Secreted Forms of the Amyloid-β Precursor Protein are Ligands for the Class A Scavenger Receptor

Journal of Biological Chemistry

Volumn 276, Issue 33, 2001, Pages 30655-30661

  Santiago García, Juan ^a   Mas Olivata, Jaime ^b   Innerarity, Thomas L ^a   Pitas, Robert E ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b INSTITUTO DE FISIOLOGÍA CELULAR   (Mexico)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CELLS; IMMUNOLOGY; MUTAGENESIS; OXIDATION;

LIGANDS; LIPOPROTEINS;

PROTEINS;

ACETYL LOW DENSITY LIPOPROTEIN; ALPHA SECRETASE; AMYLOID BETA PROTEIN; AMYLOID PRECURSOR PROTEIN; AMYLOID PRECURSOR PROTEIN 695; AMYLOID PRECURSOR PROTEIN 751; CLASS A SCAVENGER RECEPTOR; FUCOIDIN; LIGAND; NEXIN II; OXIDIZED LOW DENSITY LIPOPROTEIN; PROTEASE NEXIN I; PROTEIN; SCAVENGER RECEPTOR; SERINE PROTEINASE INHIBITOR; UNCLASSIFIED DRUG; IMMUNOGLOBULIN RECEPTOR; LIPOPROTEIN RECEPTOR; MEMBRANE PROTEIN; PROTEOGLYCAN; SCARB1 PROTEIN, MOUSE; SCAVENGER RECEPTOR A; SCAVENGER RECEPTOR B;

AMINO ACID COMPOSITION; AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ANIMAL CELL; ANIMAL EXPERIMENT; ANIMAL MODEL; ARTICLE; ATHEROSCLEROSIS; BINDING AFFINITY; CHO CELL; CONTROLLED STUDY; DELETION MUTANT; HUMAN; HUMAN CELL; IMMUNOBLOTTING; INTERNALIZATION; KUNITZ TYPE PROTEASE INHIBITOR DOMAIN; LIGAND BINDING; MACROPHAGE; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN PURIFICATION; PROTEIN SECRETION; RABBIT; THROMBOCYTE ACTIVATION; ANIMAL; CHEMISTRY; METABOLISM; MOLECULAR GENETICS; THROMBOCYTE;

ANIMALIA; CRICETINAE; CRICETULUS GRISEUS; ORYCTOLAGUS CUNICULUS;

AMINO ACID SEQUENCE; AMYLOID BETA-PROTEIN PRECURSOR; ANIMALS; BLOOD PLATELETS; HUMANS; LIGANDS; MEMBRANE PROTEINS; MOLECULAR SEQUENCE DATA; PROTEOGLYCANS; RABBITS; RECEPTORS, IMMUNOLOGIC; RECEPTORS, LIPOPROTEIN; RECEPTORS, SCAVENGER; SCAVENGER RECEPTORS, CLASS A; SCAVENGER RECEPTORS, CLASS B;

EID: 0035903204     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M102879200     Document Type: Article

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