Initial characterization of a peripheral blood mononuclear cell chemoattractant derived from cultured arterial smooth muscle cells

• Published in: The American journal of pathology Vol. 117; no. 3; pp. 409 - 417
• Main Authors: Valente, AJ, Fowler, SR, Sprague, EA, Kelley, JL, Suenram, CA, Schwartz, CJ
• Format: Journal Article
• Language: English
• Published: Bethesda, MD ASIP 01.12.1984; American Society for Investigative Pathology
• Subjects: Animals; Biological and medical sciences; Cardiovascular system; Chemotactic Factors - biosynthesis; Chemotactic Factors - isolation & purification; Chemotactic Factors - physiology; Chemotaxis, Leukocyte - drug effects; Cycloheximide - pharmacology; Interleukin-8; Investigative techniques, diagnostic techniques (general aspects); Medical sciences; Molecular Weight; Monocytes - metabolism; Monocytes - physiology; Muscle, Smooth, Vascular - cytology; Muscle, Smooth, Vascular - metabolism; Neutrophils - physiology; Papio; Papio cynocephalus; Pathology. Cytology. Biochemistry. Spectrometry. Miscellaneous investigative techniques; Peptide Hydrolases - pharmacology; Pathology; Cell culture; Smooth muscle; Mononuclear cell; Artery
• ISSN: 0002-9440; 1525-2191

A mononuclear cell chemoattractant of high specific activity produced by baboon (Papio cynocephalus) aortic medial smooth-muscle cells (SMCs) in culture has been partially characterized. Smooth-muscle cells, between the third and eighth passage, were grown to confluence in Medium 199 containing 10% fetal calf serum and then incubated for 24 hours in either serumless medium (Neuman and Tytell) or Medium 199 containing 0.2% bovine serum albumin. The 24-hour SMC-conditioned medium was fractionated on Sephadex G100-Superfine and potent chemoattractant activity (SMC-CF) eluted in the 10,000-12,000 dalton region. SMC-CF displayed chemotactic and chemokinetic activity for peripheral blood mononuclear cells but not for polymorphonuclear leukocytes. Production of SMC-CF by the cells was significantly inhibited in the presence of cycloheximide, and its activity was abolished after incubation with the bacterial protease subtilisin. Chromatofocusing experiments indicate that SMC-CF is a cationic protein with a pI of greater than 10.5. The role of SMC-CF may play as an inflammatory mediator in monocyte recruitment to the arterial intima in atherogenesis is discussed.