Endogenous Substrates of Sphingosine-Dependent Kinases (SDKs) Are Chaperone Proteins:  Heat Shock Proteins, Glucose-Regulated Proteins, Protein Disulfide Isomerase, and Calreticulin†

Biochemistry ◽  
1999 ◽  
Vol 38 (11) ◽  
pp. 3369-3378 ◽  
Author(s):  
Tamar Megidish ◽  
Koji Takio ◽  
Koiti Titani ◽  
Kazuhisa Iwabuchi ◽  
Akikazu Hamaguchi ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Protein Disulfide Isomerase ◽  
Chaperone Proteins ◽  
Disulfide Isomerase ◽  
Endogenous Substrates ◽  
Shock Proteins ◽  
Protein Disulfide ◽  
Glucose Regulated Proteins

Principles of chaperone-mediated protein folding

1995 ◽  
Vol 348 (1323) ◽  
pp. 107-112 ◽  
Keyword(s):  
Protein Folding ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Molecular Chaperones ◽  
Cellular Protein ◽  
Chaperone Proteins ◽  
Shock Proteins ◽  
Polypeptide Chains

The recent discovery of molecular chaperones and their functions has changed dramatically our view of the processes underlying the folding of proteins in vivo . Rather than folding spontaneously, most newly synthesized polypeptide chains seem to acquire their native conformations in a reaction mediated by chaperone proteins. Different classes of molecular chaperones, such as the members of the Hsp70 and Hsp60 families of heat-shock proteins, cooperate in a coordinated pathway of cellular protein folding.

34 DIFFERENTIALLY EXPRESSED PROTEINS OF EARLY-STAGE PLACENTA DERIVED FROM CLONED CAT EMBRYOS USING PROTEOMICS ANALYSIS

2012 ◽  
Vol 24 (1) ◽  
pp. 129
Author(s):  
J. I. Bang ◽  
D. W. Bae ◽  
Y. S. Kwon ◽  
G. K. Deb ◽  
B. H. Choi ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Early Pregnancy ◽  
Protein Disulfide Isomerase ◽  
Triosephosphate Isomerase ◽  
Early Stage ◽  
Differentially Expressed ◽  
Differentially Expressed Proteins ◽  
Disulfide Isomerase ◽  
Protein Disulfide

We have previously demonstrated that differentially expressed proteins affect abnormal development and function of cloned term placenta. This is associated with cloned fetus morbidity and mortality. We also frequently observed loss of the cloned fetus and failed development during early pregnancy periods. To confirm the pattern of important gene expression in cloned placenta during pre- and post-implantation, we investigated expression pattern of proteins in early stage (21 days) domestic cat placentas of cloned embryo transfer (CEP; n = 2) and artificial insemination (CP; n = 4) derived pregnancy. The differentially expressed proteins were investigated by 2-DE and MALDI-TOF/MS. Twenty-three proteins were up- and down-regulated at least 1.5-fold in the CEP (P < 0.05) compared with the CP. Differentially expressed proteins were analysed using PDQest program and statistically analysed by 1-way ANOVA using the SPSS software. In CEP, 13 proteins were up-regulated, such as 78-kDa glucose-regulated protein (GRP78), annexin A2 (ANXA2), protein DJ-1 (DJ1), adenylate kinase isoenzyme 1 (AK1), protein disulfide-isomerase A3 (PDIA3), heat shock protein β-1 (HSPB1), actin, cytoplasmic 1 (ACTB), serum albumin (ALB), protein disulfide-isomerase A6 (PDIA6), G protein-regulated inducer of neurite outgrowth 1 (GRIN1) and triosephosphate isomerase (TIM). In contrast, 10 proteins were down-regulated, such as vinculin (VCL), triosephosphate isomerase (TIM), heterogeneous nuclear ribonucleoprotein H (hnRNPH), tropomyosin α-4 (TPM4), 60-kDa heat shock protein, mitochondrial (Hsp60), serum albumin (ALB), calumenin (CALU), keratin type 1 (CK1) and prohibitin (PHB). To validate the identified proteins in the CEP compared with the CP, we investigate a peptide sequences using MALDI-TOF/TOF tandem mass spectrometry. The sequence information obtained a high ions score from NCBI and Swiss-Prot databases. In conclusion, we did identify abnormal expression of proteins that might be associated with impaired development of CEP, which may endanger the cloned fetus during early pregnancy. This work was partly supported by the BK21 program and the KOSEF (10525010001-05N2501-00110) and the Next-generation BioGreen21 program (No. PJ007990012011).

Stress protein systems of mammalian cells

1986 ◽  
Vol 250 (1) ◽  
pp. C1-C17 ◽  
Author(s):  
J. R. Subjeck ◽  
T. T. Shyy
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Mammalian Cells ◽  
Stress Proteins ◽  
Heat Exposure ◽  
Stress Protein ◽  
Protective Role ◽  
Living Organisms ◽  
Shock Proteins ◽  
Glucose Regulated Proteins

Living organisms are known to react to a heat stress by the selective induction in the synthesis of several polypeptides. In this review we list the major stress proteins of mammalian cells that are induced by heat shock and other environments and categorize these proteins into specific subgroups: the major heat shock proteins, the glucose-regulated proteins, and the low-molecular-weight heat shock proteins. Characteristics of the localization and expression of proteins in each of these subgroups are presented. Specifically, the nuclear/nucleolar locale of certain of the major heat shock proteins is considered with respect to their association with RNA and the recovery of cells after a heat exposure. The induction of these major heat shock proteins and the repression of the glucose-regulated proteins as a result of reoxygenation of anoxic cells or by the addition of glucose to glucose-deprived cultures is described. Changes in the expression of these protein systems during embryogenesis and differentiation in mammalian and nonmammalian systems is summarized, and the protective role that some of these proteins appear to play in protecting the animal against the lethal effects of a severe heat treatment and against teratogenesis is critically examined.

scholarly journals Evidence of Prognostic Relevant Expression Profiles of Heat-Shock Proteins and Glucose-Regulated Proteins in Oesophageal Adenocarcinomas

PLoS ONE ◽  
2012 ◽  
Vol 7 (7) ◽  
pp. e41420 ◽  
Author(s):  
Julia Slotta-Huspenina ◽  
Daniela Berg ◽  
Karina Bauer ◽  
Claudia Wolff ◽  
Katharina Malinowsky ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Expression Profiles ◽  
Shock Proteins ◽  
Glucose Regulated Proteins
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