Plasma glycoprotein member of the serpin superfamily which inhibits TRYPSIN; NEUTROPHIL ELASTASE; and other PROTEOLYTIC ENZYMES.
Deficiency of the protease inhibitor ALPHA 1-ANTITRYPSIN that manifests primarily as PULMONARY EMPHYSEMA and LIVER CIRRHOSIS.
Enlargement of air spaces distal to the TERMINAL BRONCHIOLES where gas-exchange normally takes place. This is usually due to destruction of the alveolar wall. Pulmonary emphysema can be classified by the location and distribution of the lesions.
A protease of broad specificity, obtained from dried pancreas. Molecular weight is approximately 25,000. The enzyme breaks down elastin, the specific protein of elastic fibers, and digests other proteins such as fibrin, hemoglobin, and albumin. EC 3.4.21.36.
Glycoprotein found in alpha(1)-globulin region in human serum. It inhibits chymotrypsin-like proteinases in vivo and has cytotoxic killer-cell activity in vitro. The protein also has a role as an acute-phase protein and is active in the control of immunologic and inflammatory processes, and as a tumor marker. It is a member of the serpin superfamily.
A pathological accumulation of air in tissues or organs.
Serine proteinase inhibitors which inhibit trypsin. They may be endogenous or exogenous compounds.
An enzyme that catalyzes the hydrolysis of proteins, including elastin. It cleaves preferentially bonds at the carboxyl side of Ala and Val, with greater specificity for Ala. EC 3.4.21.37.
One of the two major pharmacological subdivisions of adrenergic receptors that were originally defined by the relative potencies of various adrenergic compounds. The alpha receptors were initially described as excitatory receptors that post-junctionally stimulate SMOOTH MUSCLE contraction. However, further analysis has revealed a more complex picture involving several alpha receptor subtypes and their involvement in feedback regulation.
Hypoxia-inducible factor 1, alpha subunit is a basic helix-loop-helix transcription factor that is regulated by OXYGEN availability and is targeted for degradation by VHL TUMOR SUPPRESSOR PROTEIN.
A family of serine proteinase inhibitors which are similar in amino acid sequence and mechanism of inhibition, but differ in their specificity toward proteolytic enzymes. This family includes alpha 1-antitrypsin, angiotensinogen, ovalbumin, antiplasmin, alpha 1-antichymotrypsin, thyroxine-binding protein, complement 1 inactivators, antithrombin III, heparin cofactor II, plasminogen inactivators, gene Y protein, placental plasminogen activator inhibitor, and barley Z protein. Some members of the serpin family may be substrates rather than inhibitors of SERINE ENDOPEPTIDASES, and some serpins occur in plants where their function is not known.
Exogenous or endogenous compounds which inhibit SERINE ENDOPEPTIDASES.
The outward appearance of the individual. It is the product of interactions between genes, and between the GENOTYPE and the environment.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
A member of the NICOTINIC ACETYLCHOLINE RECEPTOR subfamily of the LIGAND-GATED ION CHANNEL family. It consists entirely of pentameric a7 subunits expressed in the CNS, autonomic nervous system, vascular system, lymphocytes and spleen.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
Electrophoresis in which a pH gradient is established in a gel medium and proteins migrate until they reach the site (or focus) at which the pH is equal to their isoelectric point.
A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.
Cell surface receptor for LAMININ, epiligrin, FIBRONECTINS, entactin, and COLLAGEN. Integrin alpha3beta1 is the major integrin present in EPITHELIAL CELLS, where it plays a role in the assembly of BASEMENT MEMBRANE as well as in cell migration, and may regulate the functions of other integrins. Two alternatively spliced isoforms of the alpha subunit (INTEGRIN ALPHA3), are differentially expressed in different cell types.
An integrin alpha subunit that is unique in that it does not contain an I domain, and its proteolytic cleavage site is near the middle of the extracellular portion of the polypeptide rather than close to the membrane as in other integrin alpha subunits.
An integrin alpha subunit that primarily associates with INTEGRIN BETA1 or INTEGRIN BETA4 to form laminin-binding heterodimers. Integrin alpha6 has two alternatively spliced isoforms: integrin alpha6A and integrin alpha6B, which differ in their cytoplasmic domains and are regulated in a tissue-specific and developmental stage-specific manner.
Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.
Proteins prepared by recombinant DNA technology.
An integrin found in FIBROBLASTS; PLATELETS; MONOCYTES, and LYMPHOCYTES. Integrin alpha5beta1 is the classical receptor for FIBRONECTIN, but it also functions as a receptor for LAMININ and several other EXTRACELLULAR MATRIX PROTEINS.
Orosomucoid, also known as alpha-1-acid glycoprotein, is an acute phase protein involved in the immune response, functioning as a pattern recognition receptor and having the ability to bind various ligands including drugs and hormones.
The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.
Integrin alpha4beta1 is a FIBRONECTIN and VCAM-1 receptor present on LYMPHOCYTES; MONOCYTES; EOSINOPHILS; NK CELLS and thymocytes. It is involved in both cell-cell and cell- EXTRACELLULAR MATRIX adhesion and plays a role in INFLAMMATION, hematopoietic cell homing and immune function, and has been implicated in skeletal MYOGENESIS; NEURAL CREST migration and proliferation, lymphocyte maturation and morphogenesis of the PLACENTA and HEART.
An interleukin-1 subtype that occurs as a membrane-bound pro-protein form that is cleaved by proteases to form a secreted mature form. Unlike INTERLEUKIN-1BETA both membrane-bound and secreted forms of interleukin-1alpha are biologically active.
Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.
Pathological processes of the LIVER.
The rate dynamics in chemical or physical systems.
An integrin found on fibroblasts, platelets, endothelial and epithelial cells, and lymphocytes where it functions as a receptor for COLLAGEN and LAMININ. Although originally referred to as the collagen receptor, it is one of several receptors for collagen. Ligand binding to integrin alpha2beta1 triggers a cascade of intracellular signaling, including activation of p38 MAP kinase.
The parts of a macromolecule that directly participate in its specific combination with another molecule.
Hepatocyte nuclear factor 1-alpha is a transcription factor found in the LIVER; PANCREAS; and KIDNEY that regulates HOMEOSTASIS of GLUCOSE.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
A subclass of alpha-adrenergic receptors that mediate contraction of SMOOTH MUSCLE in a variety of tissues such as ARTERIOLES; VEINS; and the UTERUS. They are usually found on postsynaptic membranes and signal through GQ-G11 G-PROTEINS.
Plasma glycoproteins that form a stable complex with hemoglobin to aid the recycling of heme iron. They are encoded in man by a gene on the short arm of chromosome 16.
The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).
This integrin alpha subunit combines with INTEGRIN BETA1 to form a receptor (INTEGRIN ALPHA5BETA1) that binds FIBRONECTIN and LAMININ. It undergoes posttranslational cleavage into a heavy and a light chain that are connected by disulfide bonds.
Integrin alpha1beta1 functions as a receptor for LAMININ and COLLAGEN. It is widely expressed during development, but in the adult is the predominant laminin receptor (RECEPTORS, LAMININ) in mature SMOOTH MUSCLE CELLS, where it is important for maintenance of the differentiated phenotype of these cells. Integrin alpha1beta1 is also found in LYMPHOCYTES and microvascular endothelial cells, and may play a role in angiogenesis. In SCHWANN CELLS and neural crest cells, it is involved in cell migration. Integrin alpha1beta1 is also known as VLA-1 and CD49a-CD29.
A subclass of alpha-adrenergic receptors found on both presynaptic and postsynaptic membranes where they signal through Gi-Go G-PROTEINS. While postsynaptic alpha-2 receptors play a traditional role in mediating the effects of ADRENERGIC AGONISTS, the subset of alpha-2 receptors found on presynaptic membranes signal the feedback inhibition of NEUROTRANSMITTER release.
A serine endopeptidase secreted by the pancreas as its zymogen, CHYMOTRYPSINOGEN and carried in the pancreatic juice to the duodenum where it is activated by TRYPSIN. It selectively cleaves aromatic amino acids on the carboxyl side.
A cell surface receptor mediating cell adhesion to the EXTRACELLULAR MATRIX and to other cells via binding to LAMININ. It is involved in cell migration, embryonic development, leukocyte activation and tumor cell invasiveness. Integrin alpha6beta1 is the major laminin receptor on PLATELETS; LEUKOCYTES; and many EPITHELIAL CELLS, and ligand binding may activate a number of signal transduction pathways. Alternative splicing of the cytoplasmic domain of the alpha6 subunit (INTEGRIN ALPHA6) results in the formation of A and B isoforms of the heterodimer, which are expressed in a tissue-specific manner.
Pathological conditions in the INTESTINES that are characterized by the gastrointestinal loss of serum proteins, including SERUM ALBUMIN; IMMUNOGLOBULINS; and at times LYMPHOCYTES. Severe condition can result in HYPOGAMMAGLOBULINEMIA or LYMPHOPENIA. Protein-losing enteropathies are associated with a number of diseases including INTESTINAL LYMPHANGIECTASIS; WHIPPLE'S DISEASE; and NEOPLASMS of the SMALL INTESTINE.
Serum globulins with high molecular weight. (Dorland, 28th ed)
Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control (induction or repression) of gene action at the level of transcription or translation.
The uptake of naked or purified DNA by CELLS, usually meaning the process as it occurs in eukaryotic cells. It is analogous to bacterial transformation (TRANSFORMATION, BACTERIAL) and both are routinely employed in GENE TRANSFER TECHNIQUES.
This intrgrin is a key component of HEMIDESMOSOMES and is required for their formation and maintenance in epithelial cells. Integrin alpha6beta4 is also found on thymocytes, fibroblasts, and Schwann cells, where it functions as a laminin receptor (RECEPTORS, LAMININ) and is involved in wound healing, cell migration, and tumor invasiveness.
The alpha subunits of integrin heterodimers (INTEGRINS), which mediate ligand specificity. There are approximately 18 different alpha chains, exhibiting great sequence diversity; several chains are also spliced into alternative isoforms. They possess a long extracellular portion (1200 amino acids) containing a MIDAS (metal ion-dependent adhesion site) motif, and seven 60-amino acid tandem repeats, the last 4 of which form EF HAND MOTIFS. The intracellular portion is short with the exception of INTEGRIN ALPHA4.
A system of cisternae in the CYTOPLASM of many cells. In places the endoplasmic reticulum is continuous with the plasma membrane (CELL MEMBRANE) or outer membrane of the nuclear envelope. If the outer surfaces of the endoplasmic reticulum membranes are coated with ribosomes, the endoplasmic reticulum is said to be rough-surfaced (ENDOPLASMIC RETICULUM, ROUGH); otherwise it is said to be smooth-surfaced (ENDOPLASMIC RETICULUM, SMOOTH). (King & Stansfield, A Dictionary of Genetics, 4th ed)
A family of transmembrane glycoproteins (MEMBRANE GLYCOPROTEINS) consisting of noncovalent heterodimers. They interact with a wide variety of ligands including EXTRACELLULAR MATRIX PROTEINS; COMPLEMENT, and other cells, while their intracellular domains interact with the CYTOSKELETON. The integrins consist of at least three identified families: the cytoadhesin receptors(RECEPTORS, CYTOADHESIN), the leukocyte adhesion receptors (RECEPTORS, LEUKOCYTE ADHESION), and the VERY LATE ANTIGEN RECEPTORS. Each family contains a common beta-subunit (INTEGRIN BETA CHAINS) combined with one or more distinct alpha-subunits (INTEGRIN ALPHA CHAINS). These receptors participate in cell-matrix and cell-cell adhesion in many physiologically important processes, including embryological development; HEMOSTASIS; THROMBOSIS; WOUND HEALING; immune and nonimmune defense mechanisms; and oncogenic transformation.
Water-soluble proteins found in egg whites, blood, lymph, and other tissues and fluids. They coagulate upon heating.
Proteins that are present in blood serum, including SERUM ALBUMIN; BLOOD COAGULATION FACTORS; and many other types of proteins.
An integrin alpha subunit that binds COLLAGEN and LAMININ though its I domain. It combines with INTEGRIN BETA1 to form the heterodimer INTEGRIN ALPHA1BETA1.
A deoxyribonucleotide polymer that is the primary genetic material of all cells. Eukaryotic and prokaryotic organisms normally contain DNA in a double-stranded state, yet several important biological processes transiently involve single-stranded regions. DNA, which consists of a polysugar-phosphate backbone possessing projections of purines (adenine and guanine) and pyrimidines (thymine and cytosine), forms a double helix that is held together by hydrogen bonds between these purines and pyrimidines (adenine to thymine and guanine to cytosine).
Glycoproteins with a molecular weight of approximately 620,000 to 680,000. Precipitation by electrophoresis is in the alpha region. They include alpha 1-macroglobulins and alpha 2-macroglobulins. These proteins exhibit trypsin-, chymotrypsin-, thrombin-, and plasmin-binding activity and function as hormonal transporters.
A serine endopeptidase that is formed from TRYPSINOGEN in the pancreas. It is converted into its active form by ENTEROPEPTIDASE in the small intestine. It catalyzes hydrolysis of the carboxyl group of either arginine or lysine. EC 3.4.21.4.
An individual having different alleles at one or more loci regarding a specific character.
An individual in which both alleles at a given locus are identical.
Brain waves characterized by a relatively high voltage or amplitude and a frequency of 8-13 Hz. They constitute the majority of waves recorded by EEG registering the activity of the parietal and occipital lobes when the individual is awake, but relaxed with the eyes closed.
A member of the serpin family of proteins that is found in plasma and urine. It is dependent on heparin and is able to inhibit activated PROTEIN C; THROMBIN; KALLIKREIN; and other SERINE ENDOPEPTIDASES.
Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.
A serine endopeptidase found primarily in the EXTRACELLULAR MATRIX. It has specificity for cleavage of a variety of substrates including PRORENIN, pro-membrane type-1 matrix metalloproteinase, and NEURAL CELL ADHESION MOLECULE L1.
The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.
A mammalian pancreatic extract composed of enzymes with protease, amylase and lipase activities. It is used as a digestant in pancreatic malfunction.
An integrin alpha subunit that occurs as alternatively spliced isoforms. The isoforms are differentially expressed in specific cell types and at specific developmental stages. Integrin alpha3 combines with INTEGRIN BETA1 to form INTEGRIN ALPHA3BETA1 which is a heterodimer found primarily in epithelial cells.
A proprotein convertase with specificity for the proproteins of PROALBUMIN; COMPLEMENT 3C; and VON WILLEBRAND FACTOR. It has specificity for cleavage near paired ARGININE residues that are separated by two amino acids.
Variant forms of the same gene, occupying the same locus on homologous CHROMOSOMES, and governing the variants in production of the same gene product.
Inbred C57BL mice are a strain of laboratory mice that have been produced by many generations of brother-sister matings, resulting in a high degree of genetic uniformity and homozygosity, making them widely used for biomedical research, including studies on genetics, immunology, cancer, and neuroscience.

The disulfide-bonded loop of chromogranin B mediates membrane binding and directs sorting from the trans-Golgi network to secretory granules. (1/1525)

The disulfide-bonded loop of chromogranin B (CgB), a regulated secretory protein with widespread distribution in neuroendocrine cells, is known to be essential for the sorting of CgB from the trans-Golgi network (TGN) to immature secretory granules. Here we show that this loop, when fused to the constitutively secreted protein alpha1-antitrypsin (AT), is sufficient to direct the fusion protein to secretory granules. Importantly, the sorting efficiency of the AT reporter protein bearing two loops (E2/3-AT-E2/3) is much higher compared with that of AT with a single disulfide-bonded loop. In contrast to endogenous CgB, E2/3-AT-E2/3 does not undergo Ca2+/pH-dependent aggregation in the TGN. Furthermore, the disulfide-bonded loop of CgB mediates membrane binding in the TGN and does so with 5-fold higher efficiency if two loops are present on the reporter protein. The latter finding supports the concept that under physiological conditions, aggregates of CgB are the sorted units of cargo which have multiple loops on their surface leading to high membrane binding and sorting efficiency of CgB in the TGN.  (+info)

Identification of DNA polymorphisms associated with the V type alpha1-antitrypsin gene. (2/1525)

alpha1-Antitrypsin (alpha1-AT) is a highly polymorphic protein. The V allele of alpha1-AT has been shown to be associated with focal glomerulosclerosis (FGS) in Negroid and mixed race South African patients. To identify mutations and polymorphisms in the gene for the V allele of alpha1-AT in five South African patients with FGS nephrotic syndrome DNA sequence analysis and restriction fragment length polymorphisms of the coding exons were carried out. Four of the patients were heterozygous for the BstEII RFLP in exon III [M1(Val213)(Ala213)] and one patient was a M1(Ala213) homozygote. The mutation for the V allele was identified in exon II as Gly-148 (GGG)-->Arg (AGG) and in all patients was associated with a silent mutation at position 158 (AAC-->AAT). The patient who was homozygous for (Ala213) also had a silent mutation at position 256 in exon III (GAT-->GAC) which was not present in any of the other four patients. Although the V allele of alpha1-AT is not associated with severe plasma deficiency, it may be in linkage disequilibrium with other genes on chromosome 14 that predispose to FGS. Furthermore, the associated silent mutation at position 158 and the Ala213 polymorphism are of interest, as these could represent an evolutionary intermediate between the M1(Ala213) and M1(Val213) subtypes.  (+info)

The Pseudomonas aeruginosa secretory product pyocyanin inactivates alpha1 protease inhibitor: implications for the pathogenesis of cystic fibrosis lung disease. (3/1525)

Alpha1 Protease inhibitor (alpha1PI) modulates serine protease activity in the lung. Reactive oxygen species inactivate alpha1PI, and this process has been implicated in the pathogenesis of a variety of forms of lung injury. An imbalance of protease-antiprotease activity is also detected in the airways of patients with cystic fibrosis-associated lung disease who are infected with Pseudomonas aeruginosa. P. aeruginosa secretes pyocyanin, which, through its ability to redox cycle, induces cells to generate reactive oxygen species. We tested the hypothesis that redox cycling of pyocyanin could lead to inactivation of alpha1PI. When alpha1PI was exposed to NADH and pyocyanin, a combination that results in superoxide production, alpha1PI lost its ability to form an inhibitory complex with both porcine pancreatic elastase (PPE) and trypsin. Similarly, addition of pyocyanin to cultures of human airway epithelial cells to which alpha1PI was also added resulted in a loss of the ability of alpha1PI to form a complex with PPE or trypsin. Neither superoxide dismutase, catalase, nor dimethylthiourea nor depletion of the media of O2 to prevent formation of reactive oxygen species blocked pyocyanin-mediated inactivation of alpha1PI. These data raise the possibility that a direct interaction between reduced pyocyanin and alpha1PI is involved in the process. Consistent with this possibility, pretreatment of alpha1PI with the reducing agent beta-mercaptoethanol also inhibited binding of trypsin to alpha1PI. These data suggest that pyocyanin could contribute to lung injury in the P. aeruginosa-infected airway of cystic fibrosis patients by decreasing the ability of alpha1PI to control the local activity of serine proteases.  (+info)

Oligosaccharide modification in the early secretory pathway directs the selection of a misfolded glycoprotein for degradation by the proteasome. (4/1525)

The role of conformation-based quality control in the early secretory pathway is to eliminate misfolded polypeptides and unassembled multimeric protein complexes from the endoplasmic reticulum, ensuring the deployment of only functional molecules to distal sites. The intracellular fate of terminally misfolded human alpha1-antitrypsin was examined in hepatoma cells to identify the functional role of asparagine-linked oligosaccharide modification in the selection of glycoproteins for degradation by the cytosolic proteasome. Proteasomal degradation required physical interaction with the molecular chaperone calnexin. Altered sedimentation of intracellular complexes following treatment with the specific proteasome inhibitor lactacystin, and in combination with mannosidase inhibition, revealed that the removal of mannose from attached oligosaccharides abrogates the release of misfolded alpha1-antitrypsin from calnexin prior to proteasomal degradation. Intracellular turnover was arrested with kifunensine, implicating the participation of endoplasmic reticulum mannosidase I in the disposal process. Accelerated degradation occurred in a mannosidase-independent manner and was arrested by lactacystin, in response to the posttranslational inhibition of glucosidase II, demonstrating that the attenuated removal of glucose from attached oligosaccharides functions as the underlying rate-limiting step in the proteasome-mediated pathway. A model is proposed in which the removal of mannose from multiple attached oligosaccharides directs calnexin in the selection of misfolded alpha1-antitrypsin for degradation by the proteasome.  (+info)

Enhanced tumor growth and invasiveness in vivo by a carboxyl-terminal fragment of alpha1-proteinase inhibitor generated by matrix metalloproteinases: a possible modulatory role in natural killer cytotoxicity. (5/1525)

Matrix metalloproteinases (MMPs) are believed to contribute to the complex process of cancer progression. They also exhibit an alpha1-proteinase inhibitor (alphaPI)-degrading activity generating a carboxyl-terminal fragment of approximately 5 kd (alphaPI-C). This study reports that overexpression of alphaPI-C in S2-020, a cloned subline derived from the human pancreas adenocarcinoma cell line SUIT-2, potentiates the growth capability of the cells in nude mice. After stable transfection of a vector containing a chimeric cDNA encoding a signal peptide sequence of tissue inhibitor of metalloproteinase-1 followed by cDNA for alphaPI-C into S2-020 cells, three clones that stably secrete alphaPI-C were obtained. The ectopic expression of alphaPI-C did not alter in vitro cellular growth. However, subcutaneous injection of the alphaPI-C-secreting clones resulted in tumors that were 1.5 to 3-fold larger than those of control clones with an increased tendency to invasiveness and lymph node metastasis. These effects could be a result of modulation of natural killer (NK) cell-mediated control of tumor growth in nude mice, as the growth advantage of alphaPI-C-secreting clones was not observed in NK-depleted mice, and alphaPI-C-secreting clones showed decreased NK sensitivity in vitro. In addition, production of alphaPI and generation of the cleaved form of alphaPI by MMP were observed in various human tumor cell lines and in a highly metastatic subline of SUIT-2 in vitro. These results provide experimental evidence that the alphaPI-degrading activity of MMPs may play a role in tumor progression not only via the inactivation of alphaPI but also via the generation of alphaPI-C.  (+info)

Cytokines and inflammatory mediators do not indicate acute infection in cystic fibrosis. (6/1525)

Various treatment regimens and difficulties with research design are encountered with cystic fibrosis (CF) because no standard diagnostic criteria exist for defining acute respiratory exacerbations. This study evaluated the role of serial monitoring of concentrations of selected cytokines and inflammatory mediators in serum and sputum as predictors of respiratory exacerbation, as useful outcome measures for CF, and to guide therapy. Interleukin-8 (IL-8), tumor necrosis factor alpha (TNF-alpha), neutrophil elastase-alpha-1-protease inhibitor complex (NE complex), protein, and alpha-1-protease inhibitor (alpha-1-PI) were measured in serum and sputum collected from CF patients during respiratory exacerbations and periods of well-being. Levels of NE complex, protein, and alpha-1-PI in sputum rose during respiratory exacerbations and fell after institution of antibiotic therapy (P = 0.078, 0.001, and 0.002, respectively). Mean (+/- standard error of the mean) levels of IL-8 and TNF-alpha were extremely high in sputum (13,780 +/- 916 and 249.4 +/- 23.5 ng/liter, respectively) but did not change significantly with clinical deterioration of the patient (P > 0.23). IL-8 and TNF-alpha were generally undetectable in serum, and therefore these measures were unhelpful. Drop in forced expiratory volume in 1 s was the only clinical or laboratory parameter that was close to being a determinant of respiratory exacerbation (P = 0.055). This study provides evidence of intense immunological activity occurring continually within the lungs of adult CF patients. Measurement of cytokines and inflammatory mediators in CF sputum is not helpful for identifying acute respiratory exacerbations.  (+info)

Probing the unfolding pathway of alpha1-antitrypsin. (7/1525)

Protein misfolding plays a role in the pathogenesis of many diseases. alpha1-Antitrypsin misfolding leads to the accumulation of long chain polymers within the hepatocyte, reducing its plasma concentration and predisposing the patient to emphysema and liver disease. In order to understand the misfolding process, it is necessary to examine the folding of alpha1-antitrypsin through the different structures involved in this process. In this study we have used a novel technique in which unique cysteine residues were introduced at various positions into alpha1-antitrypsin and fluorescently labeled with N, N'-dimethyl-N-(iodoacetyl)-N'-(7-nitrobenz-2-oxa-1, 3-diazol-4-yl)ethylenediamine. The fluorescence properties of each protein were studied in the native state and as a function of guanidine hydrochloride-mediated unfolding. The studies found that alpha1-antitrypsin unfolded through a series of intermediate structures. From the position of the fluorescence probes, the fluorescence quenching data, and the molecular modeling, we show that unfolding of alpha1-antitrypsin occurs via disruption of the A and C beta-sheets followed by the B beta-sheet. The implications of these data on both alpha1-antitrypsin function and polymerization are discussed.  (+info)

A kinetic mechanism for the polymerization of alpha1-antitrypsin. (8/1525)

The mutation in the Z deficiency variant of alpha1-antitrypsin perturbs the structure of the protein to allow a unique intermolecular linkage. These loop-sheet polymers are retained within the endoplasmic reticulum of hepatocytes to form inclusions that are associated with neonatal hepatitis, juvenile cirrhosis, and hepatocellular carcinoma. The process of polymer formation has been investigated here by intrinsic tryptophan fluorescence, fluorescence polarization, circular dichroic spectra and extrinsic fluorescence with 8-anilino-1-naphthalenesulfonic acid and tetramethylrhodamine-5-iodoacetamide. These biophysical techniques have demonstrated that alpha1-antitrypsin polymerization is a two-stage process and have allowed the calculation of rates for both of these steps. The initial fast phase is unimolecular and likely to represent temperature-induced protein unfolding, while the slow phase is bimolecular and associated with loop-sheet interaction and polymer formation. The naturally occurring Z, S, and I variants and recombinant site-directed reactive loop and shutter domain mutants of alpha1-antitrypsin were used to demonstrate the close association between protein stability and rate of alpha1-antitrypsin polymerization. Taken together, these data allow us to propose a kinetic mechanism for alpha1-antitrypsin polymer formation that involves the generation of an unstable intermediate, which can form polymers or generate latent protein.  (+info)

Alpha 1-antitrypsin (AAT, or α1-antiproteinase, A1AP) is a protein that is primarily produced by the liver and released into the bloodstream. It belongs to a group of proteins called serine protease inhibitors, which help regulate inflammation and protect tissues from damage caused by enzymes involved in the immune response.

Alpha 1-antitrypsin is particularly important for protecting the lungs from damage caused by neutrophil elastase, an enzyme released by white blood cells called neutrophils during inflammation. In the lungs, AAT binds to and inhibits neutrophil elastase, preventing it from degrading the extracellular matrix and damaging lung tissue.

Deficiency in alpha 1-antitrypsin can lead to chronic obstructive pulmonary disease (COPD) and liver disease. The most common cause of AAT deficiency is a genetic mutation that results in abnormal folding and accumulation of the protein within liver cells, leading to reduced levels of functional AAT in the bloodstream. This condition is called alpha 1-antitrypsin deficiency (AATD) and can be inherited in an autosomal codominant manner. Individuals with severe AATD may require augmentation therapy with intravenous infusions of purified human AAT to help prevent lung damage.

Alpha 1-Antitrypsin (AAT) deficiency is a genetic disorder that results from insufficient levels of the protective protein AAT in the blood and lungs. This protein is produced by the liver and helps to protect the lungs from damage caused by inflammation and the action of enzymes, such as neutrophil elastase, that are released during the immune response.

In people with AAT deficiency, the lack of adequate AAT levels leads to an uncontrolled increase in neutrophil elastase activity, which can cause damage to lung tissue and result in emphysema, a condition characterized by shortness of breath, coughing, and wheezing. Additionally, some individuals with AAT deficiency may develop liver disease due to the accumulation of abnormal AAT proteins in liver cells.

There are different variants or genotypes associated with AAT deficiency, with the most common and severe form being the PiZZ genotype. This variant is caused by mutations in the SERPINA1 gene, which encodes for the AAT protein. Individuals who inherit two copies of this mutated gene (one from each parent) will have very low levels of AAT in their blood and are at increased risk of developing emphysema and liver disease.

Diagnosis of AAT deficiency typically involves measuring AAT levels in the blood and performing genetic testing to identify specific variants of the SERPINA1 gene. Treatment may include lifestyle modifications, such as smoking cessation, bronchodilators, and corticosteroids to manage lung symptoms, as well as augmentation therapy with intravenous infusions of AAT protein to help slow disease progression in individuals with severe deficiency. Liver transplantation may be considered for those with advanced liver disease.

Pulmonary emphysema is a chronic respiratory disease characterized by abnormal, permanent enlargement of the airspaces distal to the terminal bronchioles, accompanied by destruction of their walls and without obvious fibrosis. This results in loss of elastic recoil, which leads to trappling of air within the lungs and difficulty exhaling. It is often caused by cigarette smoking or long-term exposure to harmful pollutants. The disease is part of a group of conditions known as chronic obstructive pulmonary disease (COPD), which also includes chronic bronchitis.

Pancreatic elastase is a type of elastase that is specifically produced by the pancreas. It is an enzyme that helps in digesting proteins found in the food we eat. Pancreatic elastase breaks down elastin, a protein that provides elasticity to tissues and organs in the body.

In clinical practice, pancreatic elastase is often measured in stool samples as a diagnostic tool to assess exocrine pancreatic function. Low levels of pancreatic elastase in stool may indicate malabsorption or exocrine pancreatic insufficiency, which can be caused by various conditions such as chronic pancreatitis, cystic fibrosis, or pancreatic cancer.

Alpha 1-Antichymotrypsin (ACT), also known as Serpin A1, is a protein found in the blood that belongs to the serine protease inhibitor family. It functions to regulate enzymes that break down other proteins in the body. ACT helps to prevent excessive and potentially harmful proteolytic activity, which can contribute to tissue damage and inflammation.

Deficiency or dysfunction of alpha 1-Antichymotrypsin has been associated with several medical conditions, including:

1. Alpha 1-Antichymotrypsin Deficiency: A rare genetic disorder characterized by low levels of ACT in the blood, which can lead to increased risk of developing lung and liver diseases.
2. Alzheimer's Disease: Increased levels of ACT have been found in the brains of individuals with Alzheimer's disease, suggesting a possible role in the pathogenesis of this neurodegenerative disorder.
3. Cancer: Elevated levels of ACT have been observed in various types of cancer, including lung, breast, and prostate cancers, potentially contributing to tumor growth and metastasis.
4. Inflammatory and immune-mediated disorders: Increased ACT levels are associated with several inflammatory conditions, such as rheumatoid arthritis, systemic lupus erythematosus (SLE), and vasculitis, suggesting its involvement in the regulation of the immune response.
5. Cardiovascular diseases: Elevated ACT levels have been linked to an increased risk of developing cardiovascular diseases, including atherosclerosis and myocardial infarction (heart attack).

Understanding the role of alpha 1-Antichymotrypsin in various physiological and pathological processes can provide valuable insights into disease mechanisms and potential therapeutic targets.

Emphysema is a chronic respiratory disease characterized by abnormal, permanent enlargement of the airspaces called alveoli in the lungs, accompanied by destruction of their walls. This results in loss of elasticity and decreased gas exchange efficiency, causing shortness of breath and coughing. It is often caused by smoking or exposure to harmful pollutants. The damage to the lungs is irreversible, but quitting smoking and using medications can help alleviate symptoms and slow disease progression.

Trypsin inhibitors are substances that inhibit the activity of trypsin, an enzyme that helps digest proteins in the small intestine. Trypsin inhibitors can be found in various foods such as soybeans, corn, and raw egg whites. In the case of soybeans, trypsin inhibitors are denatured and inactivated during cooking and processing.

In a medical context, trypsin inhibitors may be used therapeutically to regulate excessive trypsin activity in certain conditions such as pancreatitis, where there is inflammation of the pancreas leading to the release of activated digestive enzymes, including trypsin, into the pancreas and surrounding tissues. By inhibiting trypsin activity, these inhibitors can help reduce tissue damage and inflammation.

Leukocyte elastase is a type of enzyme that is released by white blood cells (leukocytes), specifically neutrophils, during inflammation. Its primary function is to help fight infection by breaking down the proteins in bacteria and viruses. However, if not properly regulated, leukocyte elastase can also damage surrounding tissues, contributing to the progression of various diseases such as chronic obstructive pulmonary disease (COPD), acute respiratory distress syndrome (ARDS), and cystic fibrosis.

Leukocyte elastase is often measured in clinical settings as a marker of inflammation and neutrophil activation, particularly in patients with lung diseases. Inhibitors of leukocyte elastase have been developed as potential therapeutic agents for these conditions.

Adrenergic receptors are a type of G protein-coupled receptor that bind and respond to catecholamines, such as epinephrine (adrenaline) and norepinephrine (noradrenaline). Alpha adrenergic receptors (α-ARs) are a subtype of adrenergic receptors that are classified into two main categories: α1-ARs and α2-ARs.

The activation of α1-ARs leads to the activation of phospholipase C, which results in an increase in intracellular calcium levels and the activation of various signaling pathways that mediate diverse physiological responses such as vasoconstriction, smooth muscle contraction, and cell proliferation.

On the other hand, α2-ARs are primarily located on presynaptic nerve terminals where they function to inhibit the release of neurotransmitters, including norepinephrine. The activation of α2-ARs also leads to the inhibition of adenylyl cyclase and a decrease in intracellular cAMP levels, which can mediate various physiological responses such as sedation, analgesia, and hypotension.

Overall, α-ARs play important roles in regulating various physiological functions, including cardiovascular function, mood, and cognition, and are also involved in the pathophysiology of several diseases, such as hypertension, heart failure, and neurodegenerative disorders.

Hypoxia-Inducible Factor 1 (HIF-1) is a transcription factor that plays a crucial role in the body's response to low oxygen levels, also known as hypoxia. HIF-1 is a heterodimeric protein composed of two subunits: an alpha subunit (HIF-1α) and a beta subunit (HIF-1β).

The alpha subunit, HIF-1α, is the regulatory subunit that is subject to oxygen-dependent degradation. Under normal oxygen conditions (normoxia), HIF-1α is constantly produced in the cell but is rapidly degraded by proteasomes due to hydroxylation of specific proline residues by prolyl hydroxylase domain-containing proteins (PHDs). This hydroxylation reaction requires oxygen as a substrate, and under hypoxic conditions, the activity of PHDs is inhibited, leading to the stabilization and accumulation of HIF-1α.

Once stabilized, HIF-1α translocates to the nucleus, where it heterodimerizes with HIF-1β and binds to hypoxia-responsive elements (HREs) in the promoter regions of target genes. This binding results in the activation of gene transcription programs that promote cellular adaptation to low oxygen levels. These adaptive responses include increased erythropoiesis, angiogenesis, glucose metabolism, and pH regulation, among others.

Therefore, HIF-1α is a critical regulator of the body's response to hypoxia, and its dysregulation has been implicated in various pathological conditions, including cancer, cardiovascular disease, and neurodegenerative disorders.

SERPINs are an acronym for "serine protease inhibitors." They are a group of proteins that inhibit serine proteases, which are enzymes that cut other proteins. SERPINs are found in various tissues and body fluids, including blood, and play important roles in regulating biological processes such as inflammation, blood clotting, and cell death. They do this by forming covalent complexes with their target proteases, thereby preventing them from carrying out their proteolytic activities. Mutations in SERPIN genes have been associated with several genetic disorders, including emphysema, cirrhosis, and dementia.

Serine proteinase inhibitors, also known as serine protease inhibitors or serpins, are a group of proteins that inhibit serine proteases, which are enzymes that cut other proteins in a process called proteolysis. Serine proteinases are important in many biological processes such as blood coagulation, fibrinolysis, inflammation and cell death. The inhibition of these enzymes by serpin proteins is an essential regulatory mechanism to maintain the balance and prevent uncontrolled proteolytic activity that can lead to diseases.

Serpins work by forming a covalent complex with their target serine proteinases, irreversibly inactivating them. The active site of serpins contains a reactive center loop (RCL) that mimics the protease's target protein sequence and acts as a bait for the enzyme. When the protease cleaves the RCL, it gets trapped within the serpin structure, leading to its inactivation.

Serpin proteinase inhibitors play crucial roles in various physiological processes, including:

1. Blood coagulation and fibrinolysis regulation: Serpins such as antithrombin, heparin cofactor II, and protease nexin-2 control the activity of enzymes involved in blood clotting and dissolution to prevent excessive or insufficient clot formation.
2. Inflammation modulation: Serpins like α1-antitrypsin, α2-macroglobulin, and C1 inhibitor regulate the activity of proteases released during inflammation, protecting tissues from damage.
3. Cell death regulation: Some serpins, such as PI-9/SERPINB9, control apoptosis (programmed cell death) by inhibiting granzyme B, a protease involved in this process.
4. Embryonic development and tissue remodeling: Serpins like plasminogen activator inhibitor-1 (PAI-1) and PAI-2 regulate the activity of enzymes involved in extracellular matrix degradation during embryonic development and tissue remodeling.
5. Neuroprotection: Serpins such as neuroserpin protect neurons from damage by inhibiting proteases released during neuroinflammation or neurodegenerative diseases.

Dysregulation of serpins has been implicated in various pathological conditions, including thrombosis, emphysema, Alzheimer's disease, and cancer. Understanding the roles of serpins in these processes may provide insights into potential therapeutic strategies for treating these diseases.

A phenotype is the physical or biochemical expression of an organism's genes, or the observable traits and characteristics resulting from the interaction of its genetic constitution (genotype) with environmental factors. These characteristics can include appearance, development, behavior, and resistance to disease, among others. Phenotypes can vary widely, even among individuals with identical genotypes, due to differences in environmental influences, gene expression, and genetic interactions.

A base sequence in the context of molecular biology refers to the specific order of nucleotides in a DNA or RNA molecule. In DNA, these nucleotides are adenine (A), guanine (G), cytosine (C), and thymine (T). In RNA, uracil (U) takes the place of thymine. The base sequence contains genetic information that is transcribed into RNA and ultimately translated into proteins. It is the exact order of these bases that determines the genetic code and thus the function of the DNA or RNA molecule.

The alpha7 nicotinic acetylcholine receptor (α7nAChR) is a type of cholinergic receptor found in the nervous system that is activated by the neurotransmitter acetylcholine. It is a ligand-gated ion channel that is widely distributed throughout the central and peripheral nervous systems, including in the hippocampus, cortex, thalamus, and autonomic ganglia.

The α7nAChR is composed of five subunits arranged around a central pore, and it has a high permeability to calcium ions (Ca2+). When acetylcholine binds to the receptor, it triggers a conformational change that opens the ion channel, allowing Ca2+ to flow into the cell. This influx of Ca2+ can activate various intracellular signaling pathways and have excitatory or inhibitory effects on neuronal activity, depending on the location and function of the receptor.

The α7nAChR has been implicated in a variety of physiological processes, including learning and memory, attention, sensory perception, and motor control. It has also been studied as a potential therapeutic target for various neurological and psychiatric disorders, such as Alzheimer's disease, schizophrenia, and pain.

Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.

Isoelectric focusing (IEF) is a technique used in electrophoresis, which is a method for separating proteins or other molecules based on their electrical charges. In IEF, a mixture of ampholytes (molecules that can carry both positive and negative charges) is used to create a pH gradient within a gel matrix. When an electric field is applied, the proteins or molecules migrate through the gel until they reach the point in the gradient where their net charge is zero, known as their isoelectric point (pI). At this point, they focus into a sharp band and stop moving, resulting in a highly resolved separation of the different components based on their pI. This technique is widely used in protein research for applications such as protein identification, characterization, and purification.

The liver is a large, solid organ located in the upper right portion of the abdomen, beneath the diaphragm and above the stomach. It plays a vital role in several bodily functions, including:

1. Metabolism: The liver helps to metabolize carbohydrates, fats, and proteins from the food we eat into energy and nutrients that our bodies can use.
2. Detoxification: The liver detoxifies harmful substances in the body by breaking them down into less toxic forms or excreting them through bile.
3. Synthesis: The liver synthesizes important proteins, such as albumin and clotting factors, that are necessary for proper bodily function.
4. Storage: The liver stores glucose, vitamins, and minerals that can be released when the body needs them.
5. Bile production: The liver produces bile, a digestive juice that helps to break down fats in the small intestine.
6. Immune function: The liver plays a role in the immune system by filtering out bacteria and other harmful substances from the blood.

Overall, the liver is an essential organ that plays a critical role in maintaining overall health and well-being.

Integrin α3β1 is a type of cell surface receptor that is widely expressed in various tissues, including epithelial and endothelial cells. It is composed of two subunits, α3 and β1, which form a heterodimeric complex that plays a crucial role in cell-matrix adhesion and signaling.

Integrin α3β1 binds to several extracellular matrix proteins, such as laminin, fibronectin, and collagen IV, and mediates various cellular functions, including cell migration, proliferation, differentiation, and survival. It also participates in intracellular signaling pathways that regulate cell behavior and tissue homeostasis.

Mutations in the genes encoding integrin α3β1 have been associated with several human diseases, including blistering skin disorders, kidney disease, and cancer. Therefore, understanding the structure, function, and regulation of integrin α3β1 is essential for developing new therapeutic strategies to treat these conditions.

Integrin α4 (also known as CD49d or ITGA4) is a subunit of integrin proteins, which are heterodimeric transmembrane receptors that mediate cell-cell and cell-extracellular matrix interactions. Integrin α4 typically pairs with β1 (CD29 or ITGB1) or β7 (ITGB7) subunits to form integrins α4β1 and α4β7, respectively.

Integrin α4β1, also known as very late antigen-4 (VLA-4), is widely expressed on various hematopoietic cells, including lymphocytes, monocytes, eosinophils, and basophils. It plays crucial roles in the adhesion, migration, and homing of these cells to secondary lymphoid organs, as well as in the recruitment of immune cells to inflammatory sites. Integrin α4β1 binds to its ligands, vascular cell adhesion molecule-1 (VCAM-1) and fibronectin, via the arginine-glycine-aspartic acid (RGD) motif.

Integrin α4β7, on the other hand, is primarily expressed on gut-homing lymphocytes and interacts with mucosal addressin cell adhesion molecule-1 (MAdCAM-1), a protein mainly found in the high endothelial venules of intestinal Peyer's patches and mesenteric lymph nodes. This interaction facilitates the trafficking of immune cells to the gastrointestinal tract, where they participate in immune responses against pathogens and maintain gut homeostasis.

In summary, Integrin α4 is a crucial subunit of integrins that mediates cell adhesion, migration, and homing to specific tissues through its interactions with various ligands. Dysregulation of integrin α4 has been implicated in several pathological conditions, including inflammatory diseases, autoimmune disorders, and cancer metastasis.

Integrin α6 (also known as CD49f) is a type of integrin, which is a heterodimeric transmembrane receptor that mediates cell-cell and cell-extracellular matrix (ECM) interactions. Integrins play crucial roles in various biological processes such as cell adhesion, migration, proliferation, differentiation, and survival.

Integrin α6 is a 130 kDa glycoprotein that pairs with integrin β1, β4 or β5 to form three distinct heterodimeric complexes: α6β1, α6β4, and α6β5. Among these, the α6β4 integrin is the most extensively studied. It specifically binds to laminins in the basement membrane and plays essential roles in maintaining epithelial tissue architecture and function.

The α6β4 integrin has a unique structure with an extended cytoplasmic domain of β4 that can interact with intracellular signaling molecules, cytoskeletal proteins, and other adhesion receptors. This interaction allows the formation of stable adhesion complexes called hemidesmosomes, which anchor epithelial cells to the basement membrane and provide mechanical stability to tissues.

Mutations in integrin α6 or its partners can lead to various human diseases, including epidermolysis bullosa, a group of inherited skin disorders characterized by fragile skin and mucous membranes that blister and tear easily.

A mutation is a permanent change in the DNA sequence of an organism's genome. Mutations can occur spontaneously or be caused by environmental factors such as exposure to radiation, chemicals, or viruses. They may have various effects on the organism, ranging from benign to harmful, depending on where they occur and whether they alter the function of essential proteins. In some cases, mutations can increase an individual's susceptibility to certain diseases or disorders, while in others, they may confer a survival advantage. Mutations are the driving force behind evolution, as they introduce new genetic variability into populations, which can then be acted upon by natural selection.

Recombinant proteins are artificially created proteins produced through the use of recombinant DNA technology. This process involves combining DNA molecules from different sources to create a new set of genes that encode for a specific protein. The resulting recombinant protein can then be expressed, purified, and used for various applications in research, medicine, and industry.

Recombinant proteins are widely used in biomedical research to study protein function, structure, and interactions. They are also used in the development of diagnostic tests, vaccines, and therapeutic drugs. For example, recombinant insulin is a common treatment for diabetes, while recombinant human growth hormone is used to treat growth disorders.

The production of recombinant proteins typically involves the use of host cells, such as bacteria, yeast, or mammalian cells, which are engineered to express the desired protein. The host cells are transformed with a plasmid vector containing the gene of interest, along with regulatory elements that control its expression. Once the host cells are cultured and the protein is expressed, it can be purified using various chromatography techniques.

Overall, recombinant proteins have revolutionized many areas of biology and medicine, enabling researchers to study and manipulate proteins in ways that were previously impossible.

Integrin α5β1, also known as very late antigen-5 (VLA-5) or fibronectin receptor, is a heterodimeric transmembrane receptor protein composed of two subunits: α5 and β1. This integrin is widely expressed in various cell types, including endothelial cells, smooth muscle cells, and fibroblasts.

Integrin α5β1 plays a crucial role in mediating cell-matrix adhesion by binding to the arginine-glycine-aspartic acid (RGD) sequence present in the extracellular matrix protein fibronectin. The interaction between integrin α5β1 and fibronectin is essential for various biological processes, such as cell migration, proliferation, differentiation, and survival. Additionally, this integrin has been implicated in several pathological conditions, including tumor progression, angiogenesis, and fibrosis.

Orosomucoid, also known as α-1-acid glycoprotein or AAG, is a protein found in human plasma. It's a member of the acute phase proteins, which are produced in higher amounts during inflammation and infection. Orosomucoid has a molecular weight of approximately 41-43 kDa and is composed of a single polypeptide chain with five N-linked glycosylation sites. It plays a role in protecting tissues from various harmful substances, such as proteases and oxidants, by binding to them and preventing their interaction with cells. Additionally, orosomucoid has been studied as a potential biomarker for several diseases due to its altered levels during inflammation and cancer.

Protein binding, in the context of medical and biological sciences, refers to the interaction between a protein and another molecule (known as the ligand) that results in a stable complex. This process is often reversible and can be influenced by various factors such as pH, temperature, and concentration of the involved molecules.

In clinical chemistry, protein binding is particularly important when it comes to drugs, as many of them bind to proteins (especially albumin) in the bloodstream. The degree of protein binding can affect a drug's distribution, metabolism, and excretion, which in turn influence its therapeutic effectiveness and potential side effects.

Protein-bound drugs may be less available for interaction with their target tissues, as only the unbound or "free" fraction of the drug is active. Therefore, understanding protein binding can help optimize dosing regimens and minimize adverse reactions.

Integrin α4β1, also known as Very Late Antigen-4 (VLA-4), is a heterodimeric transmembrane receptor protein composed of two subunits, α4 and β1. It is involved in various cellular activities such as adhesion, migration, and signaling. This integrin plays a crucial role in the immune system by mediating the interaction between leukocytes (white blood cells) and the endothelial cells that line blood vessels. The activation of Integrin α4β1 allows leukocytes to roll along and then firmly adhere to the endothelium, followed by their migration into surrounding tissues, particularly during inflammation and immune responses. Additionally, Integrin α4β1 also interacts with extracellular matrix proteins such as fibronectin and helps regulate cell survival, proliferation, and differentiation in various cell types.

Interleukin-1 alpha (IL-1α) is a member of the interleukin-1 cytokine family, which plays a crucial role in the regulation of inflamation and immune responses. IL-1α is primarily produced by activated macrophages, epithelial cells, and fibroblasts. It is a potent proinflammatory cytokine that binds to the interleukin-1 receptor (IL-1R) and activates signaling pathways leading to the expression of genes involved in inflammation, fever, and cellular activation. IL-1α is involved in various physiological processes such as hematopoiesis, bone remodeling, and response to infection or injury. Dysregulation of IL-1α has been implicated in several pathological conditions including autoimmune diseases, atherosclerosis, and cancer.

Electrophoresis, polyacrylamide gel (EPG) is a laboratory technique used to separate and analyze complex mixtures of proteins or nucleic acids (DNA or RNA) based on their size and electrical charge. This technique utilizes a matrix made of cross-linked polyacrylamide, a type of gel, which provides a stable and uniform environment for the separation of molecules.

In this process:

1. The polyacrylamide gel is prepared by mixing acrylamide monomers with a cross-linking agent (bis-acrylamide) and a catalyst (ammonium persulfate) in the presence of a buffer solution.
2. The gel is then poured into a mold and allowed to polymerize, forming a solid matrix with uniform pore sizes that depend on the concentration of acrylamide used. Higher concentrations result in smaller pores, providing better resolution for separating smaller molecules.
3. Once the gel has set, it is placed in an electrophoresis apparatus containing a buffer solution. Samples containing the mixture of proteins or nucleic acids are loaded into wells on the top of the gel.
4. An electric field is applied across the gel, causing the negatively charged molecules to migrate towards the positive electrode (anode) while positively charged molecules move toward the negative electrode (cathode). The rate of migration depends on the size, charge, and shape of the molecules.
5. Smaller molecules move faster through the gel matrix and will migrate farther from the origin compared to larger molecules, resulting in separation based on size. Proteins and nucleic acids can be selectively stained after electrophoresis to visualize the separated bands.

EPG is widely used in various research fields, including molecular biology, genetics, proteomics, and forensic science, for applications such as protein characterization, DNA fragment analysis, cloning, mutation detection, and quality control of nucleic acid or protein samples.

Liver diseases refer to a wide range of conditions that affect the normal functioning of the liver. The liver is a vital organ responsible for various critical functions such as detoxification, protein synthesis, and production of biochemicals necessary for digestion.

Liver diseases can be categorized into acute and chronic forms. Acute liver disease comes on rapidly and can be caused by factors like viral infections (hepatitis A, B, C, D, E), drug-induced liver injury, or exposure to toxic substances. Chronic liver disease develops slowly over time, often due to long-term exposure to harmful agents or inherent disorders of the liver.

Common examples of liver diseases include hepatitis, cirrhosis (scarring of the liver tissue), fatty liver disease, alcoholic liver disease, autoimmune liver diseases, genetic/hereditary liver disorders (like Wilson's disease and hemochromatosis), and liver cancers. Symptoms may vary widely depending on the type and stage of the disease but could include jaundice, abdominal pain, fatigue, loss of appetite, nausea, and weight loss.

Early diagnosis and treatment are essential to prevent progression and potential complications associated with liver diseases.

In the context of medicine and pharmacology, "kinetics" refers to the study of how a drug moves throughout the body, including its absorption, distribution, metabolism, and excretion (often abbreviated as ADME). This field is called "pharmacokinetics."

1. Absorption: This is the process of a drug moving from its site of administration into the bloodstream. Factors such as the route of administration (e.g., oral, intravenous, etc.), formulation, and individual physiological differences can affect absorption.

2. Distribution: Once a drug is in the bloodstream, it gets distributed throughout the body to various tissues and organs. This process is influenced by factors like blood flow, protein binding, and lipid solubility of the drug.

3. Metabolism: Drugs are often chemically modified in the body, typically in the liver, through processes known as metabolism. These changes can lead to the formation of active or inactive metabolites, which may then be further distributed, excreted, or undergo additional metabolic transformations.

4. Excretion: This is the process by which drugs and their metabolites are eliminated from the body, primarily through the kidneys (urine) and the liver (bile).

Understanding the kinetics of a drug is crucial for determining its optimal dosing regimen, potential interactions with other medications or foods, and any necessary adjustments for special populations like pediatric or geriatric patients, or those with impaired renal or hepatic function.

Integrin α2β1, also known as very late antigen-2 (VLA-2) or laminin receptor, is a heterodimeric transmembrane receptor protein composed of α2 and β1 subunits. It belongs to the integrin family of adhesion molecules that play crucial roles in cell-cell and cell-extracellular matrix (ECM) interactions.

Integrin α2β1 is widely expressed on various cell types, including fibroblasts, endothelial cells, smooth muscle cells, and some hematopoietic cells. It functions as a receptor for several ECM proteins, such as collagens (type I, II, III, and V), laminin, and fibronectin. The binding of integrin α2β1 to these ECM components mediates cell adhesion, migration, proliferation, differentiation, and survival, thereby regulating various physiological and pathological processes, such as tissue repair, angiogenesis, inflammation, and tumor progression.

In addition, integrin α2β1 has been implicated in several diseases, including fibrosis, atherosclerosis, and cancer. Therefore, targeting this integrin with therapeutic strategies may provide potential benefits for treating these conditions.

In the context of medical and biological sciences, a "binding site" refers to a specific location on a protein, molecule, or cell where another molecule can attach or bind. This binding interaction can lead to various functional changes in the original protein or molecule. The other molecule that binds to the binding site is often referred to as a ligand, which can be a small molecule, ion, or even another protein.

The binding between a ligand and its target binding site can be specific and selective, meaning that only certain ligands can bind to particular binding sites with high affinity. This specificity plays a crucial role in various biological processes, such as signal transduction, enzyme catalysis, or drug action.

In the case of drug development, understanding the location and properties of binding sites on target proteins is essential for designing drugs that can selectively bind to these sites and modulate protein function. This knowledge can help create more effective and safer therapeutic options for various diseases.

Hepatocyte Nuclear Factor 1-alpha (HNF1A) is a transcription factor that plays a crucial role in the development and function of the liver. It belongs to the family of winged helix transcription factors and is primarily expressed in the hepatocytes, which are the major cell type in the liver.

HNF1A regulates the expression of various genes involved in glucose and lipid metabolism, bile acid synthesis, and drug metabolism. Mutations in the HNF1A gene have been associated with maturity-onset diabetes of the young (MODY), a form of diabetes that is typically inherited in an autosomal dominant manner and often diagnosed in early adulthood. These mutations can lead to impaired insulin secretion and decreased glucose tolerance, resulting in the development of diabetes.

In addition to its role in diabetes, HNF1A has also been implicated in liver diseases such as nonalcoholic fatty liver disease (NAFLD) and alcoholic liver disease (ALD). Dysregulation of HNF1A has been shown to contribute to the development and progression of these conditions by altering the expression of genes involved in lipid metabolism, inflammation, and fibrosis.

An amino acid sequence is the specific order of amino acids in a protein or peptide molecule, formed by the linking of the amino group (-NH2) of one amino acid to the carboxyl group (-COOH) of another amino acid through a peptide bond. The sequence is determined by the genetic code and is unique to each type of protein or peptide. It plays a crucial role in determining the three-dimensional structure and function of proteins.

Alpha-1 adrenergic receptors (also known as α1-adrenoreceptors) are a type of G protein-coupled receptor that binds catecholamines, such as norepinephrine and epinephrine. These receptors are primarily found in the smooth muscle of various organs, including the vasculature, heart, liver, kidneys, gastrointestinal tract, and genitourinary system.

When an alpha-1 adrenergic receptor is activated by a catecholamine, it triggers a signaling cascade that leads to the activation of phospholipase C, which in turn activates protein kinase C and increases intracellular calcium levels. This ultimately results in smooth muscle contraction, increased heart rate and force of contraction, and vasoconstriction.

Alpha-1 adrenergic receptors are also found in the central nervous system, where they play a role in regulating wakefulness, attention, and anxiety. There are three subtypes of alpha-1 adrenergic receptors (α1A, α1B, and α1D), each with distinct physiological roles and pharmacological properties.

In summary, alpha-1 adrenergic receptors are a type of G protein-coupled receptor that binds catecholamines and mediates various physiological responses, including smooth muscle contraction, increased heart rate and force of contraction, vasoconstriction, and regulation of wakefulness and anxiety.

Haptoglobins are proteins found in the blood that bind to free hemoglobin, which is released when red blood cells break down. The resulting complex is then removed from the bloodstream by the liver, preventing the loss of iron and potential kidney damage caused by the breakdown products of hemoglobin. Haptoglobins are produced in the liver and their levels can be measured to help diagnose various medical conditions such as hemolytic anemia, liver disease, and inflammation.

Protein conformation refers to the specific three-dimensional shape that a protein molecule assumes due to the spatial arrangement of its constituent amino acid residues and their associated chemical groups. This complex structure is determined by several factors, including covalent bonds (disulfide bridges), hydrogen bonds, van der Waals forces, and ionic bonds, which help stabilize the protein's unique conformation.

Protein conformations can be broadly classified into two categories: primary, secondary, tertiary, and quaternary structures. The primary structure represents the linear sequence of amino acids in a polypeptide chain. The secondary structure arises from local interactions between adjacent amino acid residues, leading to the formation of recurring motifs such as α-helices and β-sheets. Tertiary structure refers to the overall three-dimensional folding pattern of a single polypeptide chain, while quaternary structure describes the spatial arrangement of multiple folded polypeptide chains (subunits) that interact to form a functional protein complex.

Understanding protein conformation is crucial for elucidating protein function, as the specific three-dimensional shape of a protein directly influences its ability to interact with other molecules, such as ligands, nucleic acids, or other proteins. Any alterations in protein conformation due to genetic mutations, environmental factors, or chemical modifications can lead to loss of function, misfolding, aggregation, and disease states like neurodegenerative disorders and cancer.

Integrin α5 (also known as CD49e) is a subunit of the heterodimeric integrin receptor called very late antigen-5 (VLA-5). Integrins are transmembrane adhesion receptors that play crucial roles in cell-cell and cell-extracellular matrix interactions. The α5β1 integrin, formed by the association of α5 and β1 subunits, specifically recognizes and binds to fibronectin, a major extracellular matrix protein. This binding event is essential for various biological processes such as cell migration, proliferation, differentiation, and survival.

In summary, Integrin alpha5 (α5) is an essential subunit of the α5β1 integrin receptor that mediates cell-fibronectin interactions and contributes to several vital cellular functions.

Integrin α1β1, also known as Very Late Antigen-1 (VLA-1) or CD49a/CD29, is a heterodimeric transmembrane receptor protein composed of α1 and β1 subunits. It belongs to the integrin family of adhesion molecules that play crucial roles in cell-cell and cell-extracellular matrix (ECM) interactions.

Integrin α1β1 is primarily expressed on various cell types, including fibroblasts, endothelial cells, smooth muscle cells, and some immune cells. This integrin binds to several ECM proteins, such as collagens (type I, II, III, IV), laminin, and fibronectin, mediating cell adhesion, migration, proliferation, differentiation, and survival. Additionally, α1β1 integrin has been implicated in various physiological and pathological processes, such as tissue repair, fibrosis, and tumor progression.

Alpha-2 adrenergic receptors are a type of G protein-coupled receptor that binds catecholamines, such as norepinephrine and epinephrine. These receptors are widely distributed in the central and peripheral nervous system, as well as in various organs and tissues throughout the body.

Activation of alpha-2 adrenergic receptors leads to a variety of physiological responses, including inhibition of neurotransmitter release, vasoconstriction, and reduced heart rate. These receptors play important roles in regulating blood pressure, pain perception, and various cognitive and emotional processes.

There are several subtypes of alpha-2 adrenergic receptors, including alpha-2A, alpha-2B, and alpha-2C, which may have distinct physiological functions and be targeted by different drugs. For example, certain medications used to treat hypertension or opioid withdrawal target alpha-2 adrenergic receptors to produce their therapeutic effects.

Chymotrypsin is a proteolytic enzyme, specifically a serine protease, that is produced in the pancreas and secreted into the small intestine as an inactive precursor called chymotrypsinogen. Once activated, chymotrypsin helps to digest proteins in food by breaking down specific peptide bonds in protein molecules. Its activity is based on the recognition of large hydrophobic side chains in amino acids like phenylalanine, tryptophan, and tyrosine. Chymotrypsin plays a crucial role in maintaining normal digestion and absorption processes in the human body.

Integrin α6β1, also known as CD49f/CD29, is a heterodimeric transmembrane receptor protein composed of α6 and β1 subunits. It is widely expressed in various tissues, including epithelial cells, endothelial cells, fibroblasts, and hematopoietic cells. Integrin α6β1 plays a crucial role in cell-matrix adhesion, particularly to the laminin component of the extracellular matrix (ECM). This receptor is involved in various biological processes such as cell migration, proliferation, differentiation, and survival. Additionally, integrin α6β1 has been implicated in tumor progression, metastasis, and drug resistance in certain cancers.

Protein-losing enteropathies (PLE) refer to a group of conditions characterized by excessive loss of proteins from the gastrointestinal tract into the intestinal lumen and ultimately into the stool. This results in hypoproteinemia, which is a decrease in the concentration of proteins in the bloodstream, particularly albumin.

The protein loss can occur due to various reasons such as increased permeability of the intestinal mucosa, lymphatic obstruction, or inflammatory processes affecting the gastrointestinal tract. Common causes of PLE include conditions such as inflammatory bowel disease, intestinal lymphangiectasia, celiac disease, Whipple's disease, and menetrier's disease.

Symptoms of PLE may include edema, ascites, weight loss, diarrhea, and fatigue. The diagnosis of PLE typically involves measuring the concentration of proteins in the stool, as well as other diagnostic tests to determine the underlying cause. Treatment of PLE depends on the underlying cause and may involve dietary modifications, medications, or surgical interventions.

Macroglobulins are high molecular weight immunoglobulins, specifically, IgM antibodies. They are called "macro" because of their large size, which is approximately 10 times larger than other types of immunoglobulins (IgG, IgA, and IgD). Macroglobulins are normally present in low concentrations in the blood, but their levels can increase in certain medical conditions such as macroglobulinemia, lymphoma, multiple myeloma, and other chronic inflammatory diseases.

Elevated levels of macroglobulins can cause various symptoms, including fatigue, weakness, bleeding, and neurological problems due to the increased viscosity of the blood. Macroglobulins can also interfere with laboratory tests, leading to false positive results for certain conditions. Treatment for elevated macroglobulins depends on the underlying cause and may include chemotherapy, radiation therapy, or other targeted therapies.

'Gene expression regulation' refers to the processes that control whether, when, and where a particular gene is expressed, meaning the production of a specific protein or functional RNA encoded by that gene. This complex mechanism can be influenced by various factors such as transcription factors, chromatin remodeling, DNA methylation, non-coding RNAs, and post-transcriptional modifications, among others. Proper regulation of gene expression is crucial for normal cellular function, development, and maintaining homeostasis in living organisms. Dysregulation of gene expression can lead to various diseases, including cancer and genetic disorders.

Transfection is a term used in molecular biology that refers to the process of deliberately introducing foreign genetic material (DNA, RNA or artificial gene constructs) into cells. This is typically done using chemical or physical methods, such as lipofection or electroporation. Transfection is widely used in research and medical settings for various purposes, including studying gene function, producing proteins, developing gene therapies, and creating genetically modified organisms. It's important to note that transfection is different from transduction, which is the process of introducing genetic material into cells using viruses as vectors.

Integrin α6β4 is a type of cell surface receptor that is composed of two subunits, α6 and β4. It is also known as CD49f/CD104. This integrin is primarily expressed in epithelial cells and plays important roles in cell adhesion, migration, and signal transduction.

Integrin α6β4 specifically binds to laminin-332 (also known as laminin-5), a component of the basement membrane, and forms a stable anchorage complex that links the cytoskeleton to the extracellular matrix. This interaction is critical for maintaining the integrity of epithelial tissues and regulating cell behavior during processes such as wound healing and tissue regeneration.

Mutations in the genes encoding integrin α6β4 have been associated with various human diseases, including epidermolysis bullosa, a group of inherited skin disorders characterized by fragile skin and blistering. Additionally, integrin α6β4 has been implicated in cancer progression and metastasis, as its expression is often upregulated in tumor cells and contributes to their invasive behavior.

Integrins are a family of cell-surface receptors that play crucial roles in various biological processes, including cell adhesion, migration, and signaling. Integrin alpha chains are one of the two subunits that make up an integrin heterodimer, with the other subunit being an integrin beta chain.

Integrin alpha chains are transmembrane glycoproteins consisting of a large extracellular domain, a single transmembrane segment, and a short cytoplasmic tail. The extracellular domain contains several domains that mediate ligand binding, while the cytoplasmic tail interacts with various cytoskeletal proteins and signaling molecules to regulate intracellular signaling pathways.

There are 18 different integrin alpha chains known in humans, each of which can pair with one or more beta chains to form distinct integrin heterodimers. These heterodimers exhibit unique ligand specificities and functions, allowing them to mediate diverse cell-matrix and cell-cell interactions.

In summary, integrin alpha chains are essential subunits of integrin receptors that play crucial roles in regulating cell adhesion, migration, and signaling by mediating interactions between cells and their extracellular environment.

The endoplasmic reticulum (ER) is a network of interconnected tubules and sacs that are present in the cytoplasm of eukaryotic cells. It is a continuous membranous organelle that plays a crucial role in the synthesis, folding, modification, and transport of proteins and lipids.

The ER has two main types: rough endoplasmic reticulum (RER) and smooth endoplasmic reticulum (SER). RER is covered with ribosomes, which give it a rough appearance, and is responsible for protein synthesis. On the other hand, SER lacks ribosomes and is involved in lipid synthesis, drug detoxification, calcium homeostasis, and steroid hormone production.

In summary, the endoplasmic reticulum is a vital organelle that functions in various cellular processes, including protein and lipid metabolism, calcium regulation, and detoxification.

Integrins are a type of cell-adhesion molecule that play a crucial role in cell-cell and cell-extracellular matrix (ECM) interactions. They are heterodimeric transmembrane receptors composed of non-covalently associated α and β subunits, which form more than 24 distinct integrin heterodimers in humans.

Integrins bind to specific ligands, such as ECM proteins (e.g., collagen, fibronectin, laminin), cell surface molecules, and soluble factors, through their extracellular domains. The intracellular domains of integrins interact with the cytoskeleton and various signaling proteins, allowing them to transduce signals from the ECM into the cell (outside-in signaling) and vice versa (inside-out signaling).

These molecular interactions are essential for numerous biological processes, including cell adhesion, migration, proliferation, differentiation, survival, and angiogenesis. Dysregulation of integrin function has been implicated in various pathological conditions, such as cancer, fibrosis, inflammation, and autoimmune diseases.

Albumins are a type of protein found in various biological fluids, including blood plasma. The most well-known albumin is serum albumin, which is produced by the liver and is the most abundant protein in blood plasma. Serum albumin plays several important roles in the body, such as maintaining oncotic pressure (which helps to regulate fluid balance in the body), transporting various substances (such as hormones, fatty acids, and drugs), and acting as an antioxidant.

Albumins are soluble in water and have a molecular weight ranging from 65,000 to 69,000 daltons. They are composed of a single polypeptide chain that contains approximately 585 amino acid residues. The structure of albumin is characterized by a high proportion of alpha-helices and beta-sheets, which give it a stable, folded conformation.

In addition to their role in human physiology, albumins are also used as diagnostic markers in medicine. For example, low serum albumin levels may indicate liver disease, malnutrition, or inflammation, while high levels may be seen in dehydration or certain types of kidney disease. Albumins may also be used as a replacement therapy in patients with severe protein loss, such as those with nephrotic syndrome or burn injuries.

Blood proteins, also known as serum proteins, are a group of complex molecules present in the blood that are essential for various physiological functions. These proteins include albumin, globulins (alpha, beta, and gamma), and fibrinogen. They play crucial roles in maintaining oncotic pressure, transporting hormones, enzymes, vitamins, and minerals, providing immune defense, and contributing to blood clotting.

Albumin is the most abundant protein in the blood, accounting for about 60% of the total protein mass. It functions as a transporter of various substances, such as hormones, fatty acids, and drugs, and helps maintain oncotic pressure, which is essential for fluid balance between the blood vessels and surrounding tissues.

Globulins are divided into three main categories: alpha, beta, and gamma globulins. Alpha and beta globulins consist of transport proteins like lipoproteins, hormone-binding proteins, and enzymes. Gamma globulins, also known as immunoglobulins or antibodies, are essential for the immune system's defense against pathogens.

Fibrinogen is a protein involved in blood clotting. When an injury occurs, fibrinogen is converted into fibrin, which forms a mesh to trap platelets and form a clot, preventing excessive bleeding.

Abnormal levels of these proteins can indicate various medical conditions, such as liver or kidney disease, malnutrition, infections, inflammation, or autoimmune disorders. Blood protein levels are typically measured through laboratory tests like serum protein electrophoresis (SPE) and immunoelectrophoresis (IEP).

Integrin α1 (also known as ITGA1 or CD49a) is a subunit of a heterodimeric integrin receptor, specifically the collagen receptor α1β1. Integrins are transmembrane proteins that play crucial roles in cell-cell and cell-extracellular matrix (ECM) adhesion, signaling, migration, proliferation, and differentiation. The α1β1 integrin binds to various collagen types, such as collagens I, II, III, and V, and mediates cellular responses upon binding to these ECM components.

The gene encoding Integrin α1 is located on chromosome 5 (5q31) in humans. Mutations in the ITGA1 gene can lead to various diseases, including leukocyte adhesion deficiency type II and some forms of epidermolysis bullosa.

Deoxyribonucleic acid (DNA) is the genetic material present in the cells of organisms where it is responsible for the storage and transmission of hereditary information. DNA is a long molecule that consists of two strands coiled together to form a double helix. Each strand is made up of a series of four nucleotide bases - adenine (A), guanine (G), cytosine (C), and thymine (T) - that are linked together by phosphate and sugar groups. The sequence of these bases along the length of the molecule encodes genetic information, with A always pairing with T and C always pairing with G. This base-pairing allows for the replication and transcription of DNA, which are essential processes in the functioning and reproduction of all living organisms.

Alpha-macroglobulins are a type of large protein molecule found in blood plasma, which play a crucial role in the human body's immune system. They are called "macro" globulins because of their large size, and "alpha" refers to their electrophoretic mobility, which is a laboratory technique used to separate proteins based on their electrical charge.

Alpha-macroglobulins function as protease inhibitors, which means they help regulate the activity of enzymes called proteases that can break down other proteins in the body. By inhibiting these proteases, alpha-macroglobulins help protect tissues and organs from excessive protein degradation and also help maintain the balance of various biological processes.

One of the most well-known alpha-macroglobulins is alpha-1-antitrypsin, which helps protect the lungs from damage caused by inflammation and protease activity. Deficiencies in this protein have been linked to lung diseases such as emphysema and chronic obstructive pulmonary disease (COPD).

Overall, alpha-macroglobulins are an essential component of the human immune system and play a critical role in maintaining homeostasis and preventing excessive tissue damage.

Trypsin is a proteolytic enzyme, specifically a serine protease, that is secreted by the pancreas as an inactive precursor, trypsinogen. Trypsinogen is converted into its active form, trypsin, in the small intestine by enterokinase, which is produced by the intestinal mucosa.

Trypsin plays a crucial role in digestion by cleaving proteins into smaller peptides at specific arginine and lysine residues. This enzyme helps to break down dietary proteins into amino acids, allowing for their absorption and utilization by the body. Additionally, trypsin can activate other zymogenic pancreatic enzymes, such as chymotrypsinogen and procarboxypeptidases, thereby contributing to overall protein digestion.

A heterozygote is an individual who has inherited two different alleles (versions) of a particular gene, one from each parent. This means that the individual's genotype for that gene contains both a dominant and a recessive allele. The dominant allele will be expressed phenotypically (outwardly visible), while the recessive allele may or may not have any effect on the individual's observable traits, depending on the specific gene and its function. Heterozygotes are often represented as 'Aa', where 'A' is the dominant allele and 'a' is the recessive allele.

A homozygote is an individual who has inherited the same allele (version of a gene) from both parents and therefore possesses two identical copies of that allele at a specific genetic locus. This can result in either having two dominant alleles (homozygous dominant) or two recessive alleles (homozygous recessive). In contrast, a heterozygote has inherited different alleles from each parent for a particular gene.

The term "homozygote" is used in genetics to describe the genetic makeup of an individual at a specific locus on their chromosomes. Homozygosity can play a significant role in determining an individual's phenotype (observable traits), as having two identical alleles can strengthen the expression of certain characteristics compared to having just one dominant and one recessive allele.

Alpha rhythm is a type of brain wave that is typically observed in the electroencephalogram (EEG) of normal, awake individuals when they have their eyes closed. It is characterized by sinusoidal waves with a frequency range of 8-13 Hz and is most prominent over the occipital region of the head, which is located at the back of the skull above the brain's visual cortex.

Alpha rhythm is typically associated with relaxed wakefulness, and its presence may indicate that an individual is awake but not engaged in any mentally demanding tasks. It can be blocked or suppressed by various stimuli, such as opening one's eyes, hearing a loud noise, or engaging in mental activity.

Disruptions in alpha rhythm have been observed in various neurological and psychiatric conditions, including epilepsy, dementia, depression, and anxiety disorders. However, more research is needed to fully understand the clinical significance of these abnormalities.

Protein C inhibitor is a natural anticoagulant protein found in the blood. It plays a crucial role in regulating the coagulation system by controlling the activity of activated protein C, which is a key enzyme that helps to break down clots and prevent excessive bleeding. Protein C inhibitor works by binding to and inhibiting the activity of activated protein C, thereby ensuring that the coagulation process is balanced and that clots are formed only when necessary.

Inherited or acquired deficiencies in protein C inhibitor can lead to an increased risk of thrombosis or abnormal blood clotting, which can cause serious health complications such as deep vein thrombosis (DVT), pulmonary embolism (PE), and disseminated intravascular coagulation (DIC). Therefore, protein C inhibitor is an essential component of the coagulation system and its activity is tightly regulated to maintain normal hemostasis.

Molecular models are three-dimensional representations of molecular structures that are used in the field of molecular biology and chemistry to visualize and understand the spatial arrangement of atoms and bonds within a molecule. These models can be physical or computer-generated and allow researchers to study the shape, size, and behavior of molecules, which is crucial for understanding their function and interactions with other molecules.

Physical molecular models are often made up of balls (representing atoms) connected by rods or sticks (representing bonds). These models can be constructed manually using materials such as plastic or wooden balls and rods, or they can be created using 3D printing technology.

Computer-generated molecular models, on the other hand, are created using specialized software that allows researchers to visualize and manipulate molecular structures in three dimensions. These models can be used to simulate molecular interactions, predict molecular behavior, and design new drugs or chemicals with specific properties. Overall, molecular models play a critical role in advancing our understanding of molecular structures and their functions.

Proprotein convertase 5 (PC5, also known as PCSK5 or PACE4) is a serine protease enzyme that belongs to the family of proprotein convertases. These enzymes play crucial roles in processing and activating various protein precursors by cleaving them at specific recognition sites.

PC5 is primarily involved in the activation of other proteins through proteolytic processing, which means it cuts large protein precursors into their smaller, active forms. It has a wide range of substrates, including hormones, growth factors, receptors, and adhesion molecules. PC5 is synthesized as an inactive zymogen and undergoes autocatalytic activation to become fully functional.

PC5 is expressed in various tissues, such as the brain, pancreas, testis, ovary, and placenta. Its dysregulation has been implicated in several diseases, including cancer, neurodegenerative disorders, and viral infections. However, more research is needed to fully understand its functions and therapeutic potential.

Molecular cloning is a laboratory technique used to create multiple copies of a specific DNA sequence. This process involves several steps:

1. Isolation: The first step in molecular cloning is to isolate the DNA sequence of interest from the rest of the genomic DNA. This can be done using various methods such as PCR (polymerase chain reaction), restriction enzymes, or hybridization.
2. Vector construction: Once the DNA sequence of interest has been isolated, it must be inserted into a vector, which is a small circular DNA molecule that can replicate independently in a host cell. Common vectors used in molecular cloning include plasmids and phages.
3. Transformation: The constructed vector is then introduced into a host cell, usually a bacterial or yeast cell, through a process called transformation. This can be done using various methods such as electroporation or chemical transformation.
4. Selection: After transformation, the host cells are grown in selective media that allow only those cells containing the vector to grow. This ensures that the DNA sequence of interest has been successfully cloned into the vector.
5. Amplification: Once the host cells have been selected, they can be grown in large quantities to amplify the number of copies of the cloned DNA sequence.

Molecular cloning is a powerful tool in molecular biology and has numerous applications, including the production of recombinant proteins, gene therapy, functional analysis of genes, and genetic engineering.

Pancreatin is a mixture of digestive enzymes, including amylase, lipase, and proteases, naturally produced by the pancreas in humans and other mammals. These enzymes aid in the digestion of carbohydrates, fats, and proteins, respectively, in the small intestine. Pancreatin is often used as a replacement therapy for individuals with conditions like cystic fibrosis, chronic pancreatitis, or pancreatectomy, who have impaired pancreatic function and struggle to digest food properly. It can be obtained from animal pancreases, typically from pigs, and is available in various forms such as tablets, capsules, or powders for medical use.

Integrin α3 (also known as ITGA3) is a subunit of a type of cell-surface receptor called an integrin. Integrins are involved in cell-cell and cell-extracellular matrix (ECM) interactions, and play important roles in various biological processes such as cell adhesion, migration, and survival.

Integrin α3 combines with the β1 subunit to form the integrin heterodimer α3β1, which is widely expressed in many tissues including epithelial cells, endothelial cells, and fibroblasts. Integrin α3β1 binds to various ECM proteins such as laminin-5, fibronectin, and collagen IV, and mediates cell adhesion and migration on these substrates.

Mutations in the ITGA3 gene have been associated with several human genetic disorders, including epidermolysis bullosa with pyloric atresia (EB-PA), a severe form of inherited skin fragility disorder, and Adams-Oliver syndrome, a rare genetic disorder characterized by scalp defects and limb abnormalities.

Furin is not a medical condition or disease, but rather it is a type of enzyme that belongs to the group of proteases. It's also known as paired basic amino acid cleaving enzyme (PACE) or convertase 6.

Furin plays an essential role in processing and activating various proteins in the body, particularly those involved in cell signaling, growth regulation, and viral infectivity. Furin works by cutting or cleaving specific amino acid sequences in proteins, allowing them to become active and perform their functions.

In a medical context, furin is often discussed in relation to its role in activating certain viruses, such as HIV, influenza, and coronaviruses (including SARS-CoV-2). Inhibiting furin activity has been explored as a potential therapeutic strategy for treating these viral infections.

An allele is a variant form of a gene that is located at a specific position on a specific chromosome. Alleles are alternative forms of the same gene that arise by mutation and are found at the same locus or position on homologous chromosomes.

Each person typically inherits two copies of each gene, one from each parent. If the two alleles are identical, a person is said to be homozygous for that trait. If the alleles are different, the person is heterozygous.

For example, the ABO blood group system has three alleles, A, B, and O, which determine a person's blood type. If a person inherits two A alleles, they will have type A blood; if they inherit one A and one B allele, they will have type AB blood; if they inherit two B alleles, they will have type B blood; and if they inherit two O alleles, they will have type O blood.

Alleles can also influence traits such as eye color, hair color, height, and other physical characteristics. Some alleles are dominant, meaning that only one copy of the allele is needed to express the trait, while others are recessive, meaning that two copies of the allele are needed to express the trait.

C57BL/6 (C57 Black 6) is an inbred strain of laboratory mouse that is widely used in biomedical research. The term "inbred" refers to a strain of animals where matings have been carried out between siblings or other closely related individuals for many generations, resulting in a population that is highly homozygous at most genetic loci.

The C57BL/6 strain was established in 1920 by crossing a female mouse from the dilute brown (DBA) strain with a male mouse from the black strain. The resulting offspring were then interbred for many generations to create the inbred C57BL/6 strain.

C57BL/6 mice are known for their robust health, longevity, and ease of handling, making them a popular choice for researchers. They have been used in a wide range of biomedical research areas, including studies of cancer, immunology, neuroscience, cardiovascular disease, and metabolism.

One of the most notable features of the C57BL/6 strain is its sensitivity to certain genetic modifications, such as the introduction of mutations that lead to obesity or impaired glucose tolerance. This has made it a valuable tool for studying the genetic basis of complex diseases and traits.

Overall, the C57BL/6 inbred mouse strain is an important model organism in biomedical research, providing a valuable resource for understanding the genetic and molecular mechanisms underlying human health and disease.

Owen MC, Brennan SO, Lewis JH, Carrell RW (September 1983). "Mutation of antitrypsin to antithrombin. alpha 1-antitrypsin ... DeMeo DL, Silverman EK (March 2004). "Alpha1-antitrypsin deficiency. 2: genetic aspects of alpha(1)-antitrypsin deficiency: ... The alpha region can be further divided into two sub-regions, termed "1" and "2". Alpha-1 antitrypsin is the main protein of ... Alpha-1 antitrypsin or α1-antitrypsin (A1AT, α1AT, A1A, or AAT) is a protein belonging to the serpin superfamily. It is encoded ...
... (A1AD or AATD) is a genetic disorder that may result in lung disease or liver disease. Onset of ... Alpha-1 antitrypsin levels in the blood depend on the genotype. Some mutant forms fail to fold properly and are, thus, targeted ... In newborns, alpha-1 antitrypsin deficiency can result in early onset jaundice followed by prolonged jaundice. Between 3% and 5 ... A1AD is due to a mutation in the SERPINA1 gene that results in not enough alpha-1 antitrypsin (A1AT). Risk factors for lung ...
"Alpha-1 Antitrypsin Deficiency". MedlinePlus. Leslie, Nancy; Tinkle, Brad T. (1993). "Pompe Disease". In Pagon, Roberta A.; ... Liver damage is also a clinical feature of alpha 1-antitrypsin deficiency and glycogen storage disease type II. In ... 327 (1-2): 26-47. doi:10.1016/j.canlet.2012.01.016. PMID 22293091. Nishida N, Kudo M (2013). "Oxidative stress and epigenetic ... 25 (1): 142-63. doi:10.1128/CMR.00018-11. PMC 3255968. PMID 22232374. Suk KT, Kim MY, Baik SK (September 2014). "Alcoholic ...
... alpha 1-antitrypsin deficiency; 2% replacing previously transplanted lungs that have since failed; 24% other causes, including ... 1 May 2008. Archived from the original on 5 June 2010. Retrieved 28 July 2010. Wijesinha M, Hirshon JM, Terrin M, Magder L, ... 109 (1): 49-59. doi:10.1016/S0022-5223(95)70419-1. PMID 7815807. Merck Manual 18th ed. p. 1377 "2008 OPTN/SRTR Annual Report". ... these median survival estimates were conditional on surviving 1 year post-transplant. Sarah Murnaghan lung transplant ...
... is also used to identify alpha-1 antitrypsin globules in hepatocytes, which is a characteristic finding of ... Patel, D; Teckman, JH (November 2018). "Alpha-1-Antitrypsin Deficiency Liver Disease". Clinics in Liver Disease. 22 (4): 643- ... alpha-1 antitrypsin deficiency. PAS diastase stain is also used in diagnosing Whipple's disease, as the foamy macrophages that ...
Alpha-1 antitrypsin deficiency is a genetic risk factor that may lead to the condition presenting earlier. When associated with ... "Impact of HIV infection on α1-antitrypsin in the lung". Am J Physiol Lung Cell Mol Physiol. 314 (4): L583-L592. doi:10.1152/ ... This type of emphysema is associated with alpha-1 antitrypsin deficiency (A1AD or AATD), and Ritalin lung, and is not related ... "Alpha-1 antitrypsin deficiency: MedlinePlus Genetics". medlineplus.gov. Retrieved 26 August 2021. Sharma, R. "Ritalin lung". ...
Individuals with alpha 1-antitrypsin deficiency have been found to be particularly susceptible to bronchiectasis, due to the ... "Prevalence and impact of bronchiectasis in alpha1-antitrypsin deficiency". American Journal of Respiratory and Critical Care ... It is important to establish whether an underlying modifiable cause, such as immunoglobulin deficiency or alpha-1 antitrypsin ... Shin MS, Ho KJ (1993). "Bronchiectasis in patients with alpha 1-antitrypsin deficiency. A rare occurrence?". Chest. 104 (5): ...
Pandur E, Nagy J, Poór VS, Sarnyai A, Huszár A, Miseta A, Sipos K (April 2009). "Alpha-1 antitrypsin binds preprohepcidin ... This conversion may be regulated by alpha-1 antitrypsin. Hepcidin is a tightly folded polypeptide with 32% beta sheet character ... 93 (1): 90-97. doi:10.3324/haematol.11705. PMID 18166790. Bregman DB, Morris D, Koch TA, He A, Goodnough LT (February 2013). " ... ISBN 978-1-4649-8960-5. "Hepcidin P81172". UniProt. December 15, 1998. Zhao N, Zhang AS, Enns CA (June 2013). "Iron regulation ...
To give α1 antitrypsin to someone with alpha 1-antitrypsin deficiency. Wright, BM; Eiland EH, 3rd; Lorenz, R (March 2013). " ... Campos, MA; Lascano, J (October 2014). "α1 Antitrypsin deficiency: current best practice in testing and augmentation therapy". ...
One of the outcomes of this research was the use of alpha-amylase gene promoters to express human proteins in transgenic rice ... Sequence-specific interactions of a nuclear protein factor with the promoter of a rice gene for alpha-amylase, RAamy3D.. Nucl. ... Metabolic regulation of rice alpha-amylase and sucrose synthase genes in planta. The Plant Journal, 2(4):517-523. Huang, N., ... Organization, structure and expression of the rice alpha-amylase multigene family. In, Rice Genetics II. Manila, pp. 417-429. ...
Alpha-1 antitrypsin deficiency (A1AD) is an important risk factor for COPD. It is advised that everybody with COPD be screened ... The effectiveness of alpha-1 antitrypsin augmentation treatment for people who have alpha-1 antitrypsin deficiency is unclear. ... The only genotype is the alpha-1 antitrypsin deficiency (AATD) genetic subtype and this has a specific treatment. The cause of ... This risk is particularly high if someone deficient in alpha-1 antitrypsin (AAT) also smokes. It is responsible for about 1-5% ...
Alpha-1 antitrypsin deficiency panniculitis List of cutaneous conditions Rapini, Ronald P.; Bolognia, Jean L.; Jorizzo, Joseph ... ISBN 978-1-4160-2999-1. "Weber-Christian disease" at Dorland's Medical Dictionary Weber-Christian disease at Who Named It? ... doi:10.1111/j.1365-2133.1925.tb10003.x. Christian, Henry Asbury (1 September 1928). "Relapsing febrile nodular nonsuppurative ...
Zemaira (Alpha-1 antitrypsin), for chronic augmentation, now owned by CSL Behring. Mucosolvan Medicine for Cough - Rheumatology ... Thymoglobulin, for hemophilia A. Zemaira (Alpha-1 antitrypsin), for chronic augmentation, Now owned by CSL Behring. - ... 1 December 2021. "Sanofi in $1 bln deal to buy U.S.-based Amunix Pharma , Reuters". Reuters. 21 December 2021. Joyce Teo (20 ... 25 (1): 22-27. Sanofi-Synthélabo Form 20F for the Fiscal Year ended 31 December 2002 Denis Cosnard for Les Echos. 11 December ...
Hayes VM, Gardiner-Garden M (Oct 2003). "Are polymorphic markers within the alpha-1-antitrypsin gene associated with risk of ... 2004). "Progression of atherosclerosis is associated with variation in the alpha1-antitrypsin gene". Arterioscler. Thromb. Vasc ... 2001). "In vivo complex formation of oxidized alpha(1)-antitrypsin and LDL". Arterioscler. Thromb. Vasc. Biol. 21 (11): 1801-8 ... AMY-1-associating protein expressed in testis 1 is a protein that in humans is encoded by the MAATS1 (formerly known as C3orf15 ...
A hypothesis of alpha 1-antitrypsin deficiency was proposed by Kuzemko in 1994. Mitral stenosis was a possible, if unlikely, ... Kubba and Young pointed out a number of other conceivable, if unlikely, diagnoses, besides cystic fibrosis and alpha 1- ... antitrypsin deficiency: eosinophilic granulomatosis with polyangiitis, allergic bronchopulmonary aspergillosis, ... 44 (1): 77-84. PMID 12590184. Kubba, AK; Young, M (1998). "The long suffering of Frederic Chopin". Chest. 113 (1): 210-6. doi: ...
Injectable interferon alpha was the first therapy approved for chronic hepatitis B. It has several side effects, most of which ... In alpha-1-antitrypsin deficiency, a co-dominant mutation in the gene for alpha-1-antitrypsin results in the abnormal ... Interferon alpha has proven effective at inhibiting viral activity but only on a temporary basis. Similar to hepatitis A, ... When the liver is involved, alpha-1-antitrypsin deficiency and Wilson's disease tend to present as hepatitis in the neonatal ...
Serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 2 is a protein that in humans is encoded by ... antitrypsin like gene, it was discovered that SERPINA2 did not have any promoter but did contain substantial homology to ... Rollini P, Fournier RE (December 1997). "Molecular linkage of the human alpha 1-antitrypsin and corticosteroid-binding globulin ... "Entrez Gene: Serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 2". Retrieved 2017-09-21. Hofker ...
If stool alpha-1 antitrypsin is elevated, this suggests excessive gastrointestinal protein loss. Treatment of hypoalbuminemia ... If protein-losing enteropathy is suspected based on clinical suspicion, an alpha-1 antitrypsin test can be performed. ... 10 (1): 88. doi:10.3390/nu10010088. ISSN 2072-6643. PMC 5793316. PMID 29342898. Kooman, Jeroen P.; van der Sande, Frank M. ( ... 47 (1-3): 223-229. doi:10.1159/000494583. ISSN 1421-9735. PMC 6492508. PMID 30517920. Dekker, Marijke J. E.; van der Sande, ...
Patients with alpha-1 antitrypsin deficiency may present with hepatomegaly and elevated liver enzymes. If neonatal cholestasis ... Stoller JK, Aboussouan LS (February 2012). "A review of α1-antitrypsin deficiency". American Journal of Respiratory and ... Instead, children with alpha-1 antitrypsin deficiency are primarily managed by treating symptoms clinically. Most children will ... Some of the causes of neonatal cholestasis are listed below: Biliary atresia Choledochal cyst Cholelithiasis Malignancy Alpha-1 ...
Much of Yu's work has focused on unlocking the structure and folding of the protein alpha-1 antitrypsin, which is a serpin ... "The Z type variation of human α1-antitrypsin causes a protein folding defect". Nature Structural & Molecular Biology. 2 (5): ... She has also patented the alpha-1 antitrypsin mutein with a disulfide bond and the method for preparing it along with her ... "Single amino acid substitutions of alpha 1-antitrypsin that confer enhancement in thermal stability". The Journal of Biological ...
... comparison of complementary DNA encoding Hp alpha 1S and Hp alpha 2FS". Nucleic Acids Research. 12 (11): 4531-4538. doi:10.1093 ... "Characterization of human haptoglobin cDNAs coding for alpha 2FS beta and alpha 1S beta variants". FEBS Letters. 168 (1): 103- ... The HP gene encodes a preproprotein that is processed to yield both alpha and beta chains, which subsequently combines as a ... van der Straten A, Falque JC, Loriau R, Bollen A, Cabezón T (April 1986). "Expression of cloned human haptoglobin and alpha 1- ...
It is an alpha-globulin. This gene encodes an alpha-globulin protein with corticosteroid-binding properties. This is the major ... antitrypsin), member 6". E. Edward Bittar; Neville Bittar (1997). Molecular and Cellular Endocrinology. Elsevier. p. 238. ISBN ... "Entrez Gene: SERPINA6 serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, ... allelic association and a unique haplotype associated with alpha 1-antitrypsin deficiency". Am J Hum Genet. 55 (1): 126-33. PMC ...
"Alpha-1 antitrypsin deficiency: an overlooked cause of late hemorrhagic disease of the newborn". Journal of Pediatric ... Last revised 1/15/2013 Derived from mass values using molar mass of 90.08 g/mol Derived from mass values using molar mass of ... 1, 1999 (stating 1.9-3.3 g/L) Derived by dividing mass values with molar mass Ferritin by: Mark Levin, MD, Hematologist and ... 119 (1): 69.e1-11. doi:10.1016/j.amjmed.2005.04.029. PMID 16431187. Abbassi-Ghanavati, M.; Greer, L. G.; Cunningham, F. G. ( ...
Alpha-1 antitrypsin deficiency (A1AD) leads to uninhibited destruction of elastic fibre by elastase; the main result is ... Elastase is inhibited by the acute-phase protein α1-antitrypsin (A1AT), which binds almost irreversibly to the active site of ... break down cytokines and alpha proteinase inhibitor, cleave immunoglobulin A and G (IgA, IgG), and cleave both C3bi, a ...
Lungs: Emphysema due to alpha-1 antitrypsin deficiency is a slowly progressive pulmonary disease. Kidneys: Goodpasture's ... Pancreas: Type 1 diabetes mellitus involves rapidly progressive loss of insulin secretory capacity compared to type 2 diabetes ...
Kalsheker N, Morley S, Morgan K (2002). "Gene regulation of the serine proteinase inhibitors alpha1-antitrypsin and alpha1- ... Alpha 1-antichymotrypsin (symbol α1AC, A1AC, or a1ACT) is an alpha globulin glycoprotein that is a member of the serpin ... Alpha 1-antichymotrypsin inhibits the activity of certain enzymes called proteases, such as cathepsin G that is found in ... Alpha-1 antitrypsin, another serpin that is analogous for protecting the body from excessive effects of its own inflammatory ...
Alpha 1-antitrypsin deficiency was documented in one case, interferon-alpha therapy in another case. Similar cases of ... Shaaban, H.; Slim, J.; Choo, H. (2012). "Idiopathic granulomatous mastitis as a complication of interferon-alpha therapy". ... 11 (1): 73. doi:10.1111/j.1075-122X.2005.21404.x. PMID 15647084. S2CID 46709562. Goldberg, J.; Baute, L.; Storey, L.; Park, P ... 15 (1): 111-118. doi:10.4048/jbc.2012.15.1.111. PMC 3318162. PMID 22493637. Schelfout, K.; Tjalma, W. A.; Cooremans, I. D.; ...
The active ingredient in the drug is the protein alpha-1 antitrypsin, for patients with a genetic deficiency in that protein. ... Kamada's flagship product is Glassia, approved by the FDA to treat alpha 1-antitrypsin deficiency. ... and Baxter Enter into a Strategic Agreement for the Distribution and Manufacture of Intravenous Liquid AAT to Treat Alpha-1 ... Antitrypsin Deficiency in the US". www.businesswire.com. 2010-08-24. Retrieved 2019-05-15. גביזון, יורם (2011-08-30). "קמהדע ...
Alpha-1 antitrypsin deficiency panniculitis is a panniculitis associated with a deficiency of the α1-antitrypsin enzyme ... Alpha 1-antitrypsin deficiency Crohn's disease This is not a complete list of possible causes. Lipoatrophy or lipodystrophy ( ... ISBN 978-1-4160-2999-1. Epstein, Ervin and Oren, Mark, "Popsicle Panniculitis" "The New England Journal of Medicine", 282 (17 ... ISBN 978-1-4160-2999-1. Garg, Taru; Ahmed, Riaz; Bharadwaj, Apoorva V.; Shukla, Shailaja (April 2022). "Poststeroid ...
Serpins are characterized by a well-conserved tertiary structure that consists of 3 beta sheets and 8 or 9 alpha helices. A ... Schleef RR, Chuang TL (August 2000). "Protease inhibitor 10 inhibits tumor necrosis factor alpha -induced cell death. Evidence ... "Implications of the three-dimensional structure of alpha 1-antitrypsin for structure and function of serpins". Biochemistry. 28 ... doi:10.1007/s10038-005-0285-1. PMID 16172807. Riewald M, Schleef RR (November 1995). "Molecular cloning of bomapin (protease ...
Owen MC, Brennan SO, Lewis JH, Carrell RW (September 1983). "Mutation of antitrypsin to antithrombin. alpha 1-antitrypsin ... DeMeo DL, Silverman EK (March 2004). "Alpha1-antitrypsin deficiency. 2: genetic aspects of alpha(1)-antitrypsin deficiency: ... The alpha region can be further divided into two sub-regions, termed "1" and "2". Alpha-1 antitrypsin is the main protein of ... Alpha-1 antitrypsin or α1-antitrypsin (A1AT, α1AT, A1A, or AAT) is a protein belonging to the serpin superfamily. It is encoded ...
Alpha-1 antitrypsin deficiency is an inherited disorder that may cause lung disease and liver disease. Explore symptoms, ... Alpha1-antitrypsin deficiency. 2: genetic aspects of alpha(1)-antitrypsin deficiency: phenotypes and genetic modifiers of ... Alpha-1 antitrypsin deficiency is not a rare disease but a disease that is rarely diagnosed. Environ Health Perspect. 2003 Dec; ... Alpha-1 Antitrypsin Deficiency. 2006 Oct 27 [updated 2023 Jun 1]. In: Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE, Bean ...
Alpha-1 Antitrypsin Drugs Market Study by Global Industry Analysts, Inc. ... The Alpha-1 Antitrypsin Drugs market in the U.S. is estimated at US$651.1 Million in the year 2023. China, the world`s second ... Alpha-1 Antitrypsin Drugs. A Global Strategic Business Report. MCP10246. .accordion_2.mt-4 button.accordion{ border:none ! ... Global Alpha-1 Antitrypsin Drugs Market to Reach $4 Billion by 2030. The global market for Alpha-1 Antitrypsin Drugs estimated ...
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Cancer risk in severe alpha-1-antitrypsin deficiency. Hiller, A. M., Ekström, M., Piitulainen, E., Lindberg, A., Rönmark, E. & ... Severe alpha-1-antitrypsin deficiency increases the risk of venous thromboembolism. Basil, N., Ekström, M., Piitulainen, E., ... Low Prevalence of Mild Alpha-1-Antitrypsin Deficiency in Hospitalized COVID-19-Patients. Nygren, D., Mölstad, U., Thulesius, H. ... Cancer risk in severe alpha-1-antitrypsin deficiency: the importance of early identification. Hiller, A. M., Ekström, M., ...
Alpha-1-antitrypsin, Human, mAb 2C1. Cat# MBS584761. Supplier: MyBiosource. Available at Gentaur Genprice in 5 to 7 Working ... MBS584761 , Alpha-1-antitrypsin, Human, mAb 2C1 MyBiosource Antibodies MBS584761 , Alpha-1-antitrypsin, Human, mAb 2C1. (No ... PPAR-alpha (G17) Polyclonal Antibody , MBS3001522 , Mybiosource Product Short Name: [PPAR-alpha] Product Name Synonyme: [PPARA ... Product Short Name: [Alpha-1-antitrypsin]. Product Name Synonyme: [Alpha-1 protease inhibitor; Alpha-1-antiproteinase; Serpin ...
Smith, J.M.; Proksch, G.S.; Routh, J.I. 1972: Urinary anti trypsin and immunologically related serum inter alpha trypsin ... Lieberman, J. 1969: Frequency of heterozygous and homozygous alpha anti trypsin deficiencies in patients with pulmonary ... I. the inter-alpha-trypsin inhibitor as precursor of the acid stable trypsin-plasmin-inhibitor of the serum Klinische ... Fagerhol, M. 1972: Production and retention of alpha 1 anti trypsin in the liver of individuals with alpha 1 anti trypsin ...
alpha-1-antitrypsin, alpha-1-antitrypsin deficiency, COVID-19, PI-typing, SARS-CoV-2, SERPINA1. in International Journal of ... Introduction: Alpha-1-antitrypsin (AAT) has been shown to inhibit SARS-CoV-2 cell entry and suggested as a therapeutic agent ... Introduction: Alpha-1-antitrypsin (AAT) has been shown to inhibit SARS-CoV-2 cell entry and suggested as a therapeutic agent ... article{af240ca6-6560-4c94-b595-6ced047c9e0d, abstract = {{,p,Introduction: Alpha-1-antitrypsin (AAT) has been shown to inhibit ...
Alpha-1 Canada is INSPIRED by this story! www.ctvnews.ca/health/national… The World Health Organization (WHO), American Th… ... Alpha-1 Canadas mission is to advocate for Canadians affected by Alpha-1 Antitrypsin Deficiency and to provide education to ... It is not the intention of this website to provide specific medical advice but rather to provide the Canadian Alpha-1 Community ... Specific medical advice will not be provided and Alpha-1 Canada urges you to consult with a qualified physician for diagnosis ...
Alpha-1 Antitrypsin Deficiency - Etiology, pathophysiology, symptoms, signs, diagnosis & prognosis from the MSD Manuals - ... Classification of Alpha-1 Antitrypsin Deficiency The normal PI phenotype is PI*MM. More than 95% of people with severe alpha-1 ... Alpha-1 antitrypsin deficiency and various occupational... read more (COPD). Alpha-1 antitrypsin deficiency most commonly ... Alpha-1 antitrypsin deficiency and various occupational... read more , including dyspnea, cough, wheezing, and prolonged ...
View 1 Serpin A1c/alpha 1-Antitrypsin Proteins and Enzymes. Bio-Techne offers high-quality reagents, instruments, custom ... Serpin A1c/alpha 1-Antitrypsin: Proteins and Enzymes. The human serpin superfamily consists of at least 35 members that target ... Serpin A1c/alpha 1-Antitrypsin: Proteins and Enzymes. The human serpin superfamily consists of at least 35 members that target ... Serpin A1c/alpha 1-Antitrypsin Proteins and Enzymes in Products ... Serpin A1c/alpha 1-Antitrypsin Proteins and Enzymes in ...
... is an inhibitor of the serine protease trypsin but can inhibit many other ... Alpha-1 Antitrypsin (AAT) is an inhibitor of the serine protease trypsin, but can inhibit many other proteases as well, and is ... AAT is a protein that migrates in the alpha-1 region on serum protein electrophoresis. It is produced by the liver and is one ...
Alpha-1 Antitrypsin. Does this test have other names?. Alpha-1-antiprotease deficiency, alpha-1-antiproteinase inhibitor ... This disorder is linked to abnormally low levels or a lack of alpha-1 antitrypsin (AAT) protein in the blood. The disorder can ... It helps find out if you have a genetic disorder called alpha-1 antitrypsin deficiency. ... including the nonprofit Alpha-1 Foundation, advise talking with a genetic counselor before getting a medical test that will ...
Premilife can treat you with natural homeopathic treatment for alpha 1 antitrypsin deficiency. ...
ELISA Kit from Assay Genie is a high quality ELISA kit to measure Alpha-1-antitrypsin (SERPINA1) in serum samples ... Human Alpha-1-antitrypsin (SERPINA1) ELISA Kit. SKU:. HUEB0281. UPC:. Product Type:. ELISA Kit. Size:. 96 Assays. Uniprot:. ... Alpha-1-antitrypsin. NCBI Synonym Full Names:. serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), ... Alpha-1-antitrypsin, Alpha-1 protease inhibitor, Alpha-1-antiproteinase, Serpin A1, SERPINA1, AAT, PI, PRO0684, PRO2209. ...
I carried out a pilot study comparing the performance of many ELISA assays from different suppliers and found your kits to be one of the better performers. We observed good linearity and tight replicates.. ...
Alpha-1 antitrypsin (A1AT) is a 52-kDa, acute phase glycoprotein encoded by the protease inhibitor (PI) locus, located on the ... Alpha-1 antitrypsin (A1AT) is a 52-kDa, acute phase glycoprotein encoded by the protease inhibitor (PI) locus, located on the ... Alpha-1 Antitrypsin Deficiency: Current Perspective from Genetics to Diagnosis and Therapeutic Approaches [ Vol. 24 , Issue. 1 ... Alpha-1 antitrypsin, neutrophil elastase, genetic variants, liver disease, chronic obstructive pulmonary disease, serine ...
Jeffrey P Callen, MD is a member of the following medical societies: Alpha Omega Alpha, American Academy of Dermatology, ... Alpha 1-antitrypsin deficiency associated with panniculitis. J Am Acad Dermatol. 1988 Apr. 18(4 Pt 1):684-92. [QxMD MEDLINE ... Patients with alpha-1 antitrypsin deficiency develop severe fixed airflow obstruction at an early age, usually before age 50 ... Alpha-1 antitrypsin deficiency-associated emphysema occurs predominantly in the lung bases, as opposed to the upper lobe ...
Other Alpha products are available in stock. Specificity: Alpha Category: 1 Group: Antitrypsin Antibody ... The Alpha 1 Antitrypsin Antibody Mouse reagent is RUO (Research Use Only) to test human serum or cell culture lab samples. To ... alpha 1 Antitrypsin Antibody was previously known under catalogue number 20-272-193132 was previously known under catalogue ... alpha 1 Antitrypsin Antibody was previously known under catalogue number 18-272-198477 was previously known under catalogue ...
Global Alpha-1 Antitrypsin Deficiency (AATD) Treatment Market Size, Share, Price, Trends, Growth, Report, Forecast 2023-2028 ... Alpha-1 Antitrypsin Deficiency (AATD) Treatment Market, Alpha-1 Antitrypsin Deficiency (AATD) Treatment Market Share ... The new report by Expert Market Research titled, Global Alpha-1 Antitrypsin Deficiency (AATD) Treatment Market Share,… ...
ALPHA-1-ANTITRYPSIN. Reagent line: ACCENT-300 ACCENT-300 ALPHA-1-ANTITRYPSIN Diagnostic kit for determination of α 1- ... antitrypsin concentration used in automatic analyser ACCENT-300.. The reagents must be used only for in vitro diagnostic, by ...
Alpha-1 Antitrypsin deficiency My son, 6 years old, suffers from Alpha-1. He has not gained weig... ... My wife has had a chronic cough for 2 1/2 years. She has had sinu... ... MY SON IS 4 1/2 YEARS AND WE WERE TOLD HE HAS A SMALL WINDPIPE. ... ... i have had pressure and pain of the 1.) left side of the breast d... ...
A 2.1 ANGSTROM STRUCTURE OF AN UNCLEAVED ALPHA-1-ANTITRYPSIN SHOWS VARIABILITY OF THE REACTIVE CENTER AND OTHER LOOPS ... Kim, S. et al., A 2.1 A resolution structure of an uncleaved alpha(1)-antitrypsin shows variability of the reactive center and ... A 2.1 ANGSTROM STRUCTURE OF AN UNCLEAVED ALPHA-1-ANTITRYPSIN SHOWS VARIABILITY OF THE REACTIVE CENTER AND OTHER LOOPS ... 1 interactions with chain A, 1 interactions with chain B, 1 Ligand-Water interactions. *. Metal complexes: A:H.262, B:H.43, H2O ...
Brief Summary of Findings on the Association Between Alpha-1 Antitrypsin Deficiency and Severe COVID-19 Outcomes. [print only, ... Sep 1 2020;370:m3320. doi:10.1136/bmj.m3320. *Wei SQ, Bilodeau-Bertrand M, Liu S, Auger N. The impact of COVID-19 on pregnancy ... Jan 2022;36(1):e14492. doi:10.1111/ctr.14492. *Yekedüz E, Utkan G, Ürün Y. A systematic review and meta-analysis: the effect of ... Sep 1 2020;126(17):4023-4031. doi:10.1002/cncr.33042. *Kuderer NM, Choueiri TK, Shah DP, et al. Clinical impact of COVID-19 on ...
Adenovirus-mediated transfer of a recombinant alpha 1-antitrypsin gene to the lung epithelium in vivo. scientific article ... Adenovirus-mediated transfer of a recombinant alpha 1-antitrypsin gene to the lung epithelium in vivo (English) ... https://opencitations.net/index/coci/api/v1/citations/10.1099/0022-1317-36-1-59 ...
Intravenous augmentation therapy is the only specific treatment available for emphysema associated with alpha-1 antitrypsin ... The Alpha-l-Antitrypsin Deficiency Registry Study Group: Survival and FEVl decline in individuals with severe deficiency of ... Behalf of Alpha One International Registry (A.I.R.). Show authors. Orphanet Journal of Rare Diseases volume 8, Article number: ... Long-term variability of Desmosine/Isodesmosine as biomarker in alpha-a-antitrypsin deficiency-related COPD. COPD. 2011, 8: 329 ...
... tumor necrosis factor-alpha (TNF-alpha), and nitric oxide. ... A combination of midodrine (an oral alpha agonist), ... It develops more commonly in patients with underlying hereditary hemochromatosis or alpha-1 antitrypsin deficiency. HCC is ... and tumor necrosis factor-alpha [TNF-α]) and chemoattractant elements. Leukocyte count was positively correlated with disease ... Intravenous (IV) ceftriaxone 1 g/24 h is the antibiotic of choice and should be used for a maximum of 7 days (consider ...
... tumor necrosis factor-alpha (TNF-alpha), and nitric oxide. ... A combination of midodrine (an oral alpha agonist), ... It develops more commonly in patients with underlying hereditary hemochromatosis or alpha-1 antitrypsin deficiency. HCC is ... and tumor necrosis factor-alpha [TNF-α]) and chemoattractant elements. Leukocyte count was positively correlated with disease ... Intravenous (IV) ceftriaxone 1 g/24 h is the antibiotic of choice and should be used for a maximum of 7 days (consider ...
If the more common diagnoses of asthma and COPD are ruled out, rarer causes of obstruction should be considered.1,2 ... A 24-year-old woman presented to an emergency department with a 1-week history of increasing shortness of breath accompanied ... Methacholine challenge had not been done because of severely reduced FEV1 and the tests poor specificity in differentiating ... FEV1/FVC] of 0.54 and an FEV1 of 1.50 L [43% predicted], with no substantial change after bronchodilator use). The pattern of ...
In alpha-1 antitrypsin deficiency (AATD)-associated chronic obstructive pulmonary disease (COPD), HRQoL research remains scarce ... Individuals with lung disease and data available on ≥1 measurement on any SF-36 scale and clinically relevant characteristics ... Choate, R., Holm, K.E., Sandhaus, R.A. et al. Characteristics associated with SF-36 in alpha-1 antitrypsin deficiency- ... Individuals with alpha-1 antitrypsin deficiency (AATD) are genetically predisposed to premature loss of lung function and ...
  • When the blood contains inadequate amounts of A1AT or functionally defective A1AT (such as in alpha-1 antitrypsin deficiency), neutrophil elastase is excessively free to break down elastin, degrading the elasticity of the lungs, which results in respiratory complications, such as chronic obstructive pulmonary disease, in adults. (wikipedia.org)
  • This gene provides instructions for making a protein called alpha-1 antitrypsin, which protects the body from a powerful enzyme called neutrophil elastase. (medlineplus.gov)
  • Neutrophil elastase is released from white blood cells to fight infection, but it can attack normal tissues (especially the lungs) if not tightly controlled by alpha-1 antitrypsin. (medlineplus.gov)
  • Variants in the SERPINA1 gene can lead to a shortage (deficiency) of alpha-1 antitrypsin or an abnormal form of the protein that cannot control neutrophil elastase. (medlineplus.gov)
  • Without enough functional alpha-1 antitrypsin, neutrophil elastase destroys alveoli and causes lung disease. (medlineplus.gov)
  • Alpha-1 antitrypsin is a neutrophil elastase inhibitor (an antiprotease), the major function of which is to protect the lungs from protease-mediated tissue destruction. (msdmanuals.com)
  • In the lungs, alpha-1 antitrypsin deficiency increases neutrophil elastase activity, which facilitates tissue destruction leading to emphysema (especially in smokers, because cigarette smoke also increases protease activity). (msdmanuals.com)
  • Individuals with two copies of the Z allele (ZZ) in each cell have a high risk of developing lung disease (such as emphysema) and liver disease associated with alpha-1 antitrypsin deficiency. (medlineplus.gov)
  • Intravenous augmentation therapy is the only specific treatment available for emphysema associated with alpha-1 antitrypsin deficiency. (biomedcentral.com)
  • It helps find out if you have a genetic disorder called alpha-1 antitrypsin deficiency. (umcno.org)
  • A rare genetic condition called alpha-1 antitrypsin deficiency can also cause the disease-but it is rare. (medlineplus.gov)
  • Furthermore, epidemiological association of high prevalence of Alpha-1-antitrypsin deficiency (AATD) and regional severity of COVID-19-impact has been hypothesized. (lu.se)
  • Our understanding of the pathophysiology of COPD, but in particular emphysema was largely instigated by the observation that α 1 antitrypsin deficiency (AATD) was associated with the early onset of basal panlobular emphysema [ 1 ]. (biomedcentral.com)
  • In alpha-1 antitrypsin deficiency (AATD)-associated chronic obstructive pulmonary disease (COPD), HRQoL research remains scarce. (biomedcentral.com)
  • Individuals with alpha-1 antitrypsin deficiency (AATD) are genetically predisposed to premature loss of lung function and development of emphysema, particularly if they smoke tobacco or are exposed to environmental toxins [ 1 , 2 ]. (biomedcentral.com)
  • Alpha-1 antitrypsin or α1-antitrypsin (A1AT, α1AT, A1A, or AAT) is a protein belonging to the serpin superfamily. (wikipedia.org)
  • Disorders of this protein include alpha-1 antitrypsin deficiency, an autosomal co-dominant hereditary disorder in which a deficiency of alpha-1 antitrypsin leads to a chronic uninhibited tissue breakdown. (wikipedia.org)
  • For example, the S allele produces moderately low levels of this protein, and the Z allele produces very little alpha-1 antitrypsin. (medlineplus.gov)
  • 1 ml (100 ug/ml) 0.2 um filtered protein G purified antibody solution in PBS, containing 0.1% bovine serum albumin and 0.02% sodium azide. (biocheminfo.org)
  • AAT is a protein that migrates in the alpha-1 region on serum protein electrophoresis. (aaltoscientific.com)
  • This disorder is linked to abnormally low levels or a lack of alpha-1 antitrypsin (AAT) protein in the blood. (umcno.org)
  • Alpha-1 antitrypsin (AAT) deficiency is a clinically under-recognized genetic disorder that causes the defective production of alpha-1 antitrypsin protein. (think-ing.eu)
  • However at the end of the first growing season needles of saplings exposed to 10 or 100 μg l-1 foliage-applied TCA showed significantly more visible damage, higher activities of some detoxifying enzymes, lower protein contents and poorer water control than needles of saplings dosed with the same TCA concentrations to the soil. (who.int)
  • Like all serine protease inhibitors, A1AT has a characteristic secondary structure of beta sheets and alpha helices. (wikipedia.org)
  • Alpha-1 antitrypsin (A1AT) is a 52-kDa, acute phase glycoprotein encoded by the protease inhibitor (PI) locus, located on the long arm of chromosome 14 (14q31-32.3). (currentmedicinalchemistry.com)
  • Serum level and profile of .alpha.1-antitrypsin (.alpha.1-AT) were studied in various autoimmune diseases such as SLE and hypergammaglobulinemia purpura. (eurekamag.com)
  • The serum profile of .alpha.1-AT was analyzed by 2-dimensional immunoelectrophoresis after treatment with trypsin and was composed of 2 distinct forms, an active form and an inactive form. (eurekamag.com)
  • Serum .alpha.1-AT might be intimately anticipated with the inflammatory process in the autoimmune disease. (eurekamag.com)
  • The Alpha 1 Antitrypsin Antibody Mouse reagent is RUO (Research Use Only) to test human serum or cell culture lab samples. (microbiologystudents.com)
  • Tests for serum alpha-1 antitrypsin deficiency, glucose-6-phosphate-dehydrogenase deficiency, cadmium -disulfide genetic predisposition, isocyanate allergic reaction, and sickle cell trait hemoglobinopathies are discussed. (cdc.gov)
  • Alpha-1 antitrypsin deficiency is congenital lack of a primary lung antiprotease, alpha-1 antitrypsin, which leads to increased protease-mediated tissue destruction and emphysema in adults. (msdmanuals.com)
  • Many individuals with alpha-1 antitrypsin deficiency are likely undiagnosed, particularly people with a lung condition called chronic obstructive pulmonary disease (COPD). (medlineplus.gov)
  • Variants (also known as mutations) in the SERPINA1 gene cause alpha-1 antitrypsin deficiency. (medlineplus.gov)
  • Alpha-1 antitrypsin deficiency occurs worldwide, but its prevalence varies by population. (medlineplus.gov)
  • the terms α1-antitrypsin and protease inhibitor (Pi) are often used interchangeably. (wikipedia.org)
  • Alpha-1 Antitrypsin (AAT) is an inhibitor of the serine protease trypsin but can inhibit many other proteases as well, and is thus a general serine protease inhibitor or serpin. (aaltoscientific.com)
  • Human IgG antibody Laboratories manufactures the alpha 1 antitrypsin antibody mouse reagents distributed by Genprice. (microbiologystudents.com)
  • The most common version (allele) of the SERPINA1 gene, called M, produces normal levels of alpha-1 antitrypsin. (medlineplus.gov)
  • Abnormal alpha-1 antitrypsin can also accumulate in the liver and damage this organ. (medlineplus.gov)
  • Hepatic accumulation of abnormal alpha-1 antitrypsin can cause liver disease in both children and adults. (msdmanuals.com)
  • About 10 percent of infants with alpha-1 antitrypsin deficiency develop liver disease, which often causes yellowing of the skin and whites of the eyes (jaundice). (medlineplus.gov)
  • Methacholine challenge had not been done because of severely reduced FEV 1 and the test's poor specificity in differentiating causes of obstruction. (cmaj.ca)
  • On review of the patient's previous investigations, we noted that when she was relatively well, results of pulmonary function testing showed severe fixed airflow obstruction with air trapping (a ratio of forced expiratory volume in the first second of expiration to forced vital capacity [FEV 1 /FVC] of 0.54 and an FEV 1 of 1.50 L [43% predicted], with no substantial change after bronchodilator use). (cmaj.ca)
  • Individuals with alpha-1 antitrypsin deficiency are also at risk of developing a type of liver cancer called hepatocellular carcinoma. (medlineplus.gov)
  • This disorder affects about 1 in 1,500 to 3,500 individuals with European ancestry. (medlineplus.gov)
  • Notably, these data include all deaths in the United States that occurred throughout the pandemic, from February 2020 to July 1, 2022, including deaths among unvaccinated individuals. (cdc.gov)
  • Individuals with lung disease and data available on ≥1 measurement on any SF-36 scale and clinically relevant characteristics such as modified Medical Research Council (mMRC) scale, exacerbation frequency, productive cough, and use of oxygen were included in these analyses. (biomedcentral.com)
  • Environmental factors, such as exposure to tobacco smoke, chemicals, and dust, likely impact the severity of alpha-1 antitrypsin deficiency. (medlineplus.gov)
  • Alpha-1 antitrypsin deficiency is an inherited disorder that may cause lung disease and liver disease. (medlineplus.gov)
  • Diagnostic kit for determination of α 1-antitrypsin concentration used in automatic analyser ACCENT-300. (cormaydiagnostics.com)
  • in 7 of those households, the patient classic risk factors for NTM disease are also at risk for NTM isolate and 1 plumbing isolate exhibited the same repetitive pulmonary disease ( 11 - 13 ). (cdc.gov)
  • It is not the intention of this website to provide specific medical advice but rather to provide the Canadian Alpha-1 Community with information to better understand their health and their diagnosed disorder. (alpha1canada.ca)
  • People with alpha-1 antitrypsin deficiency usually develop the first signs and symptoms of lung disease between ages 25 and 50. (medlineplus.gov)
  • Between October 12 and November 1 of 2021, four children under the age of six years presented to the emergency department of a large pediatric hospital in Alabama. (cdc.gov)
  • Some people with alpha-1 antitrypsin deficiency are misdiagnosed with asthma. (medlineplus.gov)
  • A diverse group of girls with different qualities have …Alpha Omicron Pi was founded in 1897 with the purpose of enriching women through lifelong friendships. (think-ing.eu)
  • Eligible patients for the dose-escalation and safety lead-in phases were aged 18 years or older with histological or cytological diagnosis of advanced or metastatic solid tumours with no available standard therapy, measurable or unmeasurable disease according to the Response Evaluation Criteria in Solid Tumors version 1.1, and an Eastern Cooperative Oncology Group performance status score of 0 or 1. (bvsalud.org)
  • Workup for allergic bronchopulmonary aspergillosis, cystic fibrosis and α 1 -antitrypsin deficiency ruled out these diagnoses. (cmaj.ca)
  • [ 1 ] Its hallmark features include necrotizing granulomatous inflammation and pauci-immune vasculitis in small- and medium-sized blood vessels. (medscape.com)
  • 85th percentile) being treated with lifestyle modifications alone or with metformin, with or without basal insulin, in a 1:1:1 ratio to receive once-weekly subcutaneous injections of placebo, dulaglutide at a dose of 0.75 mg, or dulaglutide at a dose of 1.5 mg. (bvsalud.org)
  • At the end of each growing season similar elevated TCA concentrations (approximate range 200-300 ng g-1 dwt) were detected in both foliage and soil-dosed saplings exposed to 100 μg l-1 TCA solutions showing that TCA uptake can occur from both exposure routes. (who.int)
  • RESEARCH recovered from the shower of an M. avium -infected patient small (1-mm diameter after 14 days at 37°C), unpigmented were almost identical to isolates recovered from the patient, to yellow, and resembled either the transparent or opaque indicating that the household water could have been the types previously reported ( 17 ). (cdc.gov)
  • Specific medical advice will not be provided and Alpha-1 Canada urges you to consult with a qualified physician for diagnosis and for answers to your personal questions. (alpha1canada.ca)
  • DESCRIPTION (provided by applicant): In developed countries, approximately 1:1000 children are born deaf and approximately 1:300 children are born with some lesser degree of hearing loss. (sbir.gov)
  • Once-weekly treatment with dulaglutide, a glucagon-like peptide-1 receptor agonist, may have efficacy with regard to glycemic control in youths with type 2 diabetes. (bvsalud.org)
  • I have a type 1 allergy. (healthlinkusa.com)
  • CONTEXT: Tirzepatide substantially reduced hemoglobin A1c (HbA1c) and body weight in subjects with type 2 diabetes (T2D) compared with the glucagon-like peptide 1 receptor agonist dulaglutide. (bvsalud.org)
  • General sorority facts about Alpha Omicron Pi such as the alumni, number of chapters, size, and nickname. (think-ing.eu)