Immunochemical studies of the plasma and cultured fibroblast media fractions containing the cystic fibrosis ciliary inhibitor

The cystic fibrosis ciliary inhibitor (CFCI) has been fractionated from plasma of cystic fibrosis (CF) homozygotes and from the media of cultured fibroblasts derived from CF homozygotes. Plasma and fibroblast media from normal controls have been fractionated in an identical manner. Fractions from pl...

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Bibliographic Details
Published inTexas reports on biology and medicine Vol. 34; no. 1; p. 73
Main Authors Harper, B L, Barnett, D R, Bissett, J D
Format Journal Article
LanguageEnglish
Published United States 1976
Subjects
Animals
Blood Proteins - analysis
Cilia - physiology
Culture Media
Cystic Fibrosis - blood
Cystic Fibrosis - metabolism
Fibroblasts - metabolism
Hemagglutination Tests
Homozygote
Humans
Immune Sera
Immunoglobulin G - analysis
Lipoproteins, HDL - analysis
Lipoproteins, LDL - analysis
Rabbits
Serum Albumin - analysis
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Summary:The cystic fibrosis ciliary inhibitor (CFCI) has been fractionated from plasma of cystic fibrosis (CF) homozygotes and from the media of cultured fibroblasts derived from CF homozygotes. Plasma and fibroblast media from normal controls have been fractionated in an identical manner. Fractions from plasma and fibroblast culture media that demonstrate ciliary inhibitory activity contain several proteins in a molecular weight range of approximately 5,000-11,000. These proteins have been partially characterized by immunochemical analysis with antisera to 33 human serum proteins. Immunological determinants of albumin, C3 (but not C3a), C4, C5, alpha1-lipoprotein, beta-lipoprotein, beta2-microglobulin and immunoglobulin light chains have been detected by hemagglutination in fractions of CF plasma that inhibited ciliary activity and in analogous fractions from normal sera. None of the proteins were detected in media of cultured fibroblasts from either genotype. Since the same proteins and protein fragments were identified in both CF and normal plasma fractions, and were not detected in CF fibroblast media, it appears that none of these proteins can be identified as the CFCI. Identification of these proteins will permit further purification of the CFCI by immunochemical methods.
ISSN:0040-4675