PMID- 10601334
OWN - NLM
STAT- MEDLINE
DCOM- 20000111
LR  - 20190508
IS  - 0021-9525 (Print)
IS  - 0021-9525 (Linking)
VI  - 147
IP  - 6
DP  - 1999 Dec 13
TI  - Stress-associated endoplasmic reticulum protein 1 (SERP1)/Ribosome-associated
      membrane protein 4 (RAMP4) stabilizes membrane proteins during stress and
      facilitates subsequent glycosylation.
PG  - 1195-204
AB  - Application of differential display to cultured rat astrocytes subjected to
      hypoxia allowed cloning of a novel cDNA, termed stress-associated endoplasmic
      reticulum protein 1 (SERP1). Expression of SERP1 was enhanced in vitro by hypoxia
      and/or reoxygenation or other forms of stress, causing accumulation of unfolded
      proteins in endoplasmic reticulum (ER) stress, and in vivo by middle cerebral
      artery occlusion in rats. The SERP1 cDNA encodes a 66-amino acid polypeptide
      which was found to be identical to ribosome-associated membrane protein 4 (RAMP4)
      and bearing 29% identity to yeast suppressor of SecY 6 protein (YSY6p),
      suggesting participation in pathways controlling membrane protein biogenesis at
      ER. In cultured 293 cells subjected to ER stress, overexpression of SERP1/RAMP4
      suppressed aggregation and/or degradation of newly synthesized integral membrane 
      proteins, and subsequently, facilitated their glycosylation when the stress was
      removed. SERP1/RAMP4 interacted with Sec61alpha and Sec61beta, which are subunits
      of translocon, and a molecular chaperon calnexin. Furthermore, Sec61alpha and
      Sec61beta, but not SERP1/RAMP4, were found to associate with newly synthesized
      integral membrane proteins under stress. These results suggest that stabilization
      of membrane proteins in response to stress involves the concerted action of a
      rescue unit in the ER membrane comprised of SERP1/RAMP4, other components of
      translocon, and molecular chaperons in ER.
FAU - Yamaguchi, A
AU  - Yamaguchi A
AD  - Department of Anatomy and Neuroscience, Graduate School of Medicine, Osaka
      University, Suita City, Osaka 565-0871, Japan.
FAU - Hori, O
AU  - Hori O
FAU - Stern, D M
AU  - Stern DM
FAU - Hartmann, E
AU  - Hartmann E
FAU - Ogawa, S
AU  - Ogawa S
FAU - Tohyama, M
AU  - Tohyama M
LA  - eng
SI  - GENBANK/AB018546
SI  - GENBANK/AB022427
SI  - GENBANK/Z81095
PT  - Journal Article
PL  - United States
TA  - J Cell Biol
JT  - The Journal of cell biology
JID - 0375356
RN  - 0 (Calcium-Binding Proteins)
RN  - 0 (Glycoproteins)
RN  - 0 (Membrane Proteins)
RN  - 0 (Molecular Chaperones)
RN  - 0 (RNA, Messenger)
RN  - 0 (SEC Translocation Channels)
RN  - 0 (SERP1 protein, human)
RN  - 0 (Serp1 protein, rat)
RN  - 139873-08-8 (Calnexin)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Astrocytes/drug effects/metabolism/pathology
MH  - Brain Ischemia/pathology/physiopathology
MH  - Calcium-Binding Proteins/metabolism
MH  - Calnexin
MH  - Cell Hypoxia/*physiology
MH  - Cell Line
MH  - Cloning, Molecular
MH  - Endoplasmic Reticulum/metabolism
MH  - Glycoproteins/biosynthesis/genetics/metabolism
MH  - Glycosylation
MH  - Homeostasis/physiology
MH  - Humans
MH  - Male
MH  - Membrane Proteins/biosynthesis/chemistry/genetics/*metabolism
MH  - Molecular Chaperones/metabolism
MH  - Molecular Sequence Data
MH  - Protein Binding
MH  - Protein Denaturation
MH  - Protein Renaturation
MH  - RNA, Messenger/analysis/genetics
MH  - Rats
MH  - Rats, Sprague-Dawley
MH  - SEC Translocation Channels
MH  - Sequence Homology, Amino Acid
PMC - PMC2168098
EDAT- 1999/12/22 00:00
MHDA- 1999/12/22 00:01
CRDT- 1999/12/22 00:00
PHST- 1999/12/22 00:00 [pubmed]
PHST- 1999/12/22 00:01 [medline]
PHST- 1999/12/22 00:00 [entrez]
AID - 10.1083/jcb.147.6.1195 [doi]
PST - ppublish
SO  - J Cell Biol. 1999 Dec 13;147(6):1195-204. doi: 10.1083/jcb.147.6.1195.