Gene expression differences in trabecular meshwork cells, grown in culture, from normal and glaucoma-stricken human eyes
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ABSTRACT:
ORGANISM(S): Mus musculus Homo sapiens
PROVIDER: GSE27058 | GEO | 2011/02/04
SECONDARY ACCESSION(S): PRJNA137617
REPOSITORIES: GEO
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Project description:Dr. Panjwani's laboratory is focusing on the mechanism by which galectins-3 and 7 mediate corneal epithelial cell migration. We are currently performing studies to: (i) identify and characterize the corneal epithelial cell surface and extracellular matrix (ECM) molecules which serve as counterreceptors of galectin-3 and -7, to establish whether the lectins modulate corneal epithelial cell migration by binding to well known integrins, growth factor receptors, and/or ECM molecules and (ii) determine whether galectin-3 mediates corneal epithelial cell migration indirectly by modulating the expression of key adhesion and/or signal transduction molecules by using small interfering RNA, cDNA microarrays and glycogene arrays.
2011-02-04 | GSE27057 | GEO
Project description:Dr. Panjwani's laboratory is focusing on the mechanism by which galectins-3 and 7 mediate corneal epithelial cell migration. We are currently performing studies to: (i) identify and characterize the corneal epithelial cell surface and extracellular matrix (ECM) molecules which serve as counterreceptors of galectin-3 and -7, to establish whether the lectins modulate corneal epithelial cell migration by binding to well known integrins, growth factor receptors, and/or ECM molecules and (ii) determine whether galectin-3 mediates corneal epithelial cell migration indirectly by modulating the expression of key adhesion and/or signal transduction molecules by using small interfering RNA, cDNA microarrays and glycogene arrays. It is known that a carbohydrate-binding protein, ELAM, serves as a marker for glaucoma. Other preliminary studies in my lab have shown that galectin-8 plays a role in the adhesion and spreading of trabecular meshwork cells (TM;the cells which modulate ocular pressure) and galectin-3 influences phagocytic capacity of TM cells. These studies suggest that galectins as well as ELAM and their counterreceptors may contribute to the pathogenesis of glaucoma. We have RNA preparations of five each of normal and glaucoma TM samples harvested over the last year from cadavers. We have RNA preparations of five each of normal and glaucoma TM samples harvested over the last yeat from cadavers.
2011-02-04 | E-GEOD-27057 | biostudies-arrayexpress
Project description:Dr. Panjwani's laboratory is focusing on the mechanism by which galectins-3 and 7 mediate corneal epithelial cell migration. We are currently performing studies to: (i) identify and characterize the corneal epithelial cell surface and extracellular matrix (ECM) molecules which serve as counterreceptors of galectin-3 and -7, to establish whether the lectins modulate corneal epithelial cell migration by binding to well known integrins, growth factor receptors, and/or ECM molecules and (ii) determine whether galectin-3 mediates corneal epithelial cell migration indirectly by modulating the expression of key adhesion and/or signal transduction molecules by using small interfering RNA, cDNA microarrays and glycogene arrays. We have prepared three independent preparations of total RNA of corneal epithelial cells from WT mice (total six samples) for analysis of glycogene expression. Samples are Normal Cornea (Left eye) and Laser ablation + 16-18 hours healing (right eye)
2010-12-11 | E-GEOD-26009 | biostudies-arrayexpress
Project description:Dr. Panjwani's laboratory is focusing on the mechanism by which galectins-3 and 7 mediate corneal epithelial cell migration. We are currently performing studies to: (i) identify and characterize the corneal epithelial cell surface and extracellular matrix (ECM) molecules which serve as counterreceptors of galectin-3 and -7, to establish whether the lectins modulate corneal epithelial cell migration by binding to well known integrins, growth factor receptors, and/or ECM molecules and (ii) determine whether galectin-3 mediates corneal epithelial cell migration indirectly by modulating the expression of key adhesion and/or signal transduction molecules by using small interfering RNA, cDNA microarrays and glycogene arrays. This study seeks the role of carbohydrate-based recognition system in the pathogenesis of glaucoma. In this study, RNA preparations of four normal and five glaucoma TM samples harvested over the last year from cadavers were hybridized and analyzed using the GLYCOv2 array. We have an NIH RO3 grant award to study the role of carbohydrate-based recognition system in the pathogenesis of glaucoma. In particular, it is known that a carbohydrate-binding protein, ELAM, serves as a marker for glaucoma. Other preliminary studies in my lab have shown that galectin-8 plays a role in the adhesion and spreading of trabecular meshwork cells (TM; the cells which modulate ocular pressure) and galectin-3 influences phagocytic capacity of TM cells. These studies suggest that galectins as well as ELAM and their counterreceptors may contribute to the pathogenesis of glaucoma. We would therefore like to compare glycogene expression patterns of normal and glaucomatous TM tissue. To this end, last month we submitted RNA preparations of five each of normal and glaucoma TM tissue harvested over the last year from cadavers. The data of these samples are now being analyzed. Meanwhile, we have analyzed RNA preparations of TM cells grown in culture from five normal and six glaucoma eyes. It is our hope that data from the two projects will enable us conclusively identify glycogenes which are differentially expressed in normal and glaucoma TM cell. Overall, the goal is to shed light on the role of carbohydrate-based recognition system and the carbohydrate-binding proteins in the pathogenesis of glaucoma.
2011-02-04 | E-GEOD-27058 | biostudies-arrayexpress
Project description:Dr. Panjwani's laboratory is focusing on the mechanism by which galectins-3 and 7 mediate corneal epithelial cell migration.
2010-12-11 | GSE26009 | GEO
Project description:Dr. Panjwani's laboratory is focusing on the mechanism by which galectins-3 and 7 mediate corneal epithelial cell migration. Recently published studies, that we have confirmed and expended on in our laboratory, clearly demonstrate that galectin-3 mediates angiogenesis in vitro and in vivo. More interestingly we have found that bFGF- and VEGF-mediated angiogenesis can be inhibited by galectin-3 inhibitors, which suggests an important role of carbohydrate recognition systems in the process of angiogenesis. In an effort to characterize the role of carbohydrate recognition system in angiogenesis, we are interested to evaluate and compare the glyco-gene expression profile of endothelial cells stimulated with VEGF, bFGF and galectin-3 at time and concentration at which, the compounds stimulate angiogenesis in vitro. RNA preparations of Galectin-3, VEGF, bFGF, Media Control biological replicates were sent to Microarray Core (E). The RNA was amplified, labeled, and hybridized to GLYCO_v3 microarrays.
2011-04-29 | E-GEOD-28943 | biostudies-arrayexpress
Project description:Dr. Panjwani's laboratory is focusing on the mechanism by which galectins-3 and 7 mediate corneal epithelial cell migration. Recently published studies, that we have confirmed and expended on in our laboratory, clearly demonstrate that galectin-3 mediates angiogenesis in vitro and in vivo. More interestingly we have found that bFGF- and VEGF-mediated angiogenesis can be inhibited by galectin-3 inhibitors, which suggests an important role of carbohydrate recognition systems in the process of angiogenesis. In an effort to characterize the role of carbohydrate recognition system in angiogenesis, we are interested to evaluate and compare the glyco-gene expression profile of endothelial cells stimulated with VEGF, bFGF and galectin-3 at time and concentration at which, the compounds stimulate angiogenesis in vitro.
2011-04-29 | GSE28943 | GEO
Project description:The reading of glycan-encoded signals by tissue lectins is considered a major route of the flow of biological information in many (patho)physiological processes. The arising challenge for current research is to proceed from work on a distinct protein to family-wide testing of lectin function. Having previously identified homodimeric galectin-1 and chimera-type galectin-3 as molecular switches in osteoarthritis progression, we here provide proof-of-principle evidence for an intra-network cooperation of galectins with three types of modular architecture. We show that the presence of tandem-repeat-type galectin-8 significantly correlated with cartilage degeneration and that it is secreted by osteoarthritic chondrocytes. Glycan-inhibitable surface binding of galectin-8 to these cells increased gene transcription and the secretion of functional disease markers. The natural variant galectin-8 (F19Y) was less active than the prevalent form. Genome-wide array analysis revealed induction of a pro-degradative/inflammatory gene signature, largely under control of NF-κB signaling. This signature overlapped with respective gene-expression patterns elicited by galectins-1 and -3, but also presented supplementary features. Functional assays with mixtures of galectins that mimic the pathophysiological status unveiled cooperation between the three galectins. Our findings shape the novel concept to consider individual galectins as part of a so far not realized teamwork in osteoarthritis pathogenesis, with relevance beyond this disease.
2021-02-17 | GSE131822 | GEO
Project description:Dr. Liu's research group is interested in studying the expression and functions of galectin-3, -7 and -12, in particular the roles of these proteins in inflammation and neoplasm. Members of the galectin family are known to participate in cellular homeostasis by modulating cell growth, controlling cell cycle progression, and inducing or inhibiting apoptosis. It is known that some galectins have similar functions. However, it is not fully understood whether they work cooperatively or not. Recent reports suggest that gal-3 deficiency may induce changes in cellular homeostatic mechanisms, leading to changes in expression of other galectins and galectin-related proteins. To analyze the coordinate regulation of galectins in the face of gal-3 deficiency, gene expression patterns of gal-3 / and gal-3 -/- keratinocytes exposed to UVB were compared. Murine epidermal keratinocytes from gal-3 / and gal-3 -/- mice will be irradiated with 200 J/m2 of UVB. Total RNA will be extracted at 0, 6, 12 and 24 h after irradiation. Classes were prepared in triplicate for a total of 24 samples. All samples were hybridized to the custom designed CFG GLYCOv2 glycogene array.
2011-03-02 | E-GEOD-27599 | biostudies-arrayexpress
Project description:Extracellular matrix interactions play essential roles in normal physiology and many pathological processes. Here, we report a novel screening platform capable of measuring phenotypic responses to combinations of ECM molecules. While the importance of ECM interactions in metastasis is well documented, systematic approaches to identify their roles in distinct stages of tumorigenesis have not been described. Using a genetic mouse model of lung adenocarcinoma, we measured the ECM-dependent adhesion of tumor-derived cells. Hierarchical clustering of adhesion profiles generated using this platform differentially segregated metastatic cell lines from primary tumor lines. Furthermore, we uncovered that metastatic cells selectively associate with fibronectin when in combination with galectin-3, galectin-8, or laminin. These interactions appear to be mediated in part by α3β1 integrin both in vitro and in vivo. We show that these galectins also correlate with human disease at both a transcriptional and histological level. Thus, our in vitro platform allowed us to interrogate the interactions of metastatic cells with their surrounding environment, and identified ECM and integrin interactions that could lead to therapeutic targets for metastasis prevention. Cell lines derived from murine lung primary adenocarcinomas and their metastases (Winslow et al., 2011 Nature 473:101-104)
2012-10-11 | E-GEOD-40222 | biostudies-arrayexpress