scholarly journals Polyamines mediate glutamine-dependent induction of the intestinal epithelial heat shock response

2011 ◽  
Vol 301 (1) ◽  
pp. G181-G187 ◽  
Author(s):  
Yuji Iwashita ◽  
Toshio Sakiyama ◽  
Mark W. Musch ◽  
Mark J. Ropeleski ◽  
Hirohito Tsubouchi ◽  
...  
Keyword(s):  
Heat Stress ◽  
Heat Shock ◽  
Epithelial Cells ◽  
Heat Shock Response ◽  
Intestinal Epithelial Cells ◽  
Critical Role ◽  
Intestinal Epithelial ◽  
Stress Induction ◽  
Polyamine Synthesis ◽  
Shock Response

Heat shock proteins (Hsps) are highly conserved proteins that play a role in cytoprotection and maintaining intestinal homeostasis. Glutamine is essential for the optimal induction of intestinal epithelial Hsp expression, but its mechanisms of action are incompletely understood. Glutamine is a substrate for polyamine synthesis and stimulates the activity of ornithine decarboxylase (ODC), a key enzyme for polyamine synthesis, in intestinal epithelial cells. Thus we investigated whether polyamines (putrescine, spermidine, or spermine) and their precursor ornithine mediate the induction of Hsp expression in IEC-18 rat intestinal epithelial cells. As previously observed, glutamine was required for heat stress induction of Hsp70 and Hsp25, although it had little effect under basal conditions. Under conditions of glutamine depletion, supplementation of ornithine or polyamines restored the heat-induced expression of Hsp70 and Hsp25. When ODC was inhibited by α-difluoromethylornithine (DFMO), an irreversible ODC inhibitor, the heat stress induction of Hsp70 and Hsp25 was decreased significantly, even in the presence of glutamine. Ornithine, polyamines, and DFMO did not modify the nuclear localization of heat shock transcription factor 1 (HSF-1). However, DFMO dramatically reduced glutamine-dependent HSF-1 binding to an oligonucleotide with heat shock elements (HSE), which was increased by glutamine. In addition, exogenous polyamines recovered the DNA-binding activity. These results indicate that polyamines play a critical role in the glutamine-dependent induction of the intestinal epithelial heat shock response through facilitation of HSF-1 binding to HSE.

Interleukin-6 Production in Human Intestinal Epithelial Cells Increases in Association with the Heat Shock Response

1998 ◽  
Vol 77 (1) ◽  
pp. 40-44 ◽  
Author(s):  
Alexander A. Parikh ◽  
M.Ryan Moon ◽  
Christine D. Kane ◽  
Andrew L. Salzman ◽  
Josef E. Fischer ◽  
...  
Keyword(s):  
Heat Shock ◽  
Epithelial Cells ◽  
Heat Shock Response ◽  
Interleukin 6 ◽  
Intestinal Epithelial Cells ◽  
Intestinal Epithelial ◽  
Human Intestinal Epithelial Cells ◽  
Shock Response

scholarly journals Molecular Basis of the Defective Heat Stress Response in Mycobacterium leprae

2007 ◽  
Vol 189 (24) ◽  
pp. 8818-8827 ◽  
Author(s):  
Diana L. Williams ◽  
Tana L. Pittman ◽  
Mike Deshotel ◽  
Sandra Oby-Robinson ◽  
Issar Smith ◽  
...  
Keyword(s):  
Heat Stress ◽  
Stress Response ◽  
Heat Shock ◽  
Heat Shock Response ◽  
Elevated Temperatures ◽  
Transcriptional Response ◽  
Mycobacterium Leprae ◽  
Heat Stress Response ◽  
Regulatory Circuits ◽  
Shock Response

ABSTRACT Mycobacterium leprae, a major human pathogen, grows poorly at 37°C. The basis for its inability to survive at elevated temperatures was investigated. We determined that M. leprae lacks a protective heat shock response as a result of the lack of transcriptional induction of the alternative sigma factor genes sigE and sigB and the major heat shock operons, HSP70 and HSP60, even though heat shock promoters and regulatory circuits for these genes appear to be intact. M. leprae sigE was found to be capable of complementing the defective heat shock response of mycobacterial sigE knockout mutants only in the presence of a functional mycobacterial sigH, which orchestrates the mycobacterial heat shock response. Since the sigH of M. leprae is a pseudogene, these data support the conclusion that a key aspect of the defective heat shock response in M. leprae is the absence of a functional sigH. In addition, 68% of the genes induced during heat shock in M. tuberculosis were shown to be either absent from the M. leprae genome or were present as pseudogenes. Among these is the hsp/acr2 gene, whose product is essential for M. tuberculosis survival during heat shock. Taken together, these results suggest that the reduced ability of M. leprae to survive at elevated temperatures results from the lack of a functional transcriptional response to heat shock and the absence of a full repertoire of heat stress response genes, including sigH.

Sub-lethal heat stress causes apoptosis in an Antarctic fish that lacks an inducible heat shock response

2014 ◽  
Vol 44 ◽  
pp. 119-125 ◽  
Author(s):  
Isaac M. Sleadd ◽  
Marissa Lee ◽  
Daniel O. Hassumani ◽  
Tonya M.A. Stecyk ◽  
Otto K. Zeitz ◽  
...  
Keyword(s):  
Heat Stress ◽  
Heat Shock ◽  
Heat Shock Response ◽  
Antarctic Fish ◽  
Shock Response

Soluble factors fromLactobacillus GGactivate MAPKs and induce cytoprotective heat shock proteins in intestinal epithelial cells

2006 ◽  
Vol 290 (4) ◽  
pp. C1018-C1030 ◽  
Author(s):  
Yun Tao ◽  
Kenneth A. Drabik ◽  
Tonya S. Waypa ◽  
Mark W. Musch ◽  
John C. Alverdy ◽  
...  
Keyword(s):  
Signal Transduction ◽  
Heat Shock ◽  
Epithelial Cells ◽  
Map Kinases ◽  
Intestinal Epithelial Cells ◽  
Oxidant Stress ◽  
Signal Transduction Pathways ◽  
Clinical Effects ◽  
Dependent Manner ◽  
Intestinal Epithelial

Conditioned media from the probiotic Lactobacillus GG (LGG-CM) induce heat shock protein (Hsp) expression in intestinal epithelial cells. LGG-CM induces both Hsp25 and Hsp72 in a time- and concentration-dependent manner. These effects are mediated by a low-molecular-weight peptide that is acid and heat stable. DNA microarray experiments demonstrate that Hsp72 is one of the most highly upregulated genes in response to LGG-CM treatment. Real-time PCR and electrophoretic mobility shift assay confirm that regulation of Hsp induction is at least in part transcriptional in nature, involving heat shock factor-1. Although Hsps are not induced for hours after exposure, transient exposure to LGG-CM is sufficient to initiate the signal for Hsp induction, suggesting that signal transduction pathways may be involved. Experiments confirm that LGG-CM modulates the activity of certain signaling pathways in intestinal epithelial cells by activating MAP kinases. Inhibitors of p38 and JNK block the expression of Hsp72 normally induced by LGG-CM. Functional studies indicate that LGG-CM treatment of gut epithelial cells protects them from oxidant stress, perhaps by preserving cytoskeletal integrity. By inducing the expression of cytoprotective Hsps in gut epithelial cells, and by activating signal transduction pathways, the peptide product(s) secreted by LGG may contribute to the beneficial clinical effects attributed to this probiotic.

TRPC1 functions as a store-operated Ca2+ channel in intestinal epithelial cells and regulates early mucosal restitution after wounding

2006 ◽  
Vol 290 (4) ◽  
pp. G782-G792 ◽  
Author(s):  
Jaladanki N. Rao ◽  
Oleksandr Platoshyn ◽  
Vera A. Golovina ◽  
Lan Liu ◽  
Tongtong Zou ◽  
...  
Keyword(s):  
Cell Migration ◽  
Epithelial Cells ◽  
Transient Receptor Potential ◽  
Intestinal Epithelial Cells ◽  
Critical Role ◽  
Receptor Potential ◽  
Mucosal Injury ◽  
Intestinal Epithelial ◽  
Epithelial Restitution ◽  
Transient Receptor

An increase in cytosolic free Ca2+ concentration ([Ca2+]cyt) results from Ca2+ release from intracellular stores and extracellular Ca2+ influx through Ca2+-permeable ion channels and is crucial for initiating intestinal epithelial restitution to reseal superficial wounds after mucosal injury. Capacitative Ca2+ entry (CCE) induced by Ca2+ store depletion represents a major Ca2+ influx mechanism, but the exact molecular components constituting this process remain elusive. This study determined whether canonical transient receptor potential (TRPC)1 served as a candidate protein for Ca2+-permeable channels mediating CCE in intestinal epithelial cells and played an important role in early epithelial restitution. Normal intestinal epithelial cells (the IEC-6 cell line) expressed TRPC1 and TPRC5 and displayed typical records of whole cell store-operated Ca2+ currents and CCE generated by Ca2+ influx after depletion of intracellular stores. Induced TRPC1 expression by stable transfection with the TRPC1 gene increased CCE and enhanced cell migration during restitution. Differentiated IEC-Cdx2L1 cells induced by forced expression of the Cdx2 gene highly expressed endogenous TRPC1 and TRPC5 and exhibited increased CCE and cell migration. Inhibition of TRPC1 expression by small interfering RNA specially targeting TRPC1 not only reduced CCE but also inhibited cell migration after wounding. These findings strongly suggest that TRPC1 functions as store-operated Ca2+ channels and plays a critical role in intestinal epithelial restitution by regulating CCE and intracellular [Ca2+]cyt.

scholarly journals Intestinal heat shock protein 110 regulates expression of CD1d on intestinal epithelial cells

2003 ◽  
Vol 112 (5) ◽  
pp. 745-754 ◽  
Author(s):  
Sean P. Colgan ◽  
Richard S. Pitman ◽  
Takashi Nagaishi ◽  
Atsushi Mizoguchi ◽  
Emiko Mizoguchi ◽  
...  
Keyword(s):  
Heat Shock ◽  
Epithelial Cells ◽  
Heat Shock Protein ◽  
Intestinal Epithelial Cells ◽  
Intestinal Epithelial
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