Immunological Evidence for an Inactive Precursor of Collagen Proline Hydroxylase in Cultured Fibroblasts

A specific antibody to rat collagen proline hydroxylase has been used to measure the amount of ``enzyme'' protein in cultured mouse fibroblasts (L-929 cells) during normal growth, and under other conditions that cause an increase in enzyme activity. Collagen proline hydroxylase activity pe...

Full description

Saved in:
Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1971-07, Vol.68 (7), p.1585-1589
Main Authors: James O'D. Mc Gee, Langness, Uwe, Udenfriend, Sidney
Format: Article
Language:English
Subjects:
Animals
Antibodies
Antigen-Antibody Reactions
Antiserum
Binding Sites
Biological Sciences: Biochemistry
Cell growth
Chemical Precipitation
Chromatography, Gel
Chromatography, Ion Exchange
Collagen
Collagens
Cross Reactions
Cultured cells
Electrophoresis
Enzyme activity
Enzyme Precursors - analysis
Enzymes
Fibroblasts
Fibroblasts - drug effects
Fibroblasts - enzymology
Fibroblasts - growth & development
Goats
Immune Sera
Immunodiffusion
Immunoelectrophoresis
Immunology
Lactates
Lactates - pharmacology
Mice
Mixed Function Oxygenases - antagonists & inhibitors
Mixed Function Oxygenases - biosynthesis
Mixed Function Oxygenases - isolation & purification
Proline
Quaternary Ammonium Compounds
Rats
Skin - enzymology
Species Specificity
Sulfates
Citations: Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:A specific antibody to rat collagen proline hydroxylase has been used to measure the amount of ``enzyme'' protein in cultured mouse fibroblasts (L-929 cells) during normal growth, and under other conditions that cause an increase in enzyme activity. Collagen proline hydroxylase activity per mg of cell protein increased 24-fold as the cells progressed through the logarithmic to the stationary phase of growth, while the cellular concentration of immunologically reactive protein changed only slightly. Similar results were obtained with cells in early log phase in which enzyme activity was stimulated several-fold by cell concentration or lactate treatment without a corresponding change in cellular antigen. It has also been shown that the enzymatically inactive antigen in these fibroblasts competes effectively for antibody-binding sites with partially purified enzyme. It is concluded that early-log-phase fibroblasts contain an inactive form of collagen proline hydroxylase which may be a precursor of the functional enzyme.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.68.7.1585