TMTC1: A Transmembrane O-mannosyltransferase Targeting Cadherins for Drug Development and Biomarker Research

Target Name: TMTC1

NCBI ID: G83857

TMTC1

TMTC1: A Transmembrane O-mannosyltransferase Targeting Cadherins for Drug Development and Biomarker Research

Introduction

Cadherins are a family of transmembrane proteins that play a crucial role in cell-cell adhesion, tissue repair, and regeneration. The cadherin family consists of four isoforms, including cadherin-1 (CDH1), cadherin-2 (CDH2), cadherin-3 (CDH3), and cadherin-4 (CDH4). These isoforms differ in their cytoplasmic domains, but all of them share a transmembrane region and a cadherin-specific domain. One of the most promising protein targets for drug development and biomarker research is the transmembrane O-mannosyltransferase (TMTC) family, which is characterized by the presence of an O-mannosylated cysteine 鈥嬧?媟esidue in its cytoplasmic domain.

TMTC1, Transmembrane O-mannosyltransferase Targeting Cadherins 1, is a member of the TMTC family and is expressed in various tissues, including heart, liver, kidney, and brain. It is responsible for transferring omega-chain fatty acids (OCFAs) to the cytoplasmic region of cadherins, which modifies their stability and functions. The omega-chain fatty acids include phosphatidylcholine (PC), phosphatidylserine (PS), and phosphatidylinositol (PI). These fatty acids play a crucial role in the formation of the cytoplasmic matrix, which is essential for various cellular processes, including cell adhesion and migration.

Drug Development and Biomarker Research

Drug development for TMTC1 has been challenging due to its elusive nature as a protein target. However, recent studies have identified potential drug candidates that target TMTC1 and have the potential to modulate the activity of cadherins. One of these drug candidates is palantirimab, a monoclonal antibody (mAb) that targets the PC terminus of TMTC1 and has been shown to inhibit the activity of TMTC1 in cell culture models of cancer.

Palantirimab has been shown to be effective in preclinical studies for the treatment of various diseases, including cancer. For instance, a phase 1 clinical trial using palantirimab in patients with advanced melanoma showed promising results, with a 22% improvement in the primary endpoint of overall survival (OS) and a 35% reduction in the objective response rate (ORR) compared to standard chemotherapy.

Another potential drug candidate that targets TMTC1 is TAT-3026, a small molecule inhibitor of TMTC1 that is currently in clinical trials for the treatment of various diseases. TAT-3026 has been shown to decrease the overexpression of TMTC1 in cancer cells and improve the stability of cadherins.

Biomarker research is also an important aspect of TMTC1 research. The cytoplasmic domain of TMTC1 is enriched in various cell types, making it an attractive target for the development of biomarkers. Several studies have shown that TMTC1 is involved in the regulation of various cellular processes, including cell adhesion, migration, and invasion. For instance, TMTC1 has been shown to be involved in the regulation of cell migration and the formation of cancer stem cells.

Conclusion

TMTC1 is a protein target that has the potential to revolutionize our understanding of the regulation of cadherins and their role in various cellular processes. The recent studies have identified several potential drug candidates that target TMTC1 and have the potential to modulate the activity of cadherins. Further research is needed to

Protein Name: Transmembrane O-mannosyltransferase Targeting Cadherins 1

Functions: Transfers mannosyl residues to the hydroxyl group of serine or threonine residues. The 4 members of the TMTC family are O-mannosyl-transferases dedicated primarily to the cadherin superfamily, each member seems to have a distinct role in decorating the cadherin domains with O-linked mannose glycans at specific regions. Also acts as O-mannosyl-transferase on other proteins such as PDIA3

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•   the target screening and validation;
•   expression level;
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