Target Name: LGALS8
NCBI ID: G3964
Other Name(s): Galectin 8 | lectin, galactoside-binding, soluble, 8 | PCTA1 | Gal-8 | Prostate carcinoma tumor antigen 1 | PCTA-1 | Galectin-8 | galectin 8 | Po66 carbohydrate-binding protein | Galectin-8 (isoform a) | LGALS8 variant 1 | Po66-CBP | LEG8_HUMAN | Galectin 8, transcript variant 1 | prostate carcinoma tumor antigen 1 | galectin-8g | po66 carbohydrate-binding protein | Po66 carbohydrate binding protein

LGALS8: A Potential Drug Target and Biomarker for Glioblastoma

Glioblastoma, one of the most aggressive forms of cancer, has a poor treatment outcomes and a high mortality rate. Despite advances in surgical and radiation treatments, the survival rate for glioblastoma remains poor, with a five-year survival rate of only around 15%. The lack of effective treatments for this disease has led to a need for new and innovative approaches in the fight against glioblastoma.

One potential drug target that has shown promise in clinical trials is LGALS8, a protein that is expressed in high levels in human glioblastoma. LGALS8 has been identified as a potential drug target by several research groups, and recent studies have shown that targeting this protein may have promising results in treating glioblastoma.

LGALS8 is a type of transmembrane protein that is expressed in various tissues, including the brain. It is involved in several cellular processes that are important for brain function, including cell signaling, cell adhesion, and cell migration. LGALS8 has been shown to play a role in the development and progression of several types of cancer, including glioblastoma.

One of the key functions of LGALS8 is its role in cell signaling. The protein is involved in several signaling pathways that are important for cancer growth and progression. For example, LGALS8 has been shown to be involved in the regulation of the PDGF signaling pathway, a pathway that is involved in cancer cell growth, survival, and angiogenesis.

In addition to its role in cell signaling, LGALS8 has also been shown to play a role in cell adhesion and migration. The protein is involved in several processes that are important for the formation and maintenance of tight junctions, which are important for the separation of cells in tissues. It is also involved in the regulation of cell migration, a process that is critical for the development of new tumors.

Targeting LGALS8 as a drug target has the potential to be a significant advancement in the treatment of glioblastoma. By blocking the functions of LGALS8, researchers may be able to inhibit its role in cancer growth and progression. This could lead to a more effective treatment of glioblastoma, with improved survival rates and a reduced risk of recurrence.

In addition to its potential as a drug target, LGALS8 has also been identified as a potential biomarker for glioblastoma. The protein is expressed in high levels in human glioblastoma, and its levels have been shown to be associated with the severity of glioblastoma. This suggests that LGALS8 may be a useful biomarker for the diagnosis and prognosis of this disease.

While further research is needed to fully understand the role of LGALS8 in the treatment of glioblastoma, its potential as a drug target and biomarker is an encouraging development in the fight against this aggressive form of cancer. With further research, LGALS8 may prove to be a valuable tool in the development of new and more effective treatments for glioblastoma.

Protein Name: Galectin 8

Functions: Beta-galactoside-binding lectin that acts as a sensor of membrane damage caused by infection and restricts the proliferation of infecting pathogens by targeting them for autophagy (PubMed:22246324, PubMed:28077878). Detects membrane rupture by binding beta-galactoside ligands located on the lumenal side of the endosome membrane; these ligands becoming exposed to the cytoplasm following rupture (PubMed:22246324, PubMed:28077878). Restricts infection by initiating autophagy via interaction with CALCOCO2/NDP52 (PubMed:22246324, PubMed:28077878). Required to restrict infection of bacterial invasion such as S.typhimurium (PubMed:22246324). Also required to restrict infection of Picornaviridae viruses (PubMed:28077878). Has a marked preference for 3'-O-sialylated and 3'-O-sulfated glycans (PubMed:21288902)

More Common Targets

LGALS8-AS1 | LGALS9 | LGALS9B | LGALS9C | LGALSL | LGI1 | LGI2 | LGI3 | LGI4 | LGMN | LGMNP1 | LGR4 | LGR5 | LGR6 | LGSN | LHB | LHCGR | LHFPL1 | LHFPL2 | LHFPL3 | LHFPL3-AS1 | LHFPL3-AS2 | LHFPL4 | LHFPL5 | LHFPL6 | LHFPL7 | LHPP | LHX1 | LHX2 | LHX3 | LHX4 | LHX4-AS1 | LHX5 | LHX6 | LHX8 | LHX9 | LIAS | LIF | LIFR | LIFR-AS1 | LIG1 | LIG3 | LIG4 | LILRA1 | LILRA2 | LILRA3 | LILRA4 | LILRA5 | LILRA6 | LILRB1 | LILRB2 | LILRB3 | LILRB4 | LILRB5 | LILRP1 | LILRP2 | LIM domain kinase (LIMK) | LIM2 | LIMA1 | LIMASI | LIMCH1 | LIMD1 | LIMD1-AS1 | LIMD2 | LIME1 | LIMK1 | LIMK2 | LIMS1 | LIMS2 | LIMS3 | LIMS3-LOC440895 | LIMS4 | LIN28A | LIN28B | LIN28B-AS1 | LIN37 | LIN52 | LIN54 | LIN7A | LIN7B | LIN7C | LIN9 | LINC-PINT | LINC-ROR | LINC00028 | LINC00029 | LINC00032 | LINC00051 | LINC00052 | LINC00092 | LINC00102 | LINC00106 | LINC00111 | LINC00112 | LINC00113 | LINC00114 | LINC00115 | LINC00158 | LINC00159 | LINC00160