PMID- 10551807
OWN - NLM
STAT- MEDLINE
DCOM- 20000103
LR  - 20190508
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 274
IP  - 46
DP  - 1999 Nov 12
TI  - Analysis of SCAMP1 function in secretory vesicle exocytosis by means of gene
      targeting in mice.
PG  - 32551-4
AB  - Secretory carrier membrane proteins (SCAMPs) comprise a family of ubiquitous
      membrane proteins of transport vesicles with no known function. Their universal
      presence in all cells suggests a fundamental role in membrane traffic. SCAMPs are
      particularly highly expressed in organelles that undergo regulated exocytosis,
      such as synaptic vesicles and mast cell granules. Of the three currently known
      SCAMPs, SCAMP1 is the most abundant. To investigate the possible functions of
      SCAMP1, we generated mice that lack SCAMP1. SCAMP1-deficient mice are viable and 
      fertile. They exhibit no changes in the overall architecture or the protein
      composition of the brain or alterations in peripheral organs. Capacitance
      measurements in mast cells demonstrated that exocytosis could be triggered
      reliably by GTPgammaS in SCAMP1-deficient cells. The initial overall capacitance 
      of mast cells was similar between wild type and mutant mice, but the final cell
      capacitance after completion of exocytosis, was significantly smaller in
      SCAMP1-deficient cells than in wild type cells. Furthermore, there was an
      increased proportion of reversible fusion events, which may have caused the
      decrease in the overall capacitance change observed after exocytosis. Our data
      show that SCAMP1 is not essential for exocytosis, as such, and does not determine
      the stability or size of secretory vesicles, but is required for the full
      execution of stable exocytosis in mast cells. This phenotype could be the result 
      of a function of SCAMP1 in the formation of stable fusion pores during exocytosis
      or of a role of SCAMP1 in the regulation of endocytosis after formation of fusion
      pores.
FAU - Fernandez-Chacon, R
AU  - Fernandez-Chacon R
AD  - Howard Hughes Medical Institute, University of Texas Southwestern Medical Center,
      Dallas, Texas 75235, USA.
FAU - Alvarez de Toledo, G
AU  - Alvarez de Toledo G
FAU - Hammer, R E
AU  - Hammer RE
FAU - Sudhof, T C
AU  - Sudhof TC
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Carrier Proteins)
RN  - 0 (Membrane Proteins)
RN  - 0 (Scamp1 protein, mouse)
RN  - 0 (Vesicular Transport Proteins)
RN  - 37589-80-3 (Guanosine 5'-O-(3-Thiotriphosphate))
SB  - IM
MH  - Animals
MH  - Carrier Proteins/*genetics/metabolism
MH  - Cloning, Molecular
MH  - Cytoplasmic Granules/*metabolism
MH  - Electric Conductivity
MH  - Endocytosis/genetics
MH  - Exocytosis/*genetics
MH  - *Gene Targeting
MH  - Guanosine 5'-O-(3-Thiotriphosphate)/pharmacology
MH  - Mast Cells
MH  - Membrane Fusion/genetics
MH  - Membrane Proteins/*genetics/metabolism
MH  - Mice
MH  - Mice, Knockout
MH  - Phenotype
MH  - Vesicular Transport Proteins
EDAT- 1999/11/07 00:00
MHDA- 1999/11/07 00:01
CRDT- 1999/11/07 00:00
PHST- 1999/11/07 00:00 [pubmed]
PHST- 1999/11/07 00:01 [medline]
PHST- 1999/11/07 00:00 [entrez]
AID - 10.1074/jbc.274.46.32551 [doi]
PST - ppublish
SO  - J Biol Chem. 1999 Nov 12;274(46):32551-4. doi: 10.1074/jbc.274.46.32551.