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- Table of Contents
Facts about Phospholipid-transporting ATPase ABCA1.
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Human | |
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Gene Name: | ABCA1 |
Uniprot: | O95477 |
Entrez: | 19 |
Belongs to: |
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ABC transporter superfamily |
ABC1; ABC-1; ABC1ATP-binding cassette transporter A1; ABCA1; ATP-binding cassette 1; ATP-binding cassette transporter 1; ATP-binding cassette, sub-family A (ABC1), member 1; CERP; Cholesterol efflux regulatory protein; EC 2.7.7.8; EC 2.8.1.8; EC 3.6.3; EC 3.6.3.41; FLJ14958; HDLDT1; membrane-bound; MGC164864; MGC165011; TGD; TGDATP-binding cassette sub-family A member 1
Mass (kDA):
254.302 kDA
Human | |
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Location: | 9q31.1 |
Sequence: | 9; NC_000009.12 (104781006..104928232, complement) |
Widely expressed, but most abundant in macrophages.
Membrane; Multi-pass membrane protein. Cell membrane. Endosome.
You should look for boster biomarkers with specific characteristics when you are using it. The most effective biomarker is a molecule with the ABCA1 sequence. In this article, we will examine its X-Ray crystallography and molecular structure, and also its interaction with antibodies. We also discuss the detection method. The boster biomarker is applicable to scientists across the globe.
The X-Ray crystallography of the abcaA1 marker could provide an excellent structure-function correlation. This marker is a bacteriochlorophyll-containing protein derived from green photosynthetic bacteria. It is believed that it functions as an antenna for light energy. Initial crystallographic studies were not finished due to the absence of amino acid sequences, a common issue in structural biology before cDNA sequencing. In these instances, crystal structures were built with no side chains and described in the literature. Once the sequences were established, complete models could then be constructed and Xray refinement could be completed.
Further research is required to determine the function of ABCA7 for AD susceptibility. Human genome analysis is not feasible due the practical limitations. To identify risk factors and a cure the human genome has to be studied. High-throughput "omics" technologies are yielding amazing insights into AD molecular features. ABCA7 is responsible for numerous discoveries. Below is a summary of these studies.
The ABCA1 marker's molecular shape. The ABCA1 marker can be found in the plasma membranes of platelets. Patients from Tangier showed impaired responses to collagen, low levels of thrombin and ADP and an abnormally high pH. Consequently, Nofer et al. (2004) proposed that ABCA1 deficiency could result in impaired liberation of agonists during activation.
The analysis of the protein's structural structure shows an unusual conformation. The lipids present on the leaflet's inner surface of the cell still have access to the site of binding to substrates. Furthermore, the side surfaces of helices in TMD1 and TMD2 were completely exposed to lipids. Simulations are unable to predict the location of lipid binding and ABCA1's final form is undetermined.
The structural analysis of ABCA1 protein also revealed new insights into its function. The ABCA1 protein plays an important role in the handling cellular lipids. It is linked to dimeric structures and undergoes changes to higher order structures, such as tetramers, in the ATP catalytic cycling. This is why molecular assembly is an essential component of the function of the protein. The ABCA1 marker's molecular structure is a crucial element in this process. The structure of ABCA1 is critical in understanding the mechanism through which the protein works.
Tanaka et. and. They identified a 1-bp deletion of the ABCA1 gene in 1999. The deletion affected nucleotide 1764 and located to codon 548. The mutation caused premature translation stoppage of 26 amino acids downstream of the deletion site. As a result, the translation product was nonfunctional. Homozygotes had lower HDL cholesterol levels, and early coronary artery disease was a significant clinical symptom in a particular family.
Incredibly, the EGFP-tagged mutants retain the ability to dimerize. They also exhibit a reduced efficiency of oligomerization, which is in line with their ability to bind ATP. This suggests that the ABCA1 transporter doesn't entirely depend on ATP for its function. The ABCA1 marker may also be expressed in cells that express wild type or mutant.
In this study, we employed the Boster Bio ABCA1 marker to test the interaction between antibodies against this protein. The antibody was used for flow cytometry , ICC, IP, Gel suppershift assay, blocking and PCR. Additionally, we used the antibody for Chromatin Immunoprecipitation (CIP) and ELISA. The results were consistent across all samples.
ABCA1 is an ATP-binding cassette transporter. It is located on the plasma membrane and plays a role in the apo-A-associated exportation of cholesterol. It also regulates cholesterol flux between macrophages, HDL, and macrophages. In addition, it has been shown to interact with antibodies which neutralize and recognize apoA. This interaction is crucial to the determination of the phospholipid binding properties of ABCA1.
Monoclonal antibodies can be targeted against the ABCA1 binding domain. Monoclonal antibodies to this protein were induced against two regions, and it was demonstrated that they may influence the efflux and removal of cholesterol and lipids from the blood. ABCA1 can be used to prevent and treat atherosclerosis. Your cholesterol levels will be lower in the event that your HDL levels are high.
ABCA1's function is significant for a variety of reasons. It is necessary for the production of high-density lipoproteins. However, ABCA1 is mutable in humans. Mutations in this gene are responsible for Tangier disease which is defined by the absence of HDL and a lack of reverse cholesterol transport. Mutations of ABCA1 in human plasma result in hypoalphalipoproteinaemia.
The ABCA1 protein can be found in the alveolar cells of mice as well as rats, however, the level of protein in these tissues is not within the detection limits. The protein level was increased when alveolar cells were treated with 9cRA/22OH. Detection was performed by checking the intensity of a band of the ABCA1 protein to the density of the loading standard, a protein that was isolated from human fibroblasts WI38VA13.
The ABCA1 protein is one of the 100 members of the ATP-binding cassette group. The ABCA1 protein is detected by specific antibodies. The ABCA1 antisera were created with the aim of detecting the protein. These antisera are highly specific and specifically for the ABCA1 protein. However, they cannot detect all the mRNA and the RNA present in a sample.
ABCA1 gene mutations result in familial hypoalphalipoproteinemia. Tangier disease is a severe form of familial hypoalphalipoproteinemia. It is caused by a dramatic reduction in HDL-C cholesterol levels, and impairs cholesterol efflux. It is unclear if ABCA1 mutations are the reason for the localized atherosclerosis.
Murine tissues were fixed overnight in buffered neutral 10% formalin, and then reassembled. Tissue samples were processed in a Pittsburgh-based fisher-scientific tissue processer. The tissue samples were embedded in paraffin and processed using automated staining techniques. Microtome sections of 3mm were used to detect the ABCA1 marker in mouse tissues.
A Molecular analysis of samples of arterial and plasma revealed that the ABCA1 protein's expression was lower in plaques than in controls. Additionally, the ABCA1 protein was only detected in minimally atherosclerotic arteries. This method is highly sensitive, but less specific than PCR. The preliminary study isn't conclusive, and more research is needed. In the meantime, these findings could help us develop a better and more reliable detection method for ABCA1 in plaques and human arteries.
Furthermore, the significant expression of ABCA1 in the liver suggests that the liver may play a crucial role in the regulation of HDL-C levels. In mice that were exposed to a high-fat/high-cholesterol diet for 7 days, endogenous murine ABCA1 protein levels increased significantly. The mice also had higher plasma HDL-C levels, which indicated that ABCA1 mRNAs were also present in their livers.
PMID: 10884428 by Santamarina-Fojo S., et al. Complete genomic sequence of the human ABCA1 gene: analysis of the human and mouse ATP-binding cassette A promoter.
PMID: 11352567 by Qiu Y., et al. Human and mouse ABCA1 comparative sequencing and transgenesis studies revealing novel regulatory sequences.