An 11-kDa protein associated with the outer membrane of many cells including lymphocytes. It is the small subunit of the MHC class I molecule. Association with beta 2-microglobulin is generally required for the transport of class I heavy chains from the endoplasmic reticulum to the cell surface. Beta 2-microglobulin is present in small amounts in serum, csf, and urine of normal people, and to a much greater degree in the urine and plasma of patients with tubular proteinemia, renal failure, or kidney transplants.
Serum proteins with an electrophoretic mobility that falls between ALPHA-GLOBULINS and GAMMA-GLOBULINS.
Serum proteins that have the most rapid migration during ELECTROPHORESIS. This subgroup of globulins is divided into faster and slower alpha(1)- and alpha(2)-globulins.
An interleukin-1 subtype that is synthesized as an inactive membrane-bound pro-protein. Proteolytic processing of the precursor form by CASPASE 1 results in release of the active form of interleukin-1beta from the membrane.
A group of sporadic, familial and/or inherited, degenerative, and infectious disease processes, linked by the common theme of abnormal protein folding and deposition of AMYLOID. As the amyloid deposits enlarge they displace normal tissue structures, causing disruption of function. Various signs and symptoms depend on the location and size of the deposits.
Membrane glycoproteins consisting of an alpha subunit and a BETA 2-MICROGLOBULIN beta subunit. In humans, highly polymorphic genes on CHROMOSOME 6 encode the alpha subunits of class I antigens and play an important role in determining the serological specificity of the surface antigen. Class I antigens are found on most nucleated cells and are generally detected by their reactivity with alloantisera. These antigens are recognized during GRAFT REJECTION and restrict cell-mediated lysis of virus-infected cells.
A fibrous protein complex that consists of proteins folded into a specific cross beta-pleated sheet structure. This fibrillar structure has been found as an alternative folding pattern for a variety of functional proteins. Deposits of amyloid in the form of AMYLOID PLAQUES are associated with a variety of degenerative diseases. The amyloid structure has also been found in a number of functional proteins that are unrelated to disease.
A high-molecular-weight protein (approximately 22,500) containing 198 amino acid residues. It is a strong inhibitor of trypsin and human plasmin.
One of two major pharmacologically defined classes of adrenergic receptors. The beta adrenergic receptors play an important role in regulating CARDIAC MUSCLE contraction, SMOOTH MUSCLE relaxation, and GLYCOGENOLYSIS.
An integrin beta subunit of approximately 85-kDa in size which has been found in INTEGRIN ALPHAIIB-containing and INTEGRIN ALPHAV-containing heterodimers. Integrin beta3 occurs as three alternatively spliced isoforms, designated beta3A-C.
Antigens determined by leukocyte loci found on chromosome 6, the major histocompatibility loci in humans. They are polypeptides or glycoproteins found on most nucleated cells and platelets, determine tissue types for transplantation, and are associated with certain diseases.
A beta-N-Acetylhexosaminidase that catalyzes the hydrolysis of terminal, non-reducing 2-acetamido-2-deoxy-beta-glucose residues in chitobiose and higher analogs as well as in glycoproteins. Has been used widely in structural studies on bacterial cell walls and in the study of diseases such as MUCOLIPIDOSIS and various inflammatory disorders of muscle and connective tissue.
The major group of transplantation antigens in the mouse.
Poisoning occurring after exposure to cadmium compounds or fumes. It may cause gastrointestinal syndromes, anemia, or pneumonitis.
A pteridine derivative present in body fluids; elevated levels result from immune system activation, malignant disease, allograft rejection, and viral infections. (From Stedman, 26th ed) Neopterin also serves as a precursor in the biosynthesis of biopterin.
A factor synthesized in a wide variety of tissues. It acts synergistically with TGF-alpha in inducing phenotypic transformation and can also act as a negative autocrine growth factor. TGF-beta has a potential role in embryonal development, cellular differentiation, hormone secretion, and immune function. TGF-beta is found mostly as homodimer forms of separate gene products TGF-beta1, TGF-beta2 or TGF-beta3. Heterodimers composed of TGF-beta1 and 2 (TGF-beta1.2) or of TGF-beta2 and 3 (TGF-beta2.3) have been isolated. The TGF-beta proteins are synthesized as precursor proteins.
Established cell cultures that have the potential to propagate indefinitely.
Genetic loci in the vertebrate major histocompatibility complex which encode polymorphic characteristics not related to immune responsiveness or complement activity, e.g., B loci (chicken), DLA (dog), GPLA (guinea pig), H-2 (mouse), RT-1 (rat), HLA-A, -B, and -C class I genes of man.
A malignancy of mature PLASMA CELLS engaging in monoclonal immunoglobulin production. It is characterized by hyperglobulinemia, excess Bence-Jones proteins (free monoclonal IMMUNOGLOBULIN LIGHT CHAINS) in the urine, skeletal destruction, bone pain, and fractures. Other features include ANEMIA; HYPERCALCEMIA; and RENAL INSUFFICIENCY.
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.
RNA sequences that serve as templates for protein synthesis. Bacterial mRNAs are generally primary transcripts in that they do not require post-transcriptional processing. Eukaryotic mRNA is synthesized in the nucleus and must be exported to the cytoplasm for translation. Most eukaryotic mRNAs have a sequence of polyadenylic acid at the 3' end, referred to as the poly(A) tail. The function of this tail is not known for certain, but it may play a role in the export of mature mRNA from the nucleus as well as in helping stabilize some mRNA molecules by retarding their degradation in the cytoplasm.
Creatinine is a waste product that's generated from muscle metabolism, typically filtered through the kidneys and released in urine, with increased levels in blood indicating impaired kidney function.
A specific HLA-B surface antigen subtype. Members of this subtype contain alpha chains that are encoded by the HLA-B*27 allele family.
The combination of hemodialysis and hemofiltration either simultaneously or sequentially. Convective transport (hemofiltration) may be better for removal of larger molecular weight substances and diffusive transport (hemodialysis) for smaller molecular weight solutes.
Therapy for the insufficient cleansing of the BLOOD by the kidneys based on dialysis and including hemodialysis, PERITONEAL DIALYSIS, and HEMODIAFILTRATION.
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.
Also known as CD104 antigen, this protein is distinguished from other beta integrins by its relatively long cytoplasmic domain (approximately 1000 amino acids vs. approximately 50). Five alternatively spliced isoforms have been described.
Cells propagated in vitro in special media conducive to their growth. Cultured cells are used to study developmental, morphologic, metabolic, physiologic, and genetic processes, among others.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
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.
Integrin beta chains combine with integrin alpha chains to form heterodimeric cell surface receptors. Integrins have traditionally been classified into functional groups based on the identity of one of three beta chains present in the heterodimer. The beta chain is necessary and sufficient for integrin-dependent signaling. Its short cytoplasmic tail contains sequences critical for inside-out signaling.
A 44-kDa highly glycosylated plasma protein that binds phospholipids including CARDIOLIPIN; APOLIPOPROTEIN E RECEPTOR; membrane phospholipids, and other anionic phospholipid-containing moieties. It plays a role in coagulation and apoptotic processes. Formerly known as apolipoprotein H, it is an autoantigen in patients with ANTIPHOSPHOLIPID ANTIBODIES.
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.
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.
A soluble factor produced by MONOCYTES; MACROPHAGES, and other cells which activates T-lymphocytes and potentiates their response to mitogens or antigens. Interleukin-1 is a general term refers to either of the two distinct proteins, INTERLEUKIN-1ALPHA and INTERLEUKIN-1BETA. The biological effects of IL-1 include the ability to replace macrophage requirements for T-cell activation.
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.
A subclass of beta-adrenergic receptors (RECEPTORS, ADRENERGIC, BETA). The adrenergic beta-2 receptors are more sensitive to EPINEPHRINE than to NOREPINEPHRINE and have a high affinity for the agonist TERBUTALINE. They are widespread, with clinically important roles in SKELETAL MUSCLE; LIVER; and vascular, bronchial, gastrointestinal, and genitourinary SMOOTH MUSCLE.
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).
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 genetic region which contains the loci of genes which determine the structure of the serologically defined (SD) and lymphocyte-defined (LD) TRANSPLANTATION ANTIGENS, genes which control the structure of the IMMUNE RESPONSE-ASSOCIATED ANTIGENS, HUMAN; the IMMUNE RESPONSE GENES which control the ability of an animal to respond immunologically to antigenic stimuli, and genes which determine the structure and/or level of the first four components of complement.
The presence of proteins in the urine, an indicator of KIDNEY DISEASES.
Antibodies produced by a single clone of cells.
Compounds and molecular complexes that consist of very large numbers of atoms and are generally over 500 kDa in size. In biological systems macromolecular substances usually can be visualized using ELECTRON MICROSCOPY and are distinguished from ORGANELLES by the lack of a membrane structure.
Proteins prepared by recombinant DNA technology.
A group of antigens that includes both the major and minor histocompatibility antigens. The former are genetically determined by the major histocompatibility complex. They determine tissue type for transplantation and cause allograft rejections. The latter are systems of allelic alloantigens that can cause weak transplant rejection.
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.
A component of the murine major histocompatibility complex class I family. It contains one Ig-like C1-type domain and functions in processing and presentation of exogenous peptide antigens to the immune system.
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.
Integrin beta-1 chains which are expressed as heterodimers that are noncovalently associated with specific alpha-chains of the CD49 family (CD49a-f). CD29 is expressed on resting and activated leukocytes and is a marker for all of the very late activation antigens on cells. (from: Barclay et al., The Leukocyte Antigen FactsBook, 1993, p164)
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.
Measurable and quantifiable biological parameters (e.g., specific enzyme concentration, specific hormone concentration, specific gene phenotype distribution in a population, presence of biological substances) which serve as indices for health- and physiology-related assessments, such as disease risk, psychiatric disorders, environmental exposure and its effects, disease diagnosis, metabolic processes, substance abuse, pregnancy, cell line development, epidemiologic studies, etc.
Long convoluted tubules in the nephrons. They collect filtrate from blood passing through the KIDNEY GLOMERULUS and process this filtrate into URINE. Each renal tubule consists of a BOWMAN CAPSULE; PROXIMAL KIDNEY TUBULE; LOOP OF HENLE; DISTAL KIDNEY TUBULE; and KIDNEY COLLECTING DUCT leading to the central cavity of the kidney (KIDNEY PELVIS) that connects to the URETER.
An element with atomic symbol Cd, atomic number 48, and atomic weight 114. It is a metal and ingestion will lead to CADMIUM POISONING.
A subclass of beta-adrenergic receptors (RECEPTORS, ADRENERGIC, BETA). The adrenergic beta-1 receptors are equally sensitive to EPINEPHRINE and NOREPINEPHRINE and bind the agonist DOBUTAMINE and the antagonist METOPROLOL with high affinity. They are found in the HEART, juxtaglomerular cells, and in the central and peripheral nervous systems.
Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.
The rate dynamics in chemical or physical systems.
Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.
Elements of limited time intervals, contributing to particular results or situations.
Antigens on surfaces of cells, including infectious or foreign cells or viruses. They are usually protein-containing groups on cell membranes or walls and may be isolated.
Strains of mice in which certain GENES of their GENOMES have been disrupted, or "knocked-out". To produce knockouts, using RECOMBINANT DNA technology, the normal DNA sequence of the gene being studied is altered to prevent synthesis of a normal gene product. Cloned cells in which this DNA alteration is successful are then injected into mouse EMBRYOS to produce chimeric mice. The chimeric mice are then bred to yield a strain in which all the cells of the mouse contain the disrupted gene. Knockout mice are used as EXPERIMENTAL ANIMAL MODELS for diseases (DISEASE MODELS, ANIMAL) and to clarify the functions of the genes.
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.
Processes involved in the formation of TERTIARY PROTEIN STRUCTURE.
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.
Cells grown in vitro from neoplastic tissue. If they can be established as a TUMOR CELL LINE, they can be propagated in cell culture indefinitely.
A lectin found in ENDOPLASMIC RETICULUM membranes that binds to specific N-linked OLIGOSACCHARIDES found on newly synthesized proteins. It may play role in PROTEIN FOLDING or retention and degradation of misfolded proteins in the endoplasmic reticulum.
Pathological processes of the KIDNEY or its component tissues.
Body organ that filters blood for the secretion of URINE and that regulates ion concentrations.

A cytomegalovirus glycoprotein re-routes MHC class I complexes to lysosomes for degradation. (1/1648)

Mouse cytomegalovirus (MCMV) early gene expression interferes with the major histocompatibility complex class I (MHC class I) pathway of antigen presentation. Here we identify a 48 kDa type I transmembrane glycoprotein encoded by the MCMV early gene m06, which tightly binds to properly folded beta2-microglobulin (beta2m)-associated MHC class I molecules in the endoplasmic reticulum (ER). This association is mediated by the lumenal/transmembrane part of the protein. gp48-MHC class I complexes are transported out of the ER, pass the Golgi, but instead of being expressed on the cell surface, they are redirected to the endocytic route and rapidly degraded in a Lamp-1(+) compartment. As a result, m06-expressing cells are impaired in presenting antigenic peptides to CD8(+) T cells. The cytoplasmic tail of gp48 contains two di-leucine motifs. Mutation of the membrane-proximal di-leucine motif of gp48 restored surface expression of MHC class I, while mutation of the distal one had no effect. The results establish a novel viral mechanism for downregulation of MHC class I molecules by directly binding surface-destined MHC complexes and exploiting the cellular di-leucine sorting machinery for lysosomal degradation.  (+info)

Impaired lysosomal processing of beta2-microglobulin by infiltrating macrophages in dialysis amyloidosis. (2/1648)

BACKGROUND: Macrophages may participate in amyloid fibril formation by processing the protein precursor. Although this theory seems to apply for amyloidosis, in which proteolytic cleavage is a prerequisite for amyloid fibril formation, it has not been demonstrated for beta2-microglobulin (beta2m) amyloidosis. We aimed to establish the role played by macrophages in beta2m amyloidosis. METHODS: We used a double immunogold electron microscopy technique, including mouse antihuman CD68, rabbit antihuman beta2m, amyloid P component, and lysosome-associated membrane protein (LAMP-1) antibodies. Differential density labeling studies of beta2m and amyloid P component were performed extra- and intracellularly to assess protein processing by macrophages. RESULTS: The cells surrounding amyloid fibrils were found to be mostly CD68 positive, suggesting that they were of monocyte-macrophage lineage. Intracellular accumulation of amyloid fibrils was also observed; these fibrils were constantly surrounded by LAMP-1-linked gold particles, demonstrating that intracellular beta2m was almost exclusively lysosomal. The rough-surface endoplasmic reticulum was not labeled by beta2m antibody, suggesting that there was no active synthesis of beta2m by the cells. As a marker of endocytosis, protruded cytoplasmic processes in close relation with the intracellular accumulations of beta2m amyloid fibrils were observed. No difference in density labeling (extracellular vs. intracellular) was observed for beta2m, whereas intracellular P component labeling was significantly decreased. CONCLUSIONS: All of these data are strongly suggestive of phagocytosis and not synthesis of amyloid fibrils by macrophages. Further, they demonstrate an impaired lysosomal processing specific for beta2m, as other compounds of the amyloid fibrils (P component) are significantly cleared.  (+info)

Photophysical analysis of class I major histocompatibility complex protein assembly using a xanthene-derivatized beta2-microglobulin. (3/1648)

Spectral changes and a sixfold increase in the emission intensity were observed in the fluorescence of a single xanthene probe (Texas red) attached to beta2m-microglobulin (beta2m) upon assembly of beta2m into a ternary complex with mouse H-2Kd heavy chain and influenza nuclear protein peptide. Dissociation of the labeled beta2m from the ternary complex restored the probe's fluorescence and absorption spectra and reduced the emission intensity. Thus changes in xanthene probe fluorescence upon association/dissociation of the labeled beta2m molecule with/from the ternary complex provide a simple and convenient method for studying the assembly/dissociation mechanism of the class I major histocompatibility complex (MHC-I) encoded molecule. The photophysical changes in the probe can be accounted for by the oligomerization of free labeled beta2m molecules. The fluorescence at 610 nm is due to beta2m dimers, where the probes are significantly separated spatially so that their emission and excitation properties are close to those of xanthene monomers. Fluorescence around 630 nm is due to beta2m oligomers where xanthene probes interact. Minima in the steady-state excitation (550 nm) and emission (630 nm) anisotropy spectra correlate with the maxima of the high-order oligomer excitation and emission spectra, showing that their fluorescence is more depolarized. These photophysical features are explained by splitting of the first singlet excited state of interacting xanthene probes that can be modeled by exciton theory.  (+info)

Acute haemodynamic and proteinuric effects of prednisolone in patients with a nephrotic syndrome. (4/1648)

BACKGROUND: Administration of prednisolone causes an abrupt rise in proteinuria in patients with a nephrotic syndrome. METHODS: To clarify the mechanisms responsible for this increase in proteinuria we have performed a placebo controlled study in 26 patients with a nephrotic syndrome. Systemic and renal haemodynamics and urinary protein excretion were measured after prednisolone and after placebo. RESULTS: After i.v. administration of 125-150 mg prednisolone total proteinuria increased from 6.66+/-4.42 to 9.37+/-6.07 mg/min (P<0.001). By analysing the excretion of proteins with different charge and weight (albumin, transferrin, IgG, IgG4 and beta2-microglobulin) it became apparent that the increase of proteinuria was the result of a change in size selectivity rather than a change in glomerular charge selectivity or tubular protein reabsorption. Glomerular filtration rate rose from 83+/-34 ml to 95+/-43 ml/min (P<0.001) after 5 h, whereas effective renal plasma flow and endogenous creatinine clearance remained unchanged. As a result filtration fraction was increased, compatible with an increased glomerular pressure, which probably contributes to the size selectivity changes. Since corticosteroids affect both the renin-angiotensin system and renal prostaglandins, we have evaluated the effects of prednisolone on proteinuria after pretreatment with 3 months of the angiotensin-converting enzyme inhibitor lisinopril or after 2 weeks of the prostaglandin synthesis inhibitor indomethacin. Neither drug had any effect on prednisolone-induced increases of proteinuria. CONCLUSIONS: Prednisolone increases proteinuria by changing the size selective barrier of the glomerular capillary. Neither the renin-angiotensin axis nor prostaglandins seem to be involved in these effects of prednisolone on proteinuria.  (+info)

Stability of plasma levels of cytokines and soluble activation markers in patients with human immunodeficiency virus infection. (5/1648)

Cytokine and immune activation marker levels in plasma are valuable measurements of immune status and treatment effects in human immunodeficiency virus (HIV) infection and AIDS. Five populations representing various stages of disease were studied: controls, 2 AIDS groups with <50/mm3 CD4 cells, and 2 groups of HIV-positive subjects-1 with stable CD4 T cells (median, 545/mm3) and 1 with >100/mm3 CD4 cell decline in 1 year. Relatively stable levels of tumor necrosis factor (TNF)-alpha, soluble TNF receptor (R)II, soluble interleukin-2R, neopterin, and beta2-microglobulin (beta2M) were documented over 5-8 weeks in patients with AIDS and for 1-4 years in the other groups. beta2M was generally the most stable marker. Interferon-gamma levels, however, fluctuated substantially. Individuals, whether normal or HIV-positive, maintain characteristic plasma levels of cytokines and immune activation markers. Thus, documented changes, in excess of the variability observed in this study, are likely to be significant indicators of change in disease status or effects of therapy.  (+info)

Cyclooxygenase-2 expression is up-regulated in human pancreatic cancer. (6/1648)

A large body of evidence suggests that cyclooxygenase-2 (COX-2) is important in gastrointestinal cancer. The purpose of this study was to determine whether COX-2 was expressed in adenocarcinoma of the human pancreas. Quantitative reverse transcription-PCR, immunoblotting, and immunohistochemistry were used to assess the expression of COX-2 in pancreatic tissue. Levels of COX-2 mRNA were increased by >60-fold in pancreatic cancer compared to adjacent nontumorous tissue. COX-2 protein was present in 9 of 10 cases of adenocarcinoma of the pancreas but was undetectable in nontumorous pancreatic tissue. Immunohistochemical analysis showed that COX-2 was expressed in malignant epithelial cells. In cultured human pancreatic cancer cells, levels of COX-2 mRNA and protein were induced by treatment with tumor-promoting phorbol esters. Taken together, these results suggest that COX-2 may be a target for the prevention or treatment of pancreatic cancer.  (+info)

Soluble class I MHC with beta2-microglobulin covalently linked peptides: specific binding to a T cell hybridoma. (7/1648)

Soluble forms of the mouse MHC class I molecule, Dd, were produced in which the peptide binding groove was uniformly occupied by peptides attached via a covalent flexible peptide linker to the N terminus of the associated beta2-microglobulin. The MHC heavy chain and beta2-microglobulin were firmly associated, and the molecules displayed an Ab epitope requiring proper occupancy of the peptide binding groove. Soluble Dd containing a covalent version of a well-characterized Dd-binding peptide from HIV stimulated a T cell hybridoma specific for this combination. Furthermore, a tetravalent version of this molecule bound specifically with apparent high avidity to this hybridoma.  (+info)

Recognition of the major histocompatibility complex restriction element modulates CD8(+) T cell specificity and compensates for loss of T cell receptor contacts with the specific peptide. (8/1648)

Triggering of a T cell requires interaction between its specific receptor (TCR) and a peptide antigen presented by a self-major histocompatibility complex (MHC) molecule. TCR recognition of self-MHC by itself falls below the threshold of detection in most systems due to low affinity. To study this interaction, we have used a read-out system in which antigen-specific effector T cells are confronted with targets expressing high levels of MHC compared with the selecting and priming environment. More specifically, the system is based on CD8(+) T cells selected in an environment with subnormal levels of MHC class I in the absence of beta2-microglobulin. We observe that the MHC restriction element can trigger viral peptide-specific T cells independently of the peptide ligand, provided there is an increase in self-MHC density. Peptide-independent triggering required at least four times the natural in vivo level of MHC expression. Furthermore, recognition of the restriction element at expression levels below this threshold was still enough to compensate for lack of affinity to peptides carrying alanine substitutions in major TCR contact residues. Thus, the specificity in TCR recognition and T cell activation is fine tuned by the avidity for self-MHC, and TCR avidities for peptide and MHC may substitute for each other. These results demonstrate a functional role for TCR avidity for self-MHC in tuning of T cell specificity, and support a role for cross-reactivity on "self" during T cell selection and activation.  (+info)

Beta-2 microglobulin (β2M) is a small protein that is a component of the major histocompatibility complex class I molecule, which plays a crucial role in the immune system. It is found on the surface of almost all nucleated cells in the body and is involved in presenting intracellular peptides to T-cells for immune surveillance.

β2M is produced at a relatively constant rate by cells throughout the body and is freely filtered by the glomeruli in the kidneys. Under normal circumstances, most of the filtrated β2M is reabsorbed and catabolized in the proximal tubules of the nephrons. However, when the glomerular filtration rate (GFR) is decreased, as in chronic kidney disease (CKD), the reabsorption capacity of the proximal tubules becomes overwhelmed, leading to increased levels of β2M in the blood and its subsequent appearance in the urine.

Elevated serum and urinary β2M levels have been associated with various clinical conditions, such as CKD, multiple myeloma, autoimmune disorders, and certain infectious diseases. Measuring β2M concentrations can provide valuable information for diagnostic, prognostic, and monitoring purposes in these contexts.

Beta-globulins are a group of proteins found in the beta region of a serum protein electrophoresis, which is a laboratory test used to separate and identify different types of proteins in the blood. This group includes several important proteins such as:

1. Beta-lipoproteins: These are responsible for transporting fat molecules, including cholesterol, throughout the body.
2. Transferrin: A protein that binds and transports iron in the blood.
3. Complement components: These proteins play a crucial role in the immune system's response to infection and inflammation.
4. Beta-2 microglobulin: A protein involved in the functioning of the immune system, elevated levels of which can be found in various conditions such as kidney disease and autoimmune disorders.
5. Hemopexin: A protein that binds and transports heme (a component of hemoglobin) in the blood.

It is important to note that any significant increase or decrease in beta-globulins can indicate an underlying medical condition, such as liver disease, kidney disease, or an autoimmune disorder. Therefore, abnormal results should be further evaluated by a healthcare professional for proper diagnosis and treatment.

Alpha-globulins are a group of proteins present in blood plasma, which are classified based on their electrophoretic mobility. They migrate between albumin and beta-globulins during electrophoresis. Alpha-globulins include several proteins, such as alpha-1 antitrypsin, alpha-1 acid glycoprotein, and haptoglobin. These proteins play various roles in the body, including transporting and regulating other molecules, participating in immune responses, and maintaining oncotic pressure in blood vessels.

Interleukin-1 beta (IL-1β) is a member of the interleukin-1 cytokine family and is primarily produced by activated macrophages in response to inflammatory stimuli. It is a crucial mediator of the innate immune response and plays a key role in the regulation of various biological processes, including cell proliferation, differentiation, and apoptosis. IL-1β is involved in the pathogenesis of several inflammatory diseases, such as rheumatoid arthritis, inflammatory bowel disease, and atherosclerosis. It exerts its effects by binding to the interleukin-1 receptor, which triggers a signaling cascade that leads to the activation of various transcription factors and the expression of target genes.

Amyloidosis is a medical condition characterized by the abnormal accumulation of insoluble proteins called amyloid in various tissues and organs throughout the body. These misfolded protein deposits can disrupt the normal function of affected organs, leading to a range of symptoms depending on the location and extent of the amyloid deposition.

There are different types of amyloidosis, classified based on the specific proteins involved:

1. Primary (AL) Amyloidosis: This is the most common form, accounting for around 80% of cases. It results from the overproduction and misfolding of immunoglobulin light chains, typically by clonal plasma cells in the bone marrow. The amyloid deposits can affect various organs, including the heart, kidneys, liver, and nervous system.
2. Secondary (AA) Amyloidosis: This form is associated with chronic inflammatory diseases, such as rheumatoid arthritis, tuberculosis, or familial Mediterranean fever. The amyloid fibrils are composed of serum amyloid A protein (SAA), an acute-phase reactant produced during the inflammatory response. The kidneys are commonly affected in this type of amyloidosis.
3. Hereditary or Familial Amyloidosis: These forms are caused by genetic mutations that result in the production of abnormal proteins prone to misfolding and amyloid formation. Examples include transthyretin (TTR) amyloidosis, fibrinogen amyloidosis, and apolipoprotein AI amyloidosis. These forms can affect various organs, including the heart, nerves, and kidneys.
4. Dialysis-Related Amyloidosis: This form is seen in patients undergoing long-term dialysis for chronic kidney disease. The amyloid fibrils are composed of beta-2 microglobulin, a protein that accumulates due to impaired clearance during dialysis. The joints and bones are commonly affected in this type of amyloidosis.

The diagnosis of amyloidosis typically involves a combination of clinical evaluation, imaging studies, and tissue biopsy with the demonstration of amyloid deposition using special stains (e.g., Congo red). Treatment depends on the specific type and extent of organ involvement and may include supportive care, medications to target the underlying cause (e.g., chemotherapy, immunomodulatory agents), and organ transplantation in some cases.

Histocompatibility antigens, class I are proteins found on the surface of most cells in the body. They play a critical role in the immune system's ability to differentiate between "self" and "non-self." These antigens are composed of three polypeptides - two heavy chains and one light chain - and are encoded by genes in the major histocompatibility complex (MHC) on chromosome 6 in humans.

Class I MHC molecules present peptide fragments from inside the cell to CD8+ T cells, also known as cytotoxic T cells. This presentation allows the immune system to detect and destroy cells that have been infected by viruses or other intracellular pathogens, or that have become cancerous.

There are three main types of class I MHC molecules in humans: HLA-A, HLA-B, and HLA-C. The term "HLA" stands for human leukocyte antigen, which reflects the original identification of these proteins on white blood cells (leukocytes). The genes encoding these molecules are highly polymorphic, meaning there are many different variants in the population, and matching HLA types is essential for successful organ transplantation to minimize the risk of rejection.

Amyloid is a term used in medicine to describe abnormally folded protein deposits that can accumulate in various tissues and organs of the body. These misfolded proteins can form aggregates known as amyloid fibrils, which have a characteristic beta-pleated sheet structure. Amyloid deposits can be composed of different types of proteins, depending on the specific disease associated with the deposit.

In some cases, amyloid deposits can cause damage to organs and tissues, leading to various clinical symptoms. Some examples of diseases associated with amyloidosis include Alzheimer's disease (where amyloid-beta protein accumulates in the brain), systemic amyloidosis (where amyloid fibrils deposit in various organs such as the heart, kidneys, and liver), and type 2 diabetes (where amyloid deposits form in the pancreas).

It's important to note that not all amyloid deposits are harmful or associated with disease. However, when they do cause problems, treatment typically involves managing the underlying condition that is leading to the abnormal protein accumulation.

Trypsin inhibitor, Kunitz soybean, also known as Bowman-Birk inhibitor, is a type of protease inhibitor found in soybeans. It is a small protein molecule that inhibits the activity of trypsin, a digestive enzyme that helps break down proteins in the body. The Kunitz soybean trypsin inhibitor has two binding sites for trypsin and is resistant to digestion, making it biologically active in the gastrointestinal tract. It can inhibit the absorption of trypsin and regulate its activity, which may have implications for protein digestion and the regulation of certain physiological processes.

Adrenergic receptors are a type of G protein-coupled receptor that binds and responds to catecholamines, such as epinephrine (adrenaline) and norepinephrine (noradrenaline). Beta adrenergic receptors (β-adrenergic receptors) are a subtype of adrenergic receptors that include three distinct subclasses: β1, β2, and β3. These receptors are widely distributed throughout the body and play important roles in various physiological functions, including cardiovascular regulation, bronchodilation, lipolysis, and glucose metabolism.

β1-adrenergic receptors are primarily located in the heart and regulate cardiac contractility, chronotropy (heart rate), and relaxation. β2-adrenergic receptors are found in various tissues, including the lungs, vascular smooth muscle, liver, and skeletal muscle. They mediate bronchodilation, vasodilation, glycogenolysis, and lipolysis. β3-adrenergic receptors are mainly expressed in adipose tissue, where they stimulate lipolysis and thermogenesis.

Agonists of β-adrenergic receptors include catecholamines like epinephrine and norepinephrine, as well as synthetic drugs such as dobutamine (a β1-selective agonist) and albuterol (a non-selective β2-agonist). Antagonists of β-adrenergic receptors are commonly used in the treatment of various conditions, including hypertension, angina pectoris, heart failure, and asthma. Examples of β-blockers include metoprolol (a β1-selective antagonist) and carvedilol (a non-selective β-blocker with additional α1-adrenergic receptor blocking activity).

Integrin β3 is a subunit of certain integrin heterodimers, which are transmembrane receptors that mediate cell-cell and cell-extracellular matrix (ECM) adhesion. Integrin β3 combines with either integrin αv (to form the integrin αvβ3) or integrin αIIb (to form the integrin αIIbβ3). These integrins are involved in various cellular processes, including platelet aggregation, angiogenesis, and tumor metastasis.

Integrin αIIbβ3 is primarily expressed on platelets and mediates platelet aggregation by binding to fibrinogen, von Willebrand factor, and other adhesive proteins in the ECM. Integrin αvβ3 is widely expressed in various cell types and participates in diverse functions such as cell migration, proliferation, differentiation, and survival. It binds to a variety of ECM proteins, including fibronectin, vitronectin, and osteopontin, as well as to soluble ligands like vascular endothelial growth factor (VEGF) and transforming growth factor-β (TGF-β).

Dysregulation of integrin β3 has been implicated in several pathological conditions, such as thrombosis, atherosclerosis, tumor metastasis, and inflammatory diseases.

HLA (Human Leukocyte Antigen) antigens are a group of proteins found on the surface of cells in our body. They play a crucial role in the immune system's ability to differentiate between "self" and "non-self." HLA antigens are encoded by a group of genes located on chromosome 6, known as the major histocompatibility complex (MHC).

There are three types of HLA antigens: HLA class I, HLA class II, and HLA class III. HLA class I antigens are found on the surface of almost all cells in the body and help the immune system recognize and destroy virus-infected or cancerous cells. They consist of three components: HLA-A, HLA-B, and HLA-C.

HLA class II antigens are primarily found on the surface of immune cells, such as macrophages, B cells, and dendritic cells. They assist in the presentation of foreign particles (like bacteria and viruses) to CD4+ T cells, which then activate other parts of the immune system. HLA class II antigens include HLA-DP, HLA-DQ, and HLA-DR.

HLA class III antigens consist of various molecules involved in immune responses, such as cytokines and complement components. They are not directly related to antigen presentation.

The genetic diversity of HLA antigens is extensive, with thousands of variations or alleles. This diversity allows for a better ability to recognize and respond to a wide range of pathogens. However, this variation can also lead to compatibility issues in organ transplantation, as the recipient's immune system may recognize the donor's HLA antigens as foreign and attack the transplanted organ.

Acetylglucosaminidase (ACG) is an enzyme that catalyzes the hydrolysis of N-acetyl-beta-D-glucosaminides, which are found in glycoproteins and glycolipids. This enzyme plays a crucial role in the degradation and recycling of these complex carbohydrates within the body.

Deficiency or malfunction of Acetylglucosaminidase can lead to various genetic disorders, such as mucolipidosis II (I-cell disease) and mucolipidosis III (pseudo-Hurler polydystrophy), which are characterized by the accumulation of glycoproteins and glycolipids in lysosomes, resulting in cellular dysfunction and progressive damage to multiple organs.

H-2 antigens are a group of cell surface proteins found in mice that play a critical role in the immune system. They are similar to the human leukocyte antigen (HLA) complex in humans and are involved in the presentation of peptide antigens to T cells, which is a crucial step in the adaptive immune response.

The H-2 antigens are encoded by a cluster of genes located on chromosome 17 in mice. They are highly polymorphic, meaning that there are many different variations of these proteins circulating in the population. This genetic diversity allows for a wide range of potential peptide antigens to be presented to T cells, thereby enhancing the ability of the immune system to recognize and respond to a variety of pathogens.

The H-2 antigens are divided into two classes based on their function and structure. Class I H-2 antigens are found on almost all nucleated cells and consist of a heavy chain, a light chain, and a peptide fragment. They present endogenous peptides, such as those derived from viruses that infect the cell, to CD8+ T cells.

Class II H-2 antigens, on the other hand, are found primarily on professional antigen-presenting cells, such as dendritic cells and macrophages. They consist of an alpha chain and a beta chain and present exogenous peptides, such as those derived from bacteria that have been engulfed by the cell, to CD4+ T cells.

Overall, H-2 antigens are essential components of the mouse immune system, allowing for the recognition and elimination of pathogens and infected cells.

Cadmium poisoning is a condition that results from the exposure to cadmium, a toxic heavy metal. This can occur through inhalation, ingestion, or skin absorption. Cadmium is found in some industrial workplaces, such as battery manufacturing, metal smelting, and phosphate fertilizer production. It can also be found in contaminated food, water, and cigarette smoke.

Acute cadmium poisoning is rare but can cause severe symptoms such as abdominal pain, vomiting, diarrhea, and muscle cramps. Chronic exposure to cadmium can lead to a range of health problems, including kidney damage, bone disease, lung damage, and anemia. It has also been linked to an increased risk of cancer, particularly lung cancer.

The treatment for cadmium poisoning typically involves removing the source of exposure, providing supportive care, and in some cases, chelation therapy to remove cadmium from the body. Prevention measures include reducing exposure to cadmium in the workplace, avoiding contaminated food and water, and not smoking.

Neopterin is a pteridine metabolite that is primarily produced by macrophages in response to the activation of the immune system, particularly in response to interferon-gamma (IFN-γ). It is commonly used as a biomarker for cellular immune activation and inflammation. Elevated levels of neopterin have been associated with various conditions such as infections, autoimmune diseases, cancer, and transplant rejection.

Transforming Growth Factor-beta (TGF-β) is a type of cytokine, which is a cell signaling protein involved in the regulation of various cellular processes, including cell growth, differentiation, and apoptosis (programmed cell death). TGF-β plays a critical role in embryonic development, tissue homeostasis, and wound healing. It also has been implicated in several pathological conditions such as fibrosis, cancer, and autoimmune diseases.

TGF-β exists in multiple isoforms (TGF-β1, TGF-β2, and TGF-β3) that are produced by many different cell types, including immune cells, epithelial cells, and fibroblasts. The protein is synthesized as a precursor molecule, which is cleaved to release the active TGF-β peptide. Once activated, TGF-β binds to its receptors on the cell surface, leading to the activation of intracellular signaling pathways that regulate gene expression and cell behavior.

In summary, Transforming Growth Factor-beta (TGF-β) is a multifunctional cytokine involved in various cellular processes, including cell growth, differentiation, apoptosis, embryonic development, tissue homeostasis, and wound healing. It has been implicated in several pathological conditions such as fibrosis, cancer, and autoimmune diseases.

A cell line is a culture of cells that are grown in a laboratory for use in research. These cells are usually taken from a single cell or group of cells, and they are able to divide and grow continuously in the lab. Cell lines can come from many different sources, including animals, plants, and humans. They are often used in scientific research to study cellular processes, disease mechanisms, and to test new drugs or treatments. Some common types of human cell lines include HeLa cells (which come from a cancer patient named Henrietta Lacks), HEK293 cells (which come from embryonic kidney cells), and HUVEC cells (which come from umbilical vein endothelial cells). It is important to note that cell lines are not the same as primary cells, which are cells that are taken directly from a living organism and have not been grown in the lab.

Major Histocompatibility Complex (MHC) class I genes are a group of genes that encode proteins found on the surface of most nucleated cells in the body. These proteins play a crucial role in the immune system by presenting pieces of protein from inside the cell to T-cells, which are a type of white blood cell. This process allows the immune system to detect and respond to cells that have been infected by viruses or become cancerous.

MHC class I genes are highly polymorphic, meaning there are many different variations of these genes in the population. This diversity is important for the immune system's ability to recognize and respond to a wide variety of pathogens. The MHC class I proteins are composed of three main regions: the heavy chain, which is encoded by the MHC class I gene; a short peptide, which is derived from inside the cell; and a light chain called beta-2 microglobulin, which is not encoded by an MHC gene.

There are three major types of MHC class I genes in humans, known as HLA-A, HLA-B, and HLA-C. These genes are located on chromosome 6 and are among the most polymorphic genes in the human genome. The products of these genes are critical for the immune system's ability to distinguish between self and non-self, and play a key role in organ transplant rejection.

Multiple myeloma is a type of cancer that forms in a type of white blood cell called a plasma cell. Plasma cells help your body fight infection by producing antibodies. In multiple myeloma, cancerous plasma cells accumulate in the bone marrow and crowd out healthy blood cells. Rather than producing useful antibodies, the cancer cells produce abnormal proteins that can cause complications such as kidney damage, bone pain and fractures.

Multiple myeloma is a type of cancer called a plasma cell neoplasm. Plasma cell neoplasms are diseases in which there is an overproduction of a single clone of plasma cells. In multiple myeloma, this results in the crowding out of normal plasma cells, red and white blood cells and platelets, leading to many of the complications associated with the disease.

The abnormal proteins produced by the cancer cells can also cause damage to organs and tissues in the body. These abnormal proteins can be detected in the blood or urine and are often used to monitor the progression of multiple myeloma.

Multiple myeloma is a relatively uncommon cancer, but it is the second most common blood cancer after non-Hodgkin lymphoma. It typically occurs in people over the age of 65, and men are more likely to develop multiple myeloma than women. While there is no cure for multiple myeloma, treatments such as chemotherapy, radiation therapy, and stem cell transplantation can help manage the disease and its symptoms, and improve quality of life.

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.

Messenger RNA (mRNA) is a type of RNA (ribonucleic acid) that carries genetic information copied from DNA in the form of a series of three-base code "words," each of which specifies a particular amino acid. This information is used by the cell's machinery to construct proteins, a process known as translation. After being transcribed from DNA, mRNA travels out of the nucleus to the ribosomes in the cytoplasm where protein synthesis occurs. Once the protein has been synthesized, the mRNA may be degraded and recycled. Post-transcriptional modifications can also occur to mRNA, such as alternative splicing and addition of a 5' cap and a poly(A) tail, which can affect its stability, localization, and translation efficiency.

Creatinine is a waste product that's produced by your muscles and removed from your body by your kidneys. Creatinine is a breakdown product of creatine, a compound found in meat and fish, as well as in the muscles of vertebrates, including humans.

In healthy individuals, the kidneys filter out most of the creatinine and eliminate it through urine. However, when the kidneys are not functioning properly, creatinine levels in the blood can rise. Therefore, measuring the amount of creatinine in the blood or urine is a common way to test how well the kidneys are working. High creatinine levels in the blood may indicate kidney damage or kidney disease.

HLA-B27 antigen is a type of human leukocyte antigen (HLA) found on the surface of white blood cells. HLAs are proteins that help the body's immune system distinguish its own cells from foreign substances such as viruses and bacteria.

HLA-B27 is a specific type of HLA-B antigen, which is part of the major histocompatibility complex (MHC) class I molecules. The presence of HLA-B27 antigen can be inherited from parents to their offspring.

While most people with the HLA-B27 antigen do not develop any health problems, this antigen is associated with an increased risk of developing certain inflammatory diseases, particularly spondyloarthritis, a group of disorders that affect the joints and spine. Examples of these conditions include ankylosing spondylitis, reactive arthritis, psoriatic arthritis, and enteropathic arthritis associated with inflammatory bowel disease. However, not everyone with HLA-B27 will develop these diseases, and many people without the antigen can still develop spondyloarthritis.

Hemodiafiltration (HDF) is a type of renal replacement therapy used for patients with severe kidney failure. It combines elements of hemodialysis and hemofiltration to provide more efficient removal of waste products, toxins, and excess fluid from the blood.

During HDF, the patient's blood is passed through a semi-permeable membrane in a dialyzer or artificial kidney. The membrane allows for the passage of smaller molecules such as urea, creatinine, and electrolytes, while retaining larger molecules like proteins. A combination of diffusion (due to the concentration gradient) and convection (due to the application of a transmembrane pressure) leads to the removal of waste products and toxins from the blood.

In addition to this, a substitution fluid is infused into the extracorporeal circuit to replace the volume of fluid removed during convection. This substitution fluid can be tailored to match the patient's electrolyte and acid-base status, allowing for better control over their biochemical parameters.

HDF has been shown to provide better clearance of middle and large molecular weight uremic toxins compared to conventional hemodialysis, potentially leading to improved clinical outcomes such as reduced inflammation, oxidative stress, and cardiovascular risk. However, more research is needed to confirm these benefits and establish the optimal dosing and prescription for HDF.

Renal dialysis is a medical procedure that is used to artificially remove waste products, toxins, and excess fluids from the blood when the kidneys are no longer able to perform these functions effectively. This process is also known as hemodialysis.

During renal dialysis, the patient's blood is circulated through a special machine called a dialyzer or an artificial kidney, which contains a semi-permeable membrane that filters out waste products and excess fluids from the blood. The cleaned blood is then returned to the patient's body.

Renal dialysis is typically recommended for patients with advanced kidney disease or kidney failure, such as those with end-stage renal disease (ESRD). It is a life-sustaining treatment that helps to maintain the balance of fluids and electrolytes in the body, prevent the buildup of waste products and toxins, and control blood pressure.

There are two main types of renal dialysis: hemodialysis and peritoneal dialysis. Hemodialysis is the most common type and involves using a dialyzer to filter the blood outside the body. Peritoneal dialysis, on the other hand, involves placing a catheter in the abdomen and using the lining of the abdomen (peritoneum) as a natural filter to remove waste products and excess fluids from the body.

Overall, renal dialysis is an essential treatment option for patients with kidney failure, helping them to maintain their quality of life and prolong their survival.

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.

Integrin beta4, also known as ITGB4 or CD104, is a type of integrin subunit that forms part of the integrin receptor along with an alpha subunit. Integrins are transmembrane proteins involved in cell-cell and cell-extracellular matrix (ECM) adhesion, signal transduction, and regulation of various cellular processes such as proliferation, differentiation, and migration.

Integrin beta4 is unique among the integrin subunits because it has a large cytoplasmic domain that can interact with several intracellular signaling molecules, making it an important regulator of cell behavior. Integrin beta4 is widely expressed in various tissues, including epithelial cells, endothelial cells, and hematopoietic cells.

Integrin beta4 forms heterodimers with integrin alpha6 to form the receptor for laminins, which are major components of the basement membrane. This receptor is involved in maintaining the integrity of epithelial tissues and regulating cell migration during development, tissue repair, and cancer progression. Mutations in ITGB4 have been associated with several human diseases, including epidermolysis bullosa, a group of inherited skin disorders characterized by fragile skin and blistering.

"Cells, cultured" is a medical term that refers to cells that have been removed from an organism and grown in controlled laboratory conditions outside of the body. This process is called cell culture and it allows scientists to study cells in a more controlled and accessible environment than they would have inside the body. Cultured cells can be derived from a variety of sources, including tissues, organs, or fluids from humans, animals, or cell lines that have been previously established in the laboratory.

Cell culture involves several steps, including isolation of the cells from the tissue, purification and characterization of the cells, and maintenance of the cells in appropriate growth conditions. The cells are typically grown in specialized media that contain nutrients, growth factors, and other components necessary for their survival and proliferation. Cultured cells can be used for a variety of purposes, including basic research, drug development and testing, and production of biological products such as vaccines and gene therapies.

It is important to note that cultured cells may behave differently than they do in the body, and results obtained from cell culture studies may not always translate directly to human physiology or disease. Therefore, it is essential to validate findings from cell culture experiments using additional models and ultimately in clinical trials involving human subjects.

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.

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.

Integrin beta chains are a type of subunit that make up integrin receptors, which are heterodimeric transmembrane proteins involved in cell-cell and cell-extracellular matrix (ECM) adhesion. These receptors play crucial roles in various biological processes such as cell signaling, migration, proliferation, and differentiation.

Integrin beta chains combine with integrin alpha chains to form functional heterodimeric receptors. In humans, there are 18 different alpha subunits and 8 different beta subunits that can combine to form at least 24 distinct integrin receptors. The beta chain contributes to the cytoplasmic domain of the integrin receptor, which is involved in intracellular signaling and cytoskeletal interactions.

The beta chains are characterized by a conserved cytoplasmic region called the beta-tail domain, which interacts with various adaptor proteins to mediate downstream signaling events. Additionally, some integrin beta chains have a large inserted (I) domain in their extracellular regions that is responsible for ligand binding specificity.

Examples of integrin beta chains include β1, β2, β3, β4, β5, β6, β7, and β8, each with distinct functions and roles in various tissues and cell types. Mutations or dysregulation of integrin beta chains have been implicated in several human diseases, including cancer, inflammation, fibrosis, and developmental disorders.

Beta 2-glycoprotein I, also known as apolipoprotein H, is a plasma protein that belongs to the family of proteins called immunoglobulin-binding proteins. It has a molecular weight of approximately 44 kDa and is composed of five domains with similar structures.

Beta 2-glycoprotein I is primarily produced in the liver and circulates in the bloodstream, where it plays a role in several physiological processes, including coagulation, complement activation, and lipid metabolism. It has been identified as an autoantigen in certain autoimmune disorders, such as antiphospholipid syndrome (APS), where autoantibodies against beta 2-glycoprotein I can cause blood clots, miscarriages, and other complications.

In medical terminology, the definition of "beta 2-glycoprotein I" is as follows:

A plasma protein that belongs to the family of immunoglobulin-binding proteins and has a molecular weight of approximately 44 kDa. It is primarily produced in the liver and circulates in the bloodstream, where it plays a role in several physiological processes, including coagulation, complement activation, and lipid metabolism. Autoantibodies against beta 2-glycoprotein I are associated with certain autoimmune disorders, such as antiphospholipid syndrome (APS), where they can cause blood clots, miscarriages, and other complications.

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.

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 (IL-1) is a type of cytokine, which are proteins that play a crucial role in cell signaling. Specifically, IL-1 is a pro-inflammatory cytokine that is involved in the regulation of immune and inflammatory responses in the body. It is produced by various cells, including monocytes, macrophages, and dendritic cells, in response to infection or injury.

IL-1 exists in two forms, IL-1α and IL-1β, which have similar biological activities but are encoded by different genes. Both forms of IL-1 bind to the same receptor, IL-1R, and activate intracellular signaling pathways that lead to the production of other cytokines, chemokines, and inflammatory mediators.

IL-1 has a wide range of biological effects, including fever induction, activation of immune cells, regulation of hematopoiesis (the formation of blood cells), and modulation of bone metabolism. Dysregulation of IL-1 production or activity has been implicated in various inflammatory diseases, such as rheumatoid arthritis, gout, and inflammatory bowel disease. Therefore, IL-1 is an important target for the development of therapies aimed at modulating the immune response and reducing inflammation.

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.

Adrenergic receptors are a type of G protein-coupled receptor that bind and respond to catecholamines, such as epinephrine (adrenaline) and norepinephrine (noradrenaline). Beta-2 adrenergic receptors (β2-ARs) are a subtype of adrenergic receptors that are widely distributed throughout the body, particularly in the lungs, heart, blood vessels, gastrointestinal tract, and skeletal muscle.

When β2-ARs are activated by catecholamines, they trigger a range of physiological responses, including relaxation of smooth muscle, increased heart rate and contractility, bronchodilation, and inhibition of insulin secretion. These effects are mediated through the activation of intracellular signaling pathways involving G proteins and second messengers such as cyclic AMP (cAMP).

β2-ARs have been a major focus of drug development for various medical conditions, including asthma, chronic obstructive pulmonary disease (COPD), heart failure, hypertension, and anxiety disorders. Agonists of β2-ARs, such as albuterol and salmeterol, are commonly used to treat asthma and COPD by relaxing bronchial smooth muscle and reducing airway obstruction. Antagonists of β2-ARs, such as propranolol, are used to treat hypertension, angina, and heart failure by blocking the effects of catecholamines on the heart and blood vessels.

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.

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.

The Major Histocompatibility Complex (MHC) is a group of cell surface proteins in vertebrates that play a central role in the adaptive immune system. They are responsible for presenting peptide antigens to T-cells, which helps the immune system distinguish between self and non-self. The MHC is divided into two classes:

1. MHC Class I: These proteins present endogenous (intracellular) peptides to CD8+ T-cells (cytotoxic T-cells). The MHC class I molecule consists of a heavy chain and a light chain, together with an antigenic peptide.

2. MHC Class II: These proteins present exogenous (extracellular) peptides to CD4+ T-cells (helper T-cells). The MHC class II molecule is composed of two heavy chains and two light chains, together with an antigenic peptide.

MHC genes are highly polymorphic, meaning there are many different alleles within a population. This diversity allows for better recognition and presentation of various pathogens, leading to a more robust immune response. The term "histocompatibility" refers to the compatibility between donor and recipient MHC molecules in tissue transplantation. Incompatible MHC molecules can lead to rejection of the transplanted tissue due to an activated immune response against the foreign MHC antigens.

Proteinuria is a medical term that refers to the presence of excess proteins, particularly albumin, in the urine. Under normal circumstances, only small amounts of proteins should be found in the urine because the majority of proteins are too large to pass through the glomeruli, which are the filtering units of the kidneys.

However, when the glomeruli become damaged or diseased, they may allow larger molecules such as proteins to leak into the urine. Persistent proteinuria is often a sign of kidney disease and can indicate damage to the glomeruli. It is usually detected through a routine urinalysis and may be confirmed with further testing.

The severity of proteinuria can vary, and it can be a symptom of various underlying conditions such as diabetes, hypertension, glomerulonephritis, and other kidney diseases. Treatment for proteinuria depends on the underlying cause and may include medications to control blood pressure, manage diabetes, or reduce protein loss in the urine.

Monoclonal antibodies are a type of antibody that are identical because they are produced by a single clone of cells. They are laboratory-produced molecules that act like human antibodies in the immune system. They can be designed to attach to specific proteins found on the surface of cancer cells, making them useful for targeting and treating cancer. Monoclonal antibodies can also be used as a therapy for other diseases, such as autoimmune disorders and inflammatory conditions.

Monoclonal antibodies are produced by fusing a single type of immune cell, called a B cell, with a tumor cell to create a hybrid cell, or hybridoma. This hybrid cell is then able to replicate indefinitely, producing a large number of identical copies of the original antibody. These antibodies can be further modified and engineered to enhance their ability to bind to specific targets, increase their stability, and improve their effectiveness as therapeutic agents.

Monoclonal antibodies have several mechanisms of action in cancer therapy. They can directly kill cancer cells by binding to them and triggering an immune response. They can also block the signals that promote cancer growth and survival. Additionally, monoclonal antibodies can be used to deliver drugs or radiation directly to cancer cells, increasing the effectiveness of these treatments while minimizing their side effects on healthy tissues.

Monoclonal antibodies have become an important tool in modern medicine, with several approved for use in cancer therapy and other diseases. They are continuing to be studied and developed as a promising approach to treating a wide range of medical conditions.

Macromolecular substances, also known as macromolecules, are large, complex molecules made up of repeating subunits called monomers. These substances are formed through polymerization, a process in which many small molecules combine to form a larger one. Macromolecular substances can be naturally occurring, such as proteins, DNA, and carbohydrates, or synthetic, such as plastics and synthetic fibers.

In the context of medicine, macromolecular substances are often used in the development of drugs and medical devices. For example, some drugs are designed to bind to specific macromolecules in the body, such as proteins or DNA, in order to alter their function and produce a therapeutic effect. Additionally, macromolecular substances may be used in the creation of medical implants, such as artificial joints and heart valves, due to their strength and durability.

It is important for healthcare professionals to have an understanding of macromolecular substances and how they function in the body, as this knowledge can inform the development and use of medical treatments.

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.

Histocompatibility antigens, also known as human leukocyte antigens (HLAs), are proteins found on the surface of most cells in the body. They play a critical role in the immune system's ability to differentiate between "self" and "non-self" cells. Histocompatibility antigens are encoded by a group of genes called the major histocompatibility complex (MHC).

There are two main types of histocompatibility antigens: class I and class II. Class I antigens are found on almost all nucleated cells, while class II antigens are primarily expressed on immune cells such as B cells, macrophages, and dendritic cells. These antigens present pieces of proteins (peptides) from both inside and outside the cell to T-cells, a type of white blood cell that plays a central role in the immune response.

When foreign peptides are presented to T-cells by histocompatibility antigens, it triggers an immune response aimed at eliminating the threat. This is why histocompatibility antigens are so important in organ transplantation - if the donor's and recipient's antigens do not match closely enough, the recipient's immune system may recognize the transplanted organ as foreign and attack it.

Understanding the role of histocompatibility antigens has been crucial in developing techniques for matching donors and recipients in organ transplantation, as well as in diagnosing and treating various autoimmune diseases and cancers.

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.

Histocompatibility antigen H-2D is a type of major histocompatibility complex (MHC) class I molecule found in mice. It is a transmembrane protein located on the surface of nucleated cells, which plays a crucial role in the adaptive immune system. The primary function of H-2D is to present endogenous peptide antigens to CD8+ T cells, also known as cytotoxic T lymphocytes (CTLs).

H-2D molecules are encoded by genes within the H-2D region of the MHC on chromosome 17. These genes have multiple alleles, resulting in a high degree of polymorphism, which contributes to the diversity of the immune response among different mouse strains. The peptide-binding groove of H-2D molecules is formed by two alpha helices and eight beta pleats, creating a specific binding site for antigenic peptides.

The peptides presented by H-2D molecules are derived from intracellular proteins that undergo degradation in the proteasome. These peptides are then transported into the endoplasmic reticulum, where they bind to H-2D molecules with the assistance of chaperone proteins like tapasin and calreticulin. The H-2D-peptide complex is then transported to the cell surface for presentation to CD8+ T cells.

Recognition of H-2D-peptide complexes by CD8+ T cells leads to their activation, proliferation, and differentiation into effector CTLs. Activated CTLs can recognize and eliminate virus-infected or malignant cells displaying specific H-2D-peptide complexes, thereby playing a critical role in the cell-mediated immune response.

In summary, histocompatibility antigen H-2D is a polymorphic MHC class I molecule in mice that presents endogenous peptide antigens to CD8+ T cells, contributing significantly to the adaptive immune response and the elimination of infected or malignant cells.

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.

CD29, also known as integrin β1, is a type of cell surface protein called an integrin that forms heterodimers with various α subunits to form different integrin receptors. These integrin receptors play important roles in various biological processes such as cell adhesion, migration, and signaling.

CD29/integrin β1 is widely expressed on many types of cells including leukocytes, endothelial cells, epithelial cells, and fibroblasts. It can bind to several extracellular matrix proteins such as collagen, laminin, and fibronectin, and mediate cell-matrix interactions. CD29/integrin β1 also participates in intracellular signaling pathways that regulate cell survival, proliferation, differentiation, and migration.

CD29/integrin β1 can function as an antigen, which is a molecule capable of inducing an immune response. Antibodies against CD29/integrin β1 have been found in some autoimmune diseases such as rheumatoid arthritis and systemic lupus erythematosus (SLE). These antibodies can contribute to the pathogenesis of these diseases by activating complement, inducing inflammation, and damaging tissues.

Therefore, CD29/integrin β1 is an important molecule in both physiological and pathological processes, and its functions as an antigen have been implicated in some autoimmune disorders.

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.

A biological marker, often referred to as a biomarker, is a measurable indicator that reflects the presence or severity of a disease state, or a response to a therapeutic intervention. Biomarkers can be found in various materials such as blood, tissues, or bodily fluids, and they can take many forms, including molecular, histologic, radiographic, or physiological measurements.

In the context of medical research and clinical practice, biomarkers are used for a variety of purposes, such as:

1. Diagnosis: Biomarkers can help diagnose a disease by indicating the presence or absence of a particular condition. For example, prostate-specific antigen (PSA) is a biomarker used to detect prostate cancer.
2. Monitoring: Biomarkers can be used to monitor the progression or regression of a disease over time. For instance, hemoglobin A1c (HbA1c) levels are monitored in diabetes patients to assess long-term blood glucose control.
3. Predicting: Biomarkers can help predict the likelihood of developing a particular disease or the risk of a negative outcome. For example, the presence of certain genetic mutations can indicate an increased risk for breast cancer.
4. Response to treatment: Biomarkers can be used to evaluate the effectiveness of a specific treatment by measuring changes in the biomarker levels before and after the intervention. This is particularly useful in personalized medicine, where treatments are tailored to individual patients based on their unique biomarker profiles.

It's important to note that for a biomarker to be considered clinically valid and useful, it must undergo rigorous validation through well-designed studies, including demonstrating sensitivity, specificity, reproducibility, and clinical relevance.

Kidney tubules are the structural and functional units of the kidney responsible for reabsorption, secretion, and excretion of various substances. They are part of the nephron, which is the basic unit of the kidney's filtration and reabsorption process.

There are three main types of kidney tubules:

1. Proximal tubule: This is the initial segment of the kidney tubule that receives the filtrate from the glomerulus. It is responsible for reabsorbing approximately 65% of the filtrate, including water, glucose, amino acids, and electrolytes.
2. Loop of Henle: This U-shaped segment of the tubule consists of a thin descending limb, a thin ascending limb, and a thick ascending limb. The loop of Henle helps to concentrate urine by creating an osmotic gradient that allows water to be reabsorbed in the collecting ducts.
3. Distal tubule: This is the final segment of the kidney tubule before it empties into the collecting duct. It is responsible for fine-tuning the concentration of electrolytes and pH balance in the urine by selectively reabsorbing or secreting substances such as sodium, potassium, chloride, and hydrogen ions.

Overall, kidney tubules play a critical role in maintaining fluid and electrolyte balance, regulating acid-base balance, and removing waste products from the body.

Cadmium is a toxic heavy metal that is a byproduct of the mining and smelting of zinc, lead, and copper. It has no taste or smell and can be found in small amounts in air, water, and soil. Cadmium can also be found in some foods, such as kidneys, liver, and shellfish.

Exposure to cadmium can cause a range of health effects, including kidney damage, lung disease, fragile bones, and cancer. Cadmium is classified as a known human carcinogen by the International Agency for Research on Cancer (IARC) and the National Toxicology Program (NTP).

Occupational exposure to cadmium can occur in industries that produce or use cadmium, such as battery manufacturing, metal plating, and pigment production. Workers in these industries may be exposed to cadmium through inhalation of cadmium-containing dusts or fumes, or through skin contact with cadmium-containing materials.

The general population can also be exposed to cadmium through the environment, such as by eating contaminated food or breathing secondhand smoke. Smoking is a major source of cadmium exposure for smokers and those exposed to secondhand smoke.

Prevention measures include reducing occupational exposure to cadmium, controlling emissions from industrial sources, and reducing the use of cadmium in consumer products. Regular monitoring of air, water, and soil for cadmium levels can also help identify potential sources of exposure and prevent health effects.

Beta-1 adrenergic receptors (also known as β1-adrenergic receptors) are a type of G protein-coupled receptor found in the cell membrane. They are activated by the catecholamines, particularly noradrenaline (norepinephrine) and adrenaline (epinephrine), which are released by the sympathetic nervous system as part of the "fight or flight" response.

When a catecholamine binds to a β1-adrenergic receptor, it triggers a series of intracellular signaling events that ultimately lead to an increase in the rate and force of heart contractions, as well as an increase in renin secretion from the kidneys. These effects help to prepare the body for physical activity by increasing blood flow to the muscles and improving the efficiency of the cardiovascular system.

In addition to their role in the regulation of cardiovascular function, β1-adrenergic receptors have been implicated in a variety of physiological processes, including lipolysis (the breakdown of fat), glucose metabolism, and the regulation of mood and cognition.

Dysregulation of β1-adrenergic receptor signaling has been linked to several pathological conditions, including heart failure, hypertension, and anxiety disorders. As a result, β1-adrenergic receptors are an important target for the development of therapeutics used in the treatment of these conditions.

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.

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.

A peptide fragment is a short chain of amino acids that is derived from a larger peptide or protein through various biological or chemical processes. These fragments can result from the natural breakdown of proteins in the body during regular physiological processes, such as digestion, or they can be produced experimentally in a laboratory setting for research or therapeutic purposes.

Peptide fragments are often used in research to map the structure and function of larger peptides and proteins, as well as to study their interactions with other molecules. In some cases, peptide fragments may also have biological activity of their own and can be developed into drugs or diagnostic tools. For example, certain peptide fragments derived from hormones or neurotransmitters may bind to receptors in the body and mimic or block the effects of the full-length molecule.

In the field of medicine, "time factors" refer to the duration of symptoms or time elapsed since the onset of a medical condition, which can have significant implications for diagnosis and treatment. Understanding time factors is crucial in determining the progression of a disease, evaluating the effectiveness of treatments, and making critical decisions regarding patient care.

For example, in stroke management, "time is brain," meaning that rapid intervention within a specific time frame (usually within 4.5 hours) is essential to administering tissue plasminogen activator (tPA), a clot-busting drug that can minimize brain damage and improve patient outcomes. Similarly, in trauma care, the "golden hour" concept emphasizes the importance of providing definitive care within the first 60 minutes after injury to increase survival rates and reduce morbidity.

Time factors also play a role in monitoring the progression of chronic conditions like diabetes or heart disease, where regular follow-ups and assessments help determine appropriate treatment adjustments and prevent complications. In infectious diseases, time factors are crucial for initiating antibiotic therapy and identifying potential outbreaks to control their spread.

Overall, "time factors" encompass the significance of recognizing and acting promptly in various medical scenarios to optimize patient outcomes and provide effective care.

Surface antigens are molecules found on the surface of cells that can be recognized by the immune system as being foreign or different from the host's own cells. Antigens are typically proteins or polysaccharides that are capable of stimulating an immune response, leading to the production of antibodies and activation of immune cells such as T-cells.

Surface antigens are important in the context of infectious diseases because they allow the immune system to identify and target infected cells for destruction. For example, viruses and bacteria often display surface antigens that are distinct from those found on host cells, allowing the immune system to recognize and attack them. In some cases, these surface antigens can also be used as targets for vaccines or other immunotherapies.

In addition to their role in infectious diseases, surface antigens are also important in the context of cancer. Tumor cells often display abnormal surface antigens that differ from those found on normal cells, allowing the immune system to potentially recognize and attack them. However, tumors can also develop mechanisms to evade the immune system, making it difficult to mount an effective response.

Overall, understanding the properties and behavior of surface antigens is crucial for developing effective immunotherapies and vaccines against infectious diseases and cancer.

A "knockout" mouse is a genetically engineered mouse in which one or more genes have been deleted or "knocked out" using molecular biology techniques. This allows researchers to study the function of specific genes and their role in various biological processes, as well as potential associations with human diseases. The mice are generated by introducing targeted DNA modifications into embryonic stem cells, which are then used to create a live animal. Knockout mice have been widely used in biomedical research to investigate gene function, disease mechanisms, and potential therapeutic targets.

'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.

Protein folding is the process by which a protein molecule naturally folds into its three-dimensional structure, following the synthesis of its amino acid chain. This complex process is determined by the sequence and properties of the amino acids, as well as various environmental factors such as temperature, pH, and the presence of molecular chaperones. The final folded conformation of a protein is crucial for its proper function, as it enables the formation of specific interactions between different parts of the molecule, which in turn define its biological activity. Protein misfolding can lead to various diseases, including neurodegenerative disorders such as Alzheimer's and Parkinson's disease.

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.

'Tumor cells, cultured' refers to the process of removing cancerous cells from a tumor and growing them in controlled laboratory conditions. This is typically done by isolating the tumor cells from a patient's tissue sample, then placing them in a nutrient-rich environment that promotes their growth and multiplication.

The resulting cultured tumor cells can be used for various research purposes, including the study of cancer biology, drug development, and toxicity testing. They provide a valuable tool for researchers to better understand the behavior and characteristics of cancer cells outside of the human body, which can lead to the development of more effective cancer treatments.

It is important to note that cultured tumor cells may not always behave exactly the same way as they do in the human body, so findings from cell culture studies must be validated through further research, such as animal models or clinical trials.

Calnexin is a type I transmembrane protein found in the endoplasmic reticulum (ER) of eukaryotic cells. It is a chaperone protein involved in the folding and quality control of newly synthesized glycoproteins. Calnexin binds to monoglucosylated oligosaccharides on unfolded or misfolded proteins, facilitating their correct folding and preventing their aggregation. Once the protein is correctly folded, calnexin dissociates from it and it can proceed through the ER for further processing and transport to its final destination in the cell. Calnexin also plays a role in the degradation of misfolded proteins by targeting them for ER-associated degradation (ERAD).

Kidney disease, also known as nephropathy or renal disease, refers to any functional or structural damage to the kidneys that impairs their ability to filter blood, regulate electrolytes, produce hormones, and maintain fluid balance. This damage can result from a wide range of causes, including diabetes, hypertension, glomerulonephritis, polycystic kidney disease, lupus, infections, drugs, toxins, and congenital or inherited disorders.

Depending on the severity and progression of the kidney damage, kidney diseases can be classified into two main categories: acute kidney injury (AKI) and chronic kidney disease (CKD). AKI is a sudden and often reversible loss of kidney function that occurs over hours to days, while CKD is a progressive and irreversible decline in kidney function that develops over months or years.

Symptoms of kidney diseases may include edema, proteinuria, hematuria, hypertension, electrolyte imbalances, metabolic acidosis, anemia, and decreased urine output. Treatment options depend on the underlying cause and severity of the disease and may include medications, dietary modifications, dialysis, or kidney transplantation.

A kidney, in medical terms, is one of two bean-shaped organs located in the lower back region of the body. They are essential for maintaining homeostasis within the body by performing several crucial functions such as:

1. Regulation of water and electrolyte balance: Kidneys help regulate the amount of water and various electrolytes like sodium, potassium, and calcium in the bloodstream to maintain a stable internal environment.

2. Excretion of waste products: They filter waste products from the blood, including urea (a byproduct of protein metabolism), creatinine (a breakdown product of muscle tissue), and other harmful substances that result from normal cellular functions or external sources like medications and toxins.

3. Endocrine function: Kidneys produce several hormones with important roles in the body, such as erythropoietin (stimulates red blood cell production), renin (regulates blood pressure), and calcitriol (activated form of vitamin D that helps regulate calcium homeostasis).

4. pH balance regulation: Kidneys maintain the proper acid-base balance in the body by excreting either hydrogen ions or bicarbonate ions, depending on whether the blood is too acidic or too alkaline.

5. Blood pressure control: The kidneys play a significant role in regulating blood pressure through the renin-angiotensin-aldosterone system (RAAS), which constricts blood vessels and promotes sodium and water retention to increase blood volume and, consequently, blood pressure.

Anatomically, each kidney is approximately 10-12 cm long, 5-7 cm wide, and 3 cm thick, with a weight of about 120-170 grams. They are surrounded by a protective layer of fat and connected to the urinary system through the renal pelvis, ureters, bladder, and urethra.

Low levels of β2 microglobulin can indicate non-progression of HIV. Levels of β2 microglobulin can be elevated in multiple ... Mice models deficient for the β2 microglobulin gene have been engineered. These mice demonstrate that β2 microglobulin is ... the β2 microglobulin protein is encoded by the B2M gene. β2 microglobulin lies beside the α3 chain on the cell surface. Unlike ... β2 microglobulin (B2M) is a component of MHC class I molecules. MHC class I molecules have α1, α2, and α3 proteins which are ...
Beta-2-microglobulin regulator is a protein in humans that is encoded by the B2MR gene. "Entrez Gene: Beta-2-microglobulin ...
The α chain is encoded by a variant HLA-A gene, and the β chain (β2-microglobulin) is an invariant β2 microglobulin molecule. ... "OMIM Entry - * 109700 - BETA-2-MICROGLOBULIN;B2M". Online Mendelian Inheritance in Man. Johns Hopkins University. 5 Aug 2016. ... The β2 microglobulin protein is encoded by the B2M gene, which is located at chromosome 15q21.1 in humans. MHC Class I ... At this point the class I complex consists of an HLA-A protein bonded to a β2-microglobulin and a short peptide. It is still ...
It can be contrasted to macroglobulin., Examples include: Beta-2 microglobulin Alpha-1-microglobulin "Definition: microglobulin ... Microglobulin is a globulin of relatively small molecular weight. ...
Zijlstra M, Auchincloss H, Loring JM, Chase CM, Russell PS, Jaenisch R (April 1992). "Skin graft rejection by beta 2- ... microglobulin-deficient mice". The Journal of Experimental Medicine. 175 (4): 885-93. doi:10.1136/gut.6.3.225. PMC 1552287. ... 66 (2): 189-203. doi:10.1016/s0016-5085(74)80102-2. PMID 4810912. Onori P, Franchitto A, Sferra R, Vetuschi A, Gaudio E (May ...
Beta-2 microglobulin is elevated in proportion to tumor mass. Coagulation abnormalities may be present. Prothrombin time, ... 109/L B2-microglobulin > 3 mg/L Serum monoclonal protein concentration > 70 g/L The risk categories are: Low: ≤ 1 adverse ... Beta-2 microglobulin and C-reactive protein test results are not specific for Waldenström macroglobulinemia. ... An M component with beta-to-gamma mobility is highly suggestive of Waldenström macroglobulinemia. Immunoelectrophoresis and ...
... the gene for beta-2 microglobulin), and SGK1. Except for the t(14:18)(q32:q21.3) translocation and EZH2 mutations which lead to ... encoding the Ig-beta protein component of the B-cell receptor); 4) gene-inactivating mutations in TNFAIP3, CD58 (encoding the ... high levels of Beta-2 macroglobulin or bone marrow involvement). The combination of lenalidomide with rituximab has shown good ... elevated levels of serum lactose dehydrogenase or beta-2 microglobulin; presence of localized bone lesions; kidney involvement ...
... higher levels of serum lactate dehydrogenase and Beta-2 microglobulin; and c) lower rates of bone but higher rates of soft ... It is the terminal stage and most aggressive form of these dyscrasias, constituting 2% to 4% of all cases of plasma cell ... median survival rates from the time of diagnosis for pPCL and sPCL were 8-11 months and 2-8 months, respectively, even when ...
... each half is made up of the long alpha helix and one beta strand of one partner, and four beta strands of the other partner. ... "Effect of corticosteroid therapy on serum cystatin C and beta2-microglobulin concentrations". Clinical Chemistry. 48 (7): 1123- ... Cystatin C was first described as 'gamma-trace' in 1961 as a trace protein together with other ones (such as beta-trace) in the ... Akbari A, Lepage N, Keely E, Clark HD, Jaffey J, MacKinnon M, Filler G (May 2005). "Cystatin-C and beta trace protein as ...
Ghetie V, Hubbard JG, Kim JK, Tsen MF, Lee Y, Ward ES (March 1996). "Abnormally short serum half-lives of IgG in beta 2- ... Microglobulin is important for cell surface expression and pH-dependent IgG binding of human FcRn". Journal of Cell Science. ... It is an IgG Fc receptor which is similar in structure to the MHC class I molecule and also associates with beta-2- ... microglobulin. In rodents, FcRn was originally identified as the receptor that transports maternal immunoglobulin G (IgG) from ...
... beta-2 microglobulin genes; translocations of the BCL6 and BCL2 genes; and losses of PRDM1 and TNFAIP3 genes. There is an ... low blood platelet counts and/or elevated serum beta-2-microglobulin levels; 4) CLL/SLL cells which develop deletions in the ... Finally, a study of 51 type 2 HL-RT cases showed that the RS cells expressed PAX5 in 100%, CD30 in 100%, CD15 in 92%, CD20 in ... One study found that 53% of 14 type 2 HL-RT cases had, and 47% did not have, antibody-producing gene changes in their RS cells ...
A collagen-binding, I domain-containing, beta(1)-associated integrin alpha-chain present in muscle tissues". J. Biol. Chem. 274 ... Homma N, Gejyo F, Isemura M, Arakawa M (1989). "Collagen-binding affinity of beta-2-microglobulin, a preprotein of hemodialysis ... 249 (2): 204-18. doi:10.1006/dbio.2002.0764. PMID 12221002. "Entrez Gene: EMID2 EMI domain containing 2". Lim J, Hao T, Shaw C ...
... alpha/beta T cells demonstrates preferential use of several V beta genes and an invariant TCR alpha chain". The Journal of ... Like MHC class I, MR1 is found in all a large variety of cells and associates with β2-microglobulin. However, it remains to be ... Yamaguchi H, Hashimoto K (January 2002). "Association of MR1 protein, an MHC class I-related molecule, with beta(2)- ... microglobulin". Biochemical and Biophysical Research Communications. 290 (2): 722-729. doi:10.1006/bbrc.2001.6277. PMID ...
The urinary beta-2 microglobulin test is an indirect method of measuring cadmium exposure. Under some circumstances, the ... Increased concentrations of urinary beta-2 microglobulin can be an early indicator of kidney dysfunction in persons chronically ... 2 (3): 215-229. doi:10.1007/BF03353912. hdl:2115/53361. ISSN 1867-383X. S2CID 1902243. (IARC)International Agency for Research ... 208 (1-2): 123-6. Bibcode:1997ScTEn.208..123T. doi:10.1016/S0048-9697(97)00273-8. PMID 9496656. Boparei. (2010). Kinetics and ...
1994). "Beta 2-microglobulin-independent MHC class Ib molecule expressed by human intestinal epithelium". Science. 265 (5169): ... 1999). "Immunolocalization of CD1d in human intestinal epithelial cells and identification of a beta2-microglobulin-associated ... 54 (2): 122-127. doi:10.1034/j.1399-0039.1999.540202.x. PMID 10488738. CD1d+antigen at the U.S. National Library of Medicine ... 200 (1-2): 149-156. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149. Kawano T, Cui J, Koezuka Y, et al. (1997). "CD1d- ...
Estrogen receptor beta gene (ESR2) seems to be a key to pathogenesis and response to therapy. Other genes that have been ... In addition, the cancer markers used vary with tumor type: choriocarcinomas are monitored with beta-HCG and endodermal sinus ... The OVA1 panel includes CA-125, beta-2 microglobulin, transferrin, apolipoprotein A1, and transthyretin. OVA1 above 5.0 in ... Patients who have spread of the disease to other parts of the body tend to die 2 years after the diagnosis. Extra-ovarian ...
Together with β2-microglobulin (β2m), MHC-I heavy chains form assemblies of heterodimers that act as receptors for antigenic ... Ortmann B, Androlewicz MJ, Cresswell P (April 1994). "MHC class I/beta 2-microglobulin complexes associate with TAP ... In addition to this, β2-microglobulin (β2m) is attached to the heavy chains of the heterodimers and as a whole they act as ... heavy chain and β2 microglobulin). The use of a photo-cleavable high-affinity peptide allowed researchers to form a stable ( ...
Amyloid-forming proteins aggregate into distinctive fibrillar forms with a beta-sheet structure. The beta-sheet form of amyloid ... In beta 2-microglobulin amyloidosis, males have high risk of getting carpal tunnel syndrome. Aβ2MG amyloidosis (Hemodialysis ... beta] cells and is co secreted with insulin." (Rang and Dale's Pharmacology, 2015.)[citation needed] Amyloid proteins deposit ... AL amyloidosis occurs in about 3-13 per million people per year and AA amyloidosis in about 2 per million people per year. The ...
Hallek M, Wanders L, Ostwald M, Busch R, Senekowitsch R, Stern S, Schick HD, Kuhn-Hallek I, Emmerich B (1996). "Serum beta(2)- ... microglobulin and serum thymidine kinase are independent predictors of progression-free survival in chronic lymphocytic ... beta-2 microglobulin, and thymidine kinase". Leukemia & Lymphoma. 18 (1-2): 87-92. doi:10.3109/10428199509064927. PMID 8580834 ...;2-j. PMID 2167141. Korkmaz T, Seber S, Okutur K, Basaran G, Yumuk F, Dane F, Ones T, Polat O, Madenci OC, Demir G, ...
2007). "Melanoma inhibiting activity protein (MIA), beta-2 microglobulin and lactate dehydrogenase (LDH) in metastatic melanoma ... 18 (2): 92-101. doi:10.1111/j.1600-0749.2005.00212.x. PMID 15760338. Aung PP, Oue N, Mitani Y, et al. (2006). "Systematic ... 14 (2): 91-5. doi:10.1097/00008390-200404000-00003. PMID 15057037. S2CID 1429873. Marr DG, Poser I, Shellman YG, et al. (2005 ...
September 1993). "beta 2-Microglobulin modified with advanced glycation end products is a major component of hemodialysis- ... Long-term haemodialysis results in a gradual accumulation of β2 microglobulin, a serum protein, in the blood. It accumulates ... Use of high flux dialyzers Use of Beta 2 globulin absorber Preserve the residual kidney functions Early kidney transplant In ... Destructive spondylarthropathy with b2-microglobulin deposits in a uremic patient before chronic hemodialysis. Nephron 1991; 59 ...
Because beta-2-microglobulin is a large molecule, with a molecular weight of about 11,600 daltons, it does not pass at all ... Beta-2-M is removed with high-flux dialysis, but is removed even more efficiently with IHDF. After several years (usually at ... The goal of high-flux membranes is to pass relatively large molecules such as beta-2-microglobulin (MW 11,600 daltons), but not ... Beta-2-M amyloidosis can cause very serious complications, including spondyloarthropathy, and often is associated with shoulder ...
... unexplained elevations in their blood levels of lactic acid dehydrogenase and beta-2 microglobulin in many cases; malignant ... 30 (1-2): 131-138. doi:10.1016/j.beha.2016.08.029. PMID 28288708. Abuelgasim KA, Rehan H, Alsubaie M, Al Atwi N, Al Balwi M, ... 2 years but also lethal cytokine release syndrome and neurotoxicity responses to this therapy. As a consequence of these ... 30 (1-2): 50-55. doi:10.1016/j.beha.2016.11.001. PMID 28288717. Abramson JS (September 2019). "Hitting back at lymphoma: How do ...
... factor D and beta 2-microglobulin as a measure of glomerular filtration rate". Acta Medica Scandinavica. 218 (5): 499-503. doi: ... 268 (2): 287-294. doi:10.1042/bj2680287. PMC 1131430. PMID 2363674 - via Silverchair. Barrett, A. J.; Davies, M. E.; Grubb, A ... 120 (2): 631-636. doi:10.1016/0006-291x(84)91302-0. PMID 6203523. Björck, Lars; Åkesson, Per; Bohus, Martin; Trojnar, Jerzy; ... 40 (2): 221-226. doi:10.1053/ajkd.2002.34487. PMID 12148093. Ottosson Frost, Carl; Gille-Johnson, Per; Blomstrand, Emanuel; St- ...
Examples of beta globulins include: beta-2 microglobulin plasminogen angiostatins properdin sex hormone-binding globulin ... Beta globulins are a group of globular proteins in plasma that are more mobile in alkaline or electrically charged solutions ... "Examples of Protein Electrophoretograms" at Beta-globulins at the U.S. National Library of Medicine Medical Subject ...
Furthermore, Durie showed it was possible to stratify myeloma patients based on combinations of serum beta 2 microglobulin with ... His research concluded that serum beta 2 microglobulin is the most powerful prognostic factor currently available for multiple ...;2-u. ISSN 0008-543X. PMID 1182674. Durie, B.; Salmon, S. (1975-12-12). "High speed scintillation autoradiography". ...
"The ESAT-6 Protein of Mycobacterium tuberculosis Interacts with Beta-2-Microglobulin (β2M) Affecting Antigen Presentation ...
This class I molecule is a heterodimer consisting of a heavy chain and a light chain (beta-2 microglobulin). The heavy chain is ... 52 (2): 97-103. doi:10.1016/j.patbio.2003.04.006. PMID 15001239. Tolstrup M, Ostergaard L, Laursen AL, Pedersen SF, Duch M ( ... 2 (7): 580-585. doi:10.1093/embo-reports/kve141. PMC 1083955. PMID 11463741. Langat DK, Hunt JS (November 2002). "Do nonhuman ... Exon one encodes the leader peptide, exons 2 and 3 encode the alpha1 and alpha2 domain, which both bind the peptide, exon 4 ...
They use an MHC class I molecule coupled to beta-2 microglobulin to display endogenous peptides on the cell membrane. These ... 162 (2 Pt B): 103-12. doi:10.1016/j.imlet.2014.10.011. PMID 25455596. Hivroz C, Chemin K, Tourret M, Bohineust A (2012). " ... 32 (2): 139-55. doi:10.1615/critrevimmunol.v32.i2.30. PMID 23216612. Barral DC, Brenner MB (December 2007). "CD1 antigen ...
A mouse model with deregulation of beta-catenin levels was created. The conditional stabilizing mutation in the beta-catenin ... there was substantial nuclear localization of beta-catenin as well as increased cytoplasmic beta-catenin. However, in mice fed ... Furthermore, when evaluated for ERCC1, beclin-1, and beta-catenin in the stem cell region of crypts, the colonic tissues of ... Today we know that the beta-catenin protein (part of the Wnt signaling pathway) is implicated in colorectal carcinogenesis and ...
Low levels of β2 microglobulin can indicate non-progression of HIV. Levels of β2 microglobulin can be elevated in multiple ... Mice models deficient for the β2 microglobulin gene have been engineered. These mice demonstrate that β2 microglobulin is ... the β2 microglobulin protein is encoded by the B2M gene. β2 microglobulin lies beside the α3 chain on the cell surface. Unlike ... β2 microglobulin (B2M) is a component of MHC class I molecules. MHC class I molecules have α1, α2, and α3 proteins which are ...
A beta-2 microglobulin (B2M) tumor marker test usually measures the amount of B2M in your blood. It can help find out how ... What is a beta-2 microglobulin tumor marker test?. A beta-2 microglobulin tumor marker test measures the amount of a protein ... A beta-2 microglobulin test usually uses a sample of your blood. In certain cases, you may need to provide a 24-hour urine ... A beta-2 microglobulin tumor marker test is most often used if you have been diagnosed with certain cancers of the bone marrow ...
SSBTP - Beta-trace protein (mg/L). Variable Name: SSBTP. SAS Label: Beta-trace protein (mg/L). English Text: Beta-trace protein ... β2 microglobulin was assayed using the N Latex β2 microglobulin assay, Siemens Diagnostics, IL. ... The effects of freeze-thaw on beta-trace protein and beta2-microglobulin assays after long-term sample storage. Clin Biochem. ... Beta-2 microglobulin (mg/L). English Text: Beta-2 microglobulin (mg/L). Target: Both males and females 12 YEARS - 90 YEARS. ...
Labshub completely concentrates on constant progress and monitoring ensures that we can deliver all assistance at a consistently high-quality level, via our disciplined and automated processes, which is why we are here 24/7 and 365 days for your services. ...
Beta 2 microglobulin is a small membrane protein (11,800 Dalton) associated with the heavy chains of class I major ... Serum beta 2 microglobulin levels are elevated in diseases associated with increased cell turnover. Levels are also elevated in ... Renal failure: Beta-2 microglobulin is cleared by glomerular filtration and the serum concentration increases in parallel with ... The small size allows beta 2 microglobulin to pass through the glomerular membrane, but it is almost completely reabsorbed in ...
Book Beta 2 Microglobulin, Serum Test in Amritsar with NABL-accredited Redcliffe Labs. One-stop destination for various medical ... This test measures beta-2 microglobulin levels, to diagnose certain type of cancers. ...
Beta-2-microglobulin: B. LPEP peptide from EBV, P7A, LPEPLPAGQLTAY: C. SMTL:PDB. SMTL Chain Id:. PDB Chain Id:. A. A ... 1a9b.1 , 1a9b.2 , 1a9e.1 , 1b0g.1 , 1b0g.2 , 1b0r.1 , 1bd2.1 , 1cg9.1 , 1duy.1 , 1duy.2 , 1duz.1 , 1duz.2 , 1eey.1 , 1eey.2 , ... 2° Structure. Bfactor. Bfactor Range. SOA. Entropy. Clustal. Hydrophobic. Size. Charged. Polar. Proline. Ser/Thr. Cysteine. ... 1i1y.1 , 1i1y.2 , 1i4f.1 , 1i7r.1 , 1i7r.2 , 1i7t.1 , 1i7t.2 , 1i7u.1 , 1i7u.2 , 1im3.1 , 1im3.2 , 1im3.3 , 1im3.4 , 1im9.1 , ...
Beta-2-microglobulinHLA class I histocompatibility antigen, A-2 alpha chainLeukocyte immunoglobulin-like receptor subfamily B ...
Beta-pleated sheet structure as observed by x-ray diffraction pattern Apple-green birefringence on Congo red histological sta ... Beta2-microglobulin amyloidosis ( Abeta2M). The precursor protein is a normal beta2 -microglobulin (β2 M), which is the light- ... The amyloid beta precursor protein (AβPP), which is a transmembrane glycoprotein, is the precursor protein in beta protein ... have substantial beta-pleated sheet structure, while extensive beta-sheet structure occurs in all of the deposited fibrils. ...
Glycated albumin, Beta-2 Microglobulin, Cystatin C. Released: June, 2021. Human epididymal secretory protein E4 (HE4) - Serum ( ... Cystatin C, ß-trace Protein ß2 Microglobulin. Released: April, 2012. Inhibin B, Leuteinizing Hormone and Testosterone. Released ... Glycated albumin, Beta-2 Microglobulin, Cystatin C. Released: June, 2021. Autoantibodies - Immunofluorescence Analyses. ... Glycated albumin, Beta-2 Microglobulin, Cystatin C. Released: June, 2021. Autoantibodies - Immunofluorescence Analyses. ...
The beta value at each CpG locus was calculated as the ratio of the intensity of the methylated probe to the sum of intensities ... Finally, beta values after quantile normalization were used to calculate DNA methylation-based aging indices and DNA ... The replicate sample was examined for average correlation of beta values between plates and was found to be greater than 0.99. ... beta-2 microglobulin (B2M), growth differentiation factor 15 (GDF15), Cystatin C (CystatinC), leptin (Leptin), plasminogen ...
Rat TGF-β3 (Transforming Growth Factor Beta 3) CLIA Kit , G-EC-02135 ... Rat α1-MG (α1-Microglobulin) CLIA Kit , G-EC-02157 MSRP: Was: ... Rat BMG/β2-MG (Beta-2-Microglobulin) CLIA Kit , G-EC-02159 ... Rat TGF-β2 (Transforming Growth Factor Beta 2) CLIA Kit , G-EC-02134 ... Rat VEGFR-2/KDR (Vascuoar Endothelial Growth Factor Receptor 2) CLIA Kit , G-EC-02150 ...
lysozyme; beta-2-microglobulin (beta 2 microglobulin); tumor necrosis factor (TNF), also known as tumor necrosis factor alpha ( ... 95% Air, 5% CO2. Handling procedure. To insure the highest level of viability, thaw the vial and initiate the culture as soon ... A 5% CO2 in air atmosphere is recommended if using the medium described on this product sheet. ... Thawing should be rapid (approximately 2 minutes).. *Remove the vial from the water bath as soon as the contents are thawed, ...
Compound: Beta-2-microglobulin. Species: Homo sapiens [TaxId:9606]. Database cross-references and differences (RAF-indexed): * ...
Values for blood Cd, urinary Cd, blood urea nitrogen, and urinary beta 2 microglobulin suggested significant Cd absorption and ...
Solution structure of beta(2)-microglobulin and insights into fibrillogenesis. Esposito G, Corazza A, Viglino P, Verdone G, ... microglobulin: a challenge for protein biophysics. Esposito G, Corazza A, Bellotti V. Esposito G, et al. Subcell Biochem. 2012; ... 2012 Jan 6;2:93. doi: 10.3389/fimmu.2011.00093. eCollection 2011. Front Immunol. 2012. PMID: 22566882 Free PMC article. ...
... beta 2-microglobulin; and 3) maternally transmitted factor (Mtf), the N-terminus of the mitochondrially encoded ND1 subunit of ...
Beta-2-microglobulin. 2.55e-20. EFEMP1. EGF containing fibulin extracellular matrix protein 1. 8.06e-20. ... Daniel Palmer1,3, *, , Fabio Fabris2, *, , Aoife Doherty1, , Alex A. Freitas2, , João Pedro de Magalhães1, , * 1 Integrative ... Figure 2. Overlap of the global and tissue-specific results of this meta-analysis. (A) Gives the overlap for genes ... Creatine kinase, mitochondrial 2. 9.30e-7. The value given between brackets in the p-value column header is the p-value ...
18.2 percent; p,0.001) and urine beta-2 microglobulin-to-creatinine ratio (-39.6 percent vs. +22.0 percent; p,0.001). There ... The data were presented in an oral session (Session O-2) at the 2016 Conference on Retroviruses and Opportunistic Infections ( ...
Stage I: Serum beta-2 microglobulin , 3.5 mg/L and serum albumin ≥3.5 g/dL ... Renal insufficiency: creatinine clearance , 40 mL per min or serum creatinine , 177 μmol/L (, 2 mg/dL) ...
However, it is not linked to any beta-2-microglobulin. Additionally, it interacts with viral glycoprotein (UL16) to offer CMV ... Therefore, its general structure is made up of the alpha-1 and alpha-2 domains connected to the cell membrane through the GPI ...
APP / Beta Amyloid Precursor (322) B2M / Beta 2 Microglobulin (313) BAD (361) ... 10 µg/$262; 50 µg/$339; 100 µg/$512; 200 µg/$642; 1 mg/$1,623; 500 µg/$1,214; 5 mg/$2,562; 2 mg/$1,796 ...
Dialysis doesnt remove enough of a protein called beta-2 microglobulin from the blood. Over time, this protein can build up ... 2] Quock TP, Yan T, Chang E, Guthrie S, Broder MS. Epidemiology of AL amyloidosis: a real-world study using US claims data. ... 2018;2(10):1046-1053. doi:10.1182/bloodadvances.2018016402. [3] Scarpioni R, Ricardi M, Albertazzi V, De Amicis S, Rastelli F, ... Immunoglobulin light-chain amyloidosis (AL amyloidosis), or primary amyloidosis, affects the kidneys in about 2 out of 3 people ...
At present, other surrogate markers of HIV infection (e.g., serum neopterin, beta-2-microglobulin, p24 antigen) are not helpful ... Studies are also needed to determine the usefulness of repeating anergy tests (e.g., 2- step testing as is suggested for ... 2). Among antigens routinely used in Army medical centers, mumps produced more positive reactions than Candida or tetanus ... generally defined as a reaction of greater than or equal to 2 mm of induration). There have been no comprehensive studies ...
The soluble extracellular beta-2 microglobulin chain associates primarily with the alpha-3 domain and is necessary for MHC ... MHC class I molecules are comprised of two chains: a MHC alpha chain (heavy chain), and a beta2-microglobulin chain (light ... NK cell ligand RAE-1 [ (PUBMED:12594837) ]. RAE-1 proteins (alpha, beta, delta, and gamma) are distant major histocompatibility ... MHC class I, alpha-1 and alpha-2 domains [ (PUBMED:15454423) ] * MHC class I homologue gammadelta T-cell ligand [ (PUBMED: ...
Decreased CD4-CD8- TCR-alpha beta + cells in lpr/lpr mice lacking beta 2-microglobulin. J. Immunol. ... Decreased CD4-CD8- TCR-alpha beta + cells in lpr/lpr mice lacking beta 2-microglobulin. J. Immunol. ... A role for MEK kinase 1 in TGF-{beta}/activin-induced epithelium movement and embryonic eyelid closure. EMBO J. ... A role for MEK kinase 1 in TGF-{beta}/activin-induced epithelium movement and embryonic eyelid closure. EMBO J. ...
proteasome 20S subunit beta 2 [Source:H.... PSMB4. 5692. PSMB4. proteasome 20S subunit beta 4 [Source:H.... ...
  • Renal failure: Beta-2 microglobulin is cleared by glomerular filtration and the serum concentration increases in parallel with serum creatinine in renal failure. (
  • Ninety percent of beta 2 microglobulin is eliminated via glomerular filtration and almost completely reabsorbed by the proximal tubules. (
  • In humans, the β2 microglobulin protein is encoded by the B2M gene. (
  • In a cytomegalovirus infection, a viral protein binds to β2 microglobulin, preventing assembly of MHC class I molecules and their transport to the plasma membrane. (
  • Levels of β2 microglobulin can be elevated in multiple myeloma and lymphoma, though in these cases primary amyloidosis (amyloid light chain) and secondary amyloidosis (amyloid associated protein) are more common. (
  • A beta-2 microglobulin tumor marker test measures the amount of a protein called beta-2 microglobulin (B2M) in your body fluids. (
  • Juraschek SP, Coresh J, Inker LA, Rynders GP, Eckfeldt JH, Selvin E. The effects of freeze-thaw on beta-trace protein and beta2-microglobulin assays after long-term sample storage. (
  • Beta 2 microglobulin is a small membrane protein (11,800 Dalton) associated with the heavy chains of class I major histocompatibility complex proteins and is, therefore on the surface of all nucleated cells. (
  • Pathological self-aggregation of β(2)-microglobulin: a challenge for protein biophysics. (
  • AE binding protein 2 [Source:HGNC Symbo. (
  • actin related protein 2/3 complex subun. (
  • This light-protein chain, which can be shed into serum, is called beta 2 microglobulin. (
  • Beta 2 microglobulin is an 11.8-kD protein (see first image below), which forms one of the chains of the major histocompatibility complex (MHC) class I molecule normally present on the surface of every nucleated cell in the human body. (
  • What is a beta-2 microglobulin tumor marker test? (
  • A beta-2 microglobulin tumor marker test can't diagnose cancer or any other condition. (
  • A beta-2 microglobulin tumor marker test is most often used if you have been diagnosed with certain cancers of the bone marrow or blood. (
  • Why do I need a beta-2 microglobulin tumor marker test? (
  • Serum and plasma beta 2 microglobulin values have emerged as markers for the activation of the cellular immune system, as well as a tumor marker in certain hematologic malignancies. (
  • MHC class I molecules are comprised of two chains: a MHC alpha chain (heavy chain), and a beta2-microglobulin chain (light chain), where only the alpha chain spans the membrane. (
  • HLA-class I major histocompatibility (MHC) antigens are intrinsic membrane glycoproteins expressed on nucleated cells and noncovalently associated with an invariant beta2 microglobulin. (
  • Crystal structure of beta2 microglobulin. (
  • [1] , [2] Bruton's tyrosine kinase (BTK) and B-cell lymphoma 2 (BCL-2) inhibitors have offered impressive improvements in overall survival and life expectancy and are better tolerated than CIT options. (
  • Low serum levels of beta 2 microglobulin essentially indicate decreased disease activity in conditions for which beta 2 microglobulin is used as a prognostic marker ( multiple myeloma , lymphoma, leukemia ) or the absence of such a disease process. (
  • However, low beta 2 microglobulin levels are never used to rule out a particular disease (eg, lymphoma) in the absence of other more definitive tests. (
  • Beta 2 microglobulin is a component of certain panels, such as chronic lymphocytic leukemia (CLL), lymphoma, or multiple myeloma prognostic/monitoring panels. (
  • Urine beta 2 microglobulin values indicate renal filtration disorders. (
  • The reference range of beta 2 microglobulin in urine samples is 0-0.3 µg/mL. (
  • Increased urine beta 2 microglobulin levels reflect tubular disorders of the kidney. (
  • Beta 2 microglobulin can be determined in urine, serum, or plasma samples. (
  • Thus, in individuals with chronic kidney disease, particularly end-stage renal disease, beta 2 microglobulin can accumulate in the blood. (
  • The cer is about 2%-5% and as high as 26% in most common complications include renal small-cell lung carcinoma [ 5 ]. (
  • Consequently, dermatologic manifestations of renal disease may be divided into 3 general categories including: (1) dermatologic manifestations of diseases associated with the development of ESRD, (2) dermatologic manifestations of uremia, and (3) dermatologic disorders associated with renal transplantation. (
  • Nevertheless, the β2 microglobulin gene is outside of the MHC (HLA) locus, on a different chromosome. (
  • Mice models deficient for the β2 microglobulin gene have been engineered. (
  • The human beta 2-microglobulin gene. (
  • One must consider the two types of genes involved in thalassemia to understand the inheritance pattern: the alpha-globin gene and the beta-globin gene. (
  • Each person inherits two copies of the alpha globin gene (one from each parent) and two copies of the beta-globin gene (one from each parent) for four copies. (
  • Individuals who inherit one normal copy of the beta-globin gene and one mutated copy become carriers of thalassemia minor. (
  • Carriers typically do not exhibit severe symptoms of the condition, as the presence of the normal gene compensates for the reduced production of beta-globin chains. (
  • This means the child will have two mutated copies of the beta-globin gene and be a thalassemia minor carrier. (
  • There is a 50% chance for the child to inherit one normal copy of the beta-globin gene from one parent and one mutated copy from the other parent, resulting in the child becoming a carrier of thalassemia minor like their parents. (
  • Lastly, there is a 25% chance for the child to inherit two normal copies of the beta-globin gene, meaning they will not have thalassemia minor or be carriers of the condition. (
  • β2 microglobulin lies beside the α3 chain on the cell surface. (
  • β2 microglobulin associates not only with the alpha chain of MHC class I molecules, but also with class I-like molecules such as CD1 (5 genes in humans), MR1, the neonatal Fc receptor (FcRn), and Qa-1 (a form of alloantigen). (
  • Immunoglobulin light-chain amyloidosis (AL amyloidosis), or primary amyloidosis, affects the kidneys in about 2 out of 3 people with this condition. (
  • The soluble extracellular beta-2 microglobulin chain associates primarily with the alpha-3 domain and is necessary for MHC stability. (
  • By studying around 28 prognostic variables among roughly 3,400 patients treated in clinical trials, the CLL-IPI revealed the five factors associated with overall survival were: age, Rai stage I-IV, serum beta-2 microglobulin, unmutated immunoglobulin heavy chain variable region (IGHV) genes, and del17p by fluorescence in situ hybridization (FISH) or TP53 mutation. (
  • In vitro, the synthesis and release of beta 2 microglobulin can be induced by acidosis, endotoxin, or inflammatory cytokines. (
  • fects are so similar that these 2 cytokines are almost interchangeable [ 6 ]. (
  • The small size allows beta 2 microglobulin to pass through the glomerular membrane, but it is almost completely reabsorbed in the proximal tubules. (
  • Diagnostic testing for multiple myeloma includes obtaining the β2 microglobulin level, for this level is an important prognostic indicator. (
  • citation needed] β2 microglobulin has been shown to be of high relevance for viral entry of Coxsackievirus A9 and Vaccinia virus (a Poxvirus). (
  • Serum interleukin (IL)-1, IL-6, tumour necrosis factor (TNF) and quantitative urinary -2-microglobulin (-2-m) excretion were estimated. (
  • On a estimé l'interleukine 1, l'interleukine 6, la cachectine (TNF) et l'excrétion quantitative de 2-microglobuline urinaire. (
  • Processing of the lipocalin alpha(1)-microglobulin by hemoglobin induces heme-binding and heme-degradation properties. (
  • In fact, in the absence of β2 microglobulin, very limited amounts of MHC class I (classical and non-classical) molecules can be detected on the surface (bare lymphocyte syndrome or BLS). (
  • Values for blood Cd, urinary Cd, blood urea nitrogen, and urinary beta 2 microglobulin suggested significant Cd absorption and related kidney damage in workers with heavy Cd exposure. (
  • About 95% of free -2-m is filtered by the branous and proliferative being the most normal glomerulus and a normal kidney is common [ 2 ]. (
  • Serum beta 2 microglobulin levels are elevated in diseases associated with increased cell turnover. (
  • [ 2 ] Many classic eponymic diseases were later found to be related to a diverse array of misfolded polypeptides (amyloid) that contain the common beta-pleated sheet architecture. (
  • β2 microglobulin levels cannot, however, distinguish between monoclonal gammopathy of undetermined significance (MGUS), which has a better prognosis, and smouldering (low grade) myeloma. (
  • This test measures beta-2 microglobulin levels, to diagnose certain type of cancers. (
  • Increased serum beta 2 microglobulin levels reflect increased activity of the disease process in question and can be an exquisitely sensitive marker for this purpose in many hematologic disorders. (
  • In such cases, serum beta 2 microglobulin levels are usually normal, since the dysfunction is in tubular reabsorption. (
  • Increased CSF beta 2 microglobulin levels are seen in certain conditions such as multiple sclerosis, AIDS dementia complex , and meningeal spread of hematologic tumors. (
  • In minor thalassemia anaemia, the mutation affects one of the beta-globin genes. (
  • Serum beta 2 microglobulin has now been identified as an important prognostic marker in a large number of hematologic and nonhematologic disorders. (
  • Serum TNF concentration and urinary -2-m excretion were significantly higher in the first presentation and relapse groups. (
  • minimal change nephrotic reabsorption and increased urinary excre- syndrome is most common in children 2-4 tion of -2-m [ 11 ]. (
  • β2 microglobulin (B2M) is a component of MHC class I molecules. (
  • For Coxsackievirus A9, it is likely that β2 microglobulin is required for the transport to plasma membrane of the identified receptor, the Human Neonatal Fc Receptor (FcRn). (
  • found in human fecal samples in low percentages ( 2 - 7 ). (
  • Description: The W6/32 monoclonal antibody reacts with the human major histocompatibility complex (MHC) class I, HLA-A, B, C. MHC class I antigens associated with beta 2-microglobulin are expressed by all human nucleated cells and are central in cell-mediated immune response and tumor surveillance. (
  • A beta-2 microglobulin test usually uses a sample of your blood. (
  • Individuals with thalassemia minor have decreased beta globin chains, which can lead to mild anaemia. (
  • clarification needed] The normal value of β2 microglobulin is (
  • These mutations lead to reduced synthesis of normal haemoglobin, resulting in an imbalance of the alpha and beta globin chains. (
  • These mice demonstrate that β2 microglobulin is necessary for cell surface expression of MHC class I and stability of the peptide-binding groove. (
  • Therefore, its general structure is made up of the alpha-1 and alpha-2 domains connected to the cell membrane through the GPI anchor. (
  • La concentration sérique de TNF et l'excrétion de 2-micro- globuline urinaire étaient significativement plus élevées dans les groupes de première manifestation et de ré- cidive. (
  • METHODS: We used electronic health records for asthma patients aged 2-17 years from a regional, urban, children's hospital in Ohio during 2011-2015. (
  • Leukocyte cell-derived chemotaxin 2 (LECT2) amyloidosis is a recently discovered form of amyloidosis that most often affects the kidneys and liver. (
  • 2 The other types of amyloidosis are even less common. (
  • The entire review process can range from 2-6 months. (
  • Les enfants présentant un syndrome néphrotique idiopathique ont été répartis en trois groupes de 20 : première manifestation, rémission et récidive. (
  • The synthesis rate of beta 2 microglobulin varies from 2-4 mg/kg/day, with a half-life of 2.5 hours. (
  • Bufaviruses are gastroenteritis, and in only 0.27%-4% of samples ( 2 - 8 ). (
  • Samples may be stored refrigerated at 2-8°C for 5 days. (