MGAT4B as A Potential Drug Target for Neurodegenerative Diseases

Target Name: MGAT4B

NCBI ID: G11282

MGAT4B

Other Name(s): mannosyl (alpha-1,3-)-glycoprotein beta-1,4-N-acetylglucosaminyltransferase, isozyme B | N-acetylglucosaminyltransferase IVb | GlcNAc-T IVb | UDP-N-acetylglucosamine: alpha-1,3-D-mannoside beta-1,4-N-acetylglucosaminyltransferase IVb | mannosyl (alpha-1,3-)-glycoprotein beta-1,4-N-acetylglucosaminyltransferase, isoenzyme B | GnT-IVb | UDP-N-acetylglucosamine: alpha-1,3-D-mannoside beta-1,4-N-acetylglucosaminyltransferase IV | alpha-1,3-mannosyl-glycoprotein beta-1,4-N-acetylglucosaminyltransferase | aminyltransferase | glcNAc-T IVb | N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase IVb | MGAT4B variant 2 | Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase B, transcript variant 2 | alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase B | GNT-IVB | MGT4B_HUMAN | Mannosyl (alpha-1,3-)-glycoprotein beta-1,4-N-acetylglucosaminyltransferase, isoenzyme B | Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase B | Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase B (isoform 2) | GNT-IV

MGAT4B as A Potential Drug Target for Neurodegenerative Diseases

MGAT4B (mannosyl (alpha-1,3-)-glycoprotein beta-1,4-N-acetylglucosaminyltransferase, isozyme B) is a protein that is expressed in various tissues and cells in the human body. It is a key player in the glycosylation of proteins, which is the process by which certain proteins are modified with glucose molecules to form a covalent complex with the protein. MGAT4B is a member of the B-type glycosylating enzyme family 4 (BGELF), which includes enzymes that transfer N-acetylglucosamine (NAG) to the alpha-1,3-positions of glycoproteins.

MGAT4B has been identified as a potential drug target or biomarker for various diseases, including cancer, neurodegenerative diseases, and autoimmune disorders. Its role in the regulation of protein glycosylation and its potential as a therapeutic target have been the focus of extensive research in recent years.

One of the key reasons for the interest in MGAT4B as a potential drug target is its involvement in the regulation of protein glycosylation. Protein glycosylation is a post-translational modification that involves the addition of NAG and other carbohydrates to proteins. This modification plays a crucial role in the regulation of protein function, including cell signaling, tissue structure, and inflammation. MGAT4B is a key enzyme in the BGELF family, which is responsible for transferring NAG to the alpha-1,3-positions of glycoproteins. This modification is critical for the formation of the alpha-1,3-glucosaminyl bond, which is a key structural element of the NAG carbohydrate.

MGAT4B's involvement in protein glycosylation also makes it a potential target for drugs that are designed to inhibit protein glycosylation. This is because drugs that inhibit MGAT4B activity would reduce the levels of NAG added to proteins, which would in turn decrease the formation of the alpha-1,3-glucosaminyl bond. This would have a beneficial effect on the structure and function of the protein, potentially leading to improved health outcomes.

Another potential reason for the interest in MGAT4B as a drug target is its involvement in the regulation of cell signaling. Many proteins that are involved in cell signaling are glycosylated, and MGAT4B is involved in the regulation of these proteins. For example, MGAT4B has been shown to be involved in the regulation of the protein PDGF-BB, which is a key regulator of cell signaling. Additionally, MGAT4B has been shown to be involved in the regulation of the protein TGF-beta, which is involved in cell signaling and tissue growth.

MGAT4B's involvement in cell signaling also makes it a potential target for drugs that are designed to inhibit cell signaling. This is because drugs that inhibit MGAT4B activity would reduce the levels of NAG added to proteins, which would in turn decrease the formation of the alpha-1,3-glucosaminyl bond. This would have a beneficial effect on the structure and function of the protein, potentially leading to improved health outcomes.

MGAT4B's involvement in the regulation of protein glycosylation also makes it a potential target for drugs that are designed to treat neurodegenerative diseases. Neurodegenerative diseases, such as Alzheimer's disease and Parkinson's disease, are characterized by the progressive loss of brain cells and the development of neurofibrillary tangles. The formation of these tangles is thought to be influenced by the accumulation of NAG in the alpha-1,3-positions of proteins, including MGAT4B. Therefore, drugs that are designed to inhibit MGAT4B activity

Protein Name: Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase B

Functions: Glycosyltransferase that catalyzes the transfer of GlcNAc from UDP-GlcNAc to the GlcNAcbeta1-2Manalpha1-3 arm of the core structure of N-linked glycans through a beta1-4 linkage and participates in the production of tri- and tetra-antennary N-linked sugar chains (PubMed:17006639, PubMed:10372966). Prefers complex-type N-glycans over hybrid-types (PubMed:17006639). Has lower affinities for donors or acceptors than MGAT4A, suggesting that, under physiological conditions, it is not the main contributor in N-glycan biosynthesis (PubMed:17006639)

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