Molecular dissection of the alpha-dystroglycan- and integrin-binding sites within the globular domain of human laminin-10.
AuthorsIdo H, Harada K, Futaki S, Hayashi Y, Nishiuchi R, Natsuka Y, Li S, Wada Y, Combs AC, Ervasti JM, Sekiguchi K,
JournalJ Biol Chem
PubMed ID14701821
'The adhesive interactions of cells with laminins are mediated by integrins and non-integrin-type receptors such as alpha-dystroglycan and syndecans. Laminins bind to these receptors at the C-terminal globular domain of their alpha chains, but the regions recognized by these receptors have not been mapped precisely. In this study, we sought ... More
Biological activity of follistatin isoforms and follistatin-like-3 is dependent on differential cell surface binding and specificity for activin, myostatin, and bone morphogenetic proteins.
AuthorsSidis Y, Mukherjee A, Keutmann H, Delbaere A, Sadatsuki M, Schneyer A,
JournalEndocrinology
PubMed ID16627583
Follistatin (FST) and FST-like-3 (FSTL3) are activin-binding and neutralization proteins that also bind myostatin. Three FST isoforms have been described that differ in tissue distribution and cell-surface binding activity, suggesting that the FST isoforms and FSTL3 may have some nonoverlapping biological actions. We produced recombinant FST isoforms and FSTL3 and ... More
Mutation of key residues of RPE65 abolishes its enzymatic role as isomerohydrolase in the visual cycle.
AuthorsRedmond TM, Poliakov E, Yu S, Tsai JY, Lu Z, Gentleman S,
JournalProc Natl Acad Sci U S A
PubMed ID16150724
RPE65 is essential for isomerization of vitamin A to the visual chromophore. Mutations in RPE65 cause early-onset blindness, and Rpe65-deficient mice lack 11-cis-retinal but overaccumulate alltrans-retinyl esters in the retinal pigment epithelium (RPE). RPE65 is proposed to be a substrate chaperone but may have an enzymatic role because it is ... More
Binding of anthrax toxin to its receptor is similar to alpha integrin-ligand interactions.
AuthorsBradley KA, Mogridge J, Jonah G, Rainey A, Batty S, Young JA,
JournalJ Biol Chem
PubMed ID14507921
The secreted protein toxin produced by Bacillus anthracis contributes to virulence of this pathogen and can cause many of the symptoms seen during an anthrax infection, including shock and sudden death. The cell-binding component of anthrax toxin, protective antigen, mediates entry of the toxin into cells by first binding directly ... More
A novel secreted endonuclease from Culex quinquefasciatus salivary glands.
AuthorsCalvo E, Ribeiro JM,
JournalJ Exp Biol
PubMed ID16809456
Previous analysis of the salivary gland transcriptome of Culex quinquefasciatus showed the potential presence of an endonuclease with sequence similarities to shrimp, crab and two tsetse salivary proteins. Indeed, not only was the cloned cDNA shown to encode an active double-stranded endonuclease, but also the same activity was demonstrated to ... More