Genomic organization and biosynthesis of secreted and cytoplasmic forms of gelsolin

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

Research output: Contribution to journalArticle

119 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 - Jan 1 1988

ASJC Scopus subject areas

  • Cell Biology

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