High impact information on Lamp2

• This was accompanied by a parallel time-dependent increase in other EL markers, ie, cathepsin D, Rab5, and LAMP2 in the basal forebrain region, whereas in the frontal cortex the levels of cathepsin D, and to some extent Rab5, were increased [1].
• Lysosomal import of KFERQ proteins depends on the abundance of the 96-kDa lysosomal glycoprotein protein (lgp96), and we found that EGF caused a significant decrease in lgp96 in cellular homogenates and associated with lysosomes [2].
• lgp110 is a heavily glycosylated intrinsic protein of lysosomal membranes [3].
• Partial sequencing of mouse lgp110 allowed oligonucleotide probes to be constructed for the screening of several mouse cDNA libraries [3].
• Mouse lgp110 is encoded by at least seven exons; intron positions suggest that the two homologous ectodomains of each lgp arose through gene duplication [3].

Biological context of Lamp2

• The deduced amino acid sequence indicates that LGP 96 consists of 411 amino acid residues (Mr 45,163) and the 26 NH2-terminal residues presumably constitute a cleavable signal peptide [4].
• There was a significant correlation with a regression coefficient of 0.86 in the tissue distribution between r-lamp-1 and r-lamp-2 [5].

Anatomical context of Lamp2

• The major portion of LGP 96 resides on the luminal side of the lysosome and bears a large number of N-linked heavily sialylated complex type carbohydrate chains, giving the mature molecule of 96 kDa [4].
• The bulk of both lgp110 and rab7, a small GTP-binding protein participating in vesicle fusion to late endosomes, was localized to the RB [6].
• Limited and selective localization of the lysosomal membrane glycoproteins LGP85 and LGP96 in rat osteoclasts [7].
• Cycling of two endogenous lysosomal membrane proteins, lamp-2 and acid phosphatase, between the cell surface and lysosomes in cultured rat hepatocytes [8].
• LGP107 and LGP96, which are rat homologs of lysosome-associated membrane proteins, were most useful as immunohistochemical markers of mononuclear phagocytes [9].

Associations of Lamp2 with chemical compounds

• Purification, some properties, and tissue distribution of a major lysosome-associated membrane glycoprotein (r-lamp-2) of rat liver [5].
• The purification procedures included: preparation of lysosomal membranes, elimination of LGP107 and LGP96 with immunoaffinity columns, WGA-Sepharose affinity chromatography, hydroxylapatite chromatography, and preparative polyacrylamide gel electrophoresis [10].
• The endocytic transport of HRP-YA30 mAb continued in the presence of the protein synthesis inhibitor, cycloheximide, indicating that LGP85 is cycled between the cell surface and lysosomes or endosomes, like other lysosomal membrane glycoproteins, lamp-1 and lamp-2, as reported previously [Akasaki et al. (1993) J. Biochem. 114, 598-604] [11].
• In these vesicles, LAMP2 was detected but no LIMPII or the mannose 6-phosphate receptor [12].
• The high-density compartment is denser than lysosomes, contains LAMP2 but not LIMPII or acid hydrolases, and is not disrupted with glycyl-l-phenylalanine 2-naphthylamide, a substrate for cathepsin C that selectively disrupts lysosomes [12].

Other interactions of Lamp2

• Comparison of LGP 96 and recently cloned lysosomal membrane glycoprotein sequences reveals strong similarity in the putative transmembrane domain and cytoplasmic tail [4].

Analytical, diagnostic and therapeutic context of Lamp2

• R-lamp-2 exhibited an Mr of 96,000 on SDS-PAGE and had an acidic pI of less than 3 [5].

References