Expression of annexin VI (p68, 67 kDa-calelectrin) in normal human tissues: evidence for developmental regulation in B- and T-lymphocytes.

This paper describes the tissue distribution of annexin VI, a Ca(2+)-dependent phospholipid binding protein, and a member of the annexin super-gene family. In order to determine whether annexin VI expression correlated with a particular functional phenotype, an extensive series of non-pathological human tissues were examined, in which annexin VI was detected either immunohistochemically or by immunofluorescence, using a rabbit polyclonal anti(human annexin VI)-IgG of known specificity. Although most tissues investigated were found to express annexin VI, the protein was usually confined to highly specific cell types within each tissue, the staining generally appearing cytoplasmic and diffuse. There was particularly good correlation between annexin VI expression and hormone secreting cells, with positive staining in the islet cells of the pancreas, the Leydig cells of the testis and the cells of the adrenal cortex. A notable exception was the parathyroid gland, which lacked detectable annexin VI. Although the protein was absent in most epithelia, it was expressed strongly in certain secretory epithelia; e.g. the ductal epithelial cells of the salivary glands and non-lactating breast, and the sweat glands and their ducts. The observation that the epithelial cells of lactating breast failed to stain for annexin VI suggests functional regulation of protein expression in this tissue. However, the most interesting finding was that annexin VI expression appeared to be developmentally regulated in B- and T-lymphocyte differentiation, with negative staining in the proliferating B cells of the germinal centre of the lymph nodes, but strong staining in the mature small lymphocytes of the cortex, mantle zone and paracortex.