ABTB2

Litter size is one of the most important economic traits for pig production as it is directly related to the production efficiency. As an important litter size trait in pigs, the number of piglets born alive at birth (NBA) receives widespread interests in the pig industry. However, traits of piglets born dead, including the number of stillborn piglets (NS) and the piglets mummified at birth (NM) should be noted to explain the loss of reproduction. Herein, in the present study, a total of 803 producing sows were sampled and 2807 farrowing records for NBA, NM, and NS traits were collected in a Duroc swine population. Subsequently, a genome-wide association study (GWAS) was performed for NBA, NS and NM in parity groups 1 to 5. In total, 10 putative regions were found associated with these traits. After stepwise conditional analyses around the putative regions, eight independent signals were ultimately identified for NBA, NS, and NM, and there were seven promising candidate genes related to these traits, including ARID1A, RXRG, NFATC4, ABTB2, GRAMD1B, NDRG1, and APC. Our findings contribute to the understanding of the significant genetic causes of piglets born alive and dead, and could have a positive effect on pig production efficiency and economic profits.

Formation of Lewy body inclusions (LBs) in the substantia nigra (SN) is a very well-characterized pathol. hallmark of Parkinson′s disease (PD).LBs are aggregates of many biol. inactive proteins including structural elements, alpha-synuclein (asyn)-binding proteins, synphilin-1-binding proteins, and components of the ubiquitin-proteasome system, proteins implicated in cellular responses, proteins associated with phosphorylation and signal transduction, cytoskeletal proteins, cell cycle proteins, cytosolic proteins and many more.So far almost 76 proteins have been found to be associated with the formation of LBs.Deposition of LBs in the cell bodies and neurites often leads to the metabolic impairment and eventually the death of dopaminergic (DA) neurons.Therefore, lowering the burden of LBs is a potential challenge to restore the health and function of DA neurons.The most important strategy for minimizing the accumulation of LBs is preserving mitochondrial homeostasis.In a healthy neuron, mitochondrial biogenesis (mitogenesis) is required for the production of ATP, neurotransmitter release, calcium buffering, and augmentation of synaptic strength.However, during neurodegenerative condition, increased mitogenic response might bring opposite effect as it leads to the production of more depolarized mitochondria, reactive oxygen species (ROS), different inflammatory mediators including p38MAPK, Ras, Raf; and eventually the development of LB pathol.Therefore, tight regulation between mitochondrial biosynthesis and its breakdown is critical for the maintenance of neuronal health and function.Recently, our lab has delineated the role of a novel ankyrin-rich, BTB domain containing protein BPOZ-2 or ABTB2 in LB disease, which can also be a crucial regulator of mitochondrial quality control process.Our current perspective highlights the importance of BPOZ-2 inregulating mitochondrial damage control process and its therapeutic prospect in the treatment of LB disease.

Aggregation of α‐synuclein is a pathological hallmark of sporadic or familial PD. However, the detailed molecular mechanism responsible for the aggregation of α‐synuclein has not been properly explored. In the present study, we have identified a novel role of an anti‐tumorigenic BTB/POZ domain containing protein‐2 (BPOZ‐2) in the regulation of α‐synuclein accumulation in dopaminergic (DA) neurons. MPP+, an etiological factor for PD, significantly downregulated the expression of BPOZ‐2 ahead of α‐synuclein upregulation. Moreover, siRNA knockdown of BPOZ‐2 alone stimulated the aggregation of α‐synuclein protein; the effect was further induced in presence of MPP+ in mouse primary DA neurons. Finally, the absence of BPOZ‐2 in α‐synuclein expressing neuronal populations of MPTP‐intoxicated mouse and primate nigra indicates that the suppression of BPOZ‐2 could be involved in the accumulation of α‐synuclein protein.