Expression and Function of Stress (Heat Shock) Proteins in Digestive Organs

Heat shock proteins (Hsps) form a large family of evolutionarily conserved molecular chaperones that help balance protein folding and protect cells from various stress conditions. However, there is growing evidence that Hsps may also play an active role in developmental processes. Here, we take the example of developmental expression and function of one class of Hsps characterized by low molecular weight, the small Hsps (sHsps). We discuss recent reports and genome-wide datasets that support vital sHsps functions in the developing nervous system, reproductive system, and muscles. This tissue- and time-specific sHsp expression is developmentally regulated, so that the enhancer sequence of an sHsp gene expressed in developing muscle, in addition to stress-inducible elements, also carries binding sites for myogenic regulatory factors. One possible reason for sHsp genes to switch on during development and in non-stress conditions is to protect vital developing organs from environmental insults.

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Heat Shock Proteins: Pathogenic Role in Atherosclerosis and Potential Therapeutic Implications

Autoimmune Diseases ◽

10.1155/2012/502813 ◽

2012 ◽

Vol 2012 ◽

pp. 1-9 ◽

Cited By ~ 4

Author(s):

Arman Kilic ◽

Kaushik Mandal

Keyword(s):

Heat Shock ◽

Heat Shock Proteins ◽

Vascular Endothelial Cell ◽

Vascular Wall ◽

Protective Role ◽

Therapeutic Implications ◽

Endothelial Cell Surface ◽

Disease States ◽

Shock Proteins ◽

And Function

Heat shock proteins (HSPs) are a highly conserved group of proteins that are constitutively expressed and function as molecular chaperones, aiding in protein folding and preventing the accumulation of misfolded proteins. In the arterial wall, HSPs have a protective role under normal physiologic conditions. In disease states, however, HSPs expressed on the vascular endothelial cell surface can act as targets for detrimental autoimmunity due to their highly conserved sequences. Developing therapeutic strategies for atherosclerosis based on HSPs is challenged by the need to balance such physiologic and pathologic roles of these proteins. This paper summarizes the role of HSPs in normal vascular wall processes as well as in the development and progression of atherosclerosis. The potential implications of HSPs in clinical therapies for atherosclerosis are also discussed.

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Structure and Function of Small Heat Shock Proteins from the Magnetotactic Bacterium Magnetospirillum magneticum AMB-1

KOBUNSHI RONBUNSHU ◽

10.1295/koron.67.698 ◽

2010 ◽

Vol 67 (12) ◽

pp. 698-704 ◽

Cited By ~ 1

Author(s):

Tetsuya ABE ◽

Shinpei ITO ◽

Naoya NISHI ◽

Yoshihiro TSUKADA ◽

Takuo YASUNAGA ◽

...

Keyword(s):

Heat Shock ◽

Heat Shock Proteins ◽

Small Heat Shock Proteins ◽

Structure And Function ◽

Magnetotactic Bacterium ◽

Shock Proteins ◽

And Function ◽

Magnetospirillum Magneticum

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Evolution, structure and function of the small heat shock proteins in plants

Journal of Experimental Botany ◽

10.1093/jxb/47.3.325 ◽

1996 ◽

Vol 47 (3) ◽

pp. 325-338 ◽

Cited By ~ 406

Author(s):

Elizabeth R. Waters ◽

Garrett J. Lee ◽

Elizabeth Vierling

Keyword(s):

Heat Shock ◽

Heat Shock Proteins ◽

Small Heat Shock Proteins ◽

Structure And Function ◽

Shock Proteins ◽

And Function

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Some like it hot: the structure and function of small heat-shock proteins

Nature Structural & Molecular Biology ◽

10.1038/nsmb993 ◽

2005 ◽

Vol 12 (10) ◽

pp. 842-846 ◽

Cited By ~ 556

Author(s):

Martin Haslbeck ◽

Titus Franzmann ◽

Daniel Weinfurtner ◽

Johannes Buchner

Keyword(s):

Heat Shock ◽

Heat Shock Proteins ◽

Small Heat Shock Proteins ◽

Structure And Function ◽

Shock Proteins ◽

And Function

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Contribution of small heat shock proteins to muscle development and function

FEBS Letters ◽

10.1016/j.febslet.2014.01.005 ◽

2014 ◽

Vol 588 (4) ◽

pp. 517-530 ◽

Cited By ~ 31

Author(s):

Magda Dubińska-Magiera ◽

Jadwiga Jabłońska ◽

Jolanta Saczko ◽

Julita Kulbacka ◽

Teresa Jagla ◽

...

Keyword(s):

Heat Shock ◽

Heat Shock Proteins ◽

Muscle Development ◽

Small Heat Shock Proteins ◽

Shock Proteins ◽

And Function

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Innate Immune-Related Receptors in Normal and Psoriatic Skin

Archives of Pathology & Laboratory Medicine ◽

10.5858/2003-127-178-iirrin ◽

2003 ◽

Vol 127 (2) ◽

pp. 178-186 ◽

Cited By ~ 1

Author(s):

Jonathan L. Curry ◽

Jian-Zhong Qin ◽

Brian Bonish ◽

Ryan Carrick ◽

Patricia Bacon ◽

...

Keyword(s):

Dendritic Cells ◽

Heat Shock ◽

Heat Shock Proteins ◽

Normal Skin ◽

Innate Immune ◽

Receptor Expression ◽

Interleukin 12 ◽

Psoriatic Skin ◽

Shock Proteins ◽

And Function

Abstract Context.—A precise role for the innate immune system in psoriasis remains to be determined. Surface receptors, including Toll-like receptors (TLRs) that recognize bacterial ligands and CD91, which recognizes heat shock proteins (HSPs), are implicated in both innate and adaptive immunity. Objective.—Since skin is exposed to various exogenous stimuli, which can provoke or exacerbate psoriasis, we characterized expression and function of TLRs, CD91, and HSPs in normal and psoriatic skin. Design.—A variety of skin-derived cells and blood-derived cells were analyzed both in vivo and in vitro; samples were obtained from 24 different individuals for innate immune-related receptor expression and function. By comparing and contrasting individuals with healthy skin and psoriatic patients, several specific differences were identified. Results.—Immunohistochemistry-based expression profiling revealed TLR1 expression in epidermal dendritic cells (DCs) and dermal dendritic cells (DDCs) in normal skin, as well as in pre-psoriatic skin and psoriatic plaques, with enhanced basal layer keratinocyte (KC) expression in pre-psoriatic and psoriatic plaques compared with normal skin; TLR2 expression primarily by DDCs; and TLR4 expression by epidermal DCs and DDCs, with mid-epidermal-layer KCs displaying cell surface staining. No TLR9 or CD14 was detected on DCs or KCs, although psoriatic plaques contained CD14-positive macrophages. Analysis of psoriatic epidermis revealed HSPs 27, 60, and 70. Keratinocytes were CD91 negative, but CD91 was expressed by fibroblasts and DDCs in normal and pre-psoriatic skin, with prominent accumulation of CD91-positive DDCs in psoriatic plaques. Cultured KCs revealed no surface expression of TLR2, TLR4, TLR9, or CD91. Exposure of fibroblasts, but not KCs, to lipopolysaccharide or HSPs triggered nuclear factor (NF)-κB activation. Heat shock proteins did induce maturation of blood-derived DCs accompanied by increased interleukin-12 production and enhanced antigen-presenting function. Conclusions.—These data demonstrate distinctive patterns of innate immune-related receptors by specific subsets of cells in normal and psoriatic skin, suggesting functional roles for HSPs and DCs in psoriasis.

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Differential induction and function of heat shock proteins in rat gastric mucosa regulated by neuropeptides

Gastroenterology ◽

10.1016/s0016-5085(98)81018-4 ◽

1998 ◽

Vol 114 ◽

pp. A250

Author(s):

M. Otaka ◽

M. Jin ◽

S. Itoh ◽

A. Iwabuchi ◽

H. Sasahara ◽

...

Keyword(s):

Heat Shock ◽

Gastric Mucosa ◽

Heat Shock Proteins ◽

Rat Gastric Mucosa ◽

Differential Induction ◽

Shock Proteins ◽

And Function

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α-Crystallin-Type Heat Shock Proteins: Socializing Minichaperones in the Context of a Multichaperone Network

Microbiology and Molecular Biology Reviews ◽

10.1128/mmbr.66.1.64-93.2002 ◽

2002 ◽

Vol 66 (1) ◽

pp. 64-93 ◽

Cited By ~ 379

Author(s):

Franz Narberhaus

Keyword(s):

Heat Shock ◽

Heat Shock Proteins ◽

Protein Quality ◽

Chaperone Activity ◽

Close Cooperation ◽

Irreversible Aggregation ◽

Functional Features ◽

Shock Proteins ◽

And Function ◽

Temperature Upshift

SUMMARY α-Crystallins were originally recognized as proteins contributing to the transparency of the mammalian eye lens. Subsequently, they have been found in many, but not all, members of the Archaea, Bacteria, and Eucarya. Most members of the diverse α-crystallin family have four common structural and functional features: (i) a small monomeric molecular mass between 12 and 43 kDa; (ii) the formation of large oligomeric complexes; (iii) the presence of a moderately conserved central region, the so-called α-crystallin domain; and (iv) molecular chaperone activity. Since α-crystallins are induced by a temperature upshift in many organisms, they are often referred to as small heat shock proteins (sHsps) or, more accurately, α-Hsps. α-Crystallins are integrated into a highly flexible and synergistic multichaperone network evolved to secure protein quality control in the cell. Their chaperone activity is limited to the binding of unfolding intermediates in order to protect them from irreversible aggregation. Productive release and refolding of captured proteins into the native state requires close cooperation with other cellular chaperones. In addition, α-Hsps seem to play an important role in membrane stabilization. The review compiles information on the abundance, sequence conservation, regulation, structure, and function of α-Hsps with an emphasis on the microbial members of this chaperone family.

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