatment of diverse human pathologies, including inflammatory bowel diseases, autoimmune disorders, cancer, metabolic diseases and obesity, as well as to combat bacterial and viral infections. We discuss significant advances provided by synthetic biology to fully reprogram bacteria as human therapeutics, including novel measures for strict biocontainment.

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“…Under normal conditions, HSPs perform essential biological functions such as modulating protein activity by changing protein conformation, serving as molecular chaperones in protein transport between cell organelles, promoting multiprotein complex assembly/ disassembly, and ensuring proper folding of nascent and altered proteins [25,26] . Many other more specific functions have been identified for particular HSP types and include roles in immunological processes, cell cycle regulation, transcriptional activation and signal transduction [27][28][29] . Mammalian HSPs have been classified into the following six families according to molecular size: HSP100, HSP90, HSP70, HSP60, HSP40 and small HSPs [30] .…”

Section: Heat Shock Proteinsmentioning

confidence: 99%

Tumour suppressor HLJ1: A potential diagnostic, preventive and therapeutic target in non-small cell lung cancer

Tsai¹

2014

WJCO

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Lung cancer is the leading cause of cancer-related mortality throughout the world. Non-small cell lung cancer (NSCLC) accounts for 85% of all diagnosed lung cancers. Despite considerable progress in the diagnosis and treatment of the disease, the overall 5-year survival rate of NSCLC patients remains lower than 15%. The most common causes of death in lung cancer patients are treatment failure and metastasis. Therefore, developing novel strategies that target both tumour growth and metastasis is an important and urgent mission for the next generation of anticancer therapy research. Heat shock proteins (HSPs), which are involved in the fundamental defence mechanism for maintaining cellular viability, are markedly activated during environmental or pathogenic stress. HSPs facilitate rapid cell division, metastasis, and the evasion of apoptosis in cancer development. These proteins are essential players in the development of cancer and are prime therapeutic targets. In this review, we focus on the current understanding of the molecular mechanisms responsible for HLJ1's role in lung cancer carcinogenesis and progression. HLJ1, a member of the human HSP 40 family, has been characterised as a tumour suppressor. Research studies have also reported that HLJ1 shows promising dual anticancer effects, inhibiting both tumour growth and metastasis in NSCLC. The accumulated evidence suggests that HLJ1 is a potential biomarker and treatment target for NSCLC.© 2014 Baishideng Publishing Group Inc. All rights reserved.Key words: Non-small cell lung cancer; Metastasis; HLJ1; Anticancer; Biomarker Core tip: HLJ1, a member of the human heat shock proteins 40 family, has been characterised as a tumour suppressor. Research studies have reported that HLJ1 shows promising dual anticancer effects, inhibiting both tumour growth and metastasis in non-small cell lung cancer (NSCLC). The accumulated evidence suggests that HLJ1 is a potential biomarker and treatment target for NSCLC. We propose a hypothetical model for the roles of HLJ1 stimulator in suppressing lung cancer tumourigenesis. Investigating the integrated and coordinated molecular mechanisms of HLJ1 may shed new light on the treatment of lung cancer. The development of drug targeting HLJ1 may be an effective approach for lung cancer therapy.Tsai MF, Wang CC, Chen JJW. Tumour suppressor HLJ1: A potential diagnostic, preventive and therapeutic target in nonsmall cell lung cancer.

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Heat Shock Proteins: Stimulators of Innate and Acquired Immunity

Cited by 81 publications

References 111 publications

Leukocyte integrin α4β7 associates with heat shock protein 70

Leukocyte integrin α4β7 associates with heat shock protein 70

Engineered bacteria as therapeutic agents

Tumour suppressor HLJ1: A potential diagnostic, preventive and therapeutic target in non-small cell lung cancer

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