A subpopulation of WIL-2 cell calreticulin molecules is associated with RO/SS-A ribonucleoprotein particles.

A subpopulation of human calreticulin (CR) molecules that is reactive with human Ro/SS-A autoimmune sera was identified in a nucleic acid- enriched Wil-2 cell fraction derived by anion exchange column chromatography. Further resolution of this fraction by gel filtration size separation demonstrated that the appearance of CR (true mol. weight 46 kD) coincided with the emergence of Ro/SS-A ribonucleoprotein (mol. weight > 250 kD) antigenic activity and increasing 260 nm ultraviolet absorbance. This high nucleic acid fraction could be further partitioned into four small RNA-containing Ro/SS-A antigenic subfractions by a second passage over the anion exchange column. CR was enriched in one subfraction and present in the other three subfractions as well. No CR was found in the RNA-free fraction of the repartition eluate. These results represent the first direct demonstration that CR, a high-affinity calcium binding protein, exists in a form that is directly associated with all four varieties of native, human Ro/SS-A ribonucleoprotein particles (hY1-5).