Expression of intracisternal A-type particles is increased when a B-cell lymphoma differentiates into an immunoglobulin-secreting cell.

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The murine B-cell lymphoma CH12, like many other murine cells, expresses intracisternal A-type particles (IAPs). When CH12 cells are treated with lipopolysaccharide, the cells differentiate and secrete immunoglobulin M. The expression of IAP genes was also increased, in parallel with the increased expression of immunoglobulin genes. The amount of IAP mRNA increased within 48 h of lipopolysaccharide treatment and reached a level fivefold higher than that in unactivated CH12 cells. The two major IAP transcripts (7.2 and 5.4 kilobases) were induced to similar extents. The increased level of mRNA was reflected in higher levels of the major IAP structural protein p70, whose abundance increased 3.6-fold. The number of IAP particles per cell also increased upon activation of CH12, from 67 in nonsecreting CH12 to 290 in secreting cells. All of the IAPs were confined to the cisternae of the endoplasmic reticulum (ER), regardless of the differentiation state of the cell. Accompanying the induction of p70 was the induction of the related IAP polypeptide p102. A third viral polypeptide, p120, was also made in CH12; its abundance was almost unchanged. Localization of the IAP proteins on ultrathin frozen sections showed that most were assembled into particles in the ER. However, there were small pools of unassembled proteins both in the ER and on the plasma membrane. p70 and p120 could be detected, by iodination, on the surfaces of both secreting and nonsecreting CH12 cells. Unlike p70 and p120, p102 did not seem to be membrane associated. Taken together, these observations show that IAP expression is regulated developmentally in B lymphocytes. Also, these observations point to possible interactions between IAP genes and other cellular genes.

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