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Antigen-Induced Proliferation of Guinea Pig Lymphocytes in Vitro: Functional Aspects of Antigen Handling by Macrophages

From the Department of Pathology, Vanderbilt University School of Medicine, Nashville, Tennessee 37232, and the Laboratory of Clinical Investigation, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20014

Abstract

Macrophages were incubated in vitro with purified protein derivative (PPD) under various experimental conditions, washed to remove unbound antigen, and assayed for immunogenicity by addition to cultures of purified PPD-immune lymph node lymphocytes. Proliferative responses elicited in the "indicator lymphocytes" served as semiquantitative indices of macrophage-associated immunogenicity. The accumulation of immunogenic activity by macrophages during a 1-hr pulse with PPD exhibited marked temperature dependency; immunogenicity of macrophages pulsed at 37°C exceeded that of cells pulsed at 4°C at every concentration of PPD utilized. The immunogenicity associated with macrophages pulsed with PPD at 4°C could be completely removed by trypsinization of the cells immediately after termination of the pulse. In contrast, only a fraction of the immunogenicity associated with macrophages pulsed with PPD at 37°C could be removed by trypsinization. When macrophages pulsed with antigen at 4°C were incubated at 37°C before trypsinization, the macrophage-associated immunogenicity became progressively more resistant to removal with trypsin. Kinetic studies of the accumulation of immunogenicity by macrophages pulsed with PPD at 37°C revealed that the trypsin-insensitive fraction of the total macrophage-associated immunogenicity became progressively greater with pulses of 0 to 60 min duration. The results suggest that accumulation of relevant antigen molecules by macrophages proceeds by a two step mechanism, involving membrane binding and subsequent metabolic dependent sequestration of bound antigen by the macrophage.

Footnotes

¹ Vivian Allen Medical Scholar, Vanderbilt University School of Medicine. Previously supported by United States Public Health Service Training Grant GM-00290. This work was submitted in partial fulfillment of requirements for Ph.D. in Pathology.

² Recipient of United States Public Health Service Career Development Award GM-28110. This investigation was supported in part by United States Public Health Service Grant HE-10048-07.

³ Address reprint requests to Alan S. Rosenthal, Section on Biologic Structure, Laboratory of Clinical Investigation, National Institute of Allergy and Infectious Diseases, Bldg. 10, Room 11N-224, Bethesda, Maryland 20014.