scholarly journals Application of Gene-specific mRNA Differential Display for Identification of cDNAs that Encode Small HSPs Correlated with the Heat-induced Chilling Tolerance of Tomato Fruit

HortScience ◽  
1997 ◽  
Vol 32 (3) ◽  
pp. 498D-498
Author(s):  
Konstantinos E. Vlachonasios ◽  
Dina K. Kadyrzhanova ◽  
David R. Dilley
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Differential Display ◽  
Tomato Fruit ◽  
Chilling Injury ◽  
Mrna Differential Display ◽  
Small Heat Shock Proteins ◽  
The Other ◽  
Small Hsps ◽  
Shock Proteins

Heat-treatment of mature-green tomato fruit (Lycopersicon esculentum) for 48 h at 42°C has been shown to prevent chilling injury from developing after 2 or 3 weeks at 2°C. Using mRNA differential display, we recently cloned and characterized a cDNA that encodes a cytosolic class II small heat-shock protein (Le HSP17.6). The mRNA of Le HSP17.6 is up-regulated during heat shock and the level of transcription remains high during subsequent storage at chilling temperatures. We used mRNA differential display with gene-specific primers from the other small HSPs families and find that the transcription of the other small heat-shock proteins is up-regulated during heat shock and persists at elevated levels at 2°C for at least 2 weeks. When the fruits are returned to a permissive ripening temperature after the chilling period, the mRNA of the small HSPs declines slowly for 3 days. These results suggest that the persistence of the small heat-shock proteins at low temperatures may provide protection against chilling injury.

Developmental expression of Drosophila melanogaster small heat-shock proteins

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.

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

Genome ◽  
1993 ◽  
Vol 36 (6) ◽  
pp. 1111-1118 ◽  
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.

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

2005 ◽  
Vol 288 (4) ◽  
pp. G616-G620 ◽  
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.

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

Scientifica ◽  
2012 ◽  
Vol 2012 ◽  
pp. 1-19 ◽  
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.

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

1998 ◽  
Vol 76 (4) ◽  
pp. 665-671 ◽  
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.

Small heat shock proteins and the postharvest chilling tolerance of tomato fruit

2016 ◽  
Vol 159 (2) ◽  
pp. 148-160 ◽  
Author(s):  
Martín D. Ré ◽  
Carla Gonzalez ◽  
Mariela R. Escobar ◽  
María Laura Sossi ◽  
Estela M. Valle ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Tomato Fruit ◽  
Chilling Tolerance ◽  
Small Heat Shock Proteins ◽  
Shock Proteins
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