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- Table of Contents
Facts about Lysyl oxidase homolog 2.
Shows no action against histone H3 when it is trimethylated on'Lys-9' (H3K9me3) or'Lys-27' (H3K27me3) or when'Lys-4' is monomethylated (H3K4me1) or dimethylated (H3K4me2) (PubMed:27735137). Also mediates deamination of methylated TAF10, a member of the transcription factor IID (TFIID) complex, which induces release of TAF10 from promoters, leading to inhibition of TFIID-dependent transcription (PubMed:25959397).
Human | |
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Gene Name: | LOXL2 |
Uniprot: | Q9Y4K0 |
Entrez: | 4017 |
Belongs to: |
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lysyl oxidase family |
EC 1.4.3; EC 1.4.3.-; LOL2; LOR2; LOXL2; Lysyl Oxidase Homolog 2; lysyl oxidase related 2; lysyl oxidase-like 2; Lysyl oxidase-like protein 2; Lysyl oxidase-related protein 2; Lysyl oxidase-related protein WS9-14; WS9-14
Mass (kDA):
86.725 kDA
Human | |
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Location: | 8p21.3 |
Sequence: | 8; NC_000008.11 (23296897..23404120, complement) |
Expressed in many tissues (PubMed:10212285). Highest expression in reproductive tissues, placenta, uterus and prostate (PubMed:10212285). In esophageal epithelium, expressed in the basal, prickle and granular cell layers (PubMed:22204712). Up- regulated in a number of cancers cells and tissues.
Secreted, extracellular space, extracellular matrix, basement membrane. Nucleus. Chromosome. Endoplasmic reticulum. Associated with chromatin (PubMed:27735137). It is unclear how LOXL2 is nuclear as it contains a signal sequence and has been shown to be secreted (PubMed:23319596). However, a number of reports confirm its intracellular location and its key role in transcription regulation (PubMed:22204712, PubMed:22483618).
This article will explain how LOXL2 is utilized in the treatment of cancer. It is able to crosslink collagen type IV and alter the growth of new blood vessels. We'll also discuss other ways this marker may be useful. We'll also discuss how Boster scientists are using this product around the world. These are some of the most common uses. And if you're wondering whether it's right for you, read on!
The investigation of the role of LOXL2 in crosslinking collagen type IV showed that the protein catalyzes the formation of lysyl-derived cross-links in the 7S domain. Transiently transfected with LOXL2Y689F in HE cells. The mutated protein contains Tyr-689 phenylalanine, which blocks the formation of lysyl tyrosyl quinone, a cofactor of LOXL2. This mutation resulted in a decrease in matrix crosslinking activity due to the loss of enzymatic activity and oxidase.
The function of LOXL2 is controlled by crosslinking a 7S dodecamer inside the basement membrane. Transiently transfected cell lines expressing LOXL2Y689F or LOXL2Y689F were used to analyze the PFHR-9 matrix by Western blotting using anti-LOXL2 antibodies, non-reducing SDS–PAGE, and Western blotting. After collagenase digestion, the NC1 monomer was found.
LOXL2 is a cytoplasmic enzyme that catalyzes the conversion of amino acids lysine, hydroxylysine, and lysine into lysine-aldehyde and hydroxylysine. This molecule creates cross-links that allow it to self-assemble collagen fibrils. More research is required to determine whether LOXL2 is a protein that regulates.
LOXL2 has been linked to the formation of fibrotic conditions both in the kidneys and on the skin. However, it is also associated with ECM remodeling. It is possible that LOXL2 might be increased in extracellular cells, leading to an increase in cross-linking and possibly the production of more collagen IV in the kidneys and glomerulus. Furthermore, LOXL2-mediated cross-linking of collagen IV can interfere with the homeostasis of this protein.
Inhibition of LOXL2 inhibits liver fibrotic processes by decreasing hepatic collagen levels. In addition, the inhibition of LOXL2 could perpetuate fibrotic response through HSC activation. The impact of LOXL2 in liver fibrosis could result in a decreased level of hepatic collagen, which results in increased stiffness and HSC-myofibroblast-HSC transition.
These findings could have implications for clinical trials as well as the future of research into the field of regenerative medical. LOXL2 inhibits LOX activation in the liver, which alters collagen alignments and the thinnin ECM scaffolds. This inhibition also results in a decrease in LOX levels. The effects of LOXL2 are temporary and the recombinant proteins don't are required for survival of cells.
LOXL2 is a key component of the collagen homeostasis process. In addition to the regulation of collagen, LOXL2 is important in the normal function of the myocardium and is a major element in the process of cardiac remodeling. Furthermore, the excessive expression of LOXL2 in the heart can lead to cardiac fibrosis, which decreases cardiac output and decreases the heart's function.
PFHR-9 cells express LOXL2 as the primary isoenzyme. The cells of PFHR-9 contain LOXL2 expressed in the insoluble matrix. LOXL2 is able to crosslink collagen type IV and acts as a metalloprotease within collagen. The protein is located in the glomerular matrix. Furthermore, the anti-LOXL2 antibodies can crosslink collagen type IV.
Recent research has proven that a gene named LOXL2 can regulate the sprouting of new blood vessels. The gene is a coreceptor for VEGF growth factor, which regulates a number of intracellular signaling pathways such as Erk and Akt. In this study, we analyzed whether LOXL2 could influence the proliferation of blood vessels in breast cancer patients. Interestingly, LOXL2 expression was positively related to malignancy in the tumor as well as lymphatic vessel size. Furthermore, knockdown of LOXL2 inhibited lymphangiogenesis.
The results of the BosterBio study are in line with previous studies using other markers. The markers that inhibit LOXL2 include antibodies against the human Erk1/2 and p-Akt. Boster Bio LOXL2 is one of four markers that influence the development of new blood vessels in humans. To determine which protein could prevent the growth of new blood vessels, researchers examined boster bio LOXL2 as well as human LOXL2.
The Boster Bio LOXL2 antibody was administered to mice that have MCF-7 cells, which have low levels of LOXL2 expression. The tumors were also treated with neutralizing antibodies. Additionally, the mice were weighted prior to sacrifice. The results revealed that lymphangiogenesis was blocked in MDAMB-231 cancers by the LOXL2 protein.
Boster Bio LOXL2 antibody has the capability of influence LEC invasion and tube formation. In addition, it could influence the development of new blood vessels. LOXL2 is also believed to be a factor in promoting the invasion of tumors. These results are in line with previous research. The boster Bio LOXL2 antibody is compatible with other diagnostic tests.
The boster Bio LOXL2 antibody has also been found to control lymphangiogenesis in breast cancer patients. We have shown that LOXL2 protein is positively associated with breast cancer malignancy, and it increases lymphatic vessels. This is good news because it suggests that LOXL2 could influence the growth of new blood vessels.
The fibroblasts of affluent fibroblasts express the LOXL2 gene. We found that LOXL2-educated fibroblasts produced pro-lymphangiogenic and pro-lymphangiogenic ligand including VEGF-C as well as SDF-1a. Our findings suggest that LOXL2 may also influence HIF-1a expression. LOXL2 could therefore affect the growth of blood vessels that are not yet formed.
The LOXL2 marker is helpful in cancer research. It has been linked to drug resistance in pancreatic cancer cells, as well as the development of gastric cancer. It is possible that LOXL2 could be a useful target for new treatments for cancer patients. Additionally, LOXL2 promotes tumor metastasis in hypoxia. Researchers are currently studying the role of this protein for cancer.
The LOXL2 gene is located on chromosome 8p21-22 and is synthesized as a 87 kDa proenzyme with 774 amino acids. This gene was first recognized as a transcriptional molecule that was deregulated in cancerous cells and tumors in 1997. Multiple reports have confirmed its role in the suppression of tumors. Further studies are needed to confirm the LOXL2 gene's function as a cancer marker.
Knockdown of LOXL2 results in the inhibition of EMT in DU145 cells. Additionally, LOXL2 knockdown also enhanced the rate of apoptosis in CRPC cells after irradiation. The results support the cell-based hypothesis that LOXL2 is a blocker of EMT. More research is needed to understand the exact mechanism of LOXL2 inhibition.
The increased LOXL2 expression in cancer cells is linked to cell polarity. This phenotypic marker might be beneficial in research on cancer and anti-ERB2-targeted chemotherapy may benefit breast cancer patients. This information can help us understand the causes of cancer. The research also suggests that LOXL2 can be useful in the treatment of cancer. Although there aren't any tests specific to this gene, it can be used to detect breast cancer.
To identify tumor cells with LOXL2 Researchers developed lentivirus vectors. Primers were constructed using LOXL2-targeting shRNA. The vectors were infused with DU145 cells and 10A control cells. Cells were plated onto a six-well plate with up to 105 cells per well. The siRNA that targets LOXL2 was performed using Lipofectamine 2000.
The formation of 3D invasive structures is dependent on the expression of LOXL2. This means that LOXL2 expression in tumor cells could help determine whether the cancer cell is benign or malignant. This study also suggests that LOXL2 is an important marker for research into cancer. It is also associated with an increased rate of cell migration. This research will assist doctors in distinguishing between benign and tumor tissues.
The prostate cancer cells that express LOXL2 are considered to be extremely resistant to radiotherapy. The CRPC cells are highly resistant to radiotherapy. In CRPC tumors and cell line lines it was observed that the LOXL2 gene was upregulated. It is possible that LOXL2 could play a role in radioresistance in these cells. The clonogenic assay was used to examine the genes responsible for LOXL2 and xenograft tumor experiments were performed.
One study demonstrated that LOXL2 expression induced phosphorylation in ErbB2. LOXL2 expression was shown to increase levels of phospho-ErbB2 in 10A L2 cells. The total ErbB2 was comparable in 10A cont-treated cells. The L2+ cells showed significantly higher levels of phospho-ErbB2 in addition to Erk1/2.
PMID: 9079631 by Saito H., et al. Regulation of a novel gene encoding a lysyl oxidase-related protein in cellular adhesion and senescence.
PMID: 10212285 by Jourdan-Le Saux C., et al. The LOXL2 gene encodes a new lysyl oxidase-like protein and is expressed at high levels in reproductive tissues.