Last update 19 Sep 2024

GALGT2

Last update 19 Sep 2024

Basic Info

Synonyms

B4GALNT2, Beta-1,4 N-acetylgalactosaminyltransferase 2, beta-1,4-N-acetyl-galactosaminyltransferase 2

+ [6]

Introduction

Involved in the synthesis of the Sd(a) antigen (Sia-alpha2,3-[GalNAc-beta1,4]Gal-beta1,4-GlcNAc), a carbohydrate determinant expressed on erythrocytes, the colonic mucosa and other tissues. Transfers a beta-1,4-linked GalNAc to the galactose residue of an alpha-2,3-sialylated chain.

Drugs associated with GALGT2

Galgt2 gene therapy (Nationwide Childrens Hospital)

Target

GALGT2

Mechanism

B4GALNT2 gene stimulants [+1]

Active Org.

Nationwide Children's Hospital [+2]

Originator Org.

Nationwide Children's Hospital

Active Indication

Muscular Dystrophy, Duchenne

Inactive Indication-

Drug Highest PhasePhase 2

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

Clinical Trials associated with GALGT2

NCT03333590 / Active, not recruitingPhase 1/2IIT

Phase I/IIa Gene Transfer Clinical Trial for Duchenne Muscular Dystrophy Using rAAVrh74.MCK.GALGT2

The proposed clinical trial study of rAAVrh74.MCK.GALGT2 for duchenne muscular dystrophy (DMD) patients. There will be a modified intravascular limb infusion (ILI) procedure that will be used to sequentially deliver vector to each whole lower limb of DMD subjects via a major lower limb artery.

Start Date06 Nov 2017

Sponsor / Collaborator

Nationwide Children's Hospital

NCT02704325 / WithdrawnPhase 1/2IIT

Phase I Gene Transfer Clinical Trial for Duchenne Muscular Dystrophy Using rAAVrh74.MCK.GALGT2

The proposed clinical trial study of rAAVrh74.MCK.GALGT2 for duchenne muscular dystrophy (DMD) patients that will involve direct intramuscular injection to the extensor digitorum brevis muscle (EDB).

Start Date01 Apr 2016

Sponsor / Collaborator

Nationwide Children's Hospital

100 Clinical Results associated with GALGT2

100 Translational Medicine associated with GALGT2

0 Patents (Medical) associated with GALGT2

314

Literatures (Medical) associated with GALGT2

06 Aug 2024·ACS Nano

One-Pot Self-Assembly of Sequence-Controlled Mesoporous Heterostructures via Structure-Directing Agents

Article

Author: Stefik, Morgan ; Tengco, John ; Wright, Mason ; Tang, Chuanbing ; Boebinger, Matthew G. ; Williams, Eric R. ; Zhang, Mengxue ; Larison, Taylor

Multimaterial heterostructures have led to characteristics surpassing the individual components. Nature controls the architecture and placement of multiple materials through biomineralization of nanoparticles (NPs); however, synthetic heterostructure formation remains limited and generally departs from the elegance of self-assembly. Here, a class of block polymer structure-directing agents (SDAs) are developed containing repeat units capable of persistent (covalent) NP interactions that enable the direct fabrication of nanoscale porous heterostructures, where a single material is localized at the pore surface as a continuous layer. This SDA binding motif (design rule 1) enables sequence-controlled heterostructures, where the composition profile and interfaces correspond to the synthetic addition order. This approach is generalized with 5 material sequences using an SDA with only persistent SDA-NP interactions ("P-NP₁-NP₂"; NP_i = TiO₂, Nb₂O₅, ZrO₂). Expanding these polymer SDA design guidelines, it is shown that the combination of both persistent and dynamic (noncovalent) SDA-NP interactions ("PD-NP₁-NP₂") improves the production of uniform interconnected porosity (design rule 2). The resulting competitive binding between two segments of the SDA (P- vs D-) requires additional time for the first NP type (NP₁) to reach and covalently attach to the SDA (design rule 3). The combination of these three design rules enables the direct self-assembly of heterostructures that localize a single material at the pore surface while preserving continuous porosity.

01 Jul 2024·Bioorganic & Medicinal Chemistry Letters

Fluorescence biosensor to detect microRNAs via integrating DNA hairpins transition mediated strand displacement amplification with primer exchange reaction

Article

Author: Li, Zehong ; Wan, Jiayu ; Liu, Xiaoyu ; Bu, Shengjun ; Xu, Yao ; Zhou, Hongyu ; Hao, Zhuo

Herein, we constructed a fluorescence biosensor for the ultra-sensitive analysis of microRNAs (miRNAs) by combining DNA hairpins transition triggered strand displacement amplification (DHT-SDA) with primer exchange reaction (PER). Target miRNA initiated DHT-SDA to facilitate the generation of multiple single-stranded DNA (ssDNA) as PER primer, which was extended into a long ssDNA. The biosensor is successfully utilized in detecting miRNAs with high sensitivity (limit of detection for miRNA-21 was 58 fM) and a good linear relationship between 100 nM and 100 fM. By simply changing the DNA hairpin sequence, the constructed biosensor can be extended to analyze another miRNAs. Moreover, the biosensor has the feasibility of detecting miRNAs in real samples with satisfactory accuracy and reliability. Therefore, the fluorescent biosensor has great application potential in clinical diagnosis.

01 May 2024·Xenotransplantation

Anti‐pig antibodies in swine veterinarian serum: Implications for clinical xenotransplantation

Article

Author: McGregor, Christopher G A ; Byrne, Guerard W

AbstractRecent clinical xenotransplantation and human decedent studies demonstrate that clinical hyperacute rejection of genetically engineered porcine organs can be reliably avoided but that antibody mediated rejection (AMR) continues to limit graft survival. We previously identified porcine glycans and proteins which are immunogenic after cardiac xenotransplantation in non‐human primates, but the clinical immune response to antigens present in glycan depleted triple knockout (TKO) donor pigs is poorly understood. In this study we use fluorescence barcoded human embryonic kidney cells (HEK) and HEK cell lines expressing porcine glycans (Gal and SDa) or proteins (tetraspanin‐29 [CD9], membrane cofactor protein [CD46], protectin, membrane attack complex inhibition factor [CD59], endothelial cell protein C receptor, and Annexin A2) to screen antibody reactivity in human serum from 160 swine veterinarians, a serum source with potential occupational immune challenge from porcine tissues and pathogens. High levels of anti‐Gal IgM were present in all samples and lower levels of anti‐SDa IgM were present in 41% of samples. IgM binding to porcine proteins, primarily CD9 and CD46, previously identified as immunogenic in pig to non‐human primate cardiac xenograft recipients, was detected in 28 of the 160 swine veterinarian samples. These results suggest that barcoded HEK cell lines expressing porcine protein antigens can be useful for screening human patient serum. A comprehensive analysis of sera from clinical xenotransplant recipients to define a panel of commonly immunogenic porcine antigens will likely be necessary to establish an array of porcine non‐Gal antigens for effective monitoring of patient immune responses and allow earlier therapies to reverse AMR.

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GALGT2

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