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Biology subjects

Abhilasha, K. V.

Publications and source records attributed to Abhilasha, K. V..

3 recordsLinked to original sources

Light and temperature sensitive seizures are regulated by spatially distinct cortex glial populations in the central nervous system

Significance statementAstrocytic glia are present throughout mammalian brain. Whether astrocytes in different parts of the brain regulate neuronal function in spatially circumscribed manner is an area of intense research. Cortex glia of Drosophila shares significant similarities with mammalian astrocytes in their ability to interact with neuronal soma. In this study, we established intersectional methods to restrict expression of genes of interest to cortex glia specifically located in optic lobe or central brain or ventral nerve cord. Using epilepsy models, we show that light- and temperature-sensitive seizures are differentially regulated by spatially distinct cortex glia sub-population. Central brain specific cortex glia is important for regulating light-inducible seizures, whereas ventral nerve cord specific cortex glia is essential for suppression of temperature-sensitive seizures. Epilepsy is a brain disorder, characterized by recurrent seizures due to abnormal neuronal activity originating from a population of cortical neurons. It is known that seizures are often associated with abnormal glial cell function at the seizure focus. Recent studies have shown that each glial type such as astrocytes display significant degree of heterogeneity in their development, molecular signatures, and function depending on the brain region in which they are located. It is unknown if such heterogeneity differentially influence/cause seizures. Previous studies in Drosophila have shown that aberrant cortex glial function led to light inducible seizures in Ceramide phosphoethanolamine synthase (cpes) and temperature inducible seizures in zyd mutants. Here, we have optimized Gal4/Split-Gal4/Gal80/LexA drivers to specifically express a gene of interest throughout development in cortex glial subpopulations in different parts of the brain including optic lobe (OL), central brain (CB) and ventral nerve cord (VNC). Using these tools, we performed brain region specific cortex glial rescue experiments in cpes and zyd mutants. We found that OL and CB, but not VNC specific cortex glial expression of UAS CPES, were able to significantly suppress light inducible seizures in cpes mutants. In contrast, VNC but not OL or CB specific cortex glial expression of UAS Zyd suppressed temperature sensitive seizures. Further, in a third model, expression and activation of transient receptor potential (dTrpA1) just in the VNC specific cortex glia was sufficient to induce temperature sensitive seizures in wild type flies. Our findings suggest that regionally specialized cortex glial subtypes differentially regulate seizure susceptibility in seizure models.

neuroscience↗

Differential glycosylation of alpha-1-acid glycoprotein (AGP-1) contributes to its functional diversity.

Alpha-1-acid glycoprotein (AGP-1) is a positive acute phase glycoprotein with uncertain functions. Serum AGP-1 (sAGP-1) is primarily derived from hepatocytes and circulates as 12 to 20 different glycoforms. We isolated a glycoform secreted from stimulated human neutrophils (nAGP-1). Its peptide sequence was identical to hepatocyte-derived sAGP-1, but nAGP-1 differed from sAGP-1 in its chromatographic behaviour, electrophoretic mobility, and glycosylation. The function of these two glycoforms also differed. sAGP-1 activated neutrophil adhesion, migration and NETosis in a dose-dependent fashion, while nAGP-1 was ineffective as an agonist for these events. Furthermore, sAGP-1, but not nAGP-1, inhibited LPS-stimulated NETosis. However, nAGP-1 inhibited sAGP-1-stimulated neutrophil NETosis. The discordant effect of the differentially glycosylated AGP-1 glycoforms was also observed in platelets where neither of the AGP-1 glycoforms alone stimulated aggregation of washed human platelets, but sAGP-1, and not nAGP-1, inhibited aggregation induced by Platelet-activating Factor (PAF) or ADP, but not by thrombin. These functional effects of sAGP-1 correlated with intracellular cAMP accumulation and were accompanied by phosphorylation of the PKA substrate Vasodialator stimulated phosphoprotein (VASP) and reduction of Akt, ERK, and p38 phosphorylation. Thus, the sAGP-1 glycoform limits platelet reactivity while nAGP-1 glycoform also limits pro-inflammatory actions of sAGP-1. These studies identify new functions for this acute phase glycoprotein and demonstrate that the glycosylation of AGP-1 controls its effects on two critical cells of acute inflammation.

biochemistry↗

Acute phase protein, α-1-acid glycoprotein (AGP-1), has differential effects on TLR-2 and TLR-4 mediated responses.

Alpha-1-acid glycoprotein (AGP-1) is a major positive acute phase glycoprotein with unknown functions that likely plays a role in inflammation. We tested its involvement in a variety of inflammatory responses using human AGP-1 purified to apparent homogeneity and confirmed its identity by immunoblotting and mass spectrometry. AGP-1 alone upregulated MAPK signaling in murine peritoneal macrophages. However, when given in combination with TLR ligands, AGP-1 selectively augmented MAPK activation induced by ligands of TLR-2 (Braun lipoprotein) but not TLR-4 (lipopolysaccharide). In vivo treatment of AGP-1 in a murine model of sepsis with or without TLR-2 or TLR-4 ligands, selectively potentiated TLR-2-mediated mortality, but was without significant effect on TLR-4-mediated mortality. Furthermore, in vitro, AGP-1 selectively potentiated TLR-2 mediated adhesion of human primary immune cell, neutrophils. Hence, our studies highlight a new role for the acute phase protein AGP-1 in sepsis via its interaction with TLR-2 signaling mechanisms to selectively promote responsiveness to one of the two major gram-negative endotoxins, contributing to the complicated pathobiology of sepsis.

immunology↗