Lysosome-Associated Membrane Glycoprotein 1 (LAMP1) is a single-pass type I membrane protein belonging to the LAMP family. LAMP1 is expressed largely in the endosome-lysosome membranes of cells.It shuttles between lysosomes; endosomes; and the plasma membrane. LAMP1 functions to present carbohydrate ligands to selectins and it has also been implicated in tumor cell metastasis. It has been proposed LAMP1 can be used as a therapeutic agent for certain cancers; as well as a marker for lysosomal storage disorders and degranulation on lymphocytes such as CD8+ and NK cells. Cell surface LAMP1 and LAMP2 have been shown to promote adhesion of human peripheral blood mononuclear cells(PBMC) to vascular endothelium; therefore they are possibly involved in the adhesion of PBMCs to the site of inflammation.
Lysosome-associated membrane glycoprotein 1, also known as CD107 antigen-like family member A, CD107a, and LAMP1, is a single-pass type I membrane protein which belongs to the LAMP family. CD107a is expressed largely in the endosome-lysosome membranes of cells, but is also found on the plasma membrane (1-2% of total LAMP1). LAMP1 has been implicated in a variety of cellular functions, including cancer metastasis. It has been proposed LAMP1 serves as a therapeutic agent for some cancers, as well as a marker for lysosomal storage disorders and different cell types such as cytotoxic T cells. LAMP2, also known as CD107b, may also play a role in tumor cell metastasis and functions in the protection, maintenance, and adhesion of the lysosome. Cell surface LAMP1 and LAMP2 have been shown to promote adhesion of human peripheral blood mononuclear cells (PBMC) to vascular endothelium, therefore they are possibly involved in the adhesion of PBMCs to the site of inflammation. LAMP-1 is a glycoprotein highly expressed in lysosomal membranes. LAMP-1 has been suggested to be a cell surface receptor for a specific amelogenin isoform, leucine-rich amelogenin peptide or LRAP. LAMP-1 can serve as a cell surface binding site for amelogenin on dental follicle cells and cementoblasts.
Lysosomal Associated Membrane Protein 2 (LAMP2) is a major component of lysosomal membranes. LAMP2 is a transmembrane glycoprotein about 110kDa. Mature human LAMP2 consists of a 347 amino acid (aa) intralumenal domain, a 24 aa transmembrane segment, and a 35 aa cytoplasmic tail . The lumenal domain is organized into two heavily N-glycosylated regions. Alternate splicing generates a human LAMP2 isoform (LAMP2B) with a substituted juxtamembrane lumenal region, cytoplasmic tail and transmenmbrane segment.LAMP2 itself can cleavage lysosomal luminal domain and degradation lysosomal. In the help of chaperone HSC73,LAMP2 mediates the lysosomal uptake in complex with cargo proteins and is required for the lysosomal destruction of autophagic vacuoles.
Ragulator complex protein LAMTOR2, also known as Endosomal adaptor protein p14, Late endosomal / lysosomal Mp1-interacting protein, Late endosomal / lysosomal adaptor and MAPK and MTOR activator 2, Mitogen-activated protein-binding protein-interacting protein, Roadblock domain-containing protein 3, LAMTOR2, MAPBPIP and ROBLD3, is a protein which belongs to theGAMAD family. LAMTOR2 / ROBLD3 is a regulator of the TOR pathway, a signaling cascade that promotes cell growth in response to growth factors, energy levels, and amino acids. As part of the Ragulator complex, LAMTOR2 / ROBLD3 recruits the Rag GTPases and the mTORC1 complex to lysosomes, a key step in activation of the TOR signaling cascade by amino acids. LAMTOR2 / ROBLD3 is an adapter protein that enhances the efficiency of the MAP kinase cascade facilitating the activation of MAPK2. Defects in LAMTOR2 are the cause of immunodeficiency due to defect in MAPBP-interacting protein (ID-MAPBPIP). This form of primary immunodeficiency syndrome includes congenital neutropenia, partial albinism, short stature and B-cell and cytotoxic T-cell deficiency.
Mitogen-Activated Protein Kinase Scaffold Protein 1 (MAPKSP1) was identified as an interacting protein that belongs to the LAMTOR3 family. MAPKSP1 restricted to late endosomes by the mitogen-activated protein-binding protein-interacting protein, and binds specifically to MAP kinase kinase MAP2K1/MEK1, MAP kinase MAPK3/ERK1, and MAP kinase MAPK1/ERK2. MAPKSP1 interacts with MAP2K1/MEK1 and MAPK2 and enhances the activation of MAPK2, and thus is thought to function as an adaptor to enhance the efficiency of the MAP kinase cascade.
Langerin (CD207) is a type II transmembrane glycoprotein which is member K of the C-type lectin domain family. Langerin is used as a marker for Langerhans cells (LCs) which represent the immature dendritic cells in the epidermis. Langerin is necessary and sufficient for Birbeck granule formation. Human langerin sequence contains a 43 aa cytoplasmic domain, a 21 aa transmembrane domain and a 264 aa extracellular domain (ECD) that contains a coiled-coil domain and a single C-type lectin domain. Human langerin shares 68%, 62%, 71% aa identity with mouse, rat and bovine langerin ECD, respectively. Trimerization greatly increases the lectin binding affinity. Langerin internalizes endogenous proteins such as type I procollagen. Internalization by LC is thought to lead to suppression of self reactions. Langerin also mediates endocytosis of non-peptide antigens containing mannose, N-acetyl glucosamine and fucose that are expressed by mycobacteria and fungae.
LAP3 (Leucine Aminopeptidase 3) is a Protein Coding gene. 2 alternative initiation human isoforms have been reported. LAP3, belonging to the peptidase M17 family, has been proved to catalyze the hydrolysis of leucine residues. It catalyzes the removal of unsubstituted N-terminal amino acids from various peptides and is presumably involved in the processing and regular turnover of intracellular proteins. Leucine aminopeptidases are involved in many pathological disorders and regulate cell proliferation, invasion, and/or angiogenesis of tumors. A recent study showed that LAP3 is highly expressed in several malignant and affects tumor angiogenesis. LAP3 is widely expressed in the appendix, lymph node, and other tissues. Diseases associated with LAP3 include Bacterial Vaginosis and Trichomoniasis.
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