Temporal proteomic profiling ofChlamydia trachomatis-infected HeLa-229 human cervical epithelial cells

PROTEOMICS ◽  
2016 ◽  
Vol 16 (9) ◽  
pp. 1347-1360 ◽  
Author(s):  
Grace Min Yi Tan ◽  
Hui Jing Lim ◽  
Tee Cian Yeow ◽  
Elaheh Movahed ◽  
Chung Yeng Looi ◽  
...  
2009 ◽  
Vol 199 (2) ◽  
pp. 227-235 ◽  
Author(s):  
Adam J. Potter ◽  
Stephen P. Kidd ◽  
Jennifer L. Edwards ◽  
Megan L. Falsetta ◽  
Michael A. Apicella ◽  
...  

Gene Reports ◽  
2022 ◽  
Vol 26 ◽  
pp. 101456
Author(s):  
Abbas Hadi Albosale ◽  
Olga Andreevna Garbuzova ◽  
Konstantin Alekseevich Kovalenko ◽  
Elena Vladimirovna Mashkina

2017 ◽  
Vol 7 (1) ◽  
Author(s):  
Jennifer Couret ◽  
Carley Tasker ◽  
Jaeha Kim ◽  
Tiina Sihvonen ◽  
Saahil Fruitwala ◽  
...  

Reproduction ◽  
2021 ◽  
Author(s):  
Ourlad Alzeus Gaddi Tantengco ◽  
Talar Kechichian ◽  
Kathleen L Vincent ◽  
Richard B Pyles ◽  
Paul Mark B Medina ◽  
...  

Ureaplasma parvum is a commensal bacterium in the female reproductive tract but has been associated with pregnancy complications such as preterm prelabor rupture of membranes and preterm birth (PTB). However, the pathologic effects of U. parvum in the cervix, that prevents ascending infections during pregnancy, are still poorly understood. To determine the impact of U. parvum on the cervix, ectocervical (ecto) and endocervical (endo) epithelial and stromal cells were incubated with U. parvum. Macrophages were also tested as a proxy for cervical macrophages to determine the antigenicity of U. parvum. The effects of U. parvum, including influence on cell cycle and cell death, antimicrobial peptide production, epithelial-to-mesenchymal transition (EMT), and inflammatory cytokine levels, were assessed. U. parvum colonized cervical epithelial and stromal cells 4 hours post-infection. Like uninfected control, U. parvum neither inhibited cell cycle progression and nor caused cell death in cervical epithelial and stromal cells. U. parvum increased the production of the antimicrobial peptides (AMPs) cathelicidin and human β-defensin 3 and exhibited weak signs of EMT evidenced by decreased cytokeratin 18 and increased vimentin expression in cervical epithelial cells. U. parvum induced a pro-inflammatory environment (cytokines) and increased MMP-9 in cervical epithelial cells but promoted pro- and anti-inflammatory responses in cervical stromal cells and macrophages. U. parvum may colonize the cervical epithelial layer, but induction of AMPs and anti-inflammatory response may protect the cervix and may prevent ascending infections that can cause PTB. These findings suggest that U. parvum is a weak inducer of inflammation in the cervix.


1994 ◽  
Vol 68 (2) ◽  
pp. 1173-1178 ◽  
Author(s):  
M Chen ◽  
N Popescu ◽  
C Woodworth ◽  
Z Berneman ◽  
M Corbellino ◽  
...  

1994 ◽  
Vol 58 (5) ◽  
pp. 713-720 ◽  
Author(s):  
Jie Zheng ◽  
Torsten Wahlström ◽  
Jorma Paavonen ◽  
Antti Vaheri

1993 ◽  
Vol 4 (6) ◽  
pp. 342-345 ◽  
Author(s):  
S L Patrick ◽  
T C Wright ◽  
H E Fox ◽  
H S Ginsberg

Women are infected with HIV in increasing numbers; the predominant mode of spread is through heterosexual transmission. Little is known regarding the mechanism of HIV transit through the female genital tract. We investigated whether early passaage cervical epithelial cells could be directly infected with HIV-1LAI*. Virus production was measured using the reverse transcriptase (RT) assay and direct assay for syncytia-forming units. In-situ hybridization was performed on infected cervical cell cultures. Immunostaining was carried out using a monoclonal antibody to leukocyte common antigen (LCA). Virus was recovered in the supernatants of all infected cervical cultures. Localization of HIV infection using in-situ hybridization identified rare cells in the population which gave a strong signal. These infected cells had a lymphoid morphology and were also detected using immunostaining for LAC. Cervical epithelial cells were uninfected in this in vitro model; cells in this population which supported viral replication were most likely of the macrophage/monocyte lineage.


1991 ◽  
Vol 36 (10) ◽  
pp. 737-745 ◽  
Author(s):  
J.C. Farges ◽  
M.L. Couble ◽  
A. Joffre ◽  
D.J. Hartmann ◽  
H. Magloire

2012 ◽  
Vol 302 (1) ◽  
pp. C27-C45 ◽  
Author(s):  
Boyang Zhao ◽  
Mark A. Knepper ◽  
Chung-Lin Chou ◽  
Trairak Pisitkun

Although extensive phosphoproteomic information is available for renal epithelial cells, previous emphasis has been on phosphorylation of serines and threonines with little focus on tyrosine phosphorylation. Here we have carried out large-scale identification of phosphotyrosine sites in pervanadate-treated native inner medullary collecting ducts of rat, with a view towards identification of physiological processes in epithelial cells that are potentially regulated by tyrosine phosphorylation. The method combined antibody-based affinity purification of tyrosine phosphorylated peptides coupled with immobilized metal ion chromatography to enrich tyrosine phosphopeptides, which were identified by LC-MS/MS. A total of 418 unique tyrosine phosphorylation sites in 273 proteins were identified. A large fraction of these sites have not been previously reported on standard phosphoproteomic databases. All results are accessible via an online database: http://helixweb.nih.gov/ESBL/Database/iPY/ . Analysis of surrounding sequences revealed four overrepresented motifs: [D/E]xxY*, Y*xxP, DY*, and Y*E, where the asterisk symbol indicates the site of phosphorylation. These motifs plus contextual information, integrated using the NetworKIN tool, suggest that the protein tyrosine kinases involved include members of the insulin- and ephrin-receptor kinase families. Analysis of the gene ontology (GO) terms and KEGG pathways whose protein elements are overrepresented in our data set point to structures involved in epithelial cell-cell and cell-matrix interactions (“adherens junction,” “tight junction,” and “focal adhesion”) and to components of the actin cytoskeleton as major sites of tyrosine phosphorylation in these cells. In general, these findings mesh well with evidence that tyrosine phosphorylation plays a key role in epithelial polarity determination.


1997 ◽  
Vol 75 (6) ◽  
pp. 855-859 ◽  
Author(s):  
G Castrilli ◽  
D Tatone ◽  
MG Diodoro ◽  
S Rosini ◽  
M Piantelli ◽  
...  

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