Scutellaria barbata flavonoids improve the composited Aβ-induced abnormal changes of glial cells in rats’ brain

2020 ◽  
Vol 23 ◽  
Author(s):  
Jian-Jun Cheng ◽  
Qing Guo ◽  
Xiao-Guang Wu ◽  
Shuai Ma ◽  
Yang Gao ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Protein Expression ◽  
Mrna Expression ◽  
Glial Cells ◽  
Model Group ◽  
Hsp70 Protein ◽  
Shock Proteins ◽  
Apoe Mrna ◽  
The Brain

Aim: It has been reported that glial cells are involved in Alzheimer’s disease (AD). According to our previous research, Scutellaria barbata flavonoids (SBFs) can protect the neuronal disorder and memory impairment for AD-like rats, while the effect of SBFs on the glial cells disorder in AD-like rats has been less well studied. The effects of SBFs on astrocytes(ASs), microglial cells (MGs) and oligodendrocytes (Ols), as well as heat shock proteins 70 (Hsp70) and apolipoprotein E (ApoE) were investigated in the present study. Methods: The successful model rats, screened by Morris water maze, were daily orally administrated with 35, 70 and 140 mg/kg SBFs for 36 d. The numbers of brain’s astrocytes (ASs), microglial cells (MGs) and oligodendrocytes (Ols) were examined by immunohistochemistry. The cortical glial fibrillary acidic protein (GFAP), leukocyte common antigen (LCA) (CD45), Claudin 11 and heat shock proteins 70 (Hsp70) protein expression were assayed by Western blotting, and apolipoprotein E (ApoE) mRNA expression was analyzed by real-time quantitative polymerase chain reaction (qPCR). Results: Compared with the sham-operated group, the numbers of ASs and MGs in the brain were significantly increased in the model group (P<0.05, P<0.01), and accompanied with increases of GFAP, CD45 and Hsp70 protein and ApoE mRNA expression (P<0.05, P<0.01). Both Ols number and Claudin 11 protein expression decreased in the brain in the model group (P<0.05, P<<.01). However, the above abnormal changes induced by composited Aβ were differently reversed by treatment of SBFs at three doses of 35, 70 and 140 mg/kg (P<0.05, P<0.01). Conclusions: SBFs can dramatically improve the abnormal changes of glial cells in rats’ brain induced by composited Aβ, which may be a helpful treatment of neurodegenerative diseases.

Resistance to Bortezomib Develops Slowly in MCL Cells, Extends to the Class of Proteasome Inhibitors, and Is Associated with Decreased Proliferation of the Resistant Cells.

Blood ◽  
2006 ◽  
Vol 108 (11) ◽  
pp. 4397-4397 ◽  
Author(s):  
Helena Mora-Jensen ◽  
Edgar G. Rizzatti ◽  
Adrian Wiestner
Keyword(s):  
Cell Cycle ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Protein Expression ◽  
Cell Cycle Control ◽  
Proteasome Inhibitors ◽  
D1 Protein ◽  
Hsp70 Protein ◽  
Cyclin D1 Protein ◽  
Shock Proteins

Abstract Mantle Cell Lymphoma (MCL) is a malignancy of mature B-cells. MCL has a poor prognosis and a limited response to traditional chemotherapy. Bortezomib (BZM), a new powerful inhibitor of the proteasome, can induce responses in up to 50% of relapsed MCL patients, suggesting that in at least half of the patients the lymphoma cells are intrinsically resistant to BZM or rapidly develop resistance during single agent therapy. To investigate possible mechanisms of BZM resistance, we cultured MCL cell lines continuously in sub-lethal concentrations of BZM that were then gradually increased. Resistance was slow to develop taking several months for truly resistant clones to grow out. We generated a bortezomib resistant (BR) clone of HBL-2 with an IC50 of 30nM compared to 5nM in the parental clone and several BR subclones of Jeko-1, the most resistant of which had an IC50 of 200nM compared to 3nM for the parental clone. All BR subclones also showed decreased sensitivity to three other proteasome inhibitors: MG-132, Lactacystin, and NLVS. The increase in IC50 to these drugs was between 3 and 8-fold, consistent with more off-target effects of these drugs compared to BZM. BAY11-7082, an inhibitor of NF-kB signaling, maintained its activity against the resistant cells. Resistance to BZM, once acquired, has remained stable over several months. This is remarkable because the resistant subclones grow significantly slower than the parental lines, even after having been removed from selection for extended periods of time. Consistent with slower cell proliferation, we found reduced Cyclin D1 protein expression in the BZM resistant Jeko clones; however, mRNA levels were comparable to the parental line, indicating that changes in Cyclin D1 protein translation and/or stability may be responsible for the decreased proliferation. BZM resistance has been associated with up-regulation of proteasome components and heat-shock proteins. Indeed, in the resistant HBL-2 subclone we found marked upregulation of two proteasome components (PSMA5 and PSMC1) and of Hsp70 by RT-PCR, but there was only a small change in Hsp70 protein expression. Nevertheless, upregulation of these genes could be part a more global gene expression response as seen with ER-stress and could thus reflect an adaptive change to BZM in the HBL-2 BR subclone. All three Jeko BR clones in contradistinction showed only minor changes in PSMA5, PSMC1 and Hsp70 mRNA expression and surprisingly had markedly reduced Hsp70 protein levels. Thus, in these subclones, BR resistance appears to correlate primarily with changes affecting cell cycle control. We conclude that resistance to BZM may be determined by several mechanisms that affect cell cycle control as well as expression of proteasome components and heat-shock proteins. While the slow development of resistance suggests adaptive changes, its persistence over time is more consistent with mutations or other genomic alterations that are not readily reversible. Ongoing studies aim to more precisely define the basis for BZM resistance in MCL.

scholarly journals Regional differences in colonic mucosa-associated microbiota determine the physiological expression of host heat shock proteins

2010 ◽  
Vol 299 (6) ◽  
pp. G1266-G1275 ◽  
Author(s):  
Shien Hu ◽  
Yunwei Wang ◽  
Lev Lichtenstein ◽  
Yun Tao ◽  
Mark W. Musch ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Protein Expression ◽  
Distal Colon ◽  
Proximal Colon ◽  
Intestinal Homeostasis ◽  
Hsp70 Mrna ◽  
Hsp70 Protein ◽  
Longitudinal Length ◽  
Shock Proteins

Cytoprotective heat shock proteins (Hsps) are critical for intestinal homeostasis and are known to be decreased in inflammatory bowel diseases. Signals responsible for maintenance of Hsp expression are incompletely understood. In this study, we find that Hsp25/27 and Hsp70 protein expressions are differentially regulated along the longitudinal length of the large intestine, being highest in the proximal colon and decreasing to the distal colon. This longitudinal gradient was similar in both conventionally colonized mouse colon as well as biopsies of human proximal and distal colon but was abolished in the colon of germ-free mice, suggesting a role of intestinal microbiota in the Hsp regional expression. Correspondingly, analysis of 16S ribosomal RNA genes of bacteria from each colonic segment indicated increased bacterial richness and diversity in the proximal colon. The mechanism of regulation is transcriptional, as Hsp70 mRNA followed a similar pattern to Hsp70 protein expression. Lysates of mucosa-associated bacteria from the proximal colon stimulated greater Hsp25 and Hsp70 mRNA transcription and subsequent protein expression in intestinal epithelial cells than did lysates from distal colon. In addition, transrectal administration of cecal contents stimulated Hsp25 and Hsp70 expression in the distal colon. Thus host-microbial interactions resulting in differential Hsp expression may have significant implications for the maintenance of intestinal homeostasis and possibly for development of inflammatory diseases of the bowel.

Effect of Exposure to 1,800 MHz Electromagnetic Fields on Heat Shock Proteins and Glial Cells in the Brain of Developing Rats

2010 ◽  
Vol 20 (2) ◽  
pp. 109-119 ◽  
Author(s):  
Aurélie Watilliaux ◽  
Jean-Marc Edeline ◽  
Philippe Lévêque ◽  
Thérèse M. Jay ◽  
Michel Mallat
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Electromagnetic Fields ◽  
Glial Cells ◽  
Shock Proteins ◽  
The Brain

Differential expression of heat shock proteins by human glial cells

1992 ◽  
Vol 41 (2) ◽  
pp. 231-238 ◽  
Author(s):  
Mark S. Freedman ◽  
Natalie N. Buu ◽  
Theodora C.J. Ruijs ◽  
Kenneth Williams ◽  
Jack P. Antel
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Differential Expression ◽  
Glial Cells ◽  
Shock Proteins

Differential expression of small heat shock proteins in the brain of broiler embryo; the effects of embryonic thermal manipulation

2020 ◽  
Vol 93 ◽  
pp. 102719 ◽  
Author(s):  
Mehdi Basaki ◽  
Nazila Sahraiy ◽  
Kamran Keykavusi ◽  
Ghasem Akbari ◽  
Amir Ali Shahbazfar ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Differential Expression ◽  
Small Heat Shock Proteins ◽  
Shock Proteins ◽  
The Brain ◽  
Thermal Manipulation

Study of Cell-Lipid Film Interaction by Measuring Heat Shock Proteins mRNA Expression

2000 ◽  
Vol 15 (6) ◽  
pp. 478-488 ◽  
Author(s):  
AKIO KISHIDA ◽  
TAKAHISA MATSUYAMA ◽  
MIHOKO NAKASHIMA ◽  
TAKESHI SERIZAWA ◽  
MITSURU AKASHI ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Mrna Expression ◽  
Lipid Film ◽  
Cell Lipid ◽  
Shock Proteins

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.

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