Glutamate is the most abundant excitatory neurotransmitter in the central nervous system of vertebrates. Once released into the synaptic cleft, it depolarizes the postsynaptic membrane and activates downstream signaling pathways, thereby propagating excitatory signals. The initial depolarization is primarily mediated by α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptors.
Actin is one of the most abundant proteins in eukaryotic cells and is a key component of the cytoskeleton, the internal framework of the cell. Its most remarkable characteristic is its dynamic nature—it can rapidly assemble and disassemble, thereby driving cell movement and changes in cell shape.
The transforming growth factor-β (TGF-β) superfamily comprises over 30 members, including TGF-β, Activin, Inhibin, bone morphogenetic proteins (BMPs), and growth differentiation factors (GDFs). It can be roughly divided into two subfamilies: the TGF-β/Activin/Nodal subfamily and the BMP/GDF/MIS (Müllerian inhibiting substrate) subfamily.
The transforming growth factor-β (TGF-β) superfamily comprises over 30 members, including TGF-β, Activin, Inhibin, bone morphogenetic proteins (BMPs), and growth differentiation factors (GDFs). It can be roughly divided into two subfamilies: the TGF-β/Activin/Nodal subfamily and the BMP/GDF/MIS (Müllerian inhibiting substrate) subfamily.
The first discovery of fetuin-A dates back to 1944 by K. Pedersen in the blood of a fetal calf (hence the name “fetuin”) . Many years later, the independent studies by J.F. Heremans and K. Schmid with W. Burgi in 1960 and 1961, respectively, purified fetuin-A in humans, and hence it is now also known as α2-Heremans-Schmid glycoprotein (AHSG) in recognition of the discoverers.
