Hydrophobic surfactant-associated proteins: Electrophoretic and immunologic analyses and cellular localization in human lung

S. L. Katyal, Gurmukh Singh, Lisa Ryan, Shirley Gottron

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

Pulmonary surfactant isolated from a number of animal species contains a protein of molecular weight 38,000 and several very hydrophobic proteins soluble in solvents often used to extract lipids. Although found to be intimately associated with surfactant lipids, localization of the very hydrophobic proteins to alveolar epithelial type II cells, the cells involved in the synthesis and secretion of pulmonary surfactant, has not been demonstrated. Hydrophobic proteins were extracted along with lipids from human surfactant, and, after extraction with deoxycholate, were used to raise an antiserum. The antiserum was characterized by the immunoblotting (" Western" technique, using blots of pulmonary surfactant, and of hydrophobic proteins prepared by deoxycholate extraction and by Sephadex LH-20 chromatography. The antiserum shows reactivity to a 6.5-to 18-kDa surfactant-associated hydrophobic protein, which appears to be the major component of deoxycholate extracted proteins, and has Phe as the N-terminal amino acid. In addition, 28-kDa, 40-kDa, 50-kDa, and 70-kDa bands (chemically unreduced) are seen in human pulmonary surfactant. Whether these bands represent precursors of the major surfactant-associated hydrophobic proteins, different proteolytic cleavage products of the precursor protein, distinct proteins, or associated forms of the same protein is not yet clear. When used in the immunoperoxidase staining of human lung sections, the antiserum yielded a staining pattern identical to that obtained by the use of an antiserum to the 35-kDa surfactant protein. The number, size, and location of the stained cells are consistent with their being the alveolar epithelial type II cells.

Original languageEnglish (US)
Pages (from-to)655-669
Number of pages15
JournalExperimental Lung Research
Volume14
Issue number5
DOIs
StatePublished - Jan 1 1988
Externally publishedYes

Fingerprint

Surface-Active Agents
Lung
Pulmonary Surfactants
Immune Sera
Proteins
Deoxycholic Acid
Alveolar Epithelial Cells
Lipids
Pulmonary Surfactant-Associated Proteins
Staining and Labeling
Protein Precursors
Chromatography
Molecular Weight
Western Blotting
Animals
Molecular weight
Amino Acids

ASJC Scopus subject areas

  • Molecular Biology
  • Pulmonary and Respiratory Medicine
  • Clinical Biochemistry

Cite this

Hydrophobic surfactant-associated proteins : Electrophoretic and immunologic analyses and cellular localization in human lung. / Katyal, S. L.; Singh, Gurmukh; Ryan, Lisa; Gottron, Shirley.

In: Experimental Lung Research, Vol. 14, No. 5, 01.01.1988, p. 655-669.

Research output: Contribution to journalArticle

@article{343bfd3ac118476792daeb86851b5f94,
title = "Hydrophobic surfactant-associated proteins: Electrophoretic and immunologic analyses and cellular localization in human lung",
abstract = "Pulmonary surfactant isolated from a number of animal species contains a protein of molecular weight 38,000 and several very hydrophobic proteins soluble in solvents often used to extract lipids. Although found to be intimately associated with surfactant lipids, localization of the very hydrophobic proteins to alveolar epithelial type II cells, the cells involved in the synthesis and secretion of pulmonary surfactant, has not been demonstrated. Hydrophobic proteins were extracted along with lipids from human surfactant, and, after extraction with deoxycholate, were used to raise an antiserum. The antiserum was characterized by the immunoblotting ({"} Western{"} technique, using blots of pulmonary surfactant, and of hydrophobic proteins prepared by deoxycholate extraction and by Sephadex LH-20 chromatography. The antiserum shows reactivity to a 6.5-to 18-kDa surfactant-associated hydrophobic protein, which appears to be the major component of deoxycholate extracted proteins, and has Phe as the N-terminal amino acid. In addition, 28-kDa, 40-kDa, 50-kDa, and 70-kDa bands (chemically unreduced) are seen in human pulmonary surfactant. Whether these bands represent precursors of the major surfactant-associated hydrophobic proteins, different proteolytic cleavage products of the precursor protein, distinct proteins, or associated forms of the same protein is not yet clear. When used in the immunoperoxidase staining of human lung sections, the antiserum yielded a staining pattern identical to that obtained by the use of an antiserum to the 35-kDa surfactant protein. The number, size, and location of the stained cells are consistent with their being the alveolar epithelial type II cells.",
author = "Katyal, {S. L.} and Gurmukh Singh and Lisa Ryan and Shirley Gottron",
year = "1988",
month = "1",
day = "1",
doi = "10.3109/01902148809087835",
language = "English (US)",
volume = "14",
pages = "655--669",
journal = "Experimental Lung Research",
issn = "0190-2148",
publisher = "Informa Healthcare",
number = "5",

}

TY - JOUR

T1 - Hydrophobic surfactant-associated proteins

T2 - Electrophoretic and immunologic analyses and cellular localization in human lung

AU - Katyal, S. L.

AU - Singh, Gurmukh

AU - Ryan, Lisa

AU - Gottron, Shirley

PY - 1988/1/1

Y1 - 1988/1/1

N2 - Pulmonary surfactant isolated from a number of animal species contains a protein of molecular weight 38,000 and several very hydrophobic proteins soluble in solvents often used to extract lipids. Although found to be intimately associated with surfactant lipids, localization of the very hydrophobic proteins to alveolar epithelial type II cells, the cells involved in the synthesis and secretion of pulmonary surfactant, has not been demonstrated. Hydrophobic proteins were extracted along with lipids from human surfactant, and, after extraction with deoxycholate, were used to raise an antiserum. The antiserum was characterized by the immunoblotting (" Western" technique, using blots of pulmonary surfactant, and of hydrophobic proteins prepared by deoxycholate extraction and by Sephadex LH-20 chromatography. The antiserum shows reactivity to a 6.5-to 18-kDa surfactant-associated hydrophobic protein, which appears to be the major component of deoxycholate extracted proteins, and has Phe as the N-terminal amino acid. In addition, 28-kDa, 40-kDa, 50-kDa, and 70-kDa bands (chemically unreduced) are seen in human pulmonary surfactant. Whether these bands represent precursors of the major surfactant-associated hydrophobic proteins, different proteolytic cleavage products of the precursor protein, distinct proteins, or associated forms of the same protein is not yet clear. When used in the immunoperoxidase staining of human lung sections, the antiserum yielded a staining pattern identical to that obtained by the use of an antiserum to the 35-kDa surfactant protein. The number, size, and location of the stained cells are consistent with their being the alveolar epithelial type II cells.

AB - Pulmonary surfactant isolated from a number of animal species contains a protein of molecular weight 38,000 and several very hydrophobic proteins soluble in solvents often used to extract lipids. Although found to be intimately associated with surfactant lipids, localization of the very hydrophobic proteins to alveolar epithelial type II cells, the cells involved in the synthesis and secretion of pulmonary surfactant, has not been demonstrated. Hydrophobic proteins were extracted along with lipids from human surfactant, and, after extraction with deoxycholate, were used to raise an antiserum. The antiserum was characterized by the immunoblotting (" Western" technique, using blots of pulmonary surfactant, and of hydrophobic proteins prepared by deoxycholate extraction and by Sephadex LH-20 chromatography. The antiserum shows reactivity to a 6.5-to 18-kDa surfactant-associated hydrophobic protein, which appears to be the major component of deoxycholate extracted proteins, and has Phe as the N-terminal amino acid. In addition, 28-kDa, 40-kDa, 50-kDa, and 70-kDa bands (chemically unreduced) are seen in human pulmonary surfactant. Whether these bands represent precursors of the major surfactant-associated hydrophobic proteins, different proteolytic cleavage products of the precursor protein, distinct proteins, or associated forms of the same protein is not yet clear. When used in the immunoperoxidase staining of human lung sections, the antiserum yielded a staining pattern identical to that obtained by the use of an antiserum to the 35-kDa surfactant protein. The number, size, and location of the stained cells are consistent with their being the alveolar epithelial type II cells.

UR - http://www.scopus.com/inward/record.url?scp=0023734058&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0023734058&partnerID=8YFLogxK

U2 - 10.3109/01902148809087835

DO - 10.3109/01902148809087835

M3 - Article

C2 - 3066613

AN - SCOPUS:0023734058

VL - 14

SP - 655

EP - 669

JO - Experimental Lung Research

JF - Experimental Lung Research

SN - 0190-2148

IS - 5

ER -