Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:4.1.1.6 (CAD)
 4,420 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

To establish an efficient screening system for differentially expressed genes of a phytopathogenic fungus Colletotrichum lagenarium, we constructed an equalized (normalized) cDNA library from C. lagenarium and used this library for differential screening. For the isolation of genes involved in infection-related developments of conidia, conidia undergoing appressorium differentiation were selected as the source of materials for construction of the cDNA library. The equalization of cDNA was performed twice using a kinetic method, and the products were cloned into a plasmid vector. Colony hybridization with nine probes of different abundance showed a reduction in abundance variation from at least 276-fold in the original library to 10-fold in the equalized cDNA library, which demonstrated that the cDNA was successfully equalized. By differential hybridization of 1900 cDNA clones in the equalized cDNA library and RNA blot analysis of candidate clones, we identified 11 independent cDNA clones, designated CAD1 through CAD11, that were expressed in appressorium-differentiating conidia, but not in vegetative mycelia. The transcripts of CAD1 and CAD2 hardly accumulated in preincubated conidia, whereas those of CAD3 and CAD4 accumulated highly and slightly, respectively. The amount of the four CAD transcripts increased at the early stage of the appressorium formation process. Sequence analysis of CAD1 revealed that CAD1 would encode for 101 amino acid polypeptides, which showed homology to metallothioneins. Deduced amino acid sequence of CAD2 would encode 278 amino acid polypeptides, and showed high homology to genes in aflatoxin, and sterigmatocystin gene clusters of Aspergillus parasiticus and A. nidulans, respectively.
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PMID:Construction of an equalized cDNA library from Colletotrichum lagenarium and its application to the isolation of differentially expressed genes. 1072 83

Osteoblasts (OSTs) are derived from mesenchymal stem cells (MSCs) and coexist in close proximity with MSCs in bone during development and remodelling. Interactions between these two cell types remain obscure. Through a well-defined co-culture model, the present work demonstrated that OSTs regulate MSCs through the WNT and cadherin pathways. The regulation mechanism depends on the cell-cell contact mode (indirect or direct) between the two cell types. When physically separated (indirect contact), OSTs express WNTs and stimulate the osteogenic differentiation of MSCs through the activation of the WNT pathway and suppression of the cadherin pathway. This mechanism is evidenced by: (a) the elevation of cytoplasmic and nuclear unphosphorylated beta-catenin protein levels; (b) the suppression of beta-catenin degradation; (c) the increase in WNT-related transcription factor TCF1/LEF1; and (d) the loss of major bone-related cadherins (N-CAD and CAD11). Addition of DKK1 antagonizes the WNT pathway and diminishes the stimulatory effect of OSTs on MSCs. When in direct cell-cell contact, OSTs still secrete WNTs, whose binding still stabilizes the beta-catenin in MSCs. However, direct cell-cell contact induces the upregulation of cadherin pathway in MSCs, which suppresses the WNT pathway by containing cytoplasmic beta-catenin protein at a low level; consequently, the stimulatory effect of OSTs is negated. Regulation of cytoplasmic beta-catenin protein levels through concerted action or crosstalk between the WNT and cadherin pathways is the key to the signalling transduction in these cellular communication networks.
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PMID:Murine osteoblasts regulate mesenchymal stem cells via WNT and cadherin pathways: mechanism depends on cell-cell contact mode. 1803 91

Osteoblast cadherin (OB-cadherin, also known as cadherin-11) is a Ca(2+)-dependent homophilic cell adhesion molecule that is expressed mainly in osteoblasts. OB-cadherin is expressed in prostate cancer and may be involved in the homing of metastatic prostate cancer cells to bone. The extracellular domain of OB-cadherin may be used to inhibit the adhesion between prostate cancer cells and osteoblasts. In this report, we describe the expression of the extracellular domain of OB-cadherin as an Fc fusion protein (OB-CAD-Fc) in human embryonic kidney 293FT cells using a bicistronic retroviral vector. Coexpression of GFP and OB-CAD-Fc through the bicistronic vector permitted enrichment of OB-CAD-Fc-expressing cells by fluorescence-activated cell sorting. Recombinant OB-CAD-Fc proteins were secreted into cell medium, and about 0.85 mg of purified OB-CAD-Fc protein was purified from 1l of the conditioned medium using immobilized protein A-affinity chromatography. The purified OB-CAD-Fc was biologically active because it supported the adhesion of PC3 cells and L cells transduced with OB-cadherin. The availability of OB-CAD-Fc offers opportunities to test whether OB-CAD-Fc can be used to inhibit OB-cadherin-mediated prostate cancer bone metastasis in vivo or to generate antibodies for inhibiting the adhesion between prostate cancer cells and osteoblasts.
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PMID:Expression of the extracellular domain of OB-cadherin as an Fc fusion protein using bicistronic retroviral expression vector. 1862 62