Insulin-like growth factor (IGF) binding protein complementary deoxyribonucleic acid from human HEP G2 hepatoma cells

predicted protein sequence suggests an IGF binding domain different from those of the IGF-I and IGF-II receptors

Y. L. Lee, R. L. Hintz, P. M. James, Phillip Lee, J. E. Shively, D. R. Powell

Research output: Contribution to journalArticle

191 Citations (Scopus)

Abstract

The primary structure of an insulin-like growth factor (IGF) binding protein produced by human HEP G2 hepatoma cells has been deduced from the cDNA sequence. The 234 amino acid protein has a predicted molecular mass of 25,274 and contains a single, distinctive cysteine-rich region. The N-terminal sequence of this protein is quite similar to the limited sequence data available for a rat IGF binding protein produced by BRL-3A cells and suggests a common ancestral origin. In contrast, the HEP G2 IGF binding protein sequence bears no similarity to the N-terminal 15 amino acids of a 53 kilodalton binding protein purified from human plasma. Comparison of full-length protein sequences for the IGF-I and IGF-II receptors with that of the HEP G2 IGF binding protein also fails to demonstrate any significant similarities among these three proteins, and suggests that each contains a unique binding domain for the IGF peptides.

Original languageEnglish (US)
Pages (from-to)401-411
Number of pages11
JournalMolecular Endocrinology
Volume2
Issue number5
StatePublished - 1988
Externally publishedYes

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IGF Type 2 Receptor
Insulin-Like Growth Factor Binding Proteins
Somatomedins
Insulin-Like Growth Factor I
Hepatocellular Carcinoma
DNA
Proteins
Amino Acids
Cysteine
Carrier Proteins
Complementary DNA
Peptides

ASJC Scopus subject areas

  • Molecular Biology
  • Endocrinology, Diabetes and Metabolism

Cite this

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title = "Insulin-like growth factor (IGF) binding protein complementary deoxyribonucleic acid from human HEP G2 hepatoma cells: predicted protein sequence suggests an IGF binding domain different from those of the IGF-I and IGF-II receptors",
abstract = "The primary structure of an insulin-like growth factor (IGF) binding protein produced by human HEP G2 hepatoma cells has been deduced from the cDNA sequence. The 234 amino acid protein has a predicted molecular mass of 25,274 and contains a single, distinctive cysteine-rich region. The N-terminal sequence of this protein is quite similar to the limited sequence data available for a rat IGF binding protein produced by BRL-3A cells and suggests a common ancestral origin. In contrast, the HEP G2 IGF binding protein sequence bears no similarity to the N-terminal 15 amino acids of a 53 kilodalton binding protein purified from human plasma. Comparison of full-length protein sequences for the IGF-I and IGF-II receptors with that of the HEP G2 IGF binding protein also fails to demonstrate any significant similarities among these three proteins, and suggests that each contains a unique binding domain for the IGF peptides.",
author = "Lee, {Y. L.} and Hintz, {R. L.} and James, {P. M.} and Phillip Lee and Shively, {J. E.} and Powell, {D. R.}",
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T1 - Insulin-like growth factor (IGF) binding protein complementary deoxyribonucleic acid from human HEP G2 hepatoma cells

T2 - predicted protein sequence suggests an IGF binding domain different from those of the IGF-I and IGF-II receptors

AU - Lee, Y. L.

AU - Hintz, R. L.

AU - James, P. M.

AU - Lee, Phillip

AU - Shively, J. E.

AU - Powell, D. R.

PY - 1988

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AB - The primary structure of an insulin-like growth factor (IGF) binding protein produced by human HEP G2 hepatoma cells has been deduced from the cDNA sequence. The 234 amino acid protein has a predicted molecular mass of 25,274 and contains a single, distinctive cysteine-rich region. The N-terminal sequence of this protein is quite similar to the limited sequence data available for a rat IGF binding protein produced by BRL-3A cells and suggests a common ancestral origin. In contrast, the HEP G2 IGF binding protein sequence bears no similarity to the N-terminal 15 amino acids of a 53 kilodalton binding protein purified from human plasma. Comparison of full-length protein sequences for the IGF-I and IGF-II receptors with that of the HEP G2 IGF binding protein also fails to demonstrate any significant similarities among these three proteins, and suggests that each contains a unique binding domain for the IGF peptides.

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