β-2-Microglobulin (B2M) is a secreted protein with 1 Ig-like C1-type (immunoglobulin-like) domain which belongs to the beta-2-microglobulin family. B2M component of major histocompatibility complex (MHC) class I molecules; involved in the presentation of peptide antigens to the immune system. Polymers of beta 2-microglobulin can be found in tissues from patients on long-term hemodialysis. B2M is a protein found on the surface of many cells and plentiful on the surface of white blood cells. Serum B2M concentration is increased in renal diseases; various malignant diseases and some inflammatory and autoimmune disorders. B2M may adopt the fibrillar configuration of amyloid in certain pathologic states. The capacity to assemble into amyloid fibrils is concentration dependent. B2M has been shown as a marker for monitoring inflammatory disease activity and it appears likely to have a destructive role in amyloidosis-related arthritis. B2M might be involved in the OA (osteoarthritis) pathogenesis. Defects in B2M are the cause of hypercatabolic hypoproteinemia. Affected individuals show marked reduction in serum concentrations of immunoglobulin and albumin; probably due to rapid degradation. B2M could be a potential therapeutic target in ovarian cancer.
B2M, also known as β2-Microglobulin or CDABP0092, is a component of MHC class I molecules found expression in all nucleated cells (excludes red blood cells). The major function of MHC class I moleculesis is to display fragments of proteins from within the cell to T-cells and cells containing foreign proteins will be attacked. B2M(β2-Microglobulin) is a low molecular weight protein. It was demonstrated that B2M(β2-Microglobulin) was localized in the membranes of nucleated cells and was found to be associated with HL-A antigens.B2M(β2- Microglobulin) is present in free form in various body fluids and as a subunit of histocompatibility antigens on cell surfaces lateral to theα3 chain. Unlikeα3, β2 has no transmembrane region. Directly above β2 lies the α1 chain, which itself is lateral to the α2. In the absence of B2M(β2 microglobulin), very limited amounts of MHC class I (classical and non-classical) molecules can be detected on the surface. In the absence of MHC class I, CD8 T cells, a subset of T cells involved in the development of acquired immunity cannot develop. Low levels of B2M(β2 microglobulin) can indicate non-progression of HIV.
Amylases are secreted proteins that hydrolyze 1;4-alpha-glucoside bonds in oligosaccharides and polysaccharides; and thus catalyze the first step in digestion of dietary starch and glycogen. Alpha-amylase is the major form of amylase found in humans and other mammals. Alpha-amylase hydrolyses alpha bonds of large; alpha-linked polysaccharides; such as starch and glycogen; yielding glucose and maltose. Amylases is widely expressed and is most prominent in pancreatic juice and saliva; each of which has its own isoform of human α-amylase. They behave differently on isoelectric focusing; and can also be separated in testing by using specific monoclonal antibodies.
Alpha-amylase 2B is an enzyme that in humans is encoded by the AMY2B gene. Alpha-amylase 2B is a secreted protein and belongs to the glycosyl hydrolase 13 family. It hydrolyzes 1,4-alpha-glucoside bonds in oligosaccharides and polysaccharides, and thus catalyze the first step in digestion of dietary starch and glycogen. The human genome has a cluster of several amylase genes that are expressed at high levels in either salivary gland or pancreas. This gene encodes an amylase isoenzyme produced by the pancreas. Diseases associated with AMY2B include pancreatitis, and thyroiditis, and among its related super-pathways are Metabolic pathways and MPS IIIC - Sanfilippo syndrome C.
Amyloid precursor protein (APP) is a type I transmembrane protein expressed in many tissues and concentrated in the synapses of neurons, and is suggested as a regulator of synapse formation and neural plasticity. APP can be processed by two different proteolytic pathways. In one pathway, APP is cleaved by β- and γ-secretase to produce the amyloid-β-protein (Aβ, Abeta, beta-amyloid) which is the principal component of the amyloid plaques, the major pathological hallmark of Alzheimer’s disease (AD), while in the other pathway, α-secretase is involved in the cleavage of APP whose product exerts antiamyloidogenic effect and prevention of the Aβ peptide formation. The aberrant accumulation of aggregated beta-amyloid peptides (Abeta) as plaques is a hallmark of AD neuropathology and reduction of Abeta has become a leading direction of emerging experimental therapies for the disease. Abeta may be part of a mechanism controlling synaptic activity, acting as a positive regulator presynaptically and a negative regulator postsynaptically. The pathological accumulation of oligomeric Abeta assemblies depresses excitatory transmission at the synaptic level, but also triggers aberrant patterns of neuronal circuit activity and epileptiform discharges at the network level. There is evidence that beta-amyloid can impair blood vessel function. Vascular beta-amyloid deposition, also known as cerebral amyloid angiopathy, is associated with vascular dysfunction in animal and human studies.
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