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

scholarly journals Synthesis, modification and structural binding of heat-shock proteins in tomato cell cultures

1984 ◽  
Vol 139 (2) ◽  
pp. 303-313 ◽  
Author(s):  
Lutz NOVER ◽  
Klaus-Dieter SCHARF
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Cell Cultures ◽  
Shock Proteins

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.

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.

Heat shock proteins from cell cultures of higher plants and their somatic hybrids

1985 ◽  
Vol 4 (1) ◽  
pp. 19-22 ◽  
Author(s):  
S. V. Lopato ◽  
Yu.Yu. Gleba
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Cell Cultures ◽  
Somatic Hybrids ◽  
Higher Plants ◽  
Shock Proteins

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.

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.

Two Novel Agents Boost Heat Shock Proteins

2005 ◽  
Vol 36 (10) ◽  
pp. 14
Author(s):  
PATRICE WENDLING
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Novel Agents ◽  
Shock Proteins

Heat shock proteins in willow (Salix viminalis)

1990 ◽  
Vol 80 (2) ◽  
pp. 301-306
Author(s):  
Tiina Vahala ◽  
Tage Eriksson ◽  
Peter Engstrom
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Salix Viminalis ◽  
Shock Proteins
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