Abstract

Spectrin is the major protein of the membrane erythrocyte skeleton. More recently, homologous but non-identical spectrins (fodrins) were also found in various non-erythroid tissues. Spectrin mRNA in erythroid and various non-erythroid cells was examined by direct hybridization with human alpha-spectrin, beta-spectrin (erythroid spectrins), and alpha-fodrin (non-erythroid spectrin) cDNA probes. Northern blot analysis of poly (A)+ RNA revealed a distinct pattern of expression in erythroid vs. non-erythroid cells. Erythroid cells from early erythroblasts to reticulocyte stage expressed two mRNA species of beta-spectrin, whereas they expressed only a single species of alpha-spectrin, and no alpha-fodrin mRNA. In contrast, non-erythroid cells (platelets, myeloid cells, liver, muscle, heart, cerebellum, and eye lens) expressed either no alpha-spectrin mRNA or a different molecular weight transcript(s) of this gene, and a single species of alpha-fodrin mRNA. Additionally, they also expressed from none to multiple species of beta-spectrin, and these were of different molecular size(s) from that found in erythroid cells (with the exception of platelets). Transcripts of non-erythroid spectrin, alpha-fodrin, were found as a single copy only in non-erythroid tissues. Human and murine erythroleukemia cells expressed both erythroid spectrin transcripts in addition to alpha-fodrin and raise the possibility that erythroid progenitors may have the potential to express both erythroid and non-erythroid species. These data indicated that several mRNA species of beta-spectrin could be detected in both erythroid and some non-erythroid cells. Whether multiple spectrin peptides could also be found with functional heterogeneity is unclear. However, in each case, the pattern combination observed appeared to be tissue-specific.

Full Text
Paper version not known

Talk to us

Join us for a 30 min session where you can share your feedback and ask us any queries you have

Schedule a call