BIML is one of several splice variants of BIM, a proapoptotic protein belonging to the BH-3 domain-only subgroup of Bcl-2 family members. BCL-2 family members form hetero-or homodimers and act as anti-or pro-apoptotic regulators that are involved in a wide variety of cellular activities. BIML is thought to promote apoptosis by binding and inhibiting the activity of anti-apoptotic Bcl-2 family members, thereby inducing the release of cytochrome c from mitochondria. BIML is normally sequestered in an inactive conformation from anti-apoptotic Bcl-2 family members through binding to the microtubule-associated dynein motor complex. Certain apoptotic stimuli release BIML from microtubules to neutralize anti-apoptotic Bcl-2 family members, allowing for the initiation of apoptosis.
Biotinidase, also known as biotinase and BTD, is a ubiquitous mammalian cell enzyme which expressed at high levels in the liver, serum, and kidney. Its primary function is to cleave biotin from biocytin, preserving the pool of biotin for use as a cofactor for biotin dependent enzymes, namely the 4 human carboxylases. Biotinidase also recycles biotin from enzymes in the body that use it as a helper component in order to function. These enzymes, known ascarboxylases, are important in the processing offats,carbohydrates, andproteins. Biotin is attached to these carboxylase enzymes through anamino acid(the building material of proteins) calledlysine, forming a complex calledbiocytin.
The signaling lymphocyte activation molecule (SLAM) family includes homophilic and heterophilic receptors that modulate both adaptive and innate immune responses. These receptors share a common ectodomain organization: a membrane-proximal immunoglobulin constant domain and a membrane-distal immunoglobulin variable domain that is responsible for ligand recognition. SLAM family of receptors is expressed by a wide range of immune cells. Through their cytoplasmic domain , SLAM family receptors associate with SLAM-associated protein (SAP)-related molecules , a group of cytoplasmic adaptors composed almost exclusively of an SRC homology 2 domain. SLAM family receptors , in association with SAP family adaptors , have crucial roles during normal immune reactions in innate and adaptive immune cells.Mouse SLAM family member 8 , also known as B-lymphocyte activator macrophage expressed , BCM-like membrane protein , SLAMF8 and BLAME , is a single-pass type I membrane protein. It contains one Ig-like C2-type (immunoglobulin-like) domain. SLAMF8 / BLAME is expressed in lymph node , spleen , thymus and bone marrow. It may play a role in B-lineage commitment and/or modulation of signaling through the B-cell receptor.
BLBP; also known as FABP7; is a brain fatty acid binding protein. Fatty acid binding proteins (FABPs) are a family of small; highly conserved; cytoplasmic proteins that bind long-chain fatty acids and other hydrophobic ligands. FABP7 binds DHA with the highest affinity among all of the FABPs. FABPs may play roles in fatty acid uptake; transport; and metabolism. BLBP is expressed; during development; in radial glia by the activation of notch receptors. It was shown that reelin induces FABP7 expression in neural progenitor cells via notch-1 activation. BLBP variation is linked to weak prepulse inhibition(PPI) in mice and deficit in PPI is an endophenotypic trait observed in schizophrenia patients and their relatives.
Fatty Acid-Binding Protein 7 (FABP7) is a cytoplasm protein that belongs to the Fatty-acid Binding Protein (FABP) family of calycin superfamily. Fatty acid binding proteins are a family of small; highly conserved; cytoplasmic proteins that bind long-chain fatty acids. FABP7 is predominately expressed in brain and neural tissues. FABP7 is involved in fatty acid uptake and intracellular transport and is important in brain development. FABP7 plays a critical role in the transport of a so far unknown hydrophobic ligand with potential morphogenic activity during CNS development. FABP7 is required for the establishment of the radial glial fiber system in developing brain; a system that is necessary for the migration of immature neurons to establish cortical layers.
Tyrosine-protein kinase Blk, also known as B lymphocyte kinase, p55-Blk and BLK, is a member of theprotein kinase superfamily, Tyr protein kinase family and SRC subfamily. BLK / p55-Blk is expressed in lymphatic organs, pancreatic islets, Leydig cells, striate ducts of salivary glands and hair follicles. BLK / p55-Blk is a src-family protein tyrosine kinase specifically expressed in B-lineage cells of mice. The early onset of Blk expression during B-cell development in the bone marrow and the high expression levels of Blk in mature B cells suggest a possible important role of Blk in B-cell physiology. It is a modulator of beta-cells function, acting through the up-regulation of PDX1 and NKX6-1 and consequent stimulation of insulin secretion in response to glucose. Defects in BLK are a cause of maturity-onset diabetes of the young type 11 which is a form of diabetes that is characterized by an autosomal dominant mode of inheritance, onset in childhood or early adulthood (usually before 25 years of age), a primary defect in insulin secretion and frequent insulin-independence at the beginning of the disease.
Tyrosine-Protein Kinase Blk (BLK) contains one protein kinase domain, one SH2 domain and one SH3 domain. BLK is a non-receptor tyrosine kinase, which is involved in B-lymphocyte development, differentiation and signaling. B-cell receptor (BCR) signaling requires a tight regulation of several protein tyrosine kinases and phosphatases, and associated coreceptors. Signaling through BLK plays an important role in transmitting signals through surface immunoglobulines and supports the pro-B to pre-B transition, as well as the signaling for growth arrest and apoptosis downstream of B-cell receptor. Defects in BLK are a cause of maturity-onset diabetes of the young type 11 (MODY11).
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