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Am J Physiol Heart Circ Physiol (November 14, 2002). doi:10.1152/ajpheart.00600.2002
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Articles in PresS, published online ahead of print November 14, 2002
Am J Physiol Heart Circ Physiol, 10.1152/ajpheart.00600.2002
Submitted on July 15, 2002
Accepted on November 13, 2002

The tissue specific distribution of alternatively spliced human PECAM-1 Isoforms

Yongji Wang1, Xiaojing Su1, Christine M Sorenson2, and Nader Sheibani3*

1 Department of Ophthalmology and Visual Sciences, University of Wisconsin, Madison, WI, USA
2 Department of Pediatrics, University of Wisconsin, Madison, WI, USA
3 Department of Ophthalmology and Visual Sciences, University of Wisconsin, Madison, WI, USA; Department of Pharmacology, University of Wisconsin, Madison, WI, USA

* To whom correspondence should be addressed. E-mail: nsheibanikar{at}facstaff.wisc.edu.

PECAM-1 is a cell adhesion molecule that is highly expressed on the surface of endothelial cells and some hematopoietic cells. Its cytoplasmic domain is encoded by multiple exons, which undergoes alternative splicing. Here, we demonstrate that the human PECAM-1 cytoplasmic domain undergoes alternative splicing generating six different isoforms. RT-PCR cloning and DNA sequence analysis indicated that human tissue and endothelial cells express multiple isoforms of PECAM-1 including the full length PECAM-1 and five other isoforms, which lack exons 12, 13, 14, 15, or 14&15. The full length PECAM-1 is the predominant isoform detected in human tissue and endothelial cells. This is in contrast to murine endothelium in which the PECAM-1 isoform lacking exon 14&15 ({Delta}14&15) is the predominant isoform. The {Delta}13 PECAM-1 isoform detected in human tissue and endothelial cells, is absent in murine endothelium. The expression pattern of PECAM-1 isoforms changed during tube formation of endothelial cells on Matrigel, which may indicate specialized roles for specific isoforms of PECAM-1 during angiogenesis. The data presented here demonstrate that the human PECAM-1 undergoes alternative splicing generating multiple isoforms in vascular beds of various tissues. Therefore, the regulated expression of these isoforms may influence endothelial cell adhesive properties during angiogenesis and/or vasculogenesis.




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