Activin and inhibin are two closely related protein complexes that have almost directly opposite biological effects. Activins, members of the TGF-beta superfamily, are disulfide-linked dimeric proteins originally purified from gonadal fluids as proteins that stimulated pituitary follicle stimulating hormone (FSH) release. Inhibins/activins are involved in regulating a number of diverse functions such as hypothalamic and pituitary hormone secretion, gonadal hormone secretion, germ cell development and maturation, erythroid differentiation, insulin secretion, nerve cell survival, embryonic axial development or bone growth, depending on their subunit composition. Activins are homodimers or heterodimers of the various beta subunit isoforms, while inhibins are heterodimers of a unique alpha subunit and one of the various beta subunits.
Brain-Derived Neurotrophic Factor (BDNF) is a member of the neurotrophin family. Along with other structurally related neurotrophic factors NGF; NT-3 and NT-4; BDNF binds with high affinity to the TrkB kinase receptor. It also binds with the LNGFR (for low-affinity nerve growth factor receptor; also known as p75). BDNF promotes the survival; growth and differentiation of neurons. It serves as a major regulator of synaptic transmission and plasticity at adult synapses in many regions of the CNS. BDNF expression is altered in neurodegenerative disorders such as Parkinson's and Alzheimer's disease.
Bone Morphogenetic Protein-2 (BMP-2) is one of the bone-growth regulatory factors that belong to the transforming growth factor-beta (TGF-beta) superfamily of proteins. BMPs are synthesized as large precursor molecules, which are cleaved by proteolytic enzymes. The active form of BMP-2 can consist of a dimer of two identical proteins or a heterodimer of two related bone morphogenetic proteins.
Growth/differentiation factor 8(Mstn, GDF-8) is a member of the bone morphogenetic protein (BMP) family and the TGF-beta superfamily. This group of proteins is characterized by a polybasic proteolytic processing site which is cleaved to produce a mature protein containing seven conserved cysteine residues. It is expressed specifically in developing and adult skeletal muscle. It exists as a homodimer, and interacts with WFIKKN2, leading to inhibit its activity. This protein can act specifically as a negative regulator of skeletal muscle growth. It regulates cell growth and differentiation in both embryonic and adult tissues.
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