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- Table of Contents
Facts about Lactoylglutathione lyase.
Required for normal osteoclastogenesis. .
Human | |
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Gene Name: | GLO1 |
Uniprot: | Q04760 |
Entrez: | 2739 |
Belongs to: |
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glyoxalase I family |
Aldoketomutase; EC 4.4.1.5; GLO1; GLOD1; Glx I; GLYI; glyoxalase domain containing 1; Glyoxalase I; glyoxalase Ialdoketomutase; Ketone-aldehyde mutase; lactoyl glutathione lyase; lactoylglutathione lyase; Methylglyoxalase; S-D-lactoylglutathione methylglyoxal lyase
Mass (kDA):
20.778 kDA
Human | |
---|---|
Location: | 6p21.2 |
Sequence: | 6; NC_000006.12 (38675925..38703145, complement) |
A boster bio optimizer is a must-have for any research lab. This versatile tool provides scientists with the ability to examine any DNA sample. The GLO1 marker is a universal marker for detection of DNA fragmentation. It comes in many forms comprising whole cells as well as DNA fragments and peptides. Boster Bio optimizers can help optimize experiments using different flow procedures.
A new study has revealed that the time incubation of GLO1 results in significant changes in the behavior of mice. Anxiety-like behavior has been associated to the GLO1 marker. Research in the past has found that Glo1 is essential for maintaining a healthy blood sugar level. The mechanism that causes these incredible changes is not yet clear. GLO1's incubation process has many advantages. Its short half-life, around 179 hours, makes it an ideal choice for studies that examine the long-term effects GLO1 on various diseases.
The GLO1 gene is an essential factor in the regulation of blood glucose levels, and its expression is linked with anxiety. It is present in a variety of tissues that include the brain as well as blood. In mice, Glo1 is associated with various phenotypes, including depression, neuropathic pain, and anxiety-like behaviors. Recently the gene has also been linked to psychiatric disorders.
In the study, HAECs were cultured using the GLO1 marker. 2D-DIGE was utilized to analyze the cellular proteome. Nine proteins were affected. The statistical significance of the change was p0.05. The GLO1 knockdown remained stable for at minimum 4 days. After three days, the protein levels decreased by more than half. Three siRNAs confirmed the GLO1 gene knockdown.
In this study, GLO1 was knocked down in HAECs exposed to a high glucose concentration. GLO1 knockdown reduced the apoptotic rate, and also triggered an inflammatory profile. Anoikis could be prevented by inhibiting GLO1 in aortic epithelial cells. GLO1 knockdown is a valuable tool in studies of cardiovascular disease.
GLO1 knockdown significantly reduced the death rate of HAECs. GLO1 knockdown led to cells that were more prone to apoptosis, as well as having lower viability. A proteome analysis confirmed that Annexin A1 was not significantly upregulated through binding to Annexin V-FITC on its surface.
In addition to the reduction of GLO1 MGh2 metabolites were also observed to increase in HAECs that were exposed to high glucose. These MGh2 adducts could be effectively targeted for proteolysis. The MGh2 adducts that resulted could be eliminated. The formation of adducts in HAECs was significantly increased following GLO1 knockdown after acute glucose-induced diabetes.
Blocking membranes with BSA/TBST of 5% is the first step of immunoprecipitation. Then, antibodies against phosphorylated ERK 1/2 and p65 were employed. As an anti-loading control, btubulin was used as a buffer. The membranes were then incubated with primary antibodies for at least 1 h at 4 degC. The membranes were then incubated at least 1 h at 4°C using the primary antibodies. The next step is the visualisation of protein bands using an blotting substrate (Pierce ECL) to determine the presence of each antibody.
To perform immunoblotting, we used an phototope(r)-HRP Western Blot Detection Kit. FDC supernatants of culture were collected after two and one days. The supernatants then were concentrated by vacuum evaporation. They were then incubated using the commercial Western Blot Detection Kit. The protein samples were then separated by electrophoresis using a polyacrylamide, and transferred onto membranes of nitrocellulose. After blocking the membranes, we used a rabbit anti-NAP-1 polyclonal antibody. We then added HRP-linked anti-rabbit IgG to the membranes and then visualized the signal.
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PMID: 7684374 by Kim N.-S., et al. Human glyoxalase I. cDNA cloning, expression, and sequence similarity to glyoxalase I from Pseudomonas putida.
PMID: 8449929 by Ranganathan S., et al. Cloning and characterization of human colon glyoxalase-I.