Periodic segmental anomalies induced by heat shock in the chick embryo are associated with the cell cycle

Development ◽  
1989 ◽  
Vol 105 (1) ◽  
pp. 119-130 ◽  
Author(s):  
D.R. Primmett ◽  
W.E. Norris ◽  
G.J. Carlson ◽  
R.J. Keynes ◽  
C.D. Stern
Keyword(s):  
Cell Cycle ◽  
Cell Division ◽  
Heat Shock ◽  
Simple Model ◽  
Chick Embryo ◽  
Heat Shock Proteins ◽  
Cell Division Cycle ◽  
The Other ◽  
Chick Embryos ◽  
Shock Proteins

This study provides evidence that cells destined to segment together into somites have a degree of cell division synchrony. We have measured the duration of the cell division cycle in somite and segmental plate cells of the chick embryo as 9.5 h using [3H]thymidine pulse- and-chase. Treatment of embryos with any of a variety of inhibitors known to affect the cell division cycle causes discrete periodic segmental anomalies: these anomalies appear about 6–7 somites after treatment and, in some cases, a second anomaly is observed 6 to 7 somites after the first. Since somites take 1.5 h to form, the 6- to 7- somite interval corresponds to about 9–10 h, which is the duration of the cell cycle as determined in these experiments. The anomalies are similar to those seen after heat shock of 2-day chick embryos. Heat shock and some of the other treatments induce the expression of heat-shock proteins (hsp); however, since neither the expression nor the distribution of these proteins relate to the presence or distribution of anomalies seen, we conclude that hsps are not responsible for the pattern of segmental anomalies observed. The production of periodic segmental anomalies appears to be linked to the cell cycle. A simple model is proposed, in which we suggest that the cell division cycle is involved directly in gating cells that will segment together.

Heat shock proteins and exercise: a primer

2008 ◽  
Vol 33 (5) ◽  
pp. 1050-1075 ◽  
Author(s):  
Earl G. Noble ◽  
Kevin J. Milne ◽  
C.W. James Melling
Keyword(s):  
Skeletal Muscle ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Ion Channel ◽  
The Other ◽  
Cellular Environment ◽  
Shock Proteins ◽  
Fertile Area ◽  
Area Of Study

Heat shock proteins (HSPs) are, in general, prosurvival molecules within the cellular environment, and the overexpression of even just 1 family of HSPs can lead to protection against and improvements after a variety of stressors. Not surprisingly, a fertile area of study has grown out of effors to exploit the innate biologic behaviour of HSPs. Exercise, because of the inherent physiologic stresses associated with it, is but 1 stimulus that can result in a robust increase in various HSPs in several tissues, not the least of which happen to be the heart and skeletal muscle. The purpose of this review is to introduce the reader to the major HSP families, the control of their expression, and some of their biologic functions, specifically with respect to the influence of exercise. Moreover, as the first in a series of reviews from a common symposium, we will briefly introduce the concepts presented by the other authors, which include the effects of different exercise paradigms on skeletal muscle HSPs in the adult and aged systems, HSPs as regulators of inflammation, and the ion channel stabilizing effects of HSPs.

scholarly journals Heat shock proteins IbpA and IbpB are required for NlpI-participated cell division in Escherichia coli

2015 ◽  
Vol 6 ◽  
Author(s):  
Jing Tao ◽  
Yu Sang ◽  
Qihui Teng ◽  
Jinjing Ni ◽  
Yi Yang ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Cell Division ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Shock Proteins

scholarly journals A major collagen-binding protein of chick embryo fibroblasts is a novel heat shock protein.

1986 ◽  
Vol 103 (1) ◽  
pp. 223-229 ◽  
Author(s):  
K Nagata ◽  
S Saga ◽  
K M Yamada
Keyword(s):  
Heat Shock ◽  
Chick Embryo ◽  
Heat Shock Proteins ◽  
Binding Protein ◽  
Stress Protein ◽  
Membrane Glycoprotein ◽  
Two Dimensional Gel Electrophoresis ◽  
Collagen Binding ◽  
Embryo Fibroblasts ◽  
Shock Proteins

Heat shock proteins of chick embryo fibroblasts were analyzed on SDS polyacrylamide gradient gels and were found to include not only three previously well-characterized proteins of 25,000, 73,000, and 89,000 D, but also a 47,000-D protein. Two-dimensional gel electrophoresis revealed that this protein was unusually basic (pI = 9.0) and corresponded to a recently characterized, major gelatin- and collagen-binding protein. The induction of synthesis of this 47,000-D membrane glycoprotein after heat stress of fibroblasts was particularly apparent in preparations isolated by gelatin-affinity chromatography. Regulation of this 47,000-D phosphoprotein was more sensitive than that of three major heat shock proteins in that a substantial stimulation of synthesis occurred at even 42 degrees C, as well as at higher temperature. Phosphorylation of the 47,000-D protein was not altered after heat shock. These studies establish this phosphorylated membrane glycoprotein as a member of the heat shock/stress protein family, and they add collagen binding to the unexpectedly diverse spectrum of biochemical activities induced by exposure of cells to stress.

scholarly journals Sensitivity of the Cell Division Cycle to α-Amanitin In ALLIUM ROOT TIPS

1974 ◽  
Vol 14 (3) ◽  
pp. 461-473
Author(s):  
C. DE LATORRE ◽  
M. E. FERNANDEZ-GOMEZ ◽  
G. GIMENEZ-MARTIN ◽  
A. GONZALEZ-FERNANDEZ
Keyword(s):  
Cell Cycle ◽  
Cell Division ◽  
Normal Structure ◽  
Cell Division Cycle ◽  
The Other ◽  
Root Tips ◽  
Meristematic Cells ◽  
Normal Duration ◽  
S Period ◽  
Nucleolar Rna

The effect of α-amanitin on the cell cycle in Allium cepa meristematic cells was studied: the G1 and G2 periods are prolonged respectively to 1.9 and 1.7 times the normal duration; the S-period is lengthened very little; and the prophase of mitosis is increased to twice the normal duration. It is postulated that real differences in the activity of the non-nucleolar RNA poly-merase might exist in the course of the cell division cycle and that they would account for the higher sensitivities shown by G1, G2 and prophase. On the other hand, the interphase nucleolus responds by segregation in the first few hours of α-amanitin treatment, but recovers its normal structure in continued presence of the drug; and nucleolar reorganization is inhibited in the first few hours in recently formed cells, but the process is subsequently speeded up to attain the same value 4 h after the treatment was begun as in untreated cells.

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.

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