bioRxiv Science⌕ Search

Biology subjects

Steen, J.

Publications and source records attributed to Steen, J..

2 recordsLinked to original sources

Characterization of AZ12464237 as a high affinity, non-nucleotide antagonist radioligand for the P2Y12 receptor

The purinergic receptor P2Y12 (P2Y12R) is a well-recognized target for anti-thrombotic agents. This receptor is also expressed in microglia, where it plays a key role in neuroinflammation and microglia activation. To investigate P2Y12R-mediated actions in the central nervous system (CNS), the development of novel brain-penetrant ligands is essential, along with further in vitro studies. A radiolabeled, easily accessible tool compound would significantly advance such drug discovery efforts. Herein, we describe the 3H-labeling of a non-nucleotide P2Y12R antagonist AZ12464237, and its in vitro binding properties to the receptor in membrane preparations form transfected cells, as well as on mouse brain tissues. The radioligand shows high affinity toward both the human and rat P2Y12R in transfected cells, with Kd values of 3.12 {+/-} 0.70 nM (human) and 16.6 {+/-} 3.4 nM (rat), as determined by saturation binding studies. The binding kinetics of [3H]AZ12464237 are rapid with a short target residence time ([~]1 min). We further confirmed the selectivity of the radioligand by performing competitive displacement studies, in which reported P2Y12R ligands and other P2Y receptors ligands were tested for binding against [3H]AZ12464237. Additionally, the radioligand proved useful for in vitro autoradiography studies on mouse brain tissues, although a small amount of off-target binding was observed in P2Y12R knock-out mice. This could be traced to glycogen synthase kinase 3 . Considering the growing interest in P2Y12R as a biomarker for microglia activation, [3H]AZ12464237 represents a promising tool for in vitro studies, including screening assays aimed at identifying novel P2Y12R ligands for CNS applications.

pharmacology and toxicology↗

Phosphorylation-dependent control of Arc protein by synaptic plasticity regulator TNIK

Activity-regulated cytoskeleton-associated protein (Arc) is an immediate-early gene product that support neuroplastic changes important for cognitive function and memory formation. As a protein with homology to the retroviral Gag protein, a particular characteristic of Arc is its capacity to self-assemble into virus-like capsids that can package mRNAs and transfer those transcripts to other cells. Although a lot has been uncovered about the contributions of Arc to neuron biology and behavior, very little is known about how different functions of Arc are coordinately regulated both temporally and spatially in neurons. The answer to this question we hypothesized must involve the occurrence of different protein post-translational modifications acting to confer specificity. In this study, we used mass spectrometry and sequence prediction strategies to map novel Arc phosphorylation sites. Our approach led us to recognize serine 67 (S67) and threonine 278 (T278) as residues that can be modified by TNIK, which is a kinase abundantly expressed in neurons that shares many functional overlaps with Arc and has, along with its interacting proteins such as the NMDA receptor, been implicated as a risk factor for psychiatric disorders. Furthermore, characterization of each residue using site-directed mutagenesis to create S67 and T278 mutant variants revealed that TNIK action at those amino acids can strongly influence Arcs subcellular distribution and self-assembly as capsids. Together, our findings reveal an unsuspected connection between Arc and TNIK. Better understanding of the interplay between these two proteins in neuronal cells could lead to new insights about apparition and progression of psychiatric disorders.

neuroscience↗