Skip to main content

Cell Growth, Cytoskeleton, and Heat Shock Proteins

  • Chapter
Heat Shock and Development

Part of the book series: Results and Problems in Cell Differentiation ((RESULTS,volume 17))

  • 63 Accesses

Abstract

A distinctive property of cultured mammalian cells existing in the resting state (G0) may be an unusually long delay between the shift of the culture from nonpermissive to permissive conditions for growth and the initiation of DNA synthesis. For instance, lymphocytes that had divided recently responded quickly to a stimulus, but lost this ability and became cells that responded slowly when incubated in the absence of the stimulus (Kumagai et al. 1981). We supposed that this alteration would be a result of the entrance to G0. This feature associated with various G0 cells was also seen with yeast cells arrested by certain cdc and other temperature-sensitive mutations under nonpermissive temperatures (Iida and Yahara 1984a).

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Chapter
USD 29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD 39.99
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD 54.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  • Ashbumer M, Bonner JJ (1979) The induction of gene activity in Drosophila by heat shock. Cell 17: 241–254

    Article  Google Scholar 

  • Brugge JS, Erikson E, Erikson RL (1981) The specific interaction of the Rous sarcoma virus transforming protein, pp60src, with two cellular proteins. Cell 25: 363–372

    Article  PubMed  CAS  Google Scholar 

  • Dougherty JJ, Puri RK, Toft DO (1984) Polypeptide components of two 8S forms of chicken oviduct progesterone receptor. J Biol Chem 259: 8004–8009

    PubMed  CAS  Google Scholar 

  • Friend C, Scher W, Holland JG, Sato T (1971) Hemoglobin synthesis in murine virus-induced leukemia cells in vitro: Stimulation of erythroid differentiation by dimethylsulfoxide. Proc Natl Acad Sci USA 68: 378–382

    Google Scholar 

  • Fukui Y (1978) Intranuclear actin bundles induced by dimethyl sulfoxide in interphase nucleus of Dictyostelium. J Cell Biol 76: 146–157

    Article  PubMed  CAS  Google Scholar 

  • Iida H (1988) Multistress resistance in Saccharomyces cerevisiae is generated by insertion of retrotransposon Ty into the 5’-coding region of the adenylate cyclase gene. Mol Cell Biol 8: 5555–5560

    PubMed  CAS  Google Scholar 

  • Iida H, Yahara I (1984a) Specific early-G1 blocks accompanied with stringent response in Saccharomyces cerevisiae lead to growth arrest in resting state similar to the Go of higher eucaryotes. J Cell Biol 98: 1185–1193

    Article  PubMed  CAS  Google Scholar 

  • Iida H, Yahara I (1984b) Durable synthesis of high molecular weight heat shock proteins in G0 cells of the yeast and other eucaryotes. J Cell Biol 99: 199–207

    Article  PubMed  CAS  Google Scholar 

  • Iida H, Yahara I (1984c) A heat shock-resistant mutant of Saccharomyces cerevisiae showing constitutive synthesis of two heat shock proteins and altered growth. J Cell Biol 99: 1441–1450

    Article  PubMed  CAS  Google Scholar 

  • Iida H, Yahara I (1985) Yeast heat-shock protein of Mr 48,000 is an isoprotein of enolase. Nature 315: 688–690

    Article  CAS  Google Scholar 

  • Iida K, Iida H, Yahara I (1986) Heat shock-induction of the intranuclear actin rods in cultured mammalian cells. Exp Cell Res 165: 207–215

    Article  PubMed  CAS  Google Scholar 

  • Koyasu S, Nishida E, Kadowaki T, Matsuzaki F, Iida K, Harada F, Kasuga M, Sakai H, Yahara I (1986) Two mammalian heat shock proteins, HSP90 and HSP100, are actin-binding proteins. Proc Natl Acad Sci USA 83: 8054–8058

    Article  PubMed  CAS  Google Scholar 

  • Koyasu S, Nishida E, Miyata Y, Sakai H, Yahara I (1989) HSP100, a 100-kDa heat shock protein, is a Cat+-calmodulin-regulated actin-binding protein. J Biol Chem 264: 15083–15087

    PubMed  CAS  Google Scholar 

  • Kumagai J, Akiyama H, Iwashita S, Iida H, Yahara I (1981) In vitro regeneration of resting lymphocytes from stimulated lymphocytes and its inhibition by insulin. J Immunol 126: 1249–1254

    PubMed  CAS  Google Scholar 

  • Lazarides E (1975) Tropomyosin antibody: the specific localization of tropomyosin in nonmuscle cells. J Cell Biol 65: 549–561

    Article  PubMed  CAS  Google Scholar 

  • Matsumoto K, Uno I, Ohshima Y, Ishikawa T (1982) Isolation and characterization of yeast mutants deficient in adenylate cyclase and cAMP-dependent protein kinase. Proc Natl Acad Sci USA 79: 2355–2359

    Article  PubMed  CAS  Google Scholar 

  • Matsuzaki F, Matsumoto S, Yahara I, Yonezawa N, Nishida E, Sakai H (1988) Cloning and characterization of porcine brain cofilin cDNA: cofilin contains the nuclear transport signal sequence. J Biol Chem 263: 11564–11568

    PubMed  CAS  Google Scholar 

  • Mazzarella RA, Green M (1987) ERp99, an abundant, conserved glycoprotein of the endoplasmic reticulum, is homologous to the 90-kDa heat shock protein (hsp90) and the 94-kDa glucose regulated protein (GRP94). J Biol Chem 262: 8875–8883

    PubMed  CAS  Google Scholar 

  • Miyata Y, Yahara I (1991) Cytoplasmic 8S glucocorticoid receptor binds to actin filaments through the 90-kDa heat shock protein moiety. J Biol Chem 266: 8779–8783

    PubMed  CAS  Google Scholar 

  • Moriyama K, Matsumoto S, Nishida E, Sakai H, Yahara I (1990) Nucleotide sequence of mouse cofilin cDNA ( Record ). Nucl Acids Res 18: 3053

    Google Scholar 

  • Munro S, Pelham HRB (1987) A C-terminal signal prevents secretion of luminal ER proteins. Cell 48: 899–907

    Article  PubMed  CAS  Google Scholar 

  • Nishida E, Maekawa S, Sakai H (1984) Cofilin, a protein in porcine brain that binds to actin filaments and inhibits their interactions with myosin and tropomyosin. Biochemistry 23: 5307–5313

    Article  PubMed  CAS  Google Scholar 

  • Nishida E, Koyasu S, Sakai H, Yahara I (1986) Calmodulin-regulated binding of the 90 kDa heat shock protein to actin filaments. J Biol Chem 261: 16033–16036

    PubMed  CAS  Google Scholar 

  • Nishida E, Iida K, Yonezawa N, Koyasu S, Yahara I Sakai H (1987) Cofilin is a component of intranuclear and cytoplasmic actin rods induced in cultured cells. Proc Natl Acad Sci USA 84: 5262–5266

    Article  PubMed  CAS  Google Scholar 

  • Oppermann H, Levinson W, Bishop JM (1981) A cellular protein that associates with the transforming protein of Rous sarcoma virus is also a heat shock protein. Proc Natl Acad Sci USA 78: 1067–1071

    Article  PubMed  CAS  Google Scholar 

  • Perdew GH (1988) Association of the Ah receptor with the 90-kDa heat shock protein. J Biol Chem 263: 13802–13806

    PubMed  CAS  Google Scholar 

  • Renoir JM, Buchou T, Mester J, Radanyi C, Baulieu EE (1984) Oligomeric structure of molybdatestabilized, nontransformed 8S progesterone receptor from chicken oviduct cytosol. Biochemistry 23: 6016–6023

    Article  CAS  Google Scholar 

  • Yahara I, Harada F, Sekita S, Yoshihira K, Natori S (1982) Correlation between effects of 24 different cytochalasins on cellular structures and cellular events and those on actin in vitro. J Cell Biol 92: 69–78

    Article  PubMed  CAS  Google Scholar 

  • Yahara I, Iida H, Koyasu S (1986) A heat shock-resistant variant of Chinese hamster cell line constitutively expressing heat shock protein of Mr 90,000 at high level. Cell Struct Funct 11: 65–73

    Article  PubMed  CAS  Google Scholar 

  • Yonezawa N, Nishida E, Sakai H, (1985) pH control of actin polymerization by cofilin. J Biol Chem 260: 14410–14412

    PubMed  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Editor information

Editors and Affiliations

Rights and permissions

Reprints and permissions

Copyright information

© 1991 Springer-Verlag Berlin Heidelberg

About this chapter

Cite this chapter

Yahara, I. et al. (1991). Cell Growth, Cytoskeleton, and Heat Shock Proteins. In: Hightower, L., Nover, L. (eds) Heat Shock and Development. Results and Problems in Cell Differentiation, vol 17. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-540-46712-0_14

Download citation

  • DOI: https://doi.org/10.1007/978-3-540-46712-0_14

  • Publisher Name: Springer, Berlin, Heidelberg

  • Print ISBN: 978-3-662-21993-5

  • Online ISBN: 978-3-540-46712-0

  • eBook Packages: Springer Book Archive

Publish with us

Policies and ethics