Sema3A binding to Neuropilin-1:Plexin-A complex results in conformational change of plexin-A and this conformational change permits Fes nonreceptor tyrosine kinase to bind and phosphorylate Plexin-A. The specific tyrosine residues phosphorylated in the cytoplasmic domain of plexins in response to semaphorin stimulation have not yet been identified.
Glycogenin 1 (GYG1) catalyzes its autoglycosylation reaction with UDP-glucose to form oligo (1,4)-alpha-D-glucosyl GYG1 (Moslemi et al. 2010). The oligosaccharide is annotated here as containing four glucose residues. Glycogenin occurs as a homodimer complexed with two molecules of glycogen synthase 1 (GYS1), here in an unphosphorylated (a) form (Roach et al. 2012).
Glycogenin 2 (GYG2) catalyzes its autoglycosylation reaction with UDP-glucose to form oligo (1,4)-alpha-D-glucosyl GYG2 (Mu et al. 1997). The oligosaccharide is annotated here as containing four glucose residues. Glycogenin occurs as a homodimer complexed with two molecules of glycogen synthase 1 (GYS2), here in a unphosphorylated (a) form (Roach et al. 2012).
As an alternative to LDLR-mediated uptake and degradation, a LDL particle can bind a single molecule of LPA (apolipoprotein A), forming a Lp(a) lipoprotein particle. Although LPA is synthesized in liver cells, LPA - LDL binding appears to occur primarily extracellularly in vivo, on the hepatocyte surface or in the blood (Lobentanz et al. 1998). Lp(a) particles are relatively long-lived, with a half-life in human plasma of three to four days (Krempler et al. 1980), and the molecular mechanism of their clearance from the blood in vivo remains obscure. Lp(a) particles are of clinical interest because elevated levels of them are correlated with elevated risk of coronary heart disease (reviewed by Marcovina et al. 2003).
Cytosolic glycogen branching enzyme (GBE1) associated with glycogen granules transfers terminal alpha(1,4) glucose blocks to form alpha(1,6) branches on growing glycogen molecules formed on glycogenin 1 (GYG1) complexed with unphosphorylated glycogen synthase 1 (GYS1-a) (Bao et al. 1996; Roach et al. 2012).
Cytosolic glycogen branching enzyme (GBE1) associated with glycogen granules transfers terminal alpha(1,4) glucose blocks to form alpha(1,6) branches on growing glycogen molecules formed on glycogenin 2 (GYG2) complexed with unphosphorylated glycogen synthase 2 (GYS2-a) (Bao et al. 1996; Roach et al. 2012).
Experiments using human cord blood CD4(+) T cells show 22 protein spots and 20 protein spots, upregulated and downregulated proteins respectively, following Interleukin-12 stimulation (Rosengren et.al, 2005). Among the up-regulated proteins is :Ras-related protein Ral-A(RALA).