- Silverio Perrotta1⇓,
- Fulvio Della Ragione2,
- Francesca Rossi1,
- Rosa Anna Avvisati3,
- Daniela Di Pinto1,
- Giovanna De Mieri1,
- Saverio Scianguetta1,
- Silvia Mancusi1,
- Luigia De Falco3,
- Vito Marano1 and
- Achille Iolascon3
- 1 Department of Pediatrics, Second University of Naples, Naples, Italy
- 2 Department of Biochemistry and Biophysics “F. Cedrangolo”, Second University of Naples, Naples, Italy
- 3 Medical Genetics, Department of Biochemistry and Medical Biotechnologies, University Federico II of Naples, CEINGE-Advanced Biotechnologies, Naples, Italy
- Correspondence: Silverio Perrotta, MD, Department of Pediatrics, Second University of Naples Via Luigi De Crecchio, 4 Naples, Italy. E-mail:
We describe a β-spectrin variant, named β-spectrin Bari, characterized by a truncated chain and associated with Hereditary Spherocytosis. The clinical phenotype consists of a moderately severe hemolytic anemia, splenomegaly, and spherocytes and acanthocytes in the blood smear. The occurrence of the truncated protein, that represents about 8% of the total b-spectrin occurring on the membrane, results in a marked spectrin deficiency. The altered protein is due to a single point mutation at position −2 (A->G) of the acceptor splice site of intron 16 leading to an aberrant b-spectrin message skipping exons 16 and 17 indistinguishable from the reported for β-spectrin Winston-Salem. We provide evidence that the mutated gene is transcribed but its mRNA is less abundant than either its normal counterpart or β-spectrin Winston-Salem mRNA. Our findings are an example of how mutations in different splice sites, although causing the same truncating effect, result in clearly different clinical pictures.
- Received April 14, 2009.
- Revision received June 12, 2009.
- Accepted June 16, 2009.
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