In vitro processing of tropoelastin: Investigation of a possible transport function associated with the carboxy-terminal domain

Leonard E. Grosso, Robert P. Mecham

Research output: Contribution to journalArticlepeer-review

10 Scopus citations

Abstract

In vitro translation systems were used to characterize the processing of bovine tropoelastin isoforms and to investigate the possibility that the carboxy-terminal 19 amino acids of tropoelastin encode a molecular domain that directs intracellular transport. Immuno-precipitation with domain-specific antibodies demonstrated that multiple tropoelastin isoforms corresponding to those identified in tissue and cell culture studies were correctly translated and were processed by dog pancreas microsomes. Our results demonstrate that all tropoelastin isoforms are translocated completely into the microsomal vesicle and do not remain associated with the microsomal membrane. These results exclude the possibility that the carboxy-terminal domain of tropoelastin functions as a trafficking signal by effecting an association between tropoelastin and an intracellular membraneous compartment.

Original languageEnglish
Pages (from-to)545-551
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume153
Issue number2
DOIs
StatePublished - Jun 16 1988

Fingerprint

Dive into the research topics of 'In vitro processing of tropoelastin: Investigation of a possible transport function associated with the carboxy-terminal domain'. Together they form a unique fingerprint.

Cite this