PMID- 3954360
OWN - NLM
STAT- MEDLINE
DCOM- 19860404
LR  - 20190629
IS  - 0003-9861 (Print)
IS  - 0003-9861 (Linking)
VI  - 245
IP  - 2
DP  - 1986 Mar
TI  - Structure and assembly of the endoplasmic reticulum: biosynthesis and 
      intracellular sorting of ERp61, ERp59, and ERp49, three protein components of 
      murine endoplasmic reticulum.
PG  - 389-403
AB  - Rabbit antibodies have been prepared against ERp61, ERp59, and ERp49, three 
      protein components of rough endoplasmic reticulum (RER) purified from mineral 
      oil-induced plasmacytoma 315 (MOPC-315) tissue. Analysis of subcellular fractions 
      of MOPC-315 tissue by an immunoprecipitation procedure demonstrated that all 
      three endoplasmic reticulum proteins (ERps) were most enriched in the RER. 
      Immunologically cross-reacting proteins of similar molecular weight have been 
      detected in other eucaryotic cell lines. We have used these antibodies to study 
      the post-translational processing and biosynthetic sorting of the three ERps in 
      pulse-labeled MOPC-315 cells. No larger precursor forms of the ERps were detected 
      and none of the ERps were found to possess asparagine-linked oligosaccharide 
      moieties. We have used a sucrose gradient analysis of pulse-labeled MOPC-315 
      cells to study the biosynthetic sorting of ERp61, ERp59 and ERp49 and have found 
      no evidence to suggest that these proteins ever leave the endoplasmic reticulum. 
      In addition, all three ERps appeared to have luminally exposed domains. ERp61 and 
      ERp59 were entirely protected by the ER membrane in the absence of detergent, 
      while ERp49 was a transmembrane protein that also possesses a cytoplasmically 
      exposed domain. We have used the anti-ERp antibodies to quantitate the synthesis 
      and accumulation of the three ERps during lipopolysaccharide (LPS)-induced 
      lymphocyte differentiation. After 48 h of culture in the presence of LPS, the 
      synthesis of ERp49 increased sixfold relative to that in control cells. The 
      synthesis and membrane accumulation of ERp61 and ERp59 were less affected by the 
      LPS treatment. Thus, membranes isolated from LPS-treated cells were enriched in 
      ERp49 relative to those isolated from control cells.
FAU - Lewis, M J
AU  - Lewis MJ
FAU - Mazzarella, R A
AU  - Mazzarella RA
FAU - Green, M
AU  - Green M
LA  - eng
GR  - GM-33575/GM/NIGMS NIH HHS/United States
GR  - RR05388/RR/NCRR NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Arch Biochem Biophys
JT  - Archives of biochemistry and biophysics
JID - 0372430
RN  - 0 (Membrane Proteins)
SB  - IM
MH  - Animals
MH  - Antibody Specificity
MH  - Cell Line
MH  - Chemical Phenomena
MH  - Chemical Precipitation
MH  - Chemistry
MH  - Endoplasmic Reticulum/*metabolism
MH  - Immunochemistry
MH  - Intracellular Membranes/metabolism
MH  - Lymphocyte Activation
MH  - Lymphocytes/metabolism
MH  - Membrane Proteins/*biosynthesis/isolation & purification
MH  - Mice
MH  - Mice, Inbred BALB C
MH  - Plasmacytoma
MH  - Solubility
MH  - Subcellular Fractions/metabolism
EDAT- 1986/03/01 00:00
MHDA- 1986/03/01 00:01
CRDT- 1986/03/01 00:00
PHST- 1986/03/01 00:00 [pubmed]
PHST- 1986/03/01 00:01 [medline]
PHST- 1986/03/01 00:00 [entrez]
AID - 0003-9861(86)90230-4 [pii]
AID - 10.1016/0003-9861(86)90230-4 [doi]
PST - ppublish
SO  - Arch Biochem Biophys. 1986 Mar;245(2):389-403. doi: 10.1016/0003-9861(86)90230-4.