Embryo implantation triggers dynamic spatiotemporal expression of the basement membrane toolkit during uterine reprogramming.
Basement membranes (BMs) are specialized extracellular scaffolds that influence behaviors of cells in epithelial, endothelial, muscle, nervous, and fat tissues. Throughout development and in response to injury or disease, BMs are fine-tuned with specific protein compositions, ultrastructure, and localization. These features are modulated through implements of the BM toolkit that is comprised of collagen IV, laminin, perlecan, and nidogen. Two additional proteins, peroxidasin and Goodpasture antigen-binding protein (GPBP), have recently emerged as potential members of the toolkit. In the present study, we sought to determine whether peroxidasin and GPBP undergo dynamic regulation in the assembly of uterine tissue BMs in early pregnancy as a tractable model for dynamic adult BMs. We explored these proteins in the context of collagen IV and laminin that are known to extensively change for decidualization. Electron microscopic analyses revealed: 1) a smooth continuous layer of BM in between the epithelial and stromal layers of the preimplantation endometrium; and 2) interrupted, uneven, and progressively thickened BM within the pericellular space of the postimplantation decidua. Quantification of mRNA levels by qPCR showed changes in expression levels that were complemented by immunofluorescence localization of peroxidasin, GPBP, collagen IV, and laminin. Novel BM-associated and subcellular spatiotemporal localization patterns of the four components suggest both collective pericellular functions and distinct functions in the uterus during reprogramming for embryo implantation.
Department of Pathology, Microbiology, and Immunology, Vanderbilt University Medical Center, Nashville, TN, United States; Aspirnaut, Vanderbilt University Medical Center, Nashville, TN, United States.
Celestial R
CR
Jones-Paris
Aspirnaut, Vanderbilt University Medical Center, Nashville, TN, United States.
Sayan
S
Paria
Aspirnaut, Vanderbilt University Medical Center, Nashville, TN, United States.
Taloa
T
Berg
Valencia University Medical School, Valencia, Spain; Fibrostatin, SL, Valencia, Spain.
Juan
J
Saus
Division of Nephrology and Hypertension, Department of Medicine, Vanderbilt University Medical Center, Nashville, TN, United States; Center for Matrix Biology, Vanderbilt University Medical Center, Nashville, TN, United States.
Gautam
G
Bhave
Division of Neonatology, Department of Pediatrics, Vanderbilt University Medical Center, Nashville, TN, United States. Electronic address: bc.paria@Vanderbilt.Edu.
Bibhash C
BC
Paria
Department of Pathology, Microbiology, and Immunology, Vanderbilt University Medical Center, Nashville, TN, United States; Valencia University Medical School, Valencia, Spain; Division of Nephrology and Hypertension, Department of Medicine, Vanderbilt University Medical Center, Nashville, TN, United States; Center for Matrix Biology, Vanderbilt University Medical Center, Nashville, TN, United States; Department of Biochemistry, Vanderbilt University, Nashville, TN, United States; Department of Cell and Developmental Biology, Vanderbilt University Medical Center, Nashville, TN, United States; Vanderbilt Ingram Cancer Center, Nashville, TN, United States; Vanderbilt Institute of Chemical Biology Nashville, TN, United States. Electronic address: billy.hudson@Vanderbilt.Edu.
Billy G
BG
Hudson
D000818:Animals; D001485:Basement Membrane / Q000378:metabolism*; D024141:Collagen Type IV / Q000235:genetics* / Q000378:metabolism; D010064:Embryo Implantation / Q000187:drug effects / Q000235:genetics*; D016326:Extracellular Matrix Proteins / Q000235:genetics* / Q000378:metabolism; D005260:Female; D005455:Fluorescent Antibody Technique; D005786:Gene Expression Regulation; D007267:Injections; D007797:Laminin / Q000235:genetics* / Q000378:metabolism; D051379:Mice; D010446:Peptide Fragments / Q000235:genetics / Q000378:metabolism; D009195:Peroxidase / Q000235:genetics* / Q000378:metabolism; D011247:Pregnancy; D017346:Protein Serine-Threonine Kinases / Q000235:genetics* / Q000378:metabolism; D012333:RNA, Messenger / Q000235:genetics / Q000378:metabolism; D012715:Sesame Oil / Q000008:administration & dosage; D014599:Uterus / Q000187:drug effects / Q000378:metabolism*; D000097423:Peroxidasin
D024141:Collagen Type IV; D016326:Extracellular Matrix Proteins; D007797:Laminin; D010446:Peptide Fragments; D009195:Peroxidase; D017346:Protein Serine-Threonine Kinases; D012333:RNA, Messenger; D012715:Sesame Oil; D000097423:Peroxidasin; C000619517:Col4a1 protein, mouse; C502624:Col4a2 protein, mouse; C089141:laminin gamma 1; C535066:Col4a3bp protein, mouse
Basement membrane; Collagen IV; Goodpasture antigen-binding protein (GPBP); Laminin; Peroxidasin; Uterus