Functional and possible physical association of scavenger receptor with cytoplasmic tyrosine kinase Lyn in monocytic THP-1-derived macrophages

• Published in: FEBS letters Vol. 399; no. 3; pp. 241 - 244
• Main Authors: Miki, Shunji, Tsukada, Satoshi, Nakamura, Yu, Aimoto, Saburo, Hojo, Hironobu, Sato, Bunzo, Yamamoto, Masahiro, Miki, Yoshitsugu
• Format: Journal Article
• Language: English
• Published: England Elsevier B.V 16.12.1996
• Subjects: Acetyl low-density lipoprotein; Amino Acid Sequence; Cell Line; Cytosol - enzymology; Foam Cells - metabolism; Lipoproteins, LDL - chemistry; Lipoproteins, LDL - metabolism; Lyn; Membrane Proteins; Molecular Sequence Data; Phosphorylation; Precipitin Tests; Receptors, Immunologic - chemistry; Receptors, Immunologic - metabolism; Receptors, Lipoprotein; Receptors, Scavenger; Scavenger receptor; Scavenger Receptors, Class A; Scavenger Receptors, Class B; src-Family Kinases - metabolism; THP-1-derived macrophage; Lyn; Scavenger receptor; THP-1-derived macrophage; Acetyl low-density lipoprotein
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/S0014-5793(96)01332-4

Acetyl LDL (modified low-density lipoprotein), which is thought to be taken up through scavenger receptor A (SR-A), rapidly induced the appearance of phosphotyrosine proteins in monocytic THP-1-derived macrophages in vitro. The two alternative forms of Lyn (p 53 and p 56) were found to be tyrosine-phosphorylated within 30 s after the stimulation with acetyl LDL. The catalytic activity of Lyn measured by an in vitro kinase assay had also increased in acetyl LDL-stimulated THP-1-derived macrophages. Furthermore, Lyn could be co-immunoprecipitated with SR-A from the cell lysate. These observations suggest a functional and possible physical association of SR-A with Lyn in THP-1-derived macrophages, and also imply a possible involvement of Lyn in SR-A signal transduction.