Induction of the major heat-stress protein in purified rat glial cells

Journal Article · Sun May 01 04:00:00 EDT 1988 · J. Neurosci. Res.; (United States)

DOI:https://doi.org/10.1002/jnr.490200103· OSTI ID:7055751

Nishimura, R N; Dwyer, B E; Welch, W; Cole, R; de Vellis, J; Liotta, K

Cultured purified oligodendroglia and astroglia exposed to heat stress (45 degrees C, 10 or 20 min) synthesized a 68-kDa heat-stress protein, which migrates on two-dimensional gel electrophoresis and reacts with a specific monoclonal antibody suggesting it is similar to a major 72-kDa heat-shock protein previously reported in other cell types. This protein was not detected in control glial cultures. Actinomycin D prevented synthesis of this protein demonstrating an absolute requirement for newly synthesized mRNA. The response was prolonged by increasing the period of heat stress from 10 to 20 min. In addition to the 68-kDa HSP protein, the incorporation of radioactivity into 70-, 89-, and 97-kDa proteins was also increased after heating, but in contrast to the 68 kDa protein these proteins appeared to be made in control glial cultures.

• Research Organization: Veterans Administration Hospital, Sepulveda, CA (USA)
• OSTI ID: 7055751
• Journal Information: J. Neurosci. Res.; (United States), Journal Name: J. Neurosci. Res.; (United States) Vol. 20:1; ISSN JNRED
• Country of Publication: United States
• Language: English

Related Subjects

550201* -- Biochemistry-- Tracer Techniques
59 BASIC BIOLOGICAL SCIENCES
ACTINOMYCIN
AMINO ACIDS
ANIMALS
ANTI-INFECTIVE AGENTS
ANTIBIOTICS
ANTIBODIES
ANTIMITOTIC DRUGS
ANTINEOPLASTIC DRUGS
AUTORADIOGRAPHY
BIOSYNTHESIS
CARBOXYLIC ACIDS
CELL CULTURES
DRUGS
ELECTROPHORESIS
ENERGY
HEAT
ISOTOPES
LIPOTROPIC FACTORS
MAMMALS
METHIONINE
MOLECULAR WEIGHT
MONOCLONAL ANTIBODIES
ORGANIC ACIDS
ORGANIC COMPOUNDS
ORGANIC SULFUR COMPOUNDS
PROTEINS
RADIOISOTOPES
RATS
RODENTS
SYNTHESIS
VERTEBRATES