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- W1623135052 abstract "AACR Annual Meeting-- Apr 12-16, 2008; San Diego, CA2695 Waldenstrom’s macroglobulinemia (WM) is an incurable B cell malignancy characterized by the accumulation of IgM secreting lymphoplasmacytic cells (LPC). Despite intense research efforts, the mechanism(s) by which WM LPC fail to undergo apoptosis remain to be defined. One potential mechanism for B-cell homeostasis is signaling of CD70 through CD27, which induces apoptosis in normal B-cells including CD27+ memory B-cells from which WM LPC are thought to derive. WM cells often show no or diminished expression of CD27, or secrete high levels of soluble CD27 which may lead to CD70 signaling blockade (Ho et al, Blood 2008). As part of these effort we sought to elaborate on intracellular mechanisms for CD70-CD27 signaling, by focusing on SIVA, a pro -apoptotic proteincontaining a death domain which interacts with the cytoplasmic tail of CD27. Two splice variants of SIVA ( SIVA1 and SIVA2) have so far been identified in humans . We therefore evaluated the expression patterns of SIVA in 25 WM patients and 6 healthy donors (HD). Through gene profiling, we detected the constitutive expression of SIVA 1 and its variant SIVA2 , which results from deletion of exon 2. However, in contrast to previous findings, we detected three novel aberrant splice variants of SIVA , which we have designated as SIVA-Va, -Vb, and -Vc, at least one of which alone or combination with each other were present in 25/25 patients with WM versus 1/6 HD (p=0.00004). The breakdown for the frequency of expression for these variants in WM patients was as follows: SIVA -Va (10/25); -Vb (6/25); -Vc (13/25), whereas in HD only SIVA-Vc was present in one individual. Cloning, sequencing and alignment analysis of SIVA variants from 4 WM patients revealed that SIVA-Va and SIVA-Vb resulted from partial intron retention, while SIVA-Vc was derived from the deletion of two exons. DNA alignment and bioinformatics analysis demonstrated that all splice variants of SIVA encoded for novel proteins. This prediction was verified by transient tranfection of GFP-SIVA-FL and DsRed-SIVA variant constructs into HeLa cells. As expected, SIVA-FL protein was expressed in the nucleus and transported to the membrane, while splice variants were localized on the membrane. Co-transfection analysis of SIVA-FL and splice variants verified their co-localization at the membrane 6 hours after proteins production. The results of these studies suggest that SIVA variants compete for CD27 binding and may therefore interfere with B-cell homeostasis regulated by CD70-CD27 interactions." @default.
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- W1623135052 date "2008-05-01" @default.
- W1623135052 modified "2023-09-24" @default.
- W1623135052 title "Abnormal splice variants of SIVA in Waldenstrom’s macroglobulinemia (WM)." @default.
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