Identification and Characterization of a Major Lysosomal Membrane Glycoprotein, LGP85/LIMP II in Mouse Liver.
スポンサーリンク
概要
- 論文の詳細を見る
We previously have purified and characterized a major lysosomal membrane glycoprotein termed LGP85 (LIMP II) in rat liver lysosomes. In this study, LGP85 in mouse liver lysosomes was identified and characterized by biochemical and molecular biological methods. Lysosomal membranes were isolated from murine liver by differential centrifugation. LGP85 was present in the lysosomal membrane fraction from mouse liver in a comparable amount to another lysosomal membrane glycoprotein, lamp-2. Mouse LGP85 (M-LGP85) from liver lysosomal membranes exhibited an Mr of 80, 000 on SDS-PAGE, which is smaller by 5, 000 than that of rat LGP85 (R-LGP85). M-LGP85 was immunochemically detected in the extracts of brain, heart, lung, liver, and kidney. A cDNA encoding M-LGP85 was cloned from mouse liver cDNA library. The primary protein structure deduced from a nucleotide sequence of M-LGP85 cDNA indicated that M-LGP85 consists of 478 amino acids with Mr of 54, 069. M-LGP85 showed 93.3 and 86.0% sequence similarities to its rat and human counterparts in amino acids, respectively. M-LGP85 contains 11 potential N-glycosylation sites which are heavily glycosylated, resulting in the increased Mr of M-LGP85 present in the mouse liver lysosomes. It is likely that M-LGP85 traverses the lysosomal membrane twice, with an NH2-terminal transmembrane domain, and another hydrophobic domain near the COOH-terminus. M-LGP85 has a protruding COOH-terminal cytoplasmic tail consisting of amino acid residues including the leucine-isoleucine sequence shown to be the lysosomal targeting signal of R-LGP85 and human LGP85 (H-LGP85). The high level of expression of M-LGP85 in the lysosomal membrane, the high structural similarities among M-, R-, and H-LGP85, and the occurrence of M-LGP85 in all the mouse tissues examined suggest the essential and constitutive function of LGP85 in lysosomes.
- 社団法人 日本生化学会の論文
著者
-
Akasaki Kenji
Faculty Of Pharmacy & Pharmaceutical Sciences Of Fukuyama University
-
TABUCHI Norihiko
Faculty of Pharmacy and Pharmaceutical Sciences, Fukuyama University
-
SASAKI Tomoko
Faculty of Pharmacy and Pharmaceutical Sciences, Fukuyama University
-
Kanda Naoko
Faculty Of Pharmacy And Pharmaceutical Sciences Fukuyama University
-
Sasaki Tomoko
Faculty Of Pharmacy And Pharmaceutical Sciences Fukuyama University
-
Tsuji Hiroshi
Faculty Of Pharmacy & Pharmaceutical Sciences Of Fukuyama University
関連論文
- Probucol Decreases Mevalonate Pyrophosphate Decarboxylase in the Rat Liver(Biochemistry/Molecular Biology)
- Peroxisome Proliferative Drugs Do not Induce an Increase of Rat Mevalonate Pyrophosphate Decarboxylase(Biochemistry/Molecular Biology)
- Comparison of Subcellular Distribution of Mevalonate Pyrophosphate Decarboxylase between Stroke-Prone Spontaneously Hypertensive Rat and Wistar Kyoto Rat
- Mevalonate Pyrophosphate Decarboxylase in Stroke-Prone Spontaneously Hypertensive Rat Is Reduced from the Age of Two Weeks
- Difference in Subcellular Distribution between 45- and 37-kDa Mevalonate Pyrophosphate Decarboxylase in Rat Liver
- Mevalonate Pyrophosphate Decarboxylase is Predominantly Located in the Cytosol of Rat Hepatocytes
- The Antioxidative and Antilipidemic Effects of Different Molecular Weight Chitosans in Metabolic Syndrome Model Rats
- Change in the Protein Level of Mevalonate Pyrophosphate Decarboxylase in Tissues of Mouse by Pravastatin(Biochemistry/Molecular Biology)
- Subcellular Distribution of Mouse Mevalonate Pyrophosphate Decarboxylase
- Purification and Characterization of Mouse Mevalonate Pyrophosphate Decarboxylase
- Tissue Distribution of a Major Mevalonate Pyrophosphate Decarboxylase in Rats
- Comparison of the Gene Expression Levels of Mevalonate Pyrophosphate Decarboxylase between Stroke-prone Spontaneously Hhypertensive and Wistar Kyoto Rats
- Tissue Distribution of Mevalonate Pyrophosphate Decarboxylase in Guinea Pig
- High Levels of Oxidative Stress Exist in the Brain than Serum or Kidneys in Stroke-Prone Spontaneously Hypertensive Rats at Ten Weeks of Age
- Purification and Characterization of a Major Kyotorphin-Hydrolyzing Peptidase of Rat Brain
- Distribution of a Major Lysosomal Membrane Glycoprotein, LGP85/LIMP II, in Rat Tissues
- Identification and Characterization of a Major Lysosomal Membrane Glycoprotein, LGP85/ LIMP II in Mouse Liver
- Comparison of Receptors and Enzymes Regulating Cholesterol Levels in Liver between SHR/NDmcr-cp Rats and Normotensive Wistar Kyoto Rats at Ten Weeks of Age
- Reduction of Mevalonate Pyrophosphate Decarboxylase in Mouse Melanoma Cells Treated with δ-Tocotrienol Is Not Associated with Reduction of Cholesterol Content or Release of Lysosomes and Melanosomes
- Delta-Tocotrienol Causes Decrease of Melanin Content in Mouse Melanoma Cells
- Difference in Subcellular Distribution of Mevalonate Pyrophosphate Decarboxylase Occurs by Cell Type
- Mevalonate Pyrophosphate Decarboxylase is Predominantly Located in the Cytosol of both B16 and B16F10 Cells in Mouse Melanoma Treated with Lovastatin
- The Effect of Primaquine on Lysosomal Protein in Cultured Rat Hepatocytes
- Decrease of Cholesterol in Mouse Melanoma Causes Secretion of Lysosomal Enzymes
- Disruptive Effect of Chloroquine on Lysosomes in Cultured Rat Hepatocytes(Biochemistry/Molecular Biology)
- Biosynthetic Transport of a Major Lysosome-Associated Membrane Glycoprotein 2, Lamp-2: A Significant Fraction of Newly Synthesized Lamp-2 Is Delivered to Lysosomes by Way of Early Endosomes
- Effect of Delta-Tocotrienol on Melanin Content and Enzymes for Melanin Synthesis in Mouse Melanoma Cells
- The 44-kb Linear Plasmid Molecule in the Relapsing Fever Agent Borrelia duttonii Strain Ly Serve as a Preservation of vmp Genes
- COOH-terminal isoleucine of lysosome-associated membrane protein-1 is optimal for its efficient targeting to dense secondary lysosomes
- Identification and Characterization of a Major Lysosomal Membrane Glycoprotein, LGP85/LIMP II in Mouse Liver.