Amino acid regions 357–368 and 418–427 of Streptococcus pyogenes 60kDa heat shock protein are recognized by antibodies from glaucomatous patient sera

2010 ◽  
Vol 48 (6) ◽  
pp. 239-244 ◽  
Author(s):  
Mario E. Cancino-Diaz ◽  
Martha Sanchez-Becerra ◽  
Celia Elizondo-Olascoaga ◽  
Sandra Rodríguez-Martínez ◽  
Juan C. Cancino-Diaz
Keyword(s):  
Amino Acid ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Streptococcus Pyogenes ◽  
Glaucomatous Patient

Purification of a mature form of 60kDa heat-shock protein (chaperonin homolog) from porcine kidney and its partial amino acid sequence

1992 ◽  
Vol 24 (9) ◽  
pp. 1507-1510 ◽  
Author(s):  
Wakui Hideki ◽  
Itoh Hideaki ◽  
Tashima Yohtalou ◽  
Kobayashi Ryoji ◽  
Nakamoto Yasushi ◽  
...  
Keyword(s):  
Amino Acid ◽  
Heat Shock ◽  
Amino Acid Sequence ◽  
Heat Shock Protein ◽  
Porcine Kidney ◽  
Partial Amino Acid Sequence ◽  
Mature Form

scholarly journals Members of the 70-kilodalton heat shock protein family contain a highly conserved calmodulin-binding domain.

1990 ◽  
Vol 10 (3) ◽  
pp. 1234-1238 ◽  
Author(s):  
M A Stevenson ◽  
S K Calderwood
Keyword(s):  
Amino Acid ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Alpha Helix ◽  
Cellular Protein ◽  
Binding Domain ◽  
Functional Region ◽  
Amino Acid Homology ◽  
Calmodulin Binding ◽  
Essential Components

The 70-kilodalton heat shock protein (hsp70) family members appear to be essential components in a number cellular protein-protein interactions. We report here on the characterization of a new functional region in hsp70, a calmodulin-binding site. We have identified a 21-amino-acid sequence within the hsp70 protein that contains a calmodulin-binding domain. The peptide formed a potential amphipathic alpha helix and bound calmodulin with high affinity. Comparison of amino acid homology of this calmodulin-binding sequence with analogous hsp70 sequences from other species showed a high degree of conservation.

scholarly journals Comparative Analysis of the Putative Amino Acid Sequences of Chlamydial Heat Shock Protein 60 and Escherichia coli GroEL.

2000 ◽  
Vol 62 (9) ◽  
pp. 941-945 ◽  
Author(s):  
Yoshitsugu OCHIAI ◽  
Hideto FUKUSHI ◽  
Cai YAN ◽  
Tsuyoshi YAMAGUCHI ◽  
Katsuya HIRAI
Keyword(s):  
Escherichia Coli ◽  
Comparative Analysis ◽  
Amino Acid ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Amino Acid Sequences ◽  
Heat Shock Protein 60

Heat induction of heat shock protein 25 requires cellular glutamine in intestinal epithelial cells

2006 ◽  
Vol 291 (2) ◽  
pp. C290-C299 ◽  
Author(s):  
Kittiporn Phanvijhitsiri ◽  
Mark W. Musch ◽  
Mark J. Ropeleski ◽  
Eugene B. Chang
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Heat Shock ◽  
Epithelial Cells ◽  
Heat Shock Protein ◽  
Cellular Response ◽  
Intestinal Epithelial Cells ◽  
Dependent Manner ◽  
Intestinal Epithelial ◽  
Heat Induction

Glutamine is considered a nonessential amino acid; however, it becomes conditionally essential during critical illness when consumption exceeds production. Glutamine may modulate the heat shock/stress response, an important adaptive cellular response for survival. Glutamine increases heat induction of heat shock protein (Hsp) 25 in both intestinal epithelial cells (IEC-18) and mesenchymal NIH/3T3 cells, an effect that is neither glucose nor serum dependent. Neither arginine, histidine, proline, leucine, asparagine, nor tyrosine acts as physiological substitutes for glutamine for heat induction of Hsp25. The lack of effect of these amino acids was not caused by deficient transport, although some amino acids, including glutamate (a major direct metabolite of glutamine), were transported poorly by IEC-18 cells. Glutamate uptake could be augmented in a concentration- and time-dependent manner by increasing either media concentration and/or duration of exposure. Under these conditions, glutamate promoted heat induction of Hsp25, albeit not as efficiently as glutamine. Further evidence for the role of glutamine conversion to glutamate was obtained with the glutaminase inhibitor 6-diazo-5-oxo-l-norleucine (DON), which inhibited the effect of glutamine on heat-induced Hsp25. DON inhibited phosphate-dependent glutaminase by 75% after 3 h, decreasing cell glutamate. Increased glutamine/glutamate conversion to glutathione was not involved, since the glutathione synthesis inhibitor, buthionine sulfoximine, did not block glutamine’s effect on heat induction of Hsp25. A large drop in ATP levels did not appear to account for the diminished Hsp25 induction during glutamine deficiency. In summary, glutamine is an important amino acid, and its requirement for heat-induced Hsp25 supports a role for glutamine supplementation to optimize cellular responses to pathophysiological stress.

Amino acid sequence of a chicken heat shock protein derived from the complementary DNA nucleotide sequence

Biochemistry ◽  
1986 ◽  
Vol 25 (20) ◽  
pp. 6244-6251 ◽  
Author(s):  
Markku S. Kulomaa ◽  
Nancy L. Weigel ◽  
Don A. Kleinsek ◽  
Wanda G. Beattie ◽  
Orla M. Conneely ◽  
...  
Keyword(s):  
Amino Acid ◽  
Heat Shock ◽  
Nucleotide Sequence ◽  
Amino Acid Sequence ◽  
Heat Shock Protein ◽  
Complementary Dna ◽  
Dna Nucleotide Sequence
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