Did you mean: beta microglobulin
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Scandinavian Journal of Clinical and... 1980In the sixties, Ingemar Berggård discovered, isolated and characterized the low molecular weight protein beta 2-microglobulin. The relations of beta 2-microglobulin to... (Review)
Review
In the sixties, Ingemar Berggård discovered, isolated and characterized the low molecular weight protein beta 2-microglobulin. The relations of beta 2-microglobulin to the immune system have led to intensive research on this protein. The present work reviews the purification and characterization of human beta 2-microglobulin and animal homologues, the association of beta 2-microglobulin to other molecules, the functional studies with beta 2-microglobulin and antibodies against beta 2-microglobulin, and the evolutionary studies on beta 2-microglobulin.
Topics: Animals; Beta-Globulins; Biological Evolution; Body Fluids; Chemical Phenomena; Chemistry, Physical; Cytotoxicity, Immunologic; Guinea Pigs; Humans; Immunity, Cellular; Immunoglobulin Fc Fragments; Lymphocyte Activation; Major Histocompatibility Complex; Rabbits; Rats; Tissue Distribution; beta 2-Microglobulin
PubMed: 6163192
DOI: No ID Found -
Amyloid : the International Journal of... 2009beta(2)-microglobulin (beta(2)m) is capable of forming amyloid in osteoarticular structures in kidney failure patients that undergo chronic hemodialysis treatment.... (Review)
Review
beta(2)-microglobulin (beta(2)m) is capable of forming amyloid in osteoarticular structures in kidney failure patients that undergo chronic hemodialysis treatment. Although sophisticated analytical methods have yielded comprehensive data about the conformation of the native protein both as a monomer and as the light chain of the type I major histocompatibility complex, the cause and mechanisms leading to the transformation of beta(2)m into amyloid deposits in patients with dialysis-related amyloidosis are unsettled. The impact on conformational stability of various truncations, cleavages, amino acid substitutions, and divalent cations, especially Cu(2+), however, are highly relevant for understanding beta(2)m unfolding pathways leading to amyloid formation. This review describes the current knowledge about such conformationally destabilizing and amyloidogenic factors and links these to the structure and function of beta(2)m in normal physiology and pathology. Tables listing modifications of beta(2)m found in amyloid from patients and a systematic overview of laboratory conditions conducive to beta(2)m-fibrillogenesis are also included.
Topics: Amino Acid Sequence; Amyloid; Amyloidosis; Humans; Hydrogen-Ion Concentration; Models, Molecular; Molecular Sequence Data; Point Mutation; Protein Denaturation; Protein Folding; Protein Processing, Post-Translational; Protein Structure, Tertiary; Renal Dialysis; beta 2-Microglobulin
PubMed: 19657763
DOI: 10.1080/13506120903151775 -
Journal of Dairy Science Feb 1982beta 2-Microglobulin has been isolated from several species, but only bovine beta 2-microglobulin, previously known as lactollin, has been crystallized. An improved... (Comparative Study)
Comparative Study Review
beta 2-Microglobulin has been isolated from several species, but only bovine beta 2-microglobulin, previously known as lactollin, has been crystallized. An improved method for its isolation from colostrum is described. The bovine homologue exhibits a concentration-dependent aggregation behavior. beta 2-Microglobulin is related to both immune and histocompatibility antigen systems. It exhibits homology with the constant domains of the immunoglobulin-G light and heavy chains and is an integral part of histocompatibility antigens bound to cell surface. beta 2-Microglobulin also occurs in the free state in various body fluids including milk and colostrum. The possible relationship of elevated free beta 2-microglobulin of pathological conditions is suggested for future research.
Topics: Amino Acid Sequence; Animals; Beta-Globulins; Cattle; Colostrum; HLA Antigens; Histocompatibility Antigens; Humans; Milk; beta 2-Microglobulin
PubMed: 6176605
DOI: 10.3168/jds.S0022-0302(82)82193-0 -
CRC Critical Reviews in Clinical... 1979beta 2-Microglobulin is a low molecular weight protein that is found in most biological fluids. It was originally isolated from urine of cadmium-poisoned patients. Its... (Review)
Review
beta 2-Microglobulin is a low molecular weight protein that is found in most biological fluids. It was originally isolated from urine of cadmium-poisoned patients. Its amino acid sequence was established and shown to be structurally related to immunoglobulin constant domains. With the aid of antibodies specific against beta 2-microglobulin, the protein was detected on the membranes of all nucleated cells, normal and neoplastic. Measuring the quantity of beta 2-microglobulin showed that high levels are present in patients with renal tubular deficiencies and several other pathological conditions including neoplastic diseases. Extremely high levels were detected in seminal fluid and colostrum. Despite the structural relationship to immunoglobulins, no immunological relationship was demonstrated with these proteins using antibodies specific for beta 2-microglobulin. However, such antibodies are cytotoxic to all cells carrying beta 2-microglobulin on their surfaces. The discovery that beta 2-microglobulin is an integral part of the histocompatibility antigens of human and murine origin stimulated further research and interest in this molecule. Several groups of investigators have shown that beta 2-microglobulin is the low molecular weight chain and is noncovalently bound to a high molecular weight chain which carries the histocompatibility antigens. The structure of the histocompatibility antigens of lymphocytes (HLA) was shown by immunochemical as well as biological methods, and it is now well accepted. The antibodies against beta 2-microglobulin are extremely useful in the isolation of the histocompatibility antigens for sequence studies. Furthermore, the antibody to beta 2-microglobulin revealed that other structures may be bound to beta 2-microglobulin such as phytohemoagglutimin (PHA) receptors, mixed lymphocyte culture (MLC) antigens, etc. Murine thymus leukemia (TL) antigen also contains beta 2-microglobulin as an integral part of its structure; other tumor antigens may have a similar structure. Through all these studies, beta 2-microglobulin emerged as the best known membrane protein that can serve as a model for study of the arrangement and the function of the cell membrane.
Topics: Amino Acid Sequence; Beta-Globulins; Chromatography, Ion Exchange; Electrophoresis, Starch Gel; Histocompatibility Antigens; Humans; Immunoelectrophoresis; Kidney Diseases; Kidney Transplantation; Male; Membrane Proteins; Receptors, Drug; Semen; Transplantation, Homologous; beta 2-Microglobulin
PubMed: 89022
DOI: 10.3109/10408367909147135 -
Vox Sanguinis Jun 1980beta 2-Microglobulin is a low molecular weight protein with sequence homology to immunoglobulins. As a portion of the HLA complex this protein is an important... (Review)
Review
beta 2-Microglobulin is a low molecular weight protein with sequence homology to immunoglobulins. As a portion of the HLA complex this protein is an important cell-surface structure. Under normal conditions beta 2-microglobulin is synthesized and shed by many cells, particularly lymphocytes, and is detectable in the circulation of normal individuals. Because of its small size it is normally filtered readily at the glomerulus and is catabolized by proximal tubular cells of the kidney. Impaired renal function and hyperproduction of beta 2-microglobulin are both associated with increased serum levels. A function for beta 2-microglobulin as a modulator of lymphocyte surface and as a potential regulator of the immune system is proposed.
Topics: Amino Acid Sequence; Beta-Globulins; Humans; Kidney; Lymphocytes; Receptors, Fc; T-Lymphocytes, Regulatory; beta 2-Microglobulin
PubMed: 6159720
DOI: 10.1111/j.1423-0410.1980.tb04500.x -
Ultrastructural Pathology 1994beta 2 microglobulin is a potentially amyloidogenic low molecular weight protein. Increased serum levels are seen in renal diseases that decrease glomerular filtration... (Review)
Review
beta 2 microglobulin is a potentially amyloidogenic low molecular weight protein. Increased serum levels are seen in renal diseases that decrease glomerular filtration and/or tubular reabsorption, dialysis patients, chronic inflammatory diseases, and certain malignancies. Various aspects of beta 2 microglobulin metabolism and its accumulation in the kidney are addressed.
Topics: Humans; Kidney; Kidney Diseases; beta 2-Microglobulin
PubMed: 8191651
DOI: 10.3109/01913129409016278 -
Seminars in Dialysis 2001Renal osteodystrophy is the major cause of skeletal morbidity in dialysis patients. It is characterized by beta(2)-microglobulin (beta(2)M) amyloid deposition at the... (Review)
Review
Renal osteodystrophy is the major cause of skeletal morbidity in dialysis patients. It is characterized by beta(2)-microglobulin (beta(2)M) amyloid deposition at the osteoarticular sites and a destructive arthropathy. beta(2)M is present on the surface of all nucleated cells as the small extracellular subunit of the major histocompatibility complex (MHC) class I molecule and actively participates in the immune response. Accumulating evidence suggests that beta(2)M plays a key role in the development of renal osteodystrophy through a T cell-mediated inflammatory immune mechanism.
Topics: Animals; Bone and Bones; Chronic Kidney Disease-Mineral and Bone Disorder; Cytokines; Humans; Immunity, Cellular; T-Lymphocytes; beta 2-Microglobulin
PubMed: 11264778
DOI: 10.1046/j.1525-139x.2001.00029.x -
Transplantation Aug 1995
Comparative Study Review
Topics: Animals; Humans; Transplantation Immunology; beta 2-Microglobulin
PubMed: 7645032
DOI: 10.1097/00007890-199508000-00001 -
Biochimica Et Biophysica Acta Nov 2005The solution structure of human beta(2)-microglobulin (beta(2)-m) was determined by (1)H NMR spectroscopy and restrained modeling calculations. Compared to the crystal... (Review)
Review
The solution structure of human beta(2)-microglobulin (beta(2)-m) was determined by (1)H NMR spectroscopy and restrained modeling calculations. Compared to the crystal structure of type I major histocompatibility complex (MHC-I), where the protein is associated to the heavy-chain component, several differences are observed, i.e., increased separation between strands A and B, displacements of strand C' and loop DE, shortening of strands D and E. These modifications can be considered as the prodromes of the amyloid transition. Even minor charge changes in response to pH, as is the case with H31 imidazole protonation, trigger the transition that starts with unpairing of strand A. The same mechanism accounts for the partial unfolding and fiber formation subsequent to Cu(2+) binding which is shown to occur primarily at H31. Solvation of the protected regions in MHC-I decreases the tertiary packing by breaking the contiguity of the surface hydrophobic patches via surface charge cluster. Mutants or truncated forms of beta(2)-m can be designed to remove the instability from H31 titration or to enhance the instability through surface charge suppression. By monitoring the conformational evolution of wild-type protein and variants thereof, either in response or absence of external perturbation, valuable insights into intermediate structure and fibrillogenesis mechanisms are gained.
Topics: Amyloid; Crystallography, X-Ray; Drug Stability; Evolution, Molecular; Humans; Models, Molecular; Mutation; Nuclear Magnetic Resonance, Biomolecular; Protein Conformation; Solutions; Thermodynamics; beta 2-Microglobulin
PubMed: 16081329
DOI: 10.1016/j.bbapap.2005.07.003 -
La Nouvelle Presse Medicale Nov 1976
Review
Topics: Amniotic Fluid; Beta-Globulins; Binding Sites, Antibody; Binding, Competitive; Cell Membrane; Cells, Cultured; Glomerular Filtration Rate; HLA Antigens; Humans; Kidney Concentrating Ability; Kidney Diseases; Kidney Tubules, Proximal; Lymphocytes; Protein Conformation; Proteinuria; beta 2-Microglobulin
PubMed: 63940
DOI: No ID Found