Heterogeneous expression of cell adhesion molecules by endothelial cells in ARDS

Müller, Annette; Cronen, Claus; Müller, Klaus‐Michael; Kirkpatrick, Charles James

doi:10.1002/path.1186

Cited by 65 publications

(41 citation statements)

References 29 publications

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“…Liapis and Hutton (1997) were still unable to detect specific immunoreactivity with several antibodies. A number of alternative buffers (Alsbeh and Battifora, 1995), varying the buffer pH (Grossfeld et al, 1996), or use of newly developed tissue fixatives (Muller et al, 1996) have been described. Even though the exact mechanism by which microwave heating works is still unclear (Shi et al, 1991(Shi et al, , 1995, signal detection for many commonly used antibodies is superior compared to other methods such as autoclave or water bath (Tani and Phillips, 1995).…”

Section: Discussionmentioning

confidence: 99%

Integrin characterization in pulmonary bronchioles

Blundell

Harrison

2005

Experimental and Molecular Pathology

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Integrins are a family of cell surface glycoproteins that act as receptors for ECM proteins or for membrane bound counter-receptors on other cells. The integrin receptor family of vertebrates includes at least 16 distinct a subunits and at least 8 h subunits which can associate to form more than 20 distinct integrins. So far, there are no published reports describing integrin characterization in mouse lung tissue and mouse Clara cells. This paper described the characterization of six integrins, mainly a 5 , a v , a 6 , h 1 , h 3 , and h 4 , in mouse pulmonary bronchioles and also in Clara cell cultures. a 5 , a v , a 6 , h 1 , and h 4 integrins were present in Clara cells both in tissue sections and cultures. h 3 integrin was found to be absent in mouse Clara cells.

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Section: Discussionmentioning

confidence: 99%

Integrin characterization in pulmonary bronchioles

Blundell

Harrison

2005

Experimental and Molecular Pathology

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“…HUVEC are known to express various cell adhesion molecules including ICAM-1, VCAM-1, integrins, CD44H, and E-Selectin (40,41). It was found that pretreatment of the HUVEC monolayer with 25 g/ml antibodies against E-Selectin or CD44H before introduction of galectin-3-treated HCA1.7ϩ cells resulted in significant reduction (82 Ϯ 14%, p Ͻ 0.001 and 72 Ϯ 13%, p Ͻ 0.005, respectively, ANOVA) of the cell adhesion (Fig.…”

Section: Co-immunoprecipitation Of Endogenous Galectin-3 and Muc1 In mentioning

confidence: 99%

Galectin-3 Interaction with Thomsen-Friedenreich Disaccharide on Cancer-associated MUC1 Causes Increased Cancer Cell Endothelial Adhesion

Andrews

Zhao

et al. 2007

Journal of Biological Chemistry

272

258

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Patients with metastatic cancer commonly have increased serum galectin-3 concentrations, but it is not known whether this has any functional implications for cancer progression. We report that MUC1, a large transmembrane mucin protein that is overexpressed and aberrantly glycosylated in epithelial cancer, is a natural ligand for galectin-3. Recombinant galectin-3 at concentrations (0.2-1.0 g/ml) similar to those found in the sera of patients with metastatic cancer increased adhesion of MUC1-expressing human breast ( Galectin-3 is one of 15 known members of the galectin family of naturally occurring galactoside-binding lectins that are expressed intracellularly and extracellularly by many cell types (1). Galectin-3 concentrations are increased up to 5-fold in the sera of patients with breast, gastrointestinal, or lung cancer (2). Moreover, higher galectin-3 concentrations are seen in the sera of patients with metastatic disease than in the sera of patients with localized tumors (2). The source of increased circulating galectin-3 in cancer patients is not clear, but it is probably generated by tumor cells as well as by peritumoral inflammatory and stromal cells (2). It is not known whether this increased circulating galectin-3 has any functional implications for cancer progression.Cytoplasmic galectin-3 is known to be anti-apoptotic (3), whereas nuclear galectin-3 promotes pre-mRNA splicing (4, 5). Cell surface galectin-3 is involved in various cell-cell and cellmatrix interactions (1, 6, 7) and enhances cancer cell adhesion to and invasion through basement membrane by interacting with extracellular matrix proteins such as fibronectin, collagen, or laminin (1,8,9). Galectin-3 expressed on the endothelial cell surface has been shown to promote the adhesion of breast cancer cells to endothelium by interaction with cancer-associated Thomsen-Friedenreich (galactose ␤1,3N-acetylgalactosamine ␣Ϫ (TF)) 2 antigen expressed by unknown cell surface molecules (10 -14). TF antigen is the core I structure of mucin-type O-linked glycans, but in its simplest nonsialylated, nonextended form it acts as an oncofetal antigen, and its presence/expression is increased in malignant and premalignant epithelia (15).MUC1 (also known as episialin and DF3) is a large (M r Ͼ 250,000) transmembrane mucin protein expressed on the apical surface of most normal secretory epithelia including those in the mammary gland, and the gastrointestinal, respiratory, urinary, and reproductive tracts. The MUC1 extracellular domain consists of variable numbers of 20-amino acid tandem repeat peptides (VNTR) that are rich in serines, threonines, and prolines. These tandem repeat domains are heavily glycosylated

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“…Septic lung tissue presents strong staining of ICAM-1. 33 Various proinflammatory cytokines are believed to activate the increased expression of adhesion molecules. 34 On the other hand, ATRA treatment enhanced b 2 -integrin expression in an APL cell line.…”

Section: Figurementioning

confidence: 99%

Retinoic acid syndrome in NOD/scid mice induced by injecting an acute promyelocytic leukemia cell line

et al. 2004

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All-trans retinoic acid (ATRA) induces complete remission in patients with acute promyelocytic leukemia (APL). However, ATRA sometimes causes retinoic acid syndrome (RAS) characterized by respiratory distress, pleural effusions, fever and weight gain. To investigate the pathophysiology of RAS, we generated an animal model by injecting an APL cell line, NB4, into immunodeficient mice. When NOD/scid mice were injected intravenously with fully differentiated NB4 cells (1 Â 10 7 ) and then given a daily administration of ATRA, three of 12 mice died of pulmonary edema within 14 days. Pathologically, dilated lung capillary vessels and alveolar effusions were observed. After the injection, NB4 cells were detected in the lung within 2 days and in the pleural effusion later on. The gene expression levels of CXC chemokines (MIP-2 and KC) and ICAM-1 were increased in the lung and heart by the ATRA administration. In immunohistochemical analyses, MIP-2 was clearly detected in alveolar macrophages of the lung in mice with RAS. Dexamethasone treatment prevented the development of RAS and decreased the CXC chemokine mRNA expression in the lung. These findings suggested that the activation of adhesion molecules for leukocytes and expression of CXC chemokines in the lung are closely involved in triggering RAS.

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Heterogeneous expression of cell adhesion molecules by endothelial cells in ARDS

Cited by 65 publications

References 29 publications

Integrin characterization in pulmonary bronchioles

Integrin characterization in pulmonary bronchioles

Galectin-3 Interaction with Thomsen-Friedenreich Disaccharide on Cancer-associated MUC1 Causes Increased Cancer Cell Endothelial Adhesion

Retinoic acid syndrome in NOD/scid mice induced by injecting an acute promyelocytic leukemia cell line

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