Koutcherov_2007_J.Comp.Neurol_503_392

The organization of the adult human medial preoptic nucleus was studied by using chemoarchitectonic markers for acetylcholinesterase, nonphosphorylated neurofilament protein (SMI-32), calbindin-D28k, neuropeptide Y (NPY), melanin-concentrating hormone (MCH), cocaine- and amphetamine-regulated transcript (CART), and 3-fucosyl-N-acetyl-lactosamine (CD15) to establish human homologs to the subnuclei making up MPO in the rat, where their connections and functional significance are better understood. The human MPO comprises three subnuclei, the medial MPO, the lateral MPO, and the dorsomedially positioned uncinate subnucleus. As in the rat, the human medial MPO is magnocellular and contains numerous NPY- and CART-immunoreactive fibers and terminals as well as calbindin-positive neurons. The human lateral MPO, like its homolog in the rat, distinctively features numerous MCH-positive fibers and terminals as well as SMI-32-immunoreactive fibers. The uncinate subnucleus is wedged between the lateral surface of the paraventricular nucleus and the medial MPO and is characterized by variable NPY- and CART-immunoreactive fibers and terminals, also seen in the rat central MPO, suggesting that the subnuclei are homologues. The intermediate nucleus was distinguished by CD15-positive neuronal staining, whereas the majority of its neurons also contained acetylcholinesterase. The human intermediate nucleus is positioned on the lateral surface of MPO and by its chemo- and cytoarchitecture constitutes a distinct nucleus of the preoptic area characterized by close structural association with the MPO complex. These findings demonstrate that the human MPO is organized similarly to the rat MPO, in chemo- and cytoarchitectonically distinct subnuclei, which implies differences in their functional specialization, as seen in the rat.