Genomic organization and biosynthesis of secreted and cytoplasmic forms of gelsolin

D. J. Kwiatkowski, R. Mehl, H. L. Yin

Research output: Contribution to journalArticlepeer-review

120 Scopus citations

Abstract

Gelsolin is an actin regulatory protein which is unique among vertebrates in that it is found as both an intrinsic cytoplasmic protein and as a secreted plasma protein. We demonstrate that plasma and cytoplasmic gelsolins are derived by alternative transcriptional initiation sites and message processing from a single gene 70 kb long, containing at least 14 exons. Their message and amino acid sequences are identical except at the 5' end/NH2 termini. The cytoplasmic-specific 5' sequence is derived from two exons that encode untranslated sequence, while the plasma message-specific 5' sequence is derived from a single exon that encodes untranslated sequence, the signal peptide, and the first 21 residues of the plasma protein. The two transcriptional initiation sites are separated by ≥32 kb. Biosynthetic and RNase protection studies indicate that a number of cell types make both plasma and cytoplasmic gelsolin in widely varying amounts and ratios.

Original languageEnglish (US)
Pages (from-to)375-384
Number of pages10
JournalJournal of Cell Biology
Volume106
Issue number2
DOIs
StatePublished - 1988

ASJC Scopus subject areas

  • Cell Biology

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