Cloning and analysis of cDNA sequences coding for two 16 kllodalton heat shock proteins (hsps) inCaenorhabditis elegans:homology with the small hsps ofDrosophila

Heat shock proteins (HSPs) constitute a large family of conserved proteins acting as molecular chaperones that play a key role in intracellular protein homeostasis, regulation of apoptosis, and protection from various stress factors (including hypoxia, thermal stress, oxidative stress). Apart from their intracellular localization, members of different HSP families such as small HSPs, HSP40, HSP60, HSP70 and HSP90 have been found to be localized on the plasma membrane of malignantly transformed cells. In the current article, the role of membrane-associated molecular chaperones in normal and tumor cells is comprehensively reviewed with implications of these proteins as plausible targets for cancer therapy and diagnostics.

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Cellular Functions of Small Heat Shock Proteins (HSPB) in Hepatocellular Carcinoma

Current Molecular Medicine ◽

10.2174/1573405617666210204211252 ◽

2021 ◽

Vol 21 ◽

Author(s):

Noriko Yamada ◽

Rie Matsushima-Nishiwaki ◽

Kaido Kobayashi ◽

Shota Takahata ◽

Hidenori Toyoda ◽

...

Keyword(s):

Hepatocellular Carcinoma ◽

Heat Shock ◽

Heat Shock Proteins ◽

Molecular Chaperones ◽

Low Molecular Weight ◽

Post Translational Modification ◽

Cellular Functions ◽

The Family ◽

Small Hsps ◽

Shock Proteins

Abstract: Heat shock proteins (HSPs) play an essential role as molecular chaperones in proteostasis. Small HSPs are a group of low-molecular-weight HSPs in the range of 12-43 kDa and are classified as HSPB. Within the ten members of the family, HSPB1 (HSP27), HSPB5 (B-crystallin), HSPB6 (HSP20), and HSPB8 (HSP22) ubiquitously exist in various tissues, including liver tissue. These small HSPs undergo phosphorylation as a post-translational modification, and their functions are modulated. Hepatocellular carcinoma (HCC) is one of the most frequent cancers and the fourth leading cause of cancer-related death worldwide. HSPs play a cytoprotective role as molecular chaperones. Thus, HSPB has been generally considered to protect HCC cells and help the progression of HCC. On the other hand, recent studies from our laboratories have demonstrated suppressive roles of phospho-HSPB1, HSPB6, and HSPB8 in progression of HCC. These findings may provide a basis for a novel defense system by HSPB against HCC progression. This review focuses on the cellular functions of HSPB in HCC and summarizes the current research.

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Developmental expression of Drosophila melanogaster small heat-shock proteins

Journal of Cell Science ◽

10.1242/jcs.96.3.413 ◽

1990 ◽

Vol 96 (3) ◽

pp. 413-418

Author(s):

C. Haass ◽

U. Klein ◽

P.M. Kloetzel

Keyword(s):

Nervous System ◽

Heat Shock ◽

Heat Shock Proteins ◽

Small Heat Shock Proteins ◽

Developmental Expression ◽

Germ Band ◽

Small Hsp ◽

Small Hsps ◽

Shock Proteins ◽

The Brain

We have investigated the developmental expression of the small heat-shock proteins (hsps) during embryogenesis and in adult flies by immunocytology using an antibody that specifically identifies the small hsps. Antibody staining of unstressed early embryos reveals a predominantly cytoplasmic, homogeneous distribution of the small hsps throughout the embryo. At 6h of development small hsp expression can be identified in large, neuroblast-like cells within the extended germ band and in the brain of the embryo. During germ band contraction these cells appear to migrate to the midline where they align pairwise in a segmental pattern. After germ band contraction is complete a high level of small hsp expression can be observed in the midline glia (MECs) and in a cluster of six non-neuronal cells within the midline. In contrast to several other genes that are known to be important for embryogenesis and are expressed in the central nervous system (CNS) of embryos, CNS-specific expression of the small hsps is not restricted to the embryo but is also observed in the adult fly. In adult flies strong small hsp expression is observed in the brain, the thoracic ganglion and the leg nerves. Since the small hsps seem to be expressed predominantly in the glia of the nervous system, our data suggest a protective or stabilizing function of the small hsps within the nervous system during normal fly development, which is independent of the stress response.

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Identification, characterization, and analysis of cDNA and genomic sequences encoding two different small heat shock proteins in Hordeum vulgare

Genome ◽

10.1139/g93-148 ◽

1993 ◽

Vol 36 (6) ◽

pp. 1111-1118 ◽

Cited By ~ 18

Author(s):

Nelson Marmiroli ◽

Angelo Pavesi ◽

Gabriella Di Cola ◽

Hans Hartings ◽

Giovanna Raho ◽

...

Keyword(s):

Heat Shock ◽

Hordeum Vulgare ◽

Nucleotide Sequence ◽

Heat Shock Proteins ◽

Metal Ion ◽

Genomic Sequence ◽

Small Heat Shock Proteins ◽

In Vitro Translation ◽

Small Hsps ◽

Shock Proteins

In vitro translation of mRNAs prepared from barley (Hordeum vulgare) seedlings (cv. Onice) exposed at 40 °C directed the synthesis of major heat shock proteins (HSPs) with molecular masses of 80–90, 70, 42 and 16–22 kDa. A cDNA library prepared from the 40 °C mRNAs and screened by differential hybridization led to the isolation of heat shock specific sequences. One of these (Hv hsp18) was confirmed by hybrid-arrested and hybrid-released translation as encoding for an 18-kDa HSP. The barley hsp18 sequence has an open reading frame encoding a 160 amino acid residue 18-kDa protein that is 63% identical to wheat 16.9-kDa HSP (clone C5-8), 54% identical to soybean (Glycine max) 17.5-kDa HSP, and 49% identical to Arabidopsis thaliana 17.6-kDa HSP. Lower similarities were found with class II plant small HSPs such as soybean 17.9-kDa HSP (27%), Pisum sativum 17.7-kDa HSP (30%), wheat (Triticum aestivum) 17.3-kDa HSP (clone Ta hsp 17.3) (30%), and with animal small HSPs and α-crystallins. The Hv hsp18 sequence was used to pick up Hv hsp17 genomic sequence encoding for another class I 17-kDa HSP. By computer analysis of the nucleotide sequence the TATA box, two heat shock promoter elements, a metal-ion response element, and the polyadenylation signals were identified. Barley HSP 18 has an additional cysteine-rich region when compared with HSP17 mapping at the carboxy terminal end.Key words: barley, cDNA, genomic clone, heat shock, nucleotide sequence, small heat shock proteins.

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In Vitro Anti-Viral Effects of Small Heat Shock Proteins 20 and 27: A Novel Therapeutic Approach

Current Pharmaceutical Biotechnology ◽

10.2174/1389201020666190729104648 ◽

2019 ◽

Vol 20 (12) ◽

pp. 1011-1017

Author(s):

Rouhollah Vahabpour ◽

Sepehr Soleymani ◽

Farzin Roohvand ◽

Rezvan Zabihollahi ◽

Azam Bolhassani

Keyword(s):

Heat Shock ◽

Heat Shock Proteins ◽

Vero Cells ◽

Protective Effects ◽

Herpes Simplex Virus 1 ◽

Simultaneous Treatment ◽

Small Hsps ◽

Simplex Virus ◽

Shock Proteins

Background: The protective effects of heat shock proteins (Hsps) were studied in some infectious and non-infectious diseases, but their specificity was slightly known in various disorders. Among Hsps, small Hsps (e.g. Hsp27 and Hsp20) have important roles in protein folding and translocation, and also in immunity. Methods: In this study, overexpression of Hsp20 and Hsp27 was performed by transfection of the plasmids encoding Hsp20 and Hsp27 (pEGFP-Hsp20 and pEGFP-Hsp27) into Huh7.5, Hela and Vero cells using Lipofectamine along with heat shock. Then, their anti-herpes simplex virus-1 (HSV-1), anti- human immunodeficiency virus-1 (HIV-1) and anti-hepatitis C virus (HCV) effects, as well as cytotoxicity, were evaluated in vitro, for the first time. Results: Our data showed that simultaneous treatment with Lipofectamine and heat shock augmented the rate of transfection and subsequently the expression of Hsps in these cells. Moreover, overexpression of Hsp20 in HCV-infected Huh7.5 cells, HIV-infected Hela cells and HSV-infected Vero cells reduced the replication of HCV, HIV and HSV, respectively. In contrast, overexpression of Hsp27 significantly decreased HSV replication similar to Hsp20, but it did not affect the replication of HIV and HCV. Conclusion: Generally, Hsp20 was identified as a novel anti-HCV, anti-HSV and anti-HIV agent, but Hsp27 was efficient in the suppression of HSV infection. These Hsps may act through suppression of virus entry and/ or through interaction with viral proteins. Thus, it is necessary to determine their exact mechanisms in the near future.

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Effects of chronic portal hypertension on small heat-shock proteins in mesenteric arteries

AJP Gastrointestinal and Liver Physiology ◽

10.1152/ajpgi.00439.2004 ◽

2005 ◽

Vol 288 (4) ◽

pp. G616-G620 ◽

Cited By ~ 4

Author(s):

Xuesong Chen ◽

Hai-Ying Zhang ◽

Kristin Pavlish ◽

Joseph N. Benoit

Keyword(s):

Portal Hypertension ◽

Heat Shock ◽

Heat Shock Proteins ◽

Mrna Expression ◽

Protein Level ◽

Small Heat Shock Proteins ◽

Mesenteric Arteries ◽

Protein Levels ◽

Small Hsps ◽

Shock Proteins

Previous studies have shown that impaired vasoconstrictor function in chronic portal hypertension is mediated via cAMP-dependent events. Recent data have implicated two small heat-shock proteins (HSP), namely HSP20 and HSP27, in the regulation of vascular tone. Phosphorylation of HSP20 is associated with vasorelaxation, whereas phosphorylation of HSP27 is associated with vasoconstriction. We hypothesized that alterations in the expression and/or phosphorylation of small HSPs may play a role in impaired vasoconstriction in portal hypertension. A rat model of prehepatic chronic portal hypertension was used. Studies were conducted in small mesenteric arteries isolated from normal and portal hypertensive rats. Protein levels of HSP20 and HSP27 were detected by Western blot analysis. Protein phosphorylation was analyzed by isoelectric focusing. HSP20 mRNA expression was determined by RT-PCR. To examine the role of cAMP in the regulation of small HSP phosphorylation and expression, we treated both normal and portal hypertensive vessels with a PKA inhibitor Rp-cAMPS. We found both an increased HSP20 phosphorylation and a decreased HPS20 protein level in portal hypertension, both of which were restored to normal by PKA inhibition. However, PKA did not change HSP20 mRNA expression. We conclude that decreased HSP20 protein level is mediated by cAMP-dependent pathway and that impaired vasoconstrictor function in portal hypertension may be partially explained by decreased expression of HSP20. We also suggest that the phosphorylation of HSP20 by PKA may alter HSP20 turnover.

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HSPs under Abiotic Stresses

Abiotic Stress in Plants ◽

10.5772/intechopen.93787 ◽

2021 ◽

Author(s):

Noor ul Haq ◽

Samina N. Shakeel

Keyword(s):

Molecular Weight ◽

Heat Shock ◽

Photosystem Ii ◽

Heat Shock Proteins ◽

Defense Mechanisms ◽

Chenopodium Album ◽

Transit Peptide ◽

Multiple Roles ◽

Small Hsps ◽

Shock Proteins

Different organisms respond to the altered environmental conditions by different ways. Heat shock proteins’ (HSPs) production is one among the different defense mechanisms which defend the photosystem II and thylokoid membrane in plants. There are different types of HSPs based on their size, that is, high molecular weight (60–100 kDa) and low molecular weight heat shock proteins (15–30 kDa). Small HSPs are further classified based on their localization and role in different sub-cellular organelles. Cp-sHSPs are the chloroplast-specific small HSPs that protect the photosystem II and thylokoid membrane. A model to control the Cp-sHSPs in Chenopodium album has been put forward in this chapter. According to this model, Cp-sHSPs of Chenopodium album are created in cytoplasm and are moved toward chloroplast. The transit peptide is removed on reaching to the target sub-cellular organelle, that is, chloroplast and the premature Cp-sHSPs are converted into mature ones which have multiple roles under different abiotic stress conditions.

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Pathology-Dependent Effects Linked to Small Heat Shock Proteins Expression: An Update

Scientifica ◽

10.6064/2012/185641 ◽

2012 ◽

Vol 2012 ◽

pp. 1-19 ◽

Cited By ~ 13

Author(s):

A.-P. Arrigo

Keyword(s):

Heat Shock ◽

Heat Shock Proteins ◽

Inflammatory Diseases ◽

Small Heat Shock Proteins ◽

Cell Degeneration ◽

Cellular Protection ◽

Different Types ◽

Small Hsps ◽

Client Proteins ◽

Shock Proteins

Small heat shock proteins (small Hsps) are stress-induced molecular chaperones that act as holdases towards polypeptides that have lost their folding in stress conditions or consequently of mutations in their coding sequence. A cellular protection against the deleterious effects mediated by damaged proteins is thus provided to cells. These chaperones are also highly expressed in response to protein conformational and inflammatory diseases and cancer pathologies. Through specific and reversible modifications in their phospho-oligomeric organization, small Hsps can chaperone appropriate client proteins in order to provide cells with resistance to different types of injuries or pathological conditions. By helping cells to better cope with their pathological status, their expression can be either beneficial, such as in diseases characterized by pathological cell degeneration, or deleterious when they are required for tumor cell survival. Moreover, small Hsps are actively released by cells and can act as immunogenic molecules that have dual effects depending on the pathology. The cellular consequences linked to their expression levels and relationships with other Hsps as well as therapeutic strategies are discussed in view of their dynamic structural organization required to interact with specific client polypeptides.

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Characterization of a novel group of basic small heat shock proteins in Xenopus laevis A6 kidney epithelial cells

Biochemistry and Cell Biology ◽

10.1139/o98-076 ◽

1998 ◽

Vol 76 (4) ◽

pp. 665-671 ◽

Cited By ~ 11

Author(s):

Nicholas W Ohan ◽

Ying Tam ◽

Pasan Fernando ◽

John J Heikkila

Keyword(s):

Heat Shock ◽

Heat Shock Proteins ◽

Xenopus Laevis ◽

Sodium Arsenite ◽

Cross Reactivity ◽

Small Heat Shock Proteins ◽

Herbimycin A ◽

Small Hsps ◽

Gradient Gel Electrophoresis ◽

Shock Proteins

In this study, we report the detection of a new group of five stress-inducible basic small heat shock proteins (BShsps) in Xenopus laevis kidney epithelial A6 cells by means of two-dimensional non-equilibrium pH gradient gel electrophoresis. These basic 30-kDa small hsps are distinct from the previously described X. laevis acidic hsp30 family on the basis of their charge and lack of cross-reactivity with an hsp30 antibody. Furthermore, at least two of the five BShsps were present constitutively, an observation that has not been made with the acidic hsp30 family. The heat inducibility of the BShsps was regulated at the level of transcription as indicated by their inhibited synthesis in the presence of the transcriptional inhibitor actinomycin D. Furthermore, the optimal temperature of BShsp induction, temporal pattern of synthesis, and induction of BShsps by other stressors such as herbimycin A and sodium arsenite were similar to those reported for the acidic hsp30 family. This study suggests that X. laevis contains at least two unique groups of small heat shock proteins that are coordinately expressed.Key words: Xenopus laevis, heat shock protein, hsp30, NEPHGE, basic small heat shock proteins, sodium arsenite, herbimycin A.

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