High impact information on Scamp1

• Intracellular GLUT4-containing vesicles were immunoisolated from low density microsomes by using monoclonal anti-GLUT4 (1F8) or anti-SCAMP antibodies (3F8) coupled to either agarose or acrylamide [1].
• Secretory carrier membrane proteins (SCAMPs) mark the recycling system for the insulin-responsive glucose transporter, GluT4, in rat adipocytes [2].
• Secretory carrier membrane proteins 31-35 define a common protein composition among secretory carrier membranes [3].
• A corollary of these findings is that early endosomes exist as a distinct SCAMP-containing compartment and are not formed de novo by fusion of endocytic vesicles [4].
• Secretory carrier membrane proteins (SCAMPs) 1-4 are ubiquitously expressed and are major components of the eukaryotic cell surface recycling system [4].

Anatomical context of Scamp1

• Besides these proteins, which can be considered as vesicle "cargo", GLUT-4-containing vesicles have other components, like secretory carrier-associated membrane proteins (SCAMP), Rab(s), and vesicle-associated membrane protein (VAMP)/cellubrevin, which are ubiquitous to secretory vesicles and granules from different tissues [5].

Associations of Scamp1 with chemical compounds

• Some genes were observed to change specifically in response to preconditioning: oligoadenylate synthase, chaperonin subunit epsilon, a cGMP phosphodiesterase (PDE9A1), a secretory carrier membrane protein, an amino acid transporter, and protease 28 subunit [6].

Other interactions of Scamp1

• The GLUT4 pool showing no response to insulin contained SCAMP proteins and the vSNARE proteins VAMP2 and cellubrevin, whereas only VAMP2 was found in the insulin-recruitable GLUT4 pool [7].

References