A developmental switch between electrical and neuropeptide communication in the ventromedial hypothalamus.

Dissecting neural connectivity patterns within local brain regions is an essential step to understanding the function of the brain.1 Neural microcircuits in brain regions, such as the neocortex and the hippocampus, have been extensively studied.2 By contrast, the microcircuit in the hypothalamus remains largely uncharacterized. The hypothalamus is crucial for animals' survival and reproduction.3 Knowledge of how different hypothalamic nuclei coordinate with each other and outside brain regions for hypothalamus-related functions has been significantly advanced.4-9 Although there are limited studies on the neural microcircuit in the lateral hypothalamus (LHA)10,11 and the suprachiasmatic nucleus (SCN),12,13 the patterns of neural microcircuits in most of the given hypothalamic nuclei remain largely unknown. This study applied combinatory approaches to address the local neural circuit pattern in the ventromedial hypothalamus (VMH) and other hypothalamic nuclei. We discovered a unique neural circuit design in the VMH. Neurons in the VMH were electrically coupled at the early postnatal stage like ones in the neocortex.14 However, unlike neocortical neurons,14,15 they developed very few chemical synapses after the disappearance of electrical synapses. Instead, VMH neurons communicated with neuropeptides. The similar scarceness of synaptic connectivity found in other hypothalamic nuclei further indicated that the lack of synaptic connections is a unique feature for local neural circuits in most adult hypothalamic nuclei. Thus, our findings provide a solid synaptic basis at the cellular level to understand hypothalamic functions better.

[Change characteristics of soil available nitrogen and phosphorus and heavy metal contents after long-term cultivation of vegetables].

Soil samples were collected from three vegetable fields under different years of cultivation in Changsha suburbs of Hunan Province, South-central China to study the accumulation characteristics, risks, and sources of soil available nitrogen and phosphorus and heavy metals in the fields. With the increasing year of vegetable cultivation, the soil NO3(-)-N, Olsen-P, and heavy metals contents in the fields increased significantly. The average contents of soil NO3(-)-N, Olsen-P, and Cd in the vegetable fields having been cultivated for 1-2 years in Ningxiang County, 10-15 years in Changsha County, and 30 years in Kaifu District were 21.1, 31.9 and 0.33 mg x kg(-1), 42.0, 146.9 and 0.52 mg x kg(-1), and 49.5, 219.9 and 1.40 mg x kg(-1), respectively. The cumulative index (CI) of soil heavy metals generally followed the sequence of Cd >> Cu > Pb > Ni > Zn. Principal component analysis and cluster analysis showed that compared with soil NH4 OAc-extracted potassium, pH, organic matter and NH4(+)-N, that were dominated by natural factors, the soil Olsen-P and NO3(-)-N had the similar accumulation characteristics with the soil heavy metals, being mainly controlled by fertilization. It was considered that the soil environment and health quality of the vegetable fields in Changsha suburbs were not optimistic. The longer the cultivation year of vegetables, the more the soil NO3(-)-N, Olsen-P, and heavy metals accumulated in the fields. The accumulation of these elements in the fields could be primarily due to the long-term fertilization.

Identification of protein arginine methyltransferase 2 as a coactivator for estrogen receptor alpha.

In an attempt to isolate cofactors capable of influencing estrogen receptor alpha (ERalpha) transcriptional activity, we used yeast two-hybrid screening and identified protein arginine methyltransferase 2 (PRMT2) as a new ERalpha-binding protein. PRMT2 interacted directly with three ERalpha regions including AF-1, DNA binding domain, and hormone binding domain in a ligand-independent fashion. The ERalpha-interacting region on PRMT2 has been mapped to a region encompassing amino acids 133-275. PRMT2 also binds to ERbeta, PR, TRbeta, RARalpha, PPARgamma, and RXRalpha in a ligand-independent manner. PRMT2 enhanced both ERalpha AF-1 and AF-2 transcriptional activity, and the potential methyltransferase activity of PRMT2 appeared pivotal for its coactivator function. In addition, PRMT2 enhanced PR, PPARgamma, and RARalpha-mediated transactivation. Although PRMT2 was found to interact with two other coactivators, the steroid receptor coactivator-1 (SRC-1) and the peroxisome proliferator-activated receptor-interacting protein (PRIP), no synergistic enhancement of ERalpha transcriptional activity was observed when PRMT2 was coexpressed with either PRIP or SRC-1. In this respect PRMT2 differs from coactivators PRMT1 and CARM1 (coactivator-associated arginine methyltransferase). These results suggest that PRMT2 is a novel ERalpha coactivator.