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Title: Receptors for transforming growth factor-beta (TGF-beta) on rat lung fibroblasts have higher affinity for TGF-beta 1 than for TGF-beta 2

Abstract

Most cell types have receptors for transforming growth factor-beta (TGF-beta) and respond similarly to TGF-beta 1 and TGF-beta 2. We have demonstrated the presence of a single class of high-affinity receptors (approximately 10,000 sites/cell) for TGF-beta 1 (Kd = 23 pM) and TGF-beta 2 (Kd = 41 pM) on early-passage rat lung fibroblasts (RLF). Incubation with unlabeled TGF-beta 1 and TGF-beta 2 resulted in concentration-dependent inhibition of binding of 15 pM ({sup 125}I)TGF-beta 1 (ED50, 20 and 28 pM, respectively) and ({sup 125}I)TGF-beta 2 (ED50, 36 and 56 pM, respectively). TGF-beta receptors affinity-cross-linked with 100 pM ({sup 125}I)TGF-beta 1 or ({sup 125}I)TGF-beta 2 were subjected to sodium dodecyl sulfate polyacrylamide gel electrophoresis and exhibited labeled protein bands of 68, 88, and 286 kD. Densitometric analysis of the resulting autoradiograms showed that the different molecular weight TGF-beta binding proteins exhibited separate affinities for the two forms of TGF-beta. Both TGF-beta 1 and TGF-beta 2 altered the morphology and cytoskeleton of RLF in a similar manner, but TGF-beta 1 was more potent than TGF-beta 2 in the inhibition of RLF growth and colony formation, with 50% inhibition by 0.12 pM TGF-beta 1 and 4.4 pM TGF-beta 2. Different affinities for the TGF-betamore » s may indicate selectivity among the receptor subtypes with regard to the biologic responsiveness of RLF to TGF-beta s. We believe this to be the first demonstration of biologically responsive TGF-beta receptors with different affinities for TGF-beta 1 and TGF-beta 2 on cells derived from normal, nonimmortal RLF. In establishing the basic mechanisms of pulmonary fibrosis, it will be essential to understand the biology and biochemistry of the receptors that may control cell division and production of extracellular matrix components by fibroblasts.« less

Authors:
;  [1]
  1. National Institute of Environmental Health Sciences, Research Triangle Park, NC (USA)
Publication Date:
OSTI Identifier:
5735104
Resource Type:
Journal Article
Journal Name:
American Journal of Respiratory Cell and Molecular Biology; (USA)
Additional Journal Information:
Journal Volume: 4:5; Journal ID: ISSN 1044-1549
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; GROWTH FACTORS; RECEPTORS; BIOCHEMICAL REACTION KINETICS; AFFINITY; AUTORADIOGRAPHY; COLONY FORMATION; ELECTROPHORESIS; FIBROBLASTS; IODINE 125; LUNGS; MOLECULAR WEIGHT; RATS; ANIMAL CELLS; ANIMALS; BETA DECAY RADIOISOTOPES; BODY; CONNECTIVE TISSUE CELLS; DAYS LIVING RADIOISOTOPES; ELECTRON CAPTURE RADIOISOTOPES; INTERMEDIATE MASS NUCLEI; INTERNAL CONVERSION RADIOISOTOPES; IODINE ISOTOPES; ISOTOPES; KINETICS; MAMMALS; MEMBRANE PROTEINS; MITOGENS; NUCLEI; ODD-EVEN NUCLEI; ORGANIC COMPOUNDS; ORGANS; PROTEINS; RADIOISOTOPES; REACTION KINETICS; RESPIRATORY SYSTEM; RODENTS; SOMATIC CELLS; VERTEBRATES; 550201* - Biochemistry- Tracer Techniques

Citation Formats

Kalter, V G, and Brody, A R. Receptors for transforming growth factor-beta (TGF-beta) on rat lung fibroblasts have higher affinity for TGF-beta 1 than for TGF-beta 2. United States: N. p., 1991. Web. doi:10.1165/ajrcmb/4.5.397.
Kalter, V G, & Brody, A R. Receptors for transforming growth factor-beta (TGF-beta) on rat lung fibroblasts have higher affinity for TGF-beta 1 than for TGF-beta 2. United States. https://doi.org/10.1165/ajrcmb/4.5.397
Kalter, V G, and Brody, A R. 1991. "Receptors for transforming growth factor-beta (TGF-beta) on rat lung fibroblasts have higher affinity for TGF-beta 1 than for TGF-beta 2". United States. https://doi.org/10.1165/ajrcmb/4.5.397.
@article{osti_5735104,
title = {Receptors for transforming growth factor-beta (TGF-beta) on rat lung fibroblasts have higher affinity for TGF-beta 1 than for TGF-beta 2},
author = {Kalter, V G and Brody, A R},
abstractNote = {Most cell types have receptors for transforming growth factor-beta (TGF-beta) and respond similarly to TGF-beta 1 and TGF-beta 2. We have demonstrated the presence of a single class of high-affinity receptors (approximately 10,000 sites/cell) for TGF-beta 1 (Kd = 23 pM) and TGF-beta 2 (Kd = 41 pM) on early-passage rat lung fibroblasts (RLF). Incubation with unlabeled TGF-beta 1 and TGF-beta 2 resulted in concentration-dependent inhibition of binding of 15 pM ({sup 125}I)TGF-beta 1 (ED50, 20 and 28 pM, respectively) and ({sup 125}I)TGF-beta 2 (ED50, 36 and 56 pM, respectively). TGF-beta receptors affinity-cross-linked with 100 pM ({sup 125}I)TGF-beta 1 or ({sup 125}I)TGF-beta 2 were subjected to sodium dodecyl sulfate polyacrylamide gel electrophoresis and exhibited labeled protein bands of 68, 88, and 286 kD. Densitometric analysis of the resulting autoradiograms showed that the different molecular weight TGF-beta binding proteins exhibited separate affinities for the two forms of TGF-beta. Both TGF-beta 1 and TGF-beta 2 altered the morphology and cytoskeleton of RLF in a similar manner, but TGF-beta 1 was more potent than TGF-beta 2 in the inhibition of RLF growth and colony formation, with 50% inhibition by 0.12 pM TGF-beta 1 and 4.4 pM TGF-beta 2. Different affinities for the TGF-beta s may indicate selectivity among the receptor subtypes with regard to the biologic responsiveness of RLF to TGF-beta s. We believe this to be the first demonstration of biologically responsive TGF-beta receptors with different affinities for TGF-beta 1 and TGF-beta 2 on cells derived from normal, nonimmortal RLF. In establishing the basic mechanisms of pulmonary fibrosis, it will be essential to understand the biology and biochemistry of the receptors that may control cell division and production of extracellular matrix components by fibroblasts.},
doi = {10.1165/ajrcmb/4.5.397},
url = {https://www.osti.gov/biblio/5735104}, journal = {American Journal of Respiratory Cell and Molecular Biology; (USA)},
issn = {1044-1549},
number = ,
volume = 4:5,
place = {United States},
year = {Wed May 01 00:00:00 EDT 1991},
month = {Wed May 01 00:00:00 EDT 1991}
}