scholarly journals Mechanism of Annexin I-Mediated Membrane Aggregation†

Biochemistry ◽  
2000 ◽  
Vol 39 (44) ◽  
pp. 13469-13477 ◽  
Author(s):  
Eduard Bitto ◽  
Ming Li ◽  
Aleksey M. Tikhonov ◽  
Mark L. Schlossman ◽  
Wonhwa Cho
Keyword(s):  
Annexin I ◽  
Membrane Aggregation

Reevaluation of annexin I expression in benign breast tissue and breast cancer

2006 ◽  
Vol 66 (S 01) ◽  
Author(s):  
R Speer ◽  
JD Wulfkuhle ◽  
D Wallwiener ◽  
E Solomayer ◽  
LA Liotta ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Breast Tissue ◽  
Annexin I ◽  
Benign Breast Tissue

scholarly journals Histidine Phosphorylation of Annexin I in Airway Epithelia

2000 ◽  
Vol 275 (47) ◽  
pp. 36632-36636 ◽  
Author(s):  
Richmond Muimo ◽  
Zuzanna Hornickova ◽  
Claudia E. Riemen ◽  
Volker Gerke ◽  
Harry Matthews ◽  
...  
Keyword(s):  
Airway Epithelia ◽  
Annexin I ◽  
Histidine Phosphorylation

scholarly journals The Annexin I Sequence Gln9-Ala10-Trp11-Phe12Is a Core Structure for Interaction with the Formyl Peptide Receptor 1

2010 ◽  
Vol 285 (19) ◽  
pp. 14338-14345 ◽  
Author(s):  
Charlotta Movitz ◽  
Lars Brive ◽  
Kristoffer Hellstrand ◽  
Marie-Josèphe Rabiet ◽  
Claes Dahlgren
Keyword(s):  
Core Structure ◽  
Formyl Peptide Receptor ◽  
Peptide Receptor ◽  
Annexin I ◽  
Formyl Peptide

Protein kinase C(alpha) actively downregulates through caveolae-dependent traffic to an endosomal compartment

2000 ◽  
Vol 113 (14) ◽  
pp. 2575-2584
Author(s):  
C. Prevostel ◽  
V. Alice ◽  
D. Joubert ◽  
P.J. Parker
Keyword(s):  
Plasma Membrane ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Initial Step ◽  
Receptor Internalization ◽  
Similar Process ◽  
Receptor Desensitization ◽  
Kinase C ◽  
Annexin I ◽  
Pkc Alpha

Receptor desensitization occurs through receptor internalization and targeting to endosomes, a prerequisite for sorting and degradation. Such trafficking processes may not be restricted to membrane associated receptors but may also play an important role in the downregulation of cytoplasmic transducers such as protein kinase C (PKC). It is demonstrated here that acute TPA exposure induces the transport of activated PKC(alpha) from the plasma membrane to endosomes. This process requires PKC activity and catalytically competent PKC can even promote a similar process for a truncated regulatory domain PKC(α) protein. It is established that PKC(α) is targeted to the endosome compartment as an active kinase, where it colocalizes with annexin I, a substrate of PKC. Thus, PKC(alpha) downregulation shares features with plasma membrane associated receptor sorting and degradation. However, it is shown that PKC(α) delivery to the endosome compartment is not a Rab5 mediated process in contrast to the well characterised internalisation of the transferrin receptor. An alternative route for PKC(alpha) is evidenced by the finding that the cholesterol binding drugs nystatin and filipin, known to inhibit caveolae mediated trafficking, are able to block PKC(alpha) traffic and down regulation. Consistent with this, the endosomes where PKC(alpha) is found also contain caveolin. It is concluded that the initial step in desensitisation of PKC(alpha) involves active delivery to endosomes via a caveolae mediated process.

scholarly journals Expression of lipocortins in human bronchial epithelial cells: effects of IL-1β , TNF-α, LPS and dexamethasone

1996 ◽  
Vol 5 (3) ◽  
pp. 210-217
Author(s):  
M. M. Verheggen ◽  
H. I. M. de Bont ◽  
P. W. C. Adriaansen-Soeting ◽  
B. J. A. Goense ◽  
C. J. A. M. Tak ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Bronchial Epithelium ◽  
Northern Blotting ◽  
Bronchial Epithelial Cells ◽  
Human Bronchial Epithelial Cells ◽  
Bronchial Epithelial ◽  
Annexin I ◽  
Tnf Α

In this study, we investigated the expression of lipocortin I and II (annexin I and I in the human bronchial epithelium, bothin vivoandin vitro. A clear expression of lipocortin I and II protein was found in the epithelium in sections of bronchial tissue. In cultured human bronchial epithelial cells we demonstrated the expression of lipocortin I and II mRNA and protein using Northern blotting, FACScan analysis and ELISA. No induction of lipocortin I or II mRNA or protein was observed after incubation with dexamethasone. Stimulation of bronchial epithelial cells with IL-1β, TNF-α or LPS for 24 h did not affect the lipocortin I or II mRNA or protein expression, although PGE2and 6-keto-PGF1αproduction was significantly increased. This IL-1β- and LPS-mediated increase in eicosanoids could be reduced by dexamethasone, but was not accompanied by an increase in lipocortin I or II expression. In human bronchial epithelial cells this particular glucocorticoid action is not mediated through lipocortin I or II induction.

scholarly journals Different molecular arrangements of the tetrameric annexin 2 modulate the size and dynamics of membrane aggregation

2010 ◽  
Vol 1798 (9) ◽  
pp. 1790-1796 ◽  
Author(s):  
Françoise Illien ◽  
Stefanie Finet ◽  
Olivier Lambert ◽  
Jesus Ayala-Sanmartin
Keyword(s):  
Annexin 2 ◽  
Membrane Aggregation

scholarly journals Evidence for specific annexin I-binding proteins on human monocytes

1996 ◽  
Vol 316 (2) ◽  
pp. 593-597 ◽  
Author(s):  
Nicolas J. GOULDING ◽  
L PAN ◽  
Kathleen WARDWELL ◽  
Veronica C. GUYRE ◽  
Paul M. GUYRE
Keyword(s):  
Monoclonal Antibody ◽  
Peripheral Blood ◽  
Binding Proteins ◽  
Human Peripheral Blood ◽  
Flow Cytometric Analysis ◽  
Blood Monocytes ◽  
Surface Binding ◽  
Peripheral Blood Monocytes ◽  
Cell Functions ◽  
Annexin I

Recombinant human annexin I and a monoclonal antibody specific for this protein (mAb 1B) were used to investigate surface binding of this member of the annexin family of proteins to peripheral blood monocytes. Flow cytometric analysis demonstrated trypsin-sensitive, saturable binding of annexin I to human peripheral blood monocytes but not to admixed lymphocytes. A monoclonal antibody that blocks the anti-phospholipase activity of annexin I also blocked its binding to monocytes. These findings suggest the presence of specific binding sites on monocytes. Furthermore, surface iodination, immunoprecipitation and SDS/PAGE analysis were used to identify two annexin I-binding proteins on the surface of monocytes with molecular masses of 15 kDa and 18 kDa respectively. The identification and characterization of these annexin I-binding molecules should help us to better understand the specific interactions of annexin I with monocytes that lead to down-regulation of pro-inflammatory cell functions.

Annexin-I expression modulates drug resistance in tumor cells

2004 ◽  
Vol 314 (2) ◽  
pp. 565-570 ◽  
Author(s):  
Ying Wang ◽  
Lucile Serfass ◽  
Marie-Odile Roy ◽  
Judy Wong ◽  
Anne-Marie Bonneau ◽  
...  
Keyword(s):  
Drug Resistance ◽  
Tumor Cells ◽  
Annexin I
Sign in / Sign up

Export Citation Format

Share Document