Disease relevance of MSN

• Ezrin/radixin/moesin proteins are high affinity targets for ADP-ribosylation by Pseudomonas aeruginosa ExoS [1].
• The moesin labelling in melanoma cells was downregulated with the depth of dermal invasion [2].
• Subcellular expression of moesin was studied on cultured human endothelial cells of umbilical cord veins and the mesothelioma cell line CH3LC by confocal laser scanning microscopy [3].
• The purpose of the study is to assess the shifts in cellular distribution of moesin in normal oral epithelium, oral epithelial dysplasia (OED), verrucous carcinoma (VC), and oral squamous cell carcinoma (OSCC) [4].
• Verrucous carcinoma was weakly positive, with a tendency for the moesin to be distributed in the cell membrane [5].
• Moesin was secreted from several myeloid leukemia cell lines other than UT-7, such as OUN-1 and K562, as an exosomal protein [6].

Psychiatry related information on MSN

• The course was developed for students who were in their final semester of completing requirements for an MSN degree with a major in psychiatric/mental health nursing [7].
• The American Nephrology Nurses' Association (ANNA) broke ground in specialty nursing last Fall by holding two Consensus Development Conferences in La Jolla, CA, and Chicago. In this opening presentation to conference attendees, Facilitator Anne Keane, EdD, MSN, RN, laid the groundwork to reach consensus for practice in the 21st century [8].
• In this interview, Virginia Trotter Betts, JD, MSN, RN, FAAN, a former American Nurses Association (ANA) president who has served in leading national health policy roles, discusses her current role and experiences as Commissioner of the Tennessee Department of Mental Health and Developmental Disabilities [9].

High impact information on MSN

• A novel moesin-, ezrin-, radixin-like gene is a candidate for the neurofibromatosis 2 tumor suppressor [10].
• A novel moesin-, ezrin-, radixin-like gene is a candidate for the neurofibromatosis 2 tumor suppressor [11].
• Localization of informational molecules at the oocyte posterior is strongly affected, thus indicating a role for moesin in anchoring these determinants [12].
• Treatment of cells with the Syk inhibitor piceatannol and overexpression of either a Syk dead kinase mutant or an ITAM-mutated moesin abrogated PSGL-1-induced transcriptional activation [13].
• Here, we demonstrate that TCR-induced exclusion of the large sialoprotein CD43 from the synapse is an active event mediated by its reversible binding to moesin [14].

Chemical compound and disease context of MSN

• Merlin does not localize to the same structures as either ezrin or moesin in human meningioma cells, suggesting a function distinct from these ERMs [15].
• In an ongoing phase II trial conducted in advanced breast cancer, we tested a therapy schedule consisting of continuous, 24-h infusion of 5 g/m2 ifosfamide (IFO) in 3 1 dextrose saline with mesna (MSN), repeated every 3 weeks until disease progression [16].
• MLC phosphorylation, moesin phosphorylation, and shape change were blocked by preincubating platelets with C3 transferase from Clostridium botulinum and Y-27632-specific inhibitors of Rho and Rho kinase, respectively [17].

Biological context of MSN

• Structure and localization on the X chromosome of the gene coding for the human filopodial protein moesin (MSN) [18].
• Altogether, these data indicate that moesin interacts with ICAM-3 and CD44 adhesion molecules in uropods of polarized T cells; these data also suggest that these interactions participate in the formation of links between membrane receptors and the cytoskeleton, thereby regulating morphological changes during cell locomotion [19].
• Increased phosphorylation of moesin in cells correlated with increased association of moesin with the cortical actin cytoskeleton [20].
• Here we show that C-terminal phosphorylation of full-length, dormant ezrin and moesin by protein kinase C-theta simultaneously unmasks both the F-actin and EBP50 binding sites [20].
• Moreover, the moesin-ICAM-3 association correlates with the degree of cell polarity [21].

Anatomical context of MSN

• Here, we have localized the coding gene (MSN) to Xq11.2-q12 by Southern and Western blot analyses of Chinese hamster x human somatic cell hybrids and by fluorescence chromosomal in situ hybridization [18].
• Moesin interacts with the cytoplasmic region of intercellular adhesion molecule-3 and is redistributed to the uropod of T lymphocytes during cell polarization [19].
• VCAM-1 interacted directly with moesin and ezrin in vitro, and all of these molecules colocalized at the apical surface of endothelium [22].
• Moesin (membrane-organizing extension spike protein, pronounced mó ez in) has previously been isolated from bovine uterus and characterized as a possible receptor protein for heparan sulfate [23].
• Moesin from PMA-stimulated lymphocytes, but not from unstimulated lymphocytes, bound to L-selectin tail [24].

Associations of MSN with chemical compounds

• Moesin was metabolically labeled by [32P]orthophosphate and reacted with an antibody against phosphotyrosine [3].
• Moesin also contains carbohydrate residues as demonstrated by immunostainings of digoxigenin-labeled sugar residues [3].
• Polarization and interaction of adhesion molecules P-selectin glycoprotein ligand 1 and intercellular adhesion molecule 3 with moesin and ezrin in myeloid cells [25].
• Interaction of PSGL-1 with moesin was shown in HL-60 cell lysates by isolating a complex with glutathione S-transferase fusions of the cytoplasmic domain of PSGL-1 [25].
• Merlin and moesin were found to inhibit N-WASP-mediated actin assembly in vitro, a function that appears independent of their ability to bind actin [26].

Physical interactions of MSN

• Furthermore, our data indicate that moesin is identical to the 77-kDa band that copurifies with ezrin in its isolation from human placenta [Bretscher, A. (1989) J. Cell Biol. 108, 921-930] [23].
• Our data show that moesin co-immunoprecipitated with PECAM-1 in lysates from thrombin-stimulated, but not resting platelets [27].
• Biochemical analyses showed that ezrin and moesin coimmunoprecipitated with CD43 in T lymphoblasts [28].
• Immunoprecipitation showed that moesin coprecipitates with TLR4, a well-known lipopolysaccharide receptor, suggesting an early role of moesin in the formation of the initiation complex for lipopolysaccharide signaling [29].
• We have previously shown that moesin was not involved in the binding to CD95 [30].

Co-localisations of MSN

• Furthermore, PECAM-1 co-localized with moesin at the cell periphery and in filopodia of glass-activated platelets [27].
• The adhesion molecules PSGL-1 and ICAM-3 were found to colocalize with the cytoskeletal protein moesin in the uropod of stimulated neutrophils [25].

Regulatory relationships of MSN

• Moesin-negative ES cells expressing or not expressing human CD46 formed separate pieces of fragmented syncytia which were torn apart during spreading, whereas ES cells expressing moesin exhibited typical syncytia [31].
• Exclusion of CD43 from the immunological synapse is mediated by phosphorylation-regulated relocation of the cytoskeletal adaptor moesin [14].
• Pharmacologic disruption of interactions between moesin and F-actin in cells expressing PSGL-1 resulted in a dose-dependent inhibition of rolling on P-selectin [32].
• These data suggest an important role for moesin in lipopolysaccharide-induced TNF-alpha production, highlighting its importance in lipopolysaccharide-mediated signal transduction [29].
• Moesin is a widely expressed phospho-protein that links many transmembrane molecules to the cortical actin cytoskeleton [14].
• We propose that activated moesin promotes F-actin redistribution and CD4-CXCR4 clustering and is also required for efficient X4-tropic HIV-1 infection in permissive lymphocytes [33].

Other interactions of MSN

• This association is mediated by the actin-linking proteins moesin and ezrin, which directly interact with Syk in an ITAM-dependent manner [13].
• A correlation between the degree of moesin-ICAM-3 interaction and cell polarization was found as determined by immunofluorescence and immunoprecipitation analysis done in parallel [19].
• In addition, moesin is associated with CD44, but not with ICAM-1, in polarized T lymphocytes [19].
• Our observations suggest that moesin may play a role in platelet adhesion, linking PECAM-1 with the actin cytoskeleton [27].
• Moesin is the quantitatively dominant ERM protein in these cells and the only one in platelets [34].

Analytical, diagnostic and therapeutic context of MSN

• Using immunohistochemistry we investigated the expression of moesin in normal epidermis and various kinds of epithelial skin tumors: squamous cell carcinoma, verrucous carcinoma, Bowen's disease, solar keratosis, keratoacanthoma, basal cell carcinoma, and extramammary Paget's disease [5].
• Bands of 78- and 81-kd were identified as moesin and ezrin by Western blot analysis [25].
• Dynamic fluorescence videomicroscopy analyses of migrating lymphocytes demonstrated that PSGL-1 and moesin redistributed towards the cellular uropod at the trailing edge of these cells, where activated ezrin/radixin/moesin (ERM) proteins were located [35].
• Here we show that a stable complex of ezrin and moesin can be isolated from cultured cells by immunoprecipitation with specific antibodies [36].
• Ezrin and moesin, human proteins that functionally link the cytoskeleton to the plasma membrane, were identified as Sic-binding proteins by affinity chromatography and matrix-assisted laser desorption/ionization time-of-flight mass spectrometry analysis [37].

References