Biosynthesis and in vitro translation of the major surfactant-associated protein from human lung

Joanna Floros, David Phelps, H. W. Taeusch

Research output: Contribution to journalArticle

47 Citations (Scopus)

Abstract

We have characterized a 32,000-36,000-dalton sialoglycoprotein group that is an integral component of the lipoprotein complex called pulmonary surfactant. Our results from the cell-free translation of human lung RNA show that this protein consists of two similarly-sized precursor components of about 29,000-31,000 daltons. Tunicamycin treatment of the lung tissue prevents formation of the normal protein and results in the accumulation of these precursor components which are also seen under normal conditions in very small amounts. Although in vitro translation in the presence of dog pancreatic microsomes suggests that a cleavable signal peptide sequence is present in these precursor molecules, it does not appear that this cleavage occurs in vivo.

Original languageEnglish (US)
Pages (from-to)495-500
Number of pages6
JournalJournal of Biological Chemistry
Volume260
Issue number1
StatePublished - Jan 1 1985

Fingerprint

Biosynthesis
Surface-Active Agents
Sialoglycoproteins
Pulmonary Surfactants
Tunicamycin
Lung
Protein Sorting Signals
Microsomes
Lipoproteins
Proteins
Dogs
RNA
Tissue
Molecules
In Vitro Techniques

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

@article{47c2334326e7464582e25cad7659f011,
title = "Biosynthesis and in vitro translation of the major surfactant-associated protein from human lung",
abstract = "We have characterized a 32,000-36,000-dalton sialoglycoprotein group that is an integral component of the lipoprotein complex called pulmonary surfactant. Our results from the cell-free translation of human lung RNA show that this protein consists of two similarly-sized precursor components of about 29,000-31,000 daltons. Tunicamycin treatment of the lung tissue prevents formation of the normal protein and results in the accumulation of these precursor components which are also seen under normal conditions in very small amounts. Although in vitro translation in the presence of dog pancreatic microsomes suggests that a cleavable signal peptide sequence is present in these precursor molecules, it does not appear that this cleavage occurs in vivo.",
author = "Joanna Floros and David Phelps and Taeusch, {H. W.}",
year = "1985",
month = "1",
day = "1",
language = "English (US)",
volume = "260",
pages = "495--500",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "1",

}

Biosynthesis and in vitro translation of the major surfactant-associated protein from human lung. / Floros, Joanna; Phelps, David; Taeusch, H. W.

In: Journal of Biological Chemistry, Vol. 260, No. 1, 01.01.1985, p. 495-500.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Biosynthesis and in vitro translation of the major surfactant-associated protein from human lung

AU - Floros, Joanna

AU - Phelps, David

AU - Taeusch, H. W.

PY - 1985/1/1

Y1 - 1985/1/1

N2 - We have characterized a 32,000-36,000-dalton sialoglycoprotein group that is an integral component of the lipoprotein complex called pulmonary surfactant. Our results from the cell-free translation of human lung RNA show that this protein consists of two similarly-sized precursor components of about 29,000-31,000 daltons. Tunicamycin treatment of the lung tissue prevents formation of the normal protein and results in the accumulation of these precursor components which are also seen under normal conditions in very small amounts. Although in vitro translation in the presence of dog pancreatic microsomes suggests that a cleavable signal peptide sequence is present in these precursor molecules, it does not appear that this cleavage occurs in vivo.

AB - We have characterized a 32,000-36,000-dalton sialoglycoprotein group that is an integral component of the lipoprotein complex called pulmonary surfactant. Our results from the cell-free translation of human lung RNA show that this protein consists of two similarly-sized precursor components of about 29,000-31,000 daltons. Tunicamycin treatment of the lung tissue prevents formation of the normal protein and results in the accumulation of these precursor components which are also seen under normal conditions in very small amounts. Although in vitro translation in the presence of dog pancreatic microsomes suggests that a cleavable signal peptide sequence is present in these precursor molecules, it does not appear that this cleavage occurs in vivo.

UR - http://www.scopus.com/inward/record.url?scp=0021954324&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0021954324&partnerID=8YFLogxK

M3 - Article

C2 - 3838094

AN - SCOPUS:0021954324

VL - 260

SP - 495

EP - 500

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 1

ER -