Identification and partial characterization of the secreted form of the fourth component of human complement: evidence that it is different from major plasma form.

A. C. Chan, K. R. Mitchell, T. W. Munns, D. R. Karp, J. P. Atkinson

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Abstract

Immunoprecipitation of human C4 from plasma followed by NaDodSO4/polyacrylamide gel electrophoresis under reducing conditions revealed the expected alpha, beta, and gamma chains as well as a smaller quantity of a molecule containing an alpha chain (p98) approximately equal to 5,000 daltons heavier than the normal alpha chain. Further studies on p98 indicated that it covalently incorporated methyl-amine, was present at a concentration of approximately equal to 8% of the principal plasma form of the C4 alpha chain, and was found in highly purified C4 preparations. Hep G2, a human hepatoma-derived cell line, was found to secrete a C4 molecule in which the alpha chain had a molecular weight identical to that of the p98 protein found in plasma. The secreted C4 molecule possessed hemolytic activity. The 5,000-dalton difference in the alpha chain was localized to the COOH terminus and was attributed to an additional polypeptide. We propose that p98 is the alpha chain of the secreted form of C4, which is processed extracellularly by proteolytic cleavage to the principal C4 molecule found in plasma.

Original languageEnglish (US)
Pages (from-to)268-272
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume80
Issue number1
StatePublished - Jan 1983

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Immunoprecipitation
Amines
Polyacrylamide Gel Electrophoresis
Hepatocellular Carcinoma
Molecular Weight
Cell Line
Peptides
Proteins

ASJC Scopus subject areas

  • General
  • Genetics

Cite this

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title = "Identification and partial characterization of the secreted form of the fourth component of human complement: evidence that it is different from major plasma form.",
abstract = "Immunoprecipitation of human C4 from plasma followed by NaDodSO4/polyacrylamide gel electrophoresis under reducing conditions revealed the expected alpha, beta, and gamma chains as well as a smaller quantity of a molecule containing an alpha chain (p98) approximately equal to 5,000 daltons heavier than the normal alpha chain. Further studies on p98 indicated that it covalently incorporated methyl-amine, was present at a concentration of approximately equal to 8{\%} of the principal plasma form of the C4 alpha chain, and was found in highly purified C4 preparations. Hep G2, a human hepatoma-derived cell line, was found to secrete a C4 molecule in which the alpha chain had a molecular weight identical to that of the p98 protein found in plasma. The secreted C4 molecule possessed hemolytic activity. The 5,000-dalton difference in the alpha chain was localized to the COOH terminus and was attributed to an additional polypeptide. We propose that p98 is the alpha chain of the secreted form of C4, which is processed extracellularly by proteolytic cleavage to the principal C4 molecule found in plasma.",
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T1 - Identification and partial characterization of the secreted form of the fourth component of human complement

T2 - evidence that it is different from major plasma form.

AU - Chan, A. C.

AU - Mitchell, K. R.

AU - Munns, T. W.

AU - Karp, D. R.

AU - Atkinson, J. P.

PY - 1983/1

Y1 - 1983/1

N2 - Immunoprecipitation of human C4 from plasma followed by NaDodSO4/polyacrylamide gel electrophoresis under reducing conditions revealed the expected alpha, beta, and gamma chains as well as a smaller quantity of a molecule containing an alpha chain (p98) approximately equal to 5,000 daltons heavier than the normal alpha chain. Further studies on p98 indicated that it covalently incorporated methyl-amine, was present at a concentration of approximately equal to 8% of the principal plasma form of the C4 alpha chain, and was found in highly purified C4 preparations. Hep G2, a human hepatoma-derived cell line, was found to secrete a C4 molecule in which the alpha chain had a molecular weight identical to that of the p98 protein found in plasma. The secreted C4 molecule possessed hemolytic activity. The 5,000-dalton difference in the alpha chain was localized to the COOH terminus and was attributed to an additional polypeptide. We propose that p98 is the alpha chain of the secreted form of C4, which is processed extracellularly by proteolytic cleavage to the principal C4 molecule found in plasma.

AB - Immunoprecipitation of human C4 from plasma followed by NaDodSO4/polyacrylamide gel electrophoresis under reducing conditions revealed the expected alpha, beta, and gamma chains as well as a smaller quantity of a molecule containing an alpha chain (p98) approximately equal to 5,000 daltons heavier than the normal alpha chain. Further studies on p98 indicated that it covalently incorporated methyl-amine, was present at a concentration of approximately equal to 8% of the principal plasma form of the C4 alpha chain, and was found in highly purified C4 preparations. Hep G2, a human hepatoma-derived cell line, was found to secrete a C4 molecule in which the alpha chain had a molecular weight identical to that of the p98 protein found in plasma. The secreted C4 molecule possessed hemolytic activity. The 5,000-dalton difference in the alpha chain was localized to the COOH terminus and was attributed to an additional polypeptide. We propose that p98 is the alpha chain of the secreted form of C4, which is processed extracellularly by proteolytic cleavage to the principal C4 molecule found in plasma.

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