Formation of cytoplasmic heat shock granules in tomato cell cultures and leaves

1983 ◽  
Vol 3 (9) ◽  
pp. 1648-1655
Author(s):  
L Nover ◽  
K D Scharf ◽  
D Neumann
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Cell Cultures ◽  
Structural Proteins ◽  
Lycopersicon Peruvianum ◽  
Electron Microscopic ◽  
Considerable Part ◽  
Heat Shock Granules ◽  
Simultaneous Synthesis ◽  
Shock Proteins

Biochemical and electron microscopic analyses of heat-shocked suspension cultures of Peruvian tomato (Lycopersicon peruvianum) revealed that a considerable part of the dominant small heat shock proteins (hsps) with an Mr of approximately 17,000 are structural proteins of newly forming granular aggregates in the cytoplasm (heat shock granules), whose formation strictly depends on heat shock conditions (37 to 40 degrees C) and the presence or simultaneous synthesis of hsps. However, under certain conditions, e.g., in preinduced cultures maintained at 25 degrees C, hsps also accumulate as soluble proteins without concomitant assembly of heat shock granules. Similar heat shock-induced cytoplasmic aggregates were also observed in other cell cultures and heat-shocked tomato leaves and corn coleoptiles.

scholarly journals Formation of cytoplasmic heat shock granules in tomato cell cultures and leaves.

1983 ◽  
Vol 3 (9) ◽  
pp. 1648-1655 ◽  
Author(s):  
L Nover ◽  
K D Scharf ◽  
D Neumann
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Cell Cultures ◽  
Structural Proteins ◽  
Lycopersicon Peruvianum ◽  
Electron Microscopic ◽  
Considerable Part ◽  
Heat Shock Granules ◽  
Simultaneous Synthesis ◽  
Shock Proteins

Biochemical and electron microscopic analyses of heat-shocked suspension cultures of Peruvian tomato (Lycopersicon peruvianum) revealed that a considerable part of the dominant small heat shock proteins (hsps) with an Mr of approximately 17,000 are structural proteins of newly forming granular aggregates in the cytoplasm (heat shock granules), whose formation strictly depends on heat shock conditions (37 to 40 degrees C) and the presence or simultaneous synthesis of hsps. However, under certain conditions, e.g., in preinduced cultures maintained at 25 degrees C, hsps also accumulate as soluble proteins without concomitant assembly of heat shock granules. Similar heat shock-induced cytoplasmic aggregates were also observed in other cell cultures and heat-shocked tomato leaves and corn coleoptiles.

scholarly journals Cytoplasmic heat shock granules are formed from precursor particles and are associated with a specific set of mRNAs.

1989 ◽  
Vol 9 (3) ◽  
pp. 1298-1308 ◽  
Author(s):  
L Nover ◽  
K D Scharf ◽  
D Neumann
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Cell Cultures ◽  
Animal Cells ◽  
Reversible Aggregation ◽  
Specific Subset ◽  
Messenger Ribonucleoprotein ◽  
Cscl Gradient ◽  
Heat Shock Granules ◽  
Shock Proteins

In heat-shocked tomato cell cultures, cytoplasmic heat shock granules (HSGs) are tightly associated with a specific subset of mRNAs coding mainly for the untranslated control proteins. This messenger ribonucleoprotein complex was banded in a CsCl gradient after fixation with formaldehyde (approximately 1.30 g/cm3). It contains all the heat shock proteins and most of the RNA applied to the gradient. During heat shock, a reversible aggregation of HSGs from 15S precursor particles can be shown. These pre-HSGs are not identical to the 19S plant prosomes. Ultrastructural analysis supports the ribonucleoprotein nature of HSGs and their composition of approximately 10-nm precursor particles. A model summarizes our results. It gives a reasonable explanation for the striking conservation of untranslated mRNAs during heat shock and may apply also to animal cells.

Cytoplasmic heat shock granules are formed from precursor particles and are associated with a specific set of mRNAs

1989 ◽  
Vol 9 (3) ◽  
pp. 1298-1308
Author(s):  
L Nover ◽  
K D Scharf ◽  
D Neumann
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Cell Cultures ◽  
Animal Cells ◽  
Reversible Aggregation ◽  
Specific Subset ◽  
Messenger Ribonucleoprotein ◽  
Cscl Gradient ◽  
Heat Shock Granules ◽  
Shock Proteins

In heat-shocked tomato cell cultures, cytoplasmic heat shock granules (HSGs) are tightly associated with a specific subset of mRNAs coding mainly for the untranslated control proteins. This messenger ribonucleoprotein complex was banded in a CsCl gradient after fixation with formaldehyde (approximately 1.30 g/cm3). It contains all the heat shock proteins and most of the RNA applied to the gradient. During heat shock, a reversible aggregation of HSGs from 15S precursor particles can be shown. These pre-HSGs are not identical to the 19S plant prosomes. Ultrastructural analysis supports the ribonucleoprotein nature of HSGs and their composition of approximately 10-nm precursor particles. A model summarizes our results. It gives a reasonable explanation for the striking conservation of untranslated mRNAs during heat shock and may apply also to animal cells.

Acidic extracellular environment induces only a subset of heat-shock proteins in primary mouse kidney cell cultures

1990 ◽  
Vol 68 (4) ◽  
pp. 804-807 ◽  
Author(s):  
Edward W. Khandjian
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Cell Cultures ◽  
Kidney Cell ◽  
Acidic Medium ◽  
Stress Proteins ◽  
Cdna Probe ◽  
Mouse Kidney ◽  
Primary Mouse ◽  
Shock Proteins

Exposure of primary mouse kidney cell cultures to acidic medium (pH 5.5) induced the expression of a 70 kilodalton (kDa) protein. This protein was identified as the major inducible heat-shock protein 70 (hsp70) by immunoprecipitation with anti-hsp70 serum and Northern blot analysis with a hsp70 cDNA probe. Maximum induction of the 70-kDa protein at pH 5.5 after 240 min was about 30% of that observed after 60 min of thermal treatment at 43 °C. In addition, there was an apparent induction of the glucose-regulated proteins (GRPs) of 76–78 and 98–100 kDa, but not of the other hsps. This subset induction of the heat-shock response by acidic medium suggests that different mechanisms are responsible for the induction of the various families of hsps.Key words: heat-shock proteins, stress proteins, acidic induction, viral infection, mouse kidney cells.

Secreted heat shock proteins in sunflower suspension cell cultures

1997 ◽  
Vol 16 (11) ◽  
pp. 792-796 ◽  
Author(s):  
G. Mita ◽  
G. Nocco ◽  
C. Leuci ◽  
V. Greco ◽  
P. Rampino ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Cell Cultures ◽  
Suspension Cell ◽  
Suspension Cell Cultures ◽  
Shock Proteins

146 SPERM STORAGE: EXPRESSION OF PROGESTERONE RECEPTORS, STRUCTURAL PROTEINS, AND HEAT SHOCK PROTEINS IN THE AVIAN OVIDUCT

2016 ◽  
Vol 28 (2) ◽  
pp. 203 ◽  
Author(s):  
C. Riou ◽  
M. Saint-Dizier ◽  
N. Gerard
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Detection System ◽  
Geometric Mean ◽  
Sperm Storage ◽  
Structural Proteins ◽  
Long Period ◽  
Relative Standard ◽  
Significant Difference ◽  
Shock Proteins

In avian species, sperm is stored for a long period in sperm storage tubules (SST) located in the utero-vaginal junction. It has been shown that progesterone (P4) regulates the release of sperm from SST for fertilization [Ito et al. 2011 Endocrinology 152, 3952–3621] in quails. In the same context, heat shock proteins (HSP) such as the HSP70 family activate sperm motility in quails [Hiyama et al. 2013 Reproduction 147, 167–178] and may participate in sperm release. In addition, we can hypothesise that at least some structural proteins from SST cells could play a role during sperm storage and release by interacting with sperm. Our objective was to study the potential effect of P4, HSP, and structural proteins on sperm storage potential, by analysing the expression of P4 receptors (PR and mPRα), HSPA8 and HSPB1, CNN1, TAGLN and DES genes in the avian genital tract. Uterus, vagina, and utero-vaginal junctions were collected from 2 divergent lines of hens. One lines displays a long period of sperm storage (21 days, line F+, n = 5), whereas the second displays a shorter period of sperm storage (10 days, line F–, n = 6). Total RNA was extracted and reverse transcribed, and then mRNA coding for PR, mPRα, HSPA8, HSPB1, CNN1, TAGLN and DES were assessed by qPCR (CFX96 Touch Real-Time PCR Detection System, Bio-Rad Laboratories, Hercules, CA, USA). Quantification was performed by using the relative standard curve method. Results were normalized by the geometric mean value of 2 reference genes, GAPDH and S17. Relative amounts of mRNA in each tissue were compared between lines by a Mann-Whitney test. Differences were considered significant when P < 0.05. No significant difference was observed between lines for both P4 receptors, as well as for HSPA8, regardless of the tissue. Expression of CNN1, TAGLN, and DES was significantly higher in the utero-vaginal junction of line F– than line F+ (P < 0.01). Expression of HSPB1 was significantly higher in utero-vaginal junction of line F– than of line F+ (P < 0.05). In conclusion, our data suggest that HSPB1 and structural proteins CNN1, TAGLN, and DES are involved in the regulation of sperm storage in the utero-vaginal junction in hens.

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