Inhibition of phagocyte chemotaxis by uteroglobin, an inhibitor of blastocyst rejection

Vasanthakumar, Geetha; Manjunath, Ramanathapuram; Mukherjee, Anil B.; Warabi, Haruaki; Schiffmann, Elliott

doi:10.1016/0006-2952(88)90204-3

Cited by 85 publications

(57 citation statements)

References 27 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Furthermore, exuberant neutrophil infiltration has also been reported in CCSP-deficient mice after infection with Pseudomonas aeruginosa (10) or adenovirus (8) and after ovalbumin challenge (38). CCSP has been reported to inhibit neutrophil chemotaxis in vitro (37) and to function via a receptor-mediated pathway (18). In addition, recent work has shown that peptides derived from CCSP attenuate IL-8-induced upregulation of ␤ 2 -integrins on neutrophils and subsequent adhesion to endothelial cells (42).…”

Section: Discussionmentioning

confidence: 99%

IL-13-induced Clara cell secretory protein expression in airway epithelium: role of EGFR signaling pathway

Kim

Shim

Burgel

et al. 2002

American Journal of Physiology-Lung Cellular and Molecular Phys

View full text Add to dashboard Cite

Previous work showed that the Th2 cytokine interleukin (IL)-13 induces goblet cell metaplasia via an indirect mechanism involving the expression and subsequent activation of epidermal growth factor receptor (EGFR). Because Clara cell secretory protein (CCSP) expression has been reported in cells that express mucins, we examined the effect of IL-13 on CCSP gene and protein expression in pathogen-free rat airways and in pulmonary mucoepidermoid NCI-H292 cells. Intratracheal instillation of IL-13 induced CCSP mRNA in epithelial cells without cilia within 8–16 h, maximal between 24 and 48 h; CCSP immunostaining increased in a time-dependent fashion, maximal at 48 h. The CCSP immunostaining was localized in nongranulated secretory cells and goblet cells and in the lumen. Pretreatment with the selective EGFR tyrosine kinase inhibitor BIBX1522, cyclophosphamide (an inhibitor of bone marrow leukocyte mobilization), or a blocking antibody to IL-8 prevented CCSP staining. Treatment of NCI-H292 cells with the EGFR ligand transforming growth factor-α, but not with IL-13 alone, induced CCSP gene and protein expression. Selective EGFR tyrosine kinase inhibitors, BIBX1522 and AG1478, prevented CCSP expression in NCI-H292 cells, but the platelet-derived growth factor receptor tyrosine kinase inhibitor AG1295 had no effect. These findings indicate that IL-13 induces CCSP expression via an EGFR- and leukocyte-dependent pathway.

show abstract

Section: Discussionmentioning

confidence: 99%

IL-13-induced Clara cell secretory protein expression in airway epithelium: role of EGFR signaling pathway

Kim

Shim

Burgel

et al. 2002

American Journal of Physiology-Lung Cellular and Molecular Phys

View full text Add to dashboard Cite

show abstract

“…Some of the biological properties of UG, such as masking the antigenicity of blastomeres (17)(18)(19) and epididymal spermatozoa (20), inhibition of monocyte and neutrophil chemotaxis and phagocytosis in vitro (21)(22)(23), and inhibition of ADP-and thrombin-induced (but not of arachidonic acid-induced) platelet aggregation (24), may be due, at least in part, to the potent inhibitory effect of this protein on PLA2 activity (25). A nonapeptide derived from the amino acid sequence of a-helix-3 of UG monomer (residues [39][40][41][42][43][44][45][46][47] possesses all the biological properties of the intact protein and has been identified as an active site of UG responsible for its PLA2-inhibitory and antiinflammatory activities (26)(27)(28)(29)(30)(31)(32)(33)(34)(35)(36)(37).…”

Section: Introductionmentioning

confidence: 99%

Tissue-specific expression of the gene coding for human Clara cell 10-kD protein, a phospholipase A2-inhibitory protein.

Peri

Cordella‐Miele²,

Miele³

et al. 1993

J. Clin. Invest.

119

View full text Add to dashboard Cite

“…While limited trophoblast invasion is essential for the establishment of normal pregnancy, dysregulation of this process may contribute to the pathogenesis of choriocarcinoma, a highly invasive and lethal form of cancer arising from the trophoblasts. We (6,27). Robinson et al (28) have reported an active transport of UG into the blastocoele of the preimplantation rabbit embryos, through the trophoblast layer via a carrier-mediated process.…”

mentioning

confidence: 99%

Recombinant human uteroglobin suppresses cellular invasiveness via a novel class of high-affinity cell surface binding site.

Kundu¹,

Mantile²,

Miele³

et al. 1996

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

The mechanism(s) that regulates invasion of trophoblasts through the uterine epithelium during embryo implantation and nidation in hemochorial placental mammals is poorly understood. While limited trophoblast invasion is essential for the establishment of normal pregnancy, dysregulation of this process may contribute to the pathogenesis of choriocarcinoma, a highly invasive and lethal form of cancer arising from the trophoblasts. We (6,27). Robinson et al. (28) have reported an active transport of UG into the blastocoele of the preimplantation rabbit embryos, through the trophoblast layer via a carrier-mediated process. As mentioned above, trophoblast cell migration and invasion through the endometrial epithelium is an essential prerequisite for the establishment of pregnancy. However, this invasion is a precisely regulated process, as the trophoblasts do not invade extrauterine organs. Since

show abstract

Inhibition of phagocyte chemotaxis by uteroglobin, an inhibitor of blastocyst rejection

Cited by 85 publications

References 27 publications

IL-13-induced Clara cell secretory protein expression in airway epithelium: role of EGFR signaling pathway

IL-13-induced Clara cell secretory protein expression in airway epithelium: role of EGFR signaling pathway

Tissue-specific expression of the gene coding for human Clara cell 10-kD protein, a phospholipase A2-inhibitory protein.

Recombinant human uteroglobin suppresses cellular invasiveness via a novel class of high-affinity cell surface binding site.

Contact Info

Product

Resources

About