Ask about this productRelated genes to: PIGT antibody
- Gene:
- PIGT NIH gene
- Name:
- phosphatidylinositol glycan anchor biosynthesis class T
- Previous symbol:
- -
- Synonyms:
- -
- Chromosome:
- 20q13.12
- Locus Type:
- gene with protein product
- Date approved:
- 2001-03-27
- Date modifiied:
- 2015-11-06
Related products to: PIGT antibody
Related articles to: PIGT antibody
- Colorectal cancer liver metastasis (CRLM) represents the leading cause of mortality in colorectal cancer (CRC). However, the molecular mechanisms enabling metastatic adaptation within the hepatic microenvironment remain unclear. We integrated single-cell RNA sequencing, spatial transcriptomics, and bulk transcriptomic data from CRC patients to characterize the immunometabolic landscape of CRLM. Machine learning models were used to identify key regulators, and functional assays were conducted to validate their biological roles. Nine major cell populations were delineated within CRLM, revealing enrichment of myeloid-derived suppressor cells and depletion of fibroblasts in metastatic lesions. Malignant cells displayed pronounced chromosomal instability and metabolic reprogramming. Among candidate regulators, PIGT emerged as a pivotal node linking metabolic adaptation and immune suppression. PIGT expression increased progressively from primary to metastatic states and was associated with immunosuppressive MIF, SPP1, and TGFβ signaling. Spatial transcriptomics demonstrated colocalization of PIGT-high tumor cells with ITGAM⁺ and CD163⁺ macrophages. Functionally, PIGT knockdown significantly suppressed cell invasion, migration, proliferation, and wound healing in vitro. Conversely, transcriptomic and qPCR analyses showed that PIGT-low tumors exhibited higher expression of inflammatory genes enriched in the IL-17 and TNF signaling pathways. Our integrative multi-omics and experimental analyses identify PIGT as a central regulator bridging tumor metabolism and immune modulation in CRLM. These findings highlight PIGT as a promising prognostic biomarker and potential therapeutic target for metastatic colorectal cancer. - Source: PubMed
Publication date: 2026/07/28
Yan MengzhuLi YixingLiu YunPeng LilanZhou Haibo - Glycosylphosphatidylinositols (GPIs) are complex glycolipids that function as membrane anchors for a wide array of eukaryotic proteins, collectively referred to as GPI-anchored proteins (GPI-APs). These structures are critical for various cellular processes including signal transduction, host-pathogen interactions, and immune evasion. While GPI-APs have been extensively studied, increasing attention is being paid to non-protein-linked GPI, called free GPIs, which have been identified in both protozoan parasites and mammalian cells. In protozoa such as , , , , and spp., free GPIs play roles in virulence, immune modulation, and parasite survival. In mammals, free GPIs have been detected in several tissues and pathogenic conditions of paroxysmal nocturnal hemoglobinuria caused by PIGT mutation and rare blood group phenotypes. This review provides a comparative overview of the structure and biosynthesis of free GPIs and GPI-APs across species, highlighting unique adaptations in each. We also discuss the emerging physiological and pathological roles of free GPIs, proposing that these underexplored molecules may serve as important biomarkers and therapeutic targets. Understanding the diversity and function of free GPIs offers new insights into glycobiology and host-pathogen interactions. - Source: PubMed
Publication date: 2025/11/29
Ihim Stella AmarachiFujita Morihisa - Glycosylphosphatidylinositol-anchored proteins (GPI-APs) contribute to cancer progression, with their glycolipid modification mediated by glycosylphosphatidylinositol transamidase (GPIT). Phosphatidylinositol glycan anchor biosynthesis class T (PIGT), a key GPIT subunit, influences GPI-APs biosynthesis and tumor biology. This study investigates PIGT expression in hepatocellular carcinoma (HCC) and its regulatory mechanisms. - Source: PubMed
Publication date: 2025/08/21
Huang JiaxinTan JiaqiMeng NanfengWang JunrongHan PengWang Hang - Glioma, a highly aggressive brain tumor, presents significant challenges in prognosis and treatment. This study investigates the role of PTX3 expression in glioma and its correlation with patient outcomes, addressing a gap in current research regarding its molecular mechanisms. - Source: PubMed
Publication date: 2025/07/10
Wang DelinLiu CuimeiSun BohaoZhang XiaodongZhou YejunHu ZhonglinCao DuanzhengZhang JingXu Jinfang - Phosphatidylinositol glycan class T (PIGT) is part of the glycosylphosphatidylinositol transamidase (GPI-TA) complex, crucial for various cell functions. Biallelic pathogenic variants in are associated with Multiple Congenital Anomalies-Hypotonia Seizures Syndrome 3 (MCAHS3), a rare neonatal hypotonia syndrome characterized by dysmorphic features and seizures. Diagnosing neonatal hypotonia, which has diverse congenital and acquired causes, is challenging, particularly in syndromic monogenic cases. Next-generation sequencing is essential for accurate diagnosis. This study reports a term newborn with hypotonia, dysmorphic features, seizures, and severe skeletal issues, including a humeral fracture at birth, consistent with MCAHS3. Trio whole exome sequencing (WES) analysis revealed a novel homozygous missense variant in , expanding the clinical spectrum of MCAHS3 and marking the first such case in the Thai population. The identified c.257A>G (p.His86Arg) variant manifests a severe MCAHS3 phenotype, as evidenced by reduced CD59 expression in western blot analysis, indicating impaired GPI-AP synthesis. Computational predictions suggest this mutation causes protein instability, potentially affecting GPI anchor attachment. While alkaline phosphatase (ALP), a GPI-AP crucial for skeletal mineralization, was elevated in this case, suggesting a late-stage GPI synthesis defect. The His86Arg mutation in PIGT may disrupt GPI-TA function, hindering proper protein attachment and leading to cleaved protein secretion. Further functional studies are needed to elucidate the impact of this mutation on PIGT function and MCAHS3 phenotypes. - Source: PubMed
Publication date: 2025/03/20
Klangjorhor JeerawanWiwattanadittakul NatrujeeJaimalai ThanapakThongkumkoon PatcharawadeeNoisagul PitipornKhiaomai RatchadapornSirikaew NutnichaMoonsan NonthananPasena ArnatSuksakit PathachaTeeyakasem PimpisaChaiyawat ParunyaTengsujaritkul Maliwan