Response of Cells in the Environment

In the absence of steroid, several(prenominal) steroid receptors may recruit corepressors (e.g. SMRT and NcoR) and histone deacetylase to repress transcription.

Ion channels atomic number 18 transmembrane proteins that allow ions to pass through (Overview, 2000). As to specificity, they are usually classified as calcium channels, sodium channels, potassium channels, and so on The channels may be volume-gated, ligand-gated, etc. The major grapheme of sodium and potassium channels is to regulate membrane potential drop. The major role of G-protein-coupled receptors is to transmit signals into the cell. They are characterized by having seven transmembrane segments, and crapper respond to a wide variety of agonists, including photons,

amines, hormones, neurotransmitters, and proteins. Some agonists sting to the extracellular part of the receptor and others to the transmembrane region. The G-protein-coupled receptor is actually the GTP-binding protein because in the active state it binds to GTP (guanosine triphosphate). There are two types of G-proteins: the heteromeric G protein, consisting of three subunits, and the monomeric small G protein. Adenyl cyclase catalyzes the conversion of ATP to cGMP, which is an chief(prenominal) second messenger in cells.

Signaling enzymes which are cell-surface receptors take serine/threonine kinases, guanylyl cyclase, and tyrosine kinase (Overview, 2005). Tyrosine kinase catalyzes the dephosphorylation of the tyrosine residue. Guany

Recent studies have shown that MUC1 is aberrantly convey in greater than 90 percent of breast carcinomas, further its function as a tumor antigen is not merely fully understood (Breast, 2003). Analysis of a primary military man adenocarcinoma showed that the MUC1 interacted with beta-catenin in both primary and metastatic tumors, plainly is dramatically increased in metastatic tumors.

The MUC1-cytoplasmic cosmos peptides, when added to the invasive MDA-MB-468 and MDA-MB-231 cell lines increases their invasive capability, and the peptides colocalize with both beta-catenin and the focal adhesion protein vinculin, broadly at sites of membrane invasion into a collagen matrix. This indicates that a potential for MUC1 promotion of invasive tumorigenesis in the breast is through the inflection of beta-catenin localization and subsequent cytoskeletal dynamics. MUC1 interacts not only with beta-catenin, but alike with erbB receptors, src, GSK-3beta and protein kinase Cdelta, so possibly promotes the disassembly of adherens junctions and the invasion of tumor cells.

Lacroix, M. 92000). Markers in breast firecer: MUC-1 mucin. Retrieved Feb. 27, 2005 from:

MUC1/SEC is secreted by the cells (Markers, 2000). It has an extracellular domain identical to that of MUC1/REP, but lacks a hydrophobic region that can anchor it to the cell membrane. MUC1/Y contains the cytoplasmic and transmembrane domains, but the extracellular domain is smaller, and lacks the repeat motif and its flanking regions. MUC1/Y may bear up under tyrosine and serine phosphorylation and can potentially bind second messenger proteins such(prenominal) as GRB2, initiating a cascade.

Http://web.indstate.edu/theme/mwking/signal-transdction.html

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