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J. Biol. Chem., Vol. 280, Issue 11, 10655-10663, March 18, 2005

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A Novel Protein Derived from the MUC1 Gene by Alternative Splicing and Frameshifting^*

Fiana Levitin, Amos Baruch, Mordechai Weiss¶, Keren Stiegman, Mor-li Hartmann, Merav Yoeli-Lerner, Ravit Ziv, Sheila Zrihan-Licht, Sima Shina, Andrea Gat||, Beatrice Lifschitz||, Moshe Simha**, Yona Stadler**, Alina Cholostoy, Benny Gil, David Greaves, Iafa Keydar, Joseph Zaretsky, Nechama Smorodinsky, and Daniel H. Wreschner¶

From the Department of Cell Research and Immunology, Tel-Aviv University, Ramat Aviv 69978, Israel, ^||Department of Pathology, Sourasky-Ichilov Medical Center, Tel-Aviv 64239, Israel, ^**Surgical Department A, Sourasky-Ichilov Medical Center, Tel-Aviv 64239, Israel, ^¶Department of Endocrinology, Assaf Harofe Medical Center, Tzrifin 70300, Israel, and Department of Pathology, South Parks Road, Oxford University, Oxford OX1RE, United Kingdom

Genes that have been designated the name "MUC" code for proteins comprising mucin domains. These proteins may be involved in barrier and protective functions. The first such gene to be characterized and sequenced is the MUC1 gene. Here we report a novel small protein derived from the MUC1 gene by alternative splicing that does not contain the hallmark of mucin proteins, the mucin domain. This protein termed MUC1/ZD retains the same N-terminal MUC1 sequences as all of the other known MUC1 protein isoforms. The common N-terminal sequences comprise the signal peptide and a subsequent stretch of 30 amino acids. In contrast, the MUC1/ZD C-terminal 43 amino acids are novel and result from a reading frameshift engendered by a splicing event that forms MUC1/ZD. The expression of MUC1/ZD at the protein level in human tissues is demonstrated by Western blotting, immunohistochemistry, immunoprecipitation, and an ELISA. Utilization was made of affinity-purified MUC1/ZD-specific polyclonal antibodies as well as two different monoclonal antibodies that are monospecific for the MUC1/ZD protein. The MUC1/ZD protein is expressed in tissues as an oligomeric complex composed of monomers linked by disulfide bonds contributed by MUC1/ZD cysteine residues. MUC1/ZD protein expression did not parallel that of the tandem-repeat array-containing MUC1 protein. Results presented here demonstrate for the first time the expression of a novel MUC1 protein isoform MUC1/ZD, which is generated by an alternative splicing event that both deletes the tandem-repeat array and leads to a C-terminal reading frameshift.

Received for publication, June 22, 2004 , and in revised form, December 27, 2004.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBank^TM/EBI Data Bank with accession number(s) AY466157 (locus) and AAR287641 (protein).

^* This work was supported by U. S. Army Medical Research Grant DAMD 17-00-1-0451 (to D. H. W.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Both authors contributed equally to this work.

To whom correspondence should be addressed. Tel.: 972-3-6407425; Fax: 972-3-6422046; E-mail: danielhw{at}post.tau.ac.il.

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				F. Levitin, O. Stern, M. Weiss, C. Gil-Henn, R. Ziv, Z. Prokocimer, N. I. Smorodinsky, D. B. Rubinstein, and D. H. Wreschner The MUC1 SEA Module Is a Self-cleaving Domain J. Biol. Chem., September 30, 2005; 280(39): 33374 - 33386. [Abstract] [Full Text] [PDF]