Up‐regulation of intercellular adhesion molecule 1 (ICAM‐1) on human renal cell carcinoma cells by interleukin‐4

Obiri, Nicholas I.; Tandon, Nandita; Puri, Raj K.

doi:10.1002/ijc.2910610509

Cited by 14 publications

(3 citation statements)

References 26 publications

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“…Consistent with our previous findings (4,23), the control ML neo cell line had considerable baseline expression of ICAM-1 (Fig. 4A, left panel), which was significantly enhanced by IL-13 or IL-4 treatment.…”

Section: Modulation Of Il-13r␣ and Il-13r␣ј Mrna Expression By ␥ C -Ssupporting

confidence: 92%

“…ICAM-1 mRNA expression was examined in ␥ c -positive ML␥ c and in ␥ c -negative ML neo control cells by Northern analysis (B). Ten micrograms total mRNA was electrophoresed through formaldehyde/agarose denaturing gel and analyzed for ICAM-1 mRNA expression as described previously (23). It is of interest that the ␥ c protein affected IL-13R rather than IL-4R in this manner because, although previous studies have shown that ␥ c is a natural component of IL-4R in a number of cell types, it has not been identified as a natural component of IL-13R in any cell type examined thus far (11).…”

Section: Figmentioning

confidence: 99%

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Modulation of Interleukin (IL)-13 Binding and Signaling by the γc Chain of the IL-2 Receptor

Obiri¹,

Murata²,

Debinski³

et al. 1997

Journal of Biological Chemistry

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Interleukin-13 (IL-13)1 and IL-4 are pleiotropic immune regulatory cytokines, which are predominantly produced by activated lymphocytes. Both cytokines mediate similar effects on B cells and monocytes; however, IL-13 has not been shown to have direct effects on T cells (1-3). The effects of both cytokines are mediated by cell surface receptors (R) that are specific for each of these ligands (4, 5). The receptor for IL-4 has been extensively investigated and its structure appears to vary with cell types. We have proposed three models for the structure of the IL-4R complex (6). However, despite their structural differences, all of the identified forms of the IL-4R complex are quite effective in transducing signals in response to IL-4 binding.Unlike the IL-4 receptor system, the receptor for IL-13 has not been well characterized. We have demonstrated that RCC cells express a large number of IL-13 binding sites and that these cells respond to IL-13 (4, 7). Cross-linking studies indicate that the IL-13R is predominantly composed of a ϳ65-70-kDa protein (4). RCC cells also express IL-4R, and 125

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Section: Modulation Of Il-13r␣ and Il-13r␣ј Mrna Expression By ␥ C -Ssupporting

confidence: 92%

Section: Figmentioning

confidence: 99%

Modulation of Interleukin (IL)-13 Binding and Signaling by the γc Chain of the IL-2 Receptor

Obiri¹,

Murata²,

Debinski³

et al. 1997

Journal of Biological Chemistry

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“…We also found that a variety of solid cancer cells overexpress high-affinity IL-4 receptors (IL-4R) (10)(11)(12). These receptors are functional because IL-4 is able to cause signal transduction, inhibit growth, upregulate major histocompatibility (MHC) antigens and intercellular adhesion molecule-1 (ICAM-1) on cancer cells (10)(11)(12)(13)(14)(15)(16)(17)(18)(19). IL-4R also are ex-pressed, although in low numbers, in normal immune cells such as T cells; B cells; monocytes; other blood cells, such as eosinophils, basophils, and fibroblasts; and endothelial cells (10,11).…”

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confidence: 99%

Human Breast Carcinoma Cells Express Type II IL-4 Receptors and Are Sensitive to Antitumor Activity of a Chimeric IL-4-Pseudomonas Exotoxin Fusion Protein in vitro and in vivo

Leland

Taguchi

Husain

et al. 2000

Mol Med

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IntroductionBreast cancer is the most common malignancy in women, resulting in the second most frequent Abstract Background: Human breast carcinoma cell lines express high-affinity interleukin-4 receptors (IL-4R). We examined the expression and structure of these receptors on primary and cultured breast carcinoma cell lines and normal breast epithelial cells. We also tested the antitumor activity in vitro and in vivo of a fusion protein comprised of circular permuted IL-4 and truncated Pseudomonas exotoxin, termed IL-4(38-37)-PE38KDEL. Materials and Methods: Eight different primary cell cultures and cell lines of human breast carcinomas were examined for the expression of IL-4R by radiolabeled binding, reverse transcription polymerase chain reaction (RT-PCR) and Northern analyses, and subunit structure by crosslinking studies. The antitumor activity of IL-4 toxin was tested in vitro by cytotoxicity assays and in vivo in a xenograft model in immunodeficient animals. Results: 125 I-IL-4 specifically bound to primary cell cultures and cell lines with a Kd ranging between 0.2 and 1 nM. Breast tumor cells were found to express IL-4Rͱ and IL-13RͰЈ chains, but not IL-2RͲ c chain. These cells were highly sensitive to the cytotoxic effect of IL-4(38-37)-PE38KDEL. The IC 50 (concentration inhibiting protein synthesis by 50%) ranged between approximately 0.005-1.5 nM. A normal breast epithelial cell culture was not sensitive to the cytotoxic activity of IL-4(38-37)-PE38KDEL. MDA-MB231 human breast carcinoma cell line formed a rapidly growing tumor in nude mice. Intratumor and intraperitoneal administration of IL-4(38-37)-PE38KDEL caused a dose dependent regression of established tumors. A control toxin, anti-Tac(Fv)-PE38KDEL, targeted to the IL-2 receptor Ͱ chain did not cause regression of these tumors. Conclusions: These results suggest that IL-4(38-37)-PE38KDEL may be a useful agent for targeting of IL-4 receptor positive human breast carcinomas and further studies should be performed to explore fully its potential.

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β1-integrins dominate cell traffic of leukemic cells in human bone-marrow stroma

Velde-Zimmermann¹,

Smits²,

Verdaasdonk³

et al. 1996

Int. J. Cancer

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The major function of bone marrow is growth stimulation and differentiation of hematopoietic stem cells (Dorshkind, 1990). In vitro studies of long-term bone-marrow cultures (LTBMC) have emphasized the essential role of bone-marrow stromal cells in hematopoiesis (Dorshkind, 1990). Colonization of bone-marrow precursor cells is mediated by contacts between adhesion receptors on bone-marrow stromal cells and on precursor hematopoietic cells (Leavesley et al., 1994). These precursor cells interact directly with stromal cells, but also indirectly via the extracellular matrix (ECM) proteins. As a result of this type of interaction, intracellular signalling of stromal cells can take place followed by activation and production of growth factors or cytokines. Growth factors and cytokines are essential for the regulation of cell growth and differentiation (Dorshkind, 1990). Different adhesion pathways have been described for the leukocyte-endothelial-cell interaction pathways (Elices et al., 1990). In particular, the role of integrins in cell contacts as well as in the linkage of ECM proteins with the intracellular signal transduction pathways seems to be essential in basic development of the hematopoiesis, but may also be significant in aberrant processes such as tumor-cell invasion (Juliano, 1994;Clark and Brugge, 1995). So far, for the leukemic-cell/bone-marrow stromal-cell interaction, integrins appear to be essential, but the details of this interaction remain largely unknown.The aim of this study was to investigate the variations in adhesion and migratory behavior of leukemic cells on human bone-marrow stromal cells. Therefore, we developed an in vitro model to study the basic interaction patterns of leukemic cells with human bone-marrow stromal cells. Adhesion, spreading and migration of erythroleukemic HEL92.1.7 and K562 cells together with the promyeloid HL60 cells on human BM stromal cells was monitored at the ultrastructural level and with phase-contrast microscopy. The role of adhesion molecules was studied, especially that of the pl-integrins. Discrete distribution of cell-surface molecules on these human leukemic cell lines and BM stromal cells was associated with a clear variation in adhesion and migration patterns. Adhesion and migration blocking studies using MAbs against the various adhesion molecules proved that the P1-integrins VLA-4 and VLA-5 in particular fulfil an essential function in tumor-cell adhesion and migration. MATERIAL AND METHODS Cells and culture conditionsBone-marrow stromal cells. Bone-marrow aspirates were obtained from donors without hematologic abnormalities, after informed consent. The aspirates were obtained from the sternum during coronary bypass operations and were diluted with an equal volume of RPMI 1640 containing heparin. A buf€y coat was isolated by centrifugation for 15 min at 2,000 rpm. Erythrocytes were lysed with NbCl(8.3 g/1 containing 1 g NaHC03 and 37 mg EDTA) buffer and washed 3 times with RPMI-1640 medium. The remaining cells were collected and cultured. A human b...

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Up‐regulation of intercellular adhesion molecule 1 (ICAM‐1) on human renal cell carcinoma cells by interleukin‐4

Cited by 14 publications

References 26 publications

Modulation of Interleukin (IL)-13 Binding and Signaling by the γc Chain of the IL-2 Receptor

Modulation of Interleukin (IL)-13 Binding and Signaling by the γc Chain of the IL-2 Receptor

Human Breast Carcinoma Cells Express Type II IL-4 Receptors and Are Sensitive to Antitumor Activity of a Chimeric IL-4-Pseudomonas Exotoxin Fusion Protein in vitro and in vivo

β1-integrins dominate cell traffic of leukemic cells in human bone-marrow stroma

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