MAP1A and MAP1B are microtubule-associated proteins which mediate the physical interactions between microtubules and components of the cytoskeleton. MAP1A and MAP1B each consist of a heavy chain subunit and multiple light chain subunits. The protein encoded by this gene is one of the light chain subunits and can associate with either MAP1A or MAP1B. Two transcript variants encoding different isoforms have been found for this gene. The expression of variant 1 is suppressed in many tumor cell lines, suggesting that may be involved in carcinogenesis.
LC3,also known as microtubule-associated protein 1 light chain 3 (MAP1LC3),is a mammalian homolog of the yeast Atg8p (autophagy-related 8 protein) that is involved in autophagy process. Three isoforms of LC3 exist as LC3A,LC3B,and LC3C. LC3 is first synthesized as pro-LC3,and undergoes C-terminal cleavage to yield a cytosolic precursor known as LC3-I. During autophagy LC3-I is subsequently conjugated to PE lipid as lipidated form: LC3-II. The lipidated form migrates faster on SDS-PAGE gel. The increased the level of LC3-II has been widely used as autophagy marker. This antibody recognizes both LC3-I and LC3-II.
The product of this gene is a subunit of neuronal microtubule-associated MAP1A and MAP1B proteins, which are involved in microtubule assembly and important for neurogenesis. Studies on the rat homolog implicate a role for this gene in autophagy, a process that involves the bulk degradation of cytoplasmic component.
This gene is a member of the Src family of protein tyrosine kinases (PTKs). The encoded protein is a key signaling molecule in the selection and maturation of developing T-cells. It contains N-terminal sites for myristylation and palmitylation, a PTK domain, and SH2 and SH3 domains which are involved in mediating protein-protein interactions with phosphotyrosine-containing and proline-rich motifs, respectively. The protein localizes to the plasma membrane and pericentrosomal vesicles, and binds to cell surface receptors, including CD4 and CD8, and other signaling molecules. Multiple alternatively spliced variants encoding different isoforms have been described.
This gene encodes a protein that belongs to the lipocalin family. Members of this family transport small hydrophobic molecules such as lipids, steroid hormones and retinoids. The protein encoded by this gene is a neutrophil gelatinase-associated lipocalin and plays a role in innate immunity by limiting bacterial growth as a result of sequestering iron-containing siderophores. The presence of this protein in blood and urine is an early biomarker of acute kidney injury. This protein is thought to be be involved in multiple cellular processes, including maintenance of skin homeostasis, and suppression of invasiveness and metastasis. Mice lacking this gene are more susceptible to bacterial infection than wild type mice.
Lactate dehydrogenase C catalyzes the conversion of L-lactate and NAD to pyruvate and NADH in the final step of anaerobic glycolysis. LDHC is testis-specific and belongs to the lactate dehydrogenase family. Two transcript variants have been detected which differ in the 5' untranslated region. In particular, recent researches have showed LDHC is expressed in a broad spectrum of tumours, with frequent appearance in lung cancer, melanoma and breast cancer. A recent report indicated that LDHC plays an important role in inducing breast cancer metastasis.
The low density lipoprotein receptor (LDL R) is the founding member of the LDL R family of scavenger receptors. This family contains type I transmembrane molecules that are characterized by the presence of EGF repeats, complement-like repeats, and YWTD motifs that form beta -propellers. Although members of the family were originally thought to be endocytic receptors, it is now clear that some members interact with adjacent cell-surface molecules, expanding their range of activities. Mouse LDL R is synthesized as a 864 amino acid (aa) precursor that contains a 21 aa signal sequence, a 769 aa extracellular region, a 22 aa transmembrane segment and a 52 aa cytoplasmic tail. The extracellular region is complex. It consists of seven N-terminal complement-like cysteine-rich repeats (class A LDL domains) that bind LDL. Cysteines in this region participate in intrachain disulfide bonds. This region is followed by two EGF-like domains and six class B LDL repeats that generate a beta -propeller whose blades each contain a YWTD motif. This area is likely responsible for ligand dissociation. Finally, there is a 50 aa membrane proximal Ser/Thr-rich region that shows extensive O-linked glycosylation, generating a native molecular weight for LDL R of 135 kDa. Within the 52 aa cytoplasmic region, there is an NPxY motif that links the receptor to clathrin pits and binds to select adaptor proteins. The extracellular region of mouse LDL R shares 78% and 87% aa identity with the extracellular region of human and rat LDL R, respectively. LDL R is constitutively expressed and binds apoB of LDL and apoE of VLDL. It is responsible for clearing 70% of plasma LDL in liver.
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