Genetic aspects of the hsp70 multigene family in vertebrates

Günther, Eberhard; Walter, Lutz

doi:10.1007/bf01923453

Cited by 101 publications

(82 citation statements)

References 81 publications

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“…In CD8 cells (aside from the canonical example of CD8␣͞CD8␤), the most differentially expressed gene was CCR9, a receptor for the TECK ligand on thymic dendritic cells and intestinal enterocytes. Expression of CCR9 by DP thymocytes is down-regulated on CD4 thymocytes and may distinguish recent thymic emigrants in peripheral lymphoid tissues and intestinal lamina propria (29)(30)(31) (32). Although the role of HSP70.1 in thymic development has not been established, generalized overexpression of an HSP 70.1 transgene results in selective developmental arrest of thymocyte differentiation at the DP stage (33).…”

Section: Resultsmentioning

confidence: 99%

Detailed analysis of gene expression during development of T cell lineages in the thymus

McCarty

Shinohara

et al. 2004

Proc. Natl. Acad. Sci. U.S.A.

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The genetic mechanisms that promote lineage commitment and eliminate autoreactive cells in the thymus are not well understood. To better understand this process, we have identified and quantitated transcripts in the two major thymocyte lineages by using serial analysis of gene expression. Approximately 25 genes displayed almost complete segregation to one or the other T cell lineage. Commitment to the CD4 lineage was marked by upregulation of genes associated with increased survival and chaperone function followed by expression of genes that regulate nucleosome remodeling and T cell receptor signaling. Differentiation within the CD8 lineage, on the other hand, was marked by up-regulation of genes that regulate lymphocyte homing, followed by quenching of genes that inhibit apoptosis. Definition of differential gene expression during development of the two major thymocyte lineages will allow insight into mechanisms of T cell development after positive and negative selection.serial analysis of gene expression ͉ genetic profiling ͉ CD4͞CD8 ͉ lineage commitment T he two major T cell lineages that regulate adaptive immunity are generated and purged of clones bearing autoreactive T cell receptors (TCR) in the thymus (1). Although the molecular basis of TCR expression on thymocytes and T cells is relatively well understood, the mechanisms that orchestrate development and selection of TCR-bearing thymocytes have not been clearly defined. Delineation of the expression and potential function of genes expressed during the development of each lineage represents an important step in understanding this process.Thymocyte differentiation begins with migration of common lymphoid progenitor cells from hematopoietic stem cells in adult bone marrow or fetal liver into the thymus, where they undergo cellular maturation and TCR-based selection. Distinct developmental compartments have been defined according to expression of the CD4 and CD8 coreceptors on differentiating thymocytes. The earliest compartment is composed of CD4 Ϫ 8 Ϫ double negative (DN) thymocytes, which give rise to CD4 ϩ CD8 ϩ double positive (DP) intermediates, which yield mature CD4 ϩ CD8 Ϫ (CD4) or CD4 Ϫ CD8 ϩ (CD8) single positive (SP) mature progeny. The DN stage of thymocyte differentiation is marked by genetic events that prepare cells for TCR-based selection by self-MHC, including expression of recombination activating genes (RAG-1 and RAG-2) and initiation of TCR␤ gene rearrangements. These genetic events can be demarcated according to surface markers expressed sequentially on DN thymocytes (stages DN1-DN4) in order of their appearance during development (2, 3). DN1 and DN2 thymocytes proliferate before RAG-1͞-2 expression (4, 5), whereas the DN3 3 DN4 developmental step is accompanied by expression of a pre-TCR that inhibits further RAG-1͞-2 activity and promotes a second proliferative burst of cells that express both CD4 and CD8, marking transition into the DP compartment (6).Thymocytes that express the DP phenotype (by far the most abundant in the thymus) ...

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Section: Resultsmentioning

confidence: 99%

Detailed analysis of gene expression during development of T cell lineages in the thymus

McCarty

Shinohara

et al. 2004

Proc. Natl. Acad. Sci. U.S.A.

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“…Previous data indicated that the Hsp70 chaperone family lacks a conventional signal peptide sequence that would allow them to be transported through cytosolic or plasma membranes [35]. Consequently, transport [37,40] would require either increased cell membrane permeability [29] or a specific exocytotic pathway, as already was reported from a hepatosplanchnic source [28] and from the brain [45] following body exercise.…”

Section: The Origin Of Salivary Chaperone Hsp70mentioning

confidence: 93%

Potential immunological functions of salivary Hsp70 in mucosal and periodontal defense mechanisms

Fábían

Fejérdy

Nguyen

et al. 2007

Arch. Immunol. Ther. Exp.

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Molecular chaperones were considered to be intracellular, but there is increasing evidence demonstrating their cytoprotective and immune modulator properties outside the cell. The major extracellular chaperone (Hsp70) was also found in saliva, indicating a possible effect of Hsp70 on mucosal surfaces. Here we summarize the immune-modulatory role of the 70-kDa stress protein family, with special attention on the potential impact of salivary Hsp70 on oral defense mechanisms. There are three major facets of Hsp70-induced immune activation: 1) the appearance of Hsp70 on the surface of certain tumor cells or virally infected cells, leading to their phagocytosis and subsequent lysis; 2) the role of extracellular uncomplexed Hsp70 as a danger signal, leading to the secretion of proinflammatory cytokines from antigen-presenting cells and T lymphocytes and of nitric oxide from macrophages as well as to complement activation; 3) receptor-mediated uptake of peptide-loaded Hsp70 to antigen-presenting cells and cross-presentation of the Hsp70-peptide complex as an antigen to cytotoxic T cells and natural killer lymphocytes. The immune-activating effect of salivary Hsp70 may also be highly important in oral defense, especially in areas where molecular and cellular participants of the immune response appear on the surface of the oral cavity (i.e. several lesions of the mucosa and the periodontal tissues).

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“…The mouse and human Hsp70 genes located in the MHC locus are expressed by transcription factors other than HSF1 (Morimoto et al 1990;Wu 1995). Conversely, given that the zebrafish hsp70 shows strict heat-inducible expression, it appears to undergo a simple transcriptional regulation that may involve only HSF, a system that is similar to that observed for the Drosophila and human HSP70B′ (Craig et al 1979;Voellmy et al 1985;Morimoto et al 1990;Gunther and Walter 1994).…”

Section: -1 Stress Responses In Embryosmentioning

confidence: 94%

“…3) . On the other hand, two distinct mammalian groups have been identified, namely, a Major Histocompatibility Complex (MHC)-linked group consisting of human HSP70- 1 and HSP70-2 and mouse HSP70.1 Wu et al 1985;Milner and Campbell 1990) and a group containing the human and pig HSP70B′ (Voellmy et al 1985;Gunther and Walter 1994). Thus, the heat-inducible HSP70s may have diverged into several distinct groups during vertebrate evolution.…”

Section: -2 Zebrafish Hsp70mentioning

confidence: 99%

Stress Protein HSP70 in Fish

Yamashita¹,

Yabu²,

Ojima³

2010

Aqua-BioSci. Monogr. (ABSM)

126

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Stress proteins (heat-shock proteins, HSPs), which comprise an evolutionally wellconserved protein family, are induced in response to a variety of stress conditions and metabolic insults. When cells are subjected to sudden environmental changes, stress proteins are induced and play a central role in cellular homeostasis. A response to sudden adverse environmental changes is referred to as the heat-shock or stress response and is accompanied by a rapid increase in the synthesis of stress proteins. Given the importance of stress proteins in thermal adaptation at the cellular level, we have studied the expression, regulation, and protective functions of the members of the HSP70 stress protein family under normal and stress conditions in a variety of fish species. HSP70/heat-shock cognate protein-70 (HSC70) plays essential roles in the receptor complex formation and activation of Activin/Nodal/transforming growth factor-β and bone morphogenetic protein receptors and facilitates Nodal signaling. In addition, chaperone-mediated autophagy assisted by HSP70/heat-shock cognate (HSC)70 may be responsible for the stress responses in fish cells. HSP70 and HSC70 translocated into the lysosomes were found to accelerate protein degradation and catabolism under both stressed and normal conditions.

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Genetic aspects of the hsp70 multigene family in vertebrates

Abstract: The family of genes encoding heat shock proteins of about 70 kDa (hsp70) in vertebrates is reviewed under genetic aspects. After a detailed description of the various hsp70 genes more general characteristics of the organization and evolution of the multigene family are discussed.

Cited by 101 publications

References 81 publications

Detailed analysis of gene expression during development of T cell lineages in the thymus

Detailed analysis of gene expression during development of T cell lineages in the thymus

Potential immunological functions of salivary Hsp70 in mucosal and periodontal defense mechanisms

Stress Protein HSP70 in Fish

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