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Published ahead of print on January 23, 2004, doi:10.1165/rcmb.2003-0330OC

Am. J. Respir. Cell Mol. Biol., Volume 31, Number 1, July 2004, 13-21

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Submitted on September 9, 2003
Revised on January 23, 2004

The splicing and fate of ADAM33 transcripts in primary human airways fibroblasts

Robert M Powell1*, James Wicks1, John W Holloway1, Stephen T Holgate1, and Davies E Donna1

1 RCMB, Southampton University, Southampton, United Kingdom

* To whom correspondence should be addressed. E-mail: rmp2{at}soton.ac.uk.

The ADAM (A Disintegrin And Metalloprotease) family of Zn++-dependent metalloproteases are multi-domain proteins involved in diverse cellular activities. Polymorphic variation in ADAM33 is strongly associated with asthma and bronchial hyperresponsiveness. Identification of those isoforms of ADAM33 that are expressed in airways is fundamental to dissecting the role of ADAM33 in asthma. Analysis of primary human airways fibroblasts has shown the presence of a number of alternatively spliced forms of ADAM33, including one encoding a putative secreted variant, and many transcripts lacking the metalloproteinase (MP) domain. The relative abundance of these transcripts has been quantified using reverse transcription real-time PCR, in both nuclear and cytoplasmic fractions of RNA. These results demonstrate that a number of splice variants of ADAM33 are transported into the cytoplasm. 90% of ADAM33 mRNA is retained in the nucleus and the subtle differences in the composition of nuclear and cytoplasmic RNA suggest important events in the splicing and selection of ADAM33 transcripts. Western blot analysis confirmed that several protein isoforms of ADAM33 are expressed in primary airways fibroblasts. These findings demonstrate that ADAM33 exists in multiple isoforms, suggesting that it is a complex molecule that plays multiple roles within mesenchymal cells.




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