The endoplasmic reticulum (endoplasmic meaning "within the cytoplasm," reticulum meaning "little net" in Latin) or ER is an organelle found in all eukaryotic cells that is an interconnected network of tubules, vesicles and cisternae that is responsible for several specialized functions: Protein translation, folding, and transport of proteins to be used in the cell membrane (e.g., transmembrane receptors and other integral membrane proteins), or to be secreted (exocytosed) from the cell (e.g., digestive enzymes); sequestration of calcium; and production and storage of glycogen, steroids, and other macromolecules. The endoplasmic reticulum is part of the endomembrane system. The basic structure and composition of the ER membrane is similar to the plasma membrane.
4B4
may serve as a specific marker for the
sarcoplasmic/endoplasmic reticulum Ca2+ pump system in various
cells, and can provide quantitative information about the loss
of active Ca2+ pump proteins under pathological conditions.
PMID: 2543829
Calnexin
a membrane-bound chaperone of the endoplasmic
reticulum.
PMID: 8203019
calnexin, which is itself retained within the
endoplasmic reticulum, is normally expressed on the surface of
various cells such as mastocytoma cells, murine splenocytes,
fibroblast cells, and human HeLa cells.
PMID: 10956670
Calreticulin
Calreticulin and calnexin are Ca2+-binding
proteins with chaperone activity in the endoplasmic reticulum.
PMID: 11726513
Cytochrome P450 (CYP2E1)
an endoplasmic reticulum marker.
PMID: 1918014
Disulfide Isomerase
classical ER resident. PMID: 15281078
Estrone Sulfate Sulfohydrolase
a putative endoplasmic reticulum marker.
PMID: 219149
CDP-Choline-Diacylglycerol
Cholinephosphotransferase.
a putative endoplasmic reticulum marker.
PMID: 219149
Epoxide Hydrolase
a marker for the smooth endoplasmic reticulum
in rat liver.
PMID: 4065094
ERp27
a new non-catalytic endoplasmic
reticulum-located human protein disulfide isomerase family
member, interacts with ERp57.
PMID: 16940051
ERp29
a recently discovered resident of the
endoplasmic reticulum (ER) that is abundant in brain and most
other mammalian tissues.
PMID: 15281078
ERp57
a member of the protein disulfide isomerase
(PDI) family that is located in the endoplasmic reticulum (ER)
and characterized by its specificity for glycoproteins.
PMID: 14871899
ERp72
a resident protein of the endoplasmic
reticulum (ER) is both a stress protein and a member of the
protein disulfide isomerase family of proteins.
PMID: 8216852
an abundant luminal endoplasmic reticulum
protein, contains three copies of the active site sequences of
protein disulfide isomerase.
PMID: 2295602
Glucose-6-Phosphatase (G-6-Pase)
an endoplasmic reticulum marker.
PMID: 8652599
localized consistently within the lumen of
all endoplasmic reticulum, nuclear space and subsurface
cisternae, and frequently in the concave saccules of the Golgi
apparatus.
PMID: 2552716
a cytochemical marker of endoplasmic
reticulum in human leukocytes and platelets.
PMID: 6319482
Glucosidase II
a protein of the endoplasmic reticulum with
high mannose oligosaccharide chains and a rapid turnover.
PMID: 3546312
an asparagine-linked oligosaccharide
processing enzyme, is a resident glycoprotein of the endoplasmic
reticulum. In kidney tubular cells, in contrast to previous
findings on hepatocytes, we found by light and electron
microscopy immunoreactivity for glucosidase II predominantly in
post-Golgi apparatus structures.
PMID: 2404989
GRP78/BiP
the major chaperone of the endoplasmic
reticulum (ER) lumen.
PMID: 9388233
lumenal stress protein of the endoplasmic
reticulum (ER) that interacts with polypeptide folding
intermediates transiting the secretory compartment.
PMID: 9020152
a constitutively-expressed resident protein
of the endoplasmic reticulum (ER) of all eucaryotic cells, and
belongs to the highly conserved hsp70 protein family.
PMID: 7988659
BiP/GRP78 is a member of the HSP70 family
involved in the folding and assembly of proteins in the
endoplasmic reticulum.
PMID: 8020977
induction of GRP78 is a marker for ER stress.
GRP78, also referred to as BiP, is a central regulator for ER
stress due to its role as a major ER chaperone with
anti-apoptotic properties as well as its ability to control the
activation of transmembrane ER stress sensors (IRE1, PERK, and
ATF6) through a binding-release mechanism.
PMID: 15804610
BiP is selectively retained in the cisternae
of the ER and is not free to enter Golgi-directed transport
vesicles.
PMID: 2685110
GRP94
a glycoprotein in the endoplasmic reticulum
(ER).
PMID: 9009140
endoplasmic reticulum stress protein.
PMID: 1400441
ERp99
an abundant, conserved transmembrane
glycoprotein of the endoplasmic reticulum membrane.
PMID: 3036833
Heme oxygenase-1
a cytoprotective protein that catalyzes the degradation of heme to biliverdin, iron, and carbon monoxide (CO). Endoplasmic reticulum (ER) stress induced by a variety of experimental agents stimulated a time- and concentration-dependent increase in HO-1 mRNA and protein in vascular smooth muscle cells (SMC). PMID: 15546873
HSP27
cytosolic resident heat shock protein located in the endoplasmic reticulum (ER). PMID: 16884889
Endoplasmic reticulum
stress induces the phosphorylation of small heat shock protein,
Hsp27.
PMID: 15864808
JPDI (J-domain-containing protein disulfide
isomerase-like protein)
a novel endoplasmic reticulum-resident
protein containing both a BiP-interacting J-domain and
thioredoxin-like motifs.
PMID: 12446677
Membrin
an ER-Golgi SNARE protein. PMID: 15781476
NADPH cytochrome c (cyt c) reductase and
glucose-6-phosphatase
two enzymes thought to be restricted to the endoplasmic reticulum (ER) and widely used as ER markers. PMID: 214450
PDI (Protein Disulphide Isomerase)
one such ER resident protein that has been
previously shown to interact with proteins during their folding
and assembly pathways.
PMID: 11509234
Rbet1
homologous to yeast Bet1p is primarily
associated with the pre-Golgi intermediate compartment and is
involved in vesicular transport from the endoplasmic reticulum
to the Golgi apparatus.
PMID: 9382863
Tapasin (tpn)
an essential component of the MHC class I
(MHC I) loading complex, has a canonical double lysine motif
acting as a retrieval signal, which mediates retrograde
transport of escaped endoplasmic reticulum (ER) proteins from
the Golgi back to the ER.
PMID: 16751394
a subunit of the transporter associated with
antigen processing (TAP).
PMID: 11884415
is retained in the endoplasmic reticulum by
dynamic clustering and exclusion from endoplasmic reticulum exit
sites.
PMID: 11823478
TbRab2p
localised primarily to the endoplasmic
reticulum (ER) and colocalises with BiP in wild-type
trypanosomes, is a marker for the endoplasmic reticulum of
Trypanosoma brucei, localises to the ERGIC in mammalian cells.
PMID: 9858468
UGGT
gamma -glutamyltransferase
and its isoform mediate an endoplasmic reticulum stress
response.
PMID: 11116135
Gamma-glutamyltransferase induction was
maximal 24 h after PB treatment in both the rough endoplasmic
reticulum and the plasma membranes after a single dose of
phenobarbital (PB) (75 mg kg-1 body weight).
PMID: 2886233
Other ER Markers
Two sensitive, convenient, and widely applicable assays for marker enzyme activities specific to endoplasmic reticulum. PMID: 2840001
Anti-liver-kidney microsome antibody is a marker for the rat hepatocyte endoplasmic reticulum. PMID: 3552922
Peroxidase, a marker enzyme for granular
endoplasmic reticulum in thyroid gland (proceedings).
PMID: 79388
Preneoplastic antigen as a marker for endoplasmic reticulum of putative premalignant hepatocytes during liver carcinogenesis. PMID: 193631