Stress protein systems of mammalian cells

Abstract

Living organisms are known to react to a heat stress by the selective induction in the synthesis of several polypeptides. In this review we list the major stress proteins of mammalian cells that are induced by heat shock and other environments and categorize these proteins into specific subgroups: the major heat shock proteins, the glucose-regulated proteins, and the low-molecular-weight heat shock proteins. Characteristics of the localization and expression of proteins in each of these subgroups are presented. Specifically, the nuclear/nucleolar locale of certain of the major heat shock proteins is considered with respect to their association with RNA and the recovery of cells after a heat exposure. The induction of these major heat shock proteins and the repression of the glucose-regulated proteins as a result of reoxygenation of anoxic cells or by the addition of glucose to glucose-deprived cultures is described. Changes in the expression of these protein systems during embryogenesis and differentiation in mammalian and nonmammalian systems is summarized, and the protective role that some of these proteins appear to play in protecting the animal against the lethal effects of a severe heat treatment and against teratogenesis is critically examined.

Programmed cell death: Dying cells synthesize a co‐ordinated, unique set of proteins in two different episodes of cell death

“…The striking similarity of the patterns at pupal ecdysis, when the anteriormost and posteriormost muscles are destroyed, and at adult ecdysis, when the abdominal muscles are destroyed, suggests that the co-ordinate synthesis of these proteins is a major factor in involution. Since the cells are under stress at this time and it is known that several factors, including both hypoxia and inhibition of oxidative phosphorylation, and even increases in calcium levels, can induce the synthesis of stress proteins [18][19][20], this possibility is currently being explored. The proteins appear to be too alkaline to be heat-shock proteins.…”

The expression of glucose regulated protein-94 in colorectal carcinoma cells treated by sodium butyrate

“…In mammalian cells, this system is divided into two predominant categories which appear to be structurally and functionally related: the heat shock proteins (HSPs) and the glucose-regulated proteins (GRPs). These protein sets, however, are separable basing on their differential sensitivity to different kinds of stresses [1], [2].…”

“…The most prominent HSPs of mammalian cells have molecular weights of approximately 90,000 (HSP90), and 70,000 (HSP70) [1], [3]. Many studies have suggested a possible correlation between the expression of HSPs and the growth and differentiation of tumor cells [4][5][6][7][8][9].…”

Induced Tolerance to Ischemia in Gerbil Hippocampal Neurons

“…Diverse envi ronmental changes such as high temperature, amino acid analogues, heavy metals, or inhibition of en ergy metabolism can trigger this "stress response." Since the effect of temperature elevation has been most intensively studied, this phenomenon is also called "heat-shock response," and the synthesized proteins are called "heat-shock proteins" (hsp) (for review, see Lindquist, 1986;Subjeck and Shyy, 1986). Heat-shock proteins appear to exhibit a high degree of conservation from bacteria to mammalian cells (Bardwell and Craig, 1984;Hunt and Mori moto, 1985).…”