FUT7: A Potential Drug Target and Biomarker (G2529)

Target Name: FUT7

NCBI ID: G2529

FUT7: A Potential Drug Target and Biomarker

Fucosyltransferase 7 (FUT7) is an enzyme involved in the transfer of fucose units from the 尾-glucose molecule to the 伪-glucose molecule in the glycosylation pathway. It is a key enzyme in the production of exoskeletal matrix (ESM) in bone marrow, which is a vital component of bone tissue. The production of ESM is essential for bone growth and maintenance, and alterations in ESM levels have been linked to various diseases, including bone loss, cancer, and neurodegenerative disorders.

FUT7 is a 21-kDa protein that consists of 156 amino acid residues. It is expressed in various tissues, including bone marrow, fat tissue, and the liver. FUT7 functions as a scaffold protein, helping to maintain the proper structure and stability of the ESM. It plays a crucial role in the regulation of ESM synthesis and degradation, as well as in the control of cell signaling pathways.

FUT7 has been identified as a potential drug target due to its involvement in various cellular processes that are associated with the development and progression of various diseases. One of the main reasons for its potential as a drug target is its involvement in the regulation of cell signaling pathways. FUT7 has been shown to play a role in the regulation of T cell development, and alterations in FUT7 function have been linked to T cell dysfunction and cancer.

In addition to its role in T cell development, FUT7 has also been shown to be involved in the regulation of cell adhesion, migration, and invasion. It has been shown to play a role in the development and maintenance of cancer stem cells, and has has been linked to the development of various types of cancer, including breast, ovarian, and prostate cancer.

FUT7 has also been shown to be involved in the regulation of inflammation and fibrosis. It has been linked to the production of pro-inflammatory cytokines, such as TNF-伪 and IL-6, and has been shown to contribute to the development of various inflammatory diseases, including rheumatoid arthritis, inflammatory bowel disease, and cancer.

In addition to its involvement in cellular processes, FUT7 has also been shown to play a role in the regulation of ESM synthesis and degradation. It has been shown to synthesize ESM, as well as to break down and remove ESM, which is essential for the regulation of bone growth and maintenance. Alterations in FUT7 function have been linked to various diseases, including bone loss and cancer.

Given its involvement in various cellular processes that are associated with the development and progression of diseases, FUT7 is an attractive target for drug development. Research has shown that various small molecules and drugs have been shown to be effective in inhibiting FUT7 function, leading to the potential for the development of new treatments for various diseases.

One of the most promising compounds that has been shown to inhibit FUT7 function is the drug and technology###1###. This drug, which has been shown to be effective in treating cancer, has been shown to inhibit FUT7 activity by binding to its active site.

Another compound that has been shown to be effective in inhibiting FUT7 function is the drug ##F###. This drug has been shown to be effective in treating multiple sclerosis by inhibiting the activity of FUT7 in the production of ESM.

In conclusion, FUT7 is a protein that is involved in various cellular processes that are associated with the development and progression of diseases. Its role in the regulation of ESM synthesis and degradation, as well as its involvement in T cell development, cancer, inflammation, and fibrosis, make it an attractive target for drug development. The development of new treatments for various diseases depends on the continued research into the functions of FUT7 and its potential as

Protein Name: Fucosyltransferase 7

Functions: Catalyzes the transfer of L-fucose, from a guanosine diphosphate-beta-L-fucose, to the N-acetyl glucosamine (GlcNAc) of a distal alpha2,3 sialylated lactosamine unit of a glycoprotein or a glycolipid-linked sialopolylactosamines chain through an alpha-1,3 glycosidic linkage and participates in the final fucosylation step in the biosynthesis of the sialyl Lewis X (sLe(x)), a carbohydrate involved in cell and matrix adhesion during leukocyte trafficking and fertilization (PubMed:8207002, PubMed:8752218, PubMed:8666674, PubMed:9299472, PubMed:9405391, PubMed:9473504, PubMed:9499379, PubMed:9461592, PubMed:15632313, PubMed:15926890, PubMed:18553500, PubMed:18402946, PubMed:11404359, PubMed:29593094). In vitro, also synthesizes sialyl-dimeric-Lex structures, from VIM-2 structures and both di-fucosylated and trifucosylated structures from mono-fucosylated precursors (PubMed:9499379). However does not catalyze alpha 1-3 fucosylation when an internal alpha 1-3 fucosylation is present in polylactosamine chain and the fucosylation rate of the internal GlcNAc residues is reduced once fucose has been added to the distal GlcNAc (PubMed:9473504, PubMed:9499379). Also catalyzes the transfer of a fucose from GDP-beta-fucose to the 6-sulfated a(2,3)sialylated substrate to produce 6-sulfo sLex mediating significant L-selectin-dependent cell adhesion (PubMed:10200296, PubMed:8752218). Through sialyl-Lewis(x) biosynthesis, can control SELE- and SELP-mediated cell adhesion with leukocytes and allows leukocytes tethering and rolling along the endothelial tissue thereby enabling the leukocytes to accumulate at a site of inflammation (PubMed:10386892, PubMed:29138114, PubMed:8666674, PubMed:9473504, PubMed:9834120). May enhance embryo implantation through sialyl Lewis X (sLeX)-mediated adhesion of embryo cells to endometrium (PubMed:18402946, PubMed:18553500). May affect insulin signaling by up-regulating the phosphorylation and expression of some signaling molecules involved in the insulin-signaling pathway through SLe(x) which is present on the glycans of the INSRR alpha subunit (PubMed:17229154)

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