PMID- 10366592
OWN - NLM
STAT- MEDLINE
DCOM- 19990712
LR  - 20190508
IS  - 0021-9525 (Print)
IS  - 0021-9525 (Linking)
VI  - 145
IP  - 6
DP  - 1999 Jun 14
TI  - Isolation, cloning, and localization of rat PV-1, a novel endothelial caveolar
      protein.
PG  - 1189-98
AB  - By using an immunoisolation procedure (Stan, R.-V., W.G. Roberts, K. Ihida, D.
      Predescu, L. Saucan, L. Ghitescu, and G.E. Palade. 1997. Mol. Biol. Cell.
      8:595-605) developed in our laboratory, we have isolated a caveolar subfraction
      from rat lung endothelium and we have partially characterized the proteins of
      this subfraction which include an apparently caveolae-specific glycoprotein we
      propose to call PV-1 (formerly known as gp68). The isolation and partial
      sequencing of PV-1, combined with the cloning of the full length PV-1 cDNA led to
      the following conclusions: (a) PV-1 is a novel single span type II integral
      membrane protein (438 amino acids long) which forms homodimers in situ; (b) the
      transmembrane domain of PV-1 is near the NH2 terminus defining a short
      cytoplasmic endodomain and a large COOH-terminal ectodomain exposed to the blood 
      plasma; (c) PV-1 is N-glycosylated and its glycan antennae bear terminal
      nonreducing galactosyl residues in alpha1-3 linkage. PV-1 is expressed mostly in 
      the lung but both the messenger RNA and the protein can be detected at lower
      levels also in kidney, spleen, liver, heart, muscle, and brain. No signal could
      be detected in testis and two lower molecular weight forms were detected in
      brain. Immunocytochemical studies carried out by immunodiffusion on rat lung with
      an anti-PV-1 polyclonal antibody directed against a COOH-terminal epitope reveal 
      a specific localization of PV-1 to the stomatal diaphragms of rat lung
      endothelial caveolae and confirm the extracellular orientation of the PV-1 COOH
      terminus.
FAU - Stan, R V
AU  - Stan RV
AD  - Division of Cellular and Molecular Medicine, University of California, San Diego,
      San Diego, California 92093, USA.
FAU - Ghitescu, L
AU  - Ghitescu L
FAU - Jacobson, B S
AU  - Jacobson BS
FAU - Palade, G E
AU  - Palade GE
LA  - eng
SI  - GENBANK/AF154831
GR  - HL-17080/HL/NHLBI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Cell Biol
JT  - The Journal of cell biology
JID - 0375356
RN  - 0 (Antibodies)
RN  - 0 (Carrier Proteins)
RN  - 0 (Caveolin 1)
RN  - 0 (Caveolins)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Membrane Proteins)
RN  - 0 (PV-1 protein, rat)
RN  - 0 (RNA, Messenger)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Antibodies/isolation & purification
MH  - Base Sequence
MH  - Blotting, Northern
MH  - Blotting, Western
MH  - *Carrier Proteins
MH  - Caveolin 1
MH  - *Caveolins
MH  - Cell Membrane/*chemistry/metabolism/ultrastructure
MH  - Cloning, Molecular
MH  - Dimerization
MH  - Endothelium/chemistry/*ultrastructure
MH  - Gene Expression
MH  - Gene Library
MH  - Glycosylation
MH  - Lung/chemistry/ultrastructure
MH  - Membrane Glycoproteins/chemistry/*genetics/isolation & purification/metabolism
MH  - *Membrane Proteins
MH  - Microscopy, Immunoelectron
MH  - Molecular Sequence Data
MH  - Molecular Weight
MH  - Organ Specificity
MH  - RNA, Messenger/genetics/metabolism
MH  - Rats
MH  - Sequence Analysis
PMC - PMC2133139
EDAT- 1999/06/15 00:00
MHDA- 1999/06/15 00:01
CRDT- 1999/06/15 00:00
PHST- 1999/06/15 00:00 [pubmed]
PHST- 1999/06/15 00:01 [medline]
PHST- 1999/06/15 00:00 [entrez]
AID - 10.1083/jcb.145.6.1189 [doi]
PST - ppublish
SO  - J Cell Biol. 1999 Jun 14;145(6):1189-98. doi: 10.1083/jcb.145.6.1189.