Dataset Information

Consequences of PNU 282987 treatment in GCs exposed to 1% O2 for 24 h

ABSTRACT: Previous studies suggested a role of acetylcholine (ACh) in the regulation of the ovary. A target receptor, alpha 7 nicotinic ACh receptor (CHRNA7; encoded by CHRNA7), is expressed in the human ovary, e.g. by stromal cells, oocytes and human granulosa cells (GCs). The objective of this study was to explore its functions in cultured, in vitro fertilization (IVF)-derived GCs. For this, GCs exposed to 1% O2 were treated with the selective CHRNA7-agonist PNU 282987 for 24 h.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Granulosa Cell

SUBMITTER: Thomas Fröhlich

LAB HEAD: Thomas Fröhlich

PROVIDER: PXD059511 | Pride | 2025-09-02

REPOSITORIES: Pride

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Publications

Activation of the Alpha 7 Nicotinic Acetylcholine Receptor (CHRNA7) Limits Hypoxia-induced Inflammatory Responses and Regulates Collagens in Cultured Human Granulosa Cells.

Seßenhausen Pia P Caban Karolina M KM Schneider Michaela M Eubler Katja K Kreitmair Nicole N Schneider Julia J Dissen Gregory A GA Berg Dieter D Berg Ulrike U Stöckl Jan B JB Kunz Lars L Fröhlich Thomas T Mayerhofer Artur A

Biology of reproduction 20250823

The alpha 7 nicotinic acetylcholine (ACh) receptor (CHRNA7) is targeted by ACh, choline and exogenous chemicals, including nicotine and insecticides. According to database searches, it is expressed by several cell types of the human ovary, including granulosa cells (GCs). This expression site was confirmed by immunohistochemistry in human and nonhuman primate ovaries. Cultured human GCs, derived from in vitro-fertilization, express functional CHRNA7, indicated by acutely elevated intracellular C ...[more]

PMID: 40847805

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Project description:Myeloperoxidase (MPO), an important diprotomeric glycoprotein in neutrophil-mediated immunity, produces microbicidal hypohalous acids, but the underpinning glycobiology remains elusive. Deep characterisation of neutrophil-derived MPO (nMPO) using advanced mass spectrometry demonstrated that under-processed oligomannosidic- and hyper-truncated paucimannosidic- and N-acetyl-β-D-glucosamine (GlcNAc) core-type asparagine-linked glycans decorate the protein. Occlusion of Asn355 and Asn391 and sterical hindrance of Asn323- and Asn483-glycans located in the MPO dimerisation zone were found to shape the local glycan processing thereby providing a molecular basis of the site-specific nMPO glycosylation. Native mass spectrometry, mass photometry, and glycopeptide profiling revealed extreme molecular complexity of diprotomeric nMPO arising from heterogeneous glycosylation, oxidation, chlorination and polypeptide truncation variants, and a lower-abundance monomer. Longitudinal profiling of maturing, mature, granule-separated, and pathogen-activated neutrophils demonstrated that MPO is dynamically expressed during granulopoiesis, unevenly distributed across granules and rapidly degranulated, but surprisingly carries uniform glycosylation across conditions. Complete proMPO-to-MPO maturation evidently occur during early/mid-stage granulopoiesis. The conserved Asn355- and Asn391-sequons displayed elevated GlcNAc signatures and higher oxidation and chlorination activity of the secretory vesicle/plasma membrane-resident MPO relative to MPO from other granules. Endoglycosidase H-treated nMPO displaying Asn355-/Asn391-GlcNAcylation recapitulated the activity gain and showed increased thermal stability and polypeptide accessibility relative to untreated nMPO as measured by activity assays, circular dichroism and molecular dynamics. Endoglycosidase H-treated nMPO also demonstrated elevated ceruloplasmin-mediated inhibition relative to nMPO. Modelling revealed that hyper-truncated Asn355-glycans positioned in the MPO:ceruloplasmin interface are critical for uninterrupted inhibition. We report on novel bimodal roles of the peculiar MPO glycosylation providing new insight into neutrophil glycobiology.

			Action	DRS
	Sample_Inf.csv	Csv
	checksum.txt	Txt
	hGC_PNU_CO_1_2682.d.zip	Other
	hGC_PNU_CO_2_2684.d.zip	Other
	hGC_PNU_CO_4_2688.d.zip	Other