Endoplasmic Reticulum

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Endoplasmic reticulum

An intracellular membrane system that is present in all eukaryotic cells. In most cells the endoplasmic reticulum is thought to consist of only one continuous membrane enclosing only a single space. However, in protozoa, some unicellular algae, and possibly some fungi, the endoplasmic reticulum occurs as separate, multiple vesicles. See Cell membranes

Nuclear envelope, connected to the rough and smooth endoplasmic reticulumenlarge picture
Nuclear envelope, connected to the rough and smooth endoplasmic reticulum

Several morphologically and functionally distinct domains of this continuous membrane system can be distinguished. At the level of the nuclear pores, the inner nuclear membrane is continuous with the outer nuclear membrane; both membranes together are referred to as the nuclear envelope. The outer nuclear membrane in turn is continuous with the rough endoplasmic reticulum, which contains specialized regions, termed transitional elements, and is continuous with the smooth endoplasmic reticulum. The two membranes of the nuclear envelope enclose the perinuclear space. The rough and smooth endoplasmic reticula and the transitional element enclose a space called the intracisternal space, or lumen. Both intracisternal and perinuclear spaces form a single compartment. All nucleated cells contain at least a nuclear envelope, but the amount of smooth and rough endoplasmic reticula varies greatly among different cell types. See Cell nucleus

The term rough endoplasmic reticulum is based on the morphologic appearance of attached ribosomes, which are absent from smooth endoplasmic reticulum. (Ribosomes are also associated with the outer nuclear membrane; in fact, the outer nuclear membrane and the rough endoplasmic reticulum appear to be functionally equivalent.) Another morphologic distinction is the organization of the rough endoplasmic reticulun in interconnected flattened sacs (called cisternae), whereas the smooth endoplasmic reticulum forms a tubular network (see illustration). See Ribosomes

The rough endoplasmic reticulum is the site of translocation of secretory and lysosomal proteins from the cytosol to the intracisternal space, and of integration into the membrane of integral membrane proteins. Except for integral membrane proteins of chloroplast, mitochondria, and peroxisomes, essentially all other integral membrane proteins are integrated into the endoplasmic reticulum and either remain there (resident endoplasmic reticulum membrane proteins) or are subsequently distributed to other cellular membranes.

The signal hypothesis was formulated to explain how these proteins are targeted to and then translocated across or integrated into the endoplasmic reticulum membrane. Its tenets are that all polypeptides targeted to this membrane contain a discrete sequence (termed the signal sequence), that a complex machinery recognizes this sequence, and that recognition triggers the opening of a proteinaceous channel through which the polypeptide passes across the membrane. In the case of membrane proteins, the existence of an additional topogenic sequence, the so-called stop-transfer sequence, was postulated. This sequence is thought to trigger opening of the channel to the lipid bilayer to abort translocation and thus integrate the protein into the lipid bilayer.

The rough endoplasmic reticulum also contains numerous enzymes, most of which are involved in the modification of the nascent protein chain on the cisternal side. Thus the main function of the rough endoplasmic reticulum and the outer nuclear membrane is to serve as a port of entry of secretory, lysosomal, and integral membrane proteins and as the site of their initial modification.

Secretory and lysosomal proteins as well as those integral membrane proteins that are not residents of the endoplasmic reticulum are next transported to the cis Golgi cisternae. The transitional elements represent sites of transport from the rough endoplasmic reticulum. Coated vesicles carrying proteins to be transported form at these sites and, after uncoating, eventually fuse with the cis Golgi cisternae. See Golgi apparatus

Smooth endoplasmic reticulum contains enzymes for phospholipid biosynthesis, steroid biosynthesis, and drug detoxification. See Cell (biology), Cell organization, Enzyme

McGraw-Hill Concise Encyclopedia of Bioscience. © 2002 by The McGraw-Hill Companies, Inc.
The following article is from The Great Soviet Encyclopedia (1979). It might be outdated or ideologically biased.

Endoplasmic Reticulum


in biology, an intracellular organoid that consists of a system of flat cisternae, tubules, and vesicles that are bounded by membranes. Its main function is to ensure the transfer of matter from the surrounding medium into the cytoplasm and between intracellular structures. The endoplasmic reticulum was discovered with an electron microscope in 1945 by K. Porter and other American scientists. It is usually located in the cytoplasm immediately surrounding the nucleus (the endoplasm) in all the cells, except the erythrocytes, of eukaryotes.

The structure and number of elements in the endoplasmic reticulum depend on the functional activity of the cell and on the stage of the cell cycle and differentiation. The membrane is 5–6 nm thick, and the width of the lumen between the membranes is 70–500 nanometers. Analysis of the microsomal fraction of a homogenate of cells has shown that the membranes of the endoplasmic reticulum consist of proteins, lipids, and several enzymes.

There are two principal types of endoplasmic reticulum: granular (with ribosomes attached to the membranes) and nongranular. Intermediate types also exist. Granular endoplasmic reticulum participates in protein synthesis. Injection of tagged amino acids into the body has shown that the effectiveness of synthesis is increased substantially by the attachment of ribosomes to the membranes. Granular endoplasmic reticulum attains its highest development in actively synthesizing cells whose products (proteins of secretory granules, serum proteins) are discharged from the cell. Nongranular endoplasmic reticulum participates in the synthesis and transport of lipids and steroids, in the synthesis and decomposition of glycogen, and in the neutralization of various toxic and medicinal substances, for example, Luminal and codeine. It is well developed in cells of the adrenal glands and in the parietal cells of the gastric mucosa. Both types of endoplasmic reticulum are characterized by the accumulation of products of synthesis in the lumina of the membranes and their transport to the zone of the Golgi apparatus.

A specialized form of endoplasmic reticulum, the sarcoplasmic network of the striated muscles, plays an important role in the intracellular conduction of excitation.


Alov, I. A., A. I. Braude, and M. E. Aspiz. Osnovy funktsional’noi morfologii kletki, 2nd ed. Moscow, 1969.
Robertis, E., W. Nowinski, and F. Saez. Biologiia kletki. Moscow, 1973. (Translated from English.)


The Great Soviet Encyclopedia, 3rd Edition (1970-1979). © 2010 The Gale Group, Inc. All rights reserved.

endoplasmic reticulum

[¦en·də¦plaz·mik rə′tik·yə·ləm]
(cell and molecular biology)
A vacuolar system of the cytoplasm in differentiated cells that functions in protein synthesis and sequestration. Abbreviated ER.
McGraw-Hill Dictionary of Scientific & Technical Terms, 6E, Copyright © 2003 by The McGraw-Hill Companies, Inc.
References in periodicals archive ?
XBP1, X-box binding protein 1; ERSE, endoplasmic reticulum-stress response element; BiP, binding immunoglobulin protein; GRP94, heat shock protein 90 kDa beta member 1; Herpud1, homocysteine-responsive endoplasmic reticulum-resident ubiquitin-like domain member 1 protein; UPRE, UPR element; ANOVA, analysis of variance; qPCR, quantitative real-time polymerase chain reaction; HRD1, E3 ubiquitin-protein ligase synoviolin; EDEM1, endoplasmic reticulum degradation enhancing alpha-mannosidase-like protein 1; SLC25A1, solute carrier family 25 member 1.
IRE1 couples endoplasmic reticulum load to secretory capacity by processing the XBP-1 mRNA.
Endoplasmic reticulum stress markers, phospho-PERK/PERK ratio (A), CHOP protein level (B), and GRP78 protein level (C) within the myocardium after 12 weeks of aerobic exercise (AE) and resistance exercise (RE).
Mitochondria and smooth endoplasmic reticulum aggregates of control oocyte (a), GV oocyte after IVM(b), vitrified--thawed GV oocyte after IVM (c), vitrified-thawed GV oocyte before IVM (d), M = mitochondria, SER = smooth endoplasmic reticulum, V = vacuole.
Gao et al., "Linking of autophagy to ubiquitin-proteasome system is important for the regulation of endoplasmic reticulum stress and cell viability," The American Journal of Pathology, vol.
Ikehata et al., "Proteinuria and hyperglycemia induce endoplasmic reticulum stress," Journal of the American Society of Nephrology, vol.
Skach, "Protein folding and quality control in the endoplasmic reticulum: recent lessons from yeast and mammalian cell systems," Current Opinion in Cell Biology, vol.
Mooradian, "Inhibition of endoplasmic reticulum stress and oxidative stress by vitamin D in endothelial cells," Free Radical Biology & Medicine, vol.
Prywes, "The luminal domain of ATF6 senses endoplasmic reticulum (ER) stress and causes translocation of ATF6 from the ER to the Golgi," Journal of Biological Chemistry, vol.
Kaufman, "Signaling the unfolded protein response from the endoplasmic reticulum," The Journal of Biological Chemistry, vol.
Smooth endoplasmic reticulum, rough endoplasmic reticulum, and many mitochondria were observed in the cytoplasm of the Leydig cells.
These results suggest that Salicinium induces endoplasmic reticulum stress in HK-2 mediated cells, which is in turn involved in apoptosis or autophagy.

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