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A1AT is a 52-kDa serpin and, in medicine, it is considered the most prominent serpin ; the terms α1-antitrypsin and protease inhibitor ( P < sub > i </ sub >) are often used interchangeably.
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A1AT and is
Alpha 1-antitrypsin deficiency ( α1-antitrypsin deficiency, A1AD or simply Alpha-1 ) is a genetic disorder that causes defective production of alpha 1-antitrypsin ( A1AT ), leading to decreased A1AT activity in the blood and lungs, and deposition of excessive abnormal A1AT protein in liver cells.
It is treated by avoidance of damaging inhalants, by intravenous infusions of the A1AT protein, by transplantation of the liver or lungs, and by a variety of other measures, but it usually produces some degree of disability and reduced life expectancy.
Alpha 1-antitrypsin ( A1AT ) is produced in the liver, and one of its functions is to protect the lungs from neutrophil elastase, an enzyme that can disrupt connective tissue.
However, in individuals with the PiZZ phenotype, A1AT levels are less than 15 % of normal, and patients are likely to develop panacinar emphysema at a young age ; 50 % of these patients will develop liver cirrhosis, because the A1AT is not secreted properly and instead accumulates in the liver.
It is estimated that about 1 % of all COPD patients actually have A1AT deficiency.
The initial test performed is serum A1AT level.
A1AT is further analysed by isoelectric focusing ( IEF ) in the pH range 4. 5-5. 5, where the protein migrates in a gel according to its isoelectric point or charge in a pH gradient.
Normal A1AT is termed M, as it is migrates toward the center of such an IEF gel.
Alpha 1-Antitrypsin or α < sub > 1 </ sub >- antitrypsin ( A1AT ) is a protease inhibitor belonging to the serpin superfamily.
Because A1AT is expressed in the liver, certain mutations in the gene encoding the protein can cause misfolding and impaired secretion, which can lead to liver cirrhosis.
A1AT is a single-chain glycoprotein consisting of 394 amino acids in the mature form and exhibits a number of glycoforms.
The single cysteine residue of A1AT in position 256 ( ExPASy nomenclature ) is found to be covalently linked to a free single cysteine by a disulfide bridge.
As protein electrophoresis is imprecise, A1AT is analysed by isoelectric focusing ( IEF ) in the pH range 4. 5-5. 5, where the protein migrates in a gel according to its isoelectric point or charge in a pH gradient.
Normal A1AT is termed M, as it is migrates toward the center of such an IEF gel.
Aerosolized-augmented A1AT therapy is under study.
In medicine, protease inhibitor is often used interchangeably with alpha 1-antitrypsin ( A1AT, which is abbreviated PI for this reason ).
A1AT and most
North-Western Europeans are most at risk for carrying one of the most common mutant forms of A1AT, the Z mutation ( Glu342Lys on M1A, rs28929474 ).
A1AT is indeed the protease inhibitor most often involved in disease, namely in alpha 1-antitrypsin deficiency.
A1AT and protease
Like all serine protease inhibitors, A1AT has a characteristic secondary structure of beta sheets and alpha helices.
A1AT and are
Severe A1AT deficiency causes panacinar emphysema or COPD in adult life in many people with the condition ( especially if they are exposed to cigarette smoke ), as well as various liver diseases in a minority of children and adults, and occasionally more unusual problems.
In individuals with PiSS, PiMZ and PiSZ phenotypes, blood levels of A1AT are reduced to between 40 and 60 % of normal levels.
Long-term studies of the effectiveness of A1AT replacement therapy are not available.
All three products showed minor differences compared to the normal human plasma A1AT, and are introduced during the specific purifications procedures.
A1AT and .
A1AT deficiency remains undiagnosed in many patients.
A low level of A1AT confirms the diagnosis and further assessment with A1AT protein phenotyping and A1AT genotyping should be carried out subsequently.
As protein electrophoresis does not completely distinguish between A1AT and other minor proteins at the alpha-1 position ( agarose gel ), antitrypsin can be more directly and specifically measured using a nephelometric or immunotubidimetric method.
As every person has two copies of the A1AT gene, a heterozygote with two different copies of the gene may have two different bands showing on electrofocusing, although a heterozygote with one null mutant that abolishes expression of the gene will only show one band.
Treatments currently being studied include recombinant and inhaled forms of A1AT.
is and serpin
One example of protease inhibitors is the serpin superfamily, which includes alpha 1-antitrypsin, C1-inhibitor, antithrombin, alpha 1-antichymotrypsin, plasminogen activator inhibitor-1, and neuroserpin.
* Antithrombin is a serine protease inhibitor ( serpin ) that degrades the serine proteases: thrombin, FIXa, FXa, FXIa, and FXIIa.
It is a member of the serpin family, although it is not known to inhibit other enzymes, unlike most serpins.
In terms of genomics, TBG is a serpin ; however, it has no inhibitory function like many other members of this class of proteins.
Transcortin, also known as corticosteroid-binding globulin ( CBG ) or serpin A6 is a protein that in humans is encoded by the SERPINA6 gene.
The term serpin is used to describe these latter members as well, despite their noninhibitory function.
For example, the serpin antitrypsin is primarily produced in the liver, and antitrypsin polymerisation causes liver cirrhosis.
C1-inhibitor is a serine protease inhibitor ( serpin ) protein.
Alpha 2-antiplasmin ( or α < sub > 2 </ sub >- antiplasmin or plasmin inhibitor ) is a serine protease inhibitor ( serpin ) responsible for inactivating plasmin, an important enzyme that participates in fibrinolysis and degradation of various other proteins.
Ovalbumin displays sequence and three-dimensional homology to the serpin superfamily, but unlike most serpins it is not a serine protease inhibitor.
C1-inhibitor ( C1-inh, C1 esterase inhibitor ) is a protease inhibitor belonging to the serpin superfamily.
C1-inhibitor is the largest member among the serpin superfamily of proteins.
The C-terminal serpin domain is similar to other serpins, which is the part of C1-inhibitor that provides the inhibitory activity.
Factor Xa is inactivated by protein Z-dependent protease inhibitor ( ZPI ), a serine protease inhibitor ( serpin ).
Inhibitors of factor XIa include protein Z-dependent protease inhibitor ( ZPI, a member of the serine protease inhibitor / serpin class of proteins ), which is independent of protein Z ( its action on factor X, however, is protein Z-dependent, hence its name ).
Plasminogen activator inhibitor-1 ( PAI-1 ) also known as endothelial plasminogen activator inhibitor or serpin E1 is a protein that in humans is encoded by the SERPINE1 gene.
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