PXD055537

PXD055537 is an original dataset announced via ProteomeXchange.

Title	Lysyl Oxidases are Necessary for Myometrial Contractility and On-Time Parturition in Mice
Description	The extracellular matrix (ECM) plays a pivotal role in the maintenance of tissue mechanical homeostasis. Collagens and elastic fibers are the most predominant fibrous ECM proteins providing tissue mechanical function through covalent cross-linking, which is mediated by the lysyl oxidase family of enzymes. In this study, the function of lysyl oxidases in maintaining the integrity of the extracellular matrix in the myometrium and its impact on parturition-timing was investigated. Gene and protein expression analyses demonstrate that a subset of the lysyl oxidase family of enzymes are highly induced in pregnant myometrium. Inhibition of the activity of the lysyl oxidase family of enzymes through β-aminopropionitrile (BAPN) delays parturition in mice, in part because of myometrial dysfunction. In BAPN-treated mice, the expression of genes encoding contraction-associated proteins such as connexin 43, oxytocin receptor, and prostaglandin synthase 2, is significantly reduced in the myometrium compared to the untreated control mice. Proteomic analysis revealed that the composition of the ECM is altered in response to BAPN treatment, which demonstrates that the inhibition of the activity of lysyl oxidases disrupted the integrity of the myometrial ECM. Our findings demonstrate that the lysyl oxidases-mediated ECM function is necessary for the myometrium to transition from a quiescent to a contractile phenotype at term for on-time parturition.
HostingRepository	PRIDE
AnnounceDate	2025-04-18
AnnouncementXML	Submission_2025-04-18_09:06:23.304.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Ying Wai Lam
SpeciesList	scientific name: Mus musculus (Mouse); NCBI TaxID: 10090;
ModificationList	TMT6plex-126 reporter+balance reagent acylated residue; monohydroxylated residue; iodoacetamide derivatized residue
Instrument	Orbitrap Eclipse

Revision	Datetime	Status	ChangeLog Entry
0	2024-09-04 03:32:03	ID requested
⏵ 1	2025-04-18 09:06:24	announced

10.1210/jendso/bvaf028;

Ouellette A, Do C, Cohn-Guthrie S, Lam YW, Mahendroo M, Nallasamy S, Lysyl Oxidases Are Necessary for Myometrial Contractility and On-time Parturition in Mice. J Endocr Soc, 9(5):bvaf028(2025) [pubmed]

submitter keyword: Lysyl oxidase, Pregnancy,Extracellular matrix, Myometrium, Parturition

Shanmugasundaram Nallasamy
contact affiliation	Assistant Professor, Division of Reproductive Sciences Dept. of Obstetrics, Gynecology and Reproductive Sciences University of Vermont College of Medicine 89 Beaumont Avenue, Burlington, VT 05405 USA
contact email	Shanmugasundaram.Nallasamy@med.uvm.edu
lab head
Ying Wai Lam
contact affiliation	Vermont Biomedical Research Network Proteomics Facility Department of Biology University of Vermont
contact email	ylam@uvm.edu
dataset submitter

Dataset FTP location NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2025/04/PXD055537

PRIDE project URI

• PRIDE
  1. PXD055537
     1. Label: PRIDE project
     2. Name: Lysyl Oxidases are Necessary for Myometrial Contractility and On-Time Parturition in Mice