Ultrastructural localization of acid phosphatase in rosetted T and B lymphocytes of normal human blood.

Using electron microscopy and cytochemical techniques, the authors determined the distribution of acid phosphatase (AcPase) within the organelles of lymphocytes from blood rosetted with either neuraminidase-treated sheep erythrocytes (En) or sheep erythrocytes coated with antibody and complement (EACs). Subsequently, the various reactive organelles of the rosetted lymphocytes were counted, affording a comparison of T and B cells. It was found that AcPase was present in approximately 80% of T cells and 45% of B cells and was most frequently observed in secondary lysosomes of varying size and content. Although more T cells than B cells were reactive for AcPase, the extent of reaction in some B cells clearly precludes the use of AcPase for differentiating the two cell lines. It should be recognized that while the En rosetting procedure detects T cells in a nonselective manner, the EAC rosette is a marker of a major subpopulation of B lymphocytes, ie, those bearing complement receptors. We believe that the distribution of lysosomal enzymes in B and T lymphocytes probably reflects the functional state of individual cells rather than being a reliable indicator of cell lineage. A surprising finding (which could be established only by a fine-structural study) was the fact that 20% of circulating "resting" T cells contained reaction product for AcPase within endoplasmic reticulum and the perinuclear cisterna indicating that these cells are actively synthesizing AcPase, probably due to a foregoing inductive event. Such stimulus could be the result of recent endocytosis of surface receptors in combination with antigen, antibody, or immune complexes and/or recent mitosis, or possibly some unrelated autophagic incident.