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Halofuginone: An inhibitor of collagen type I synthesis
Year:
1993
Source of publication :
BBA - General Subjects
Authors :
Granot, Irit
;
.
Hurvitz, Shmuel (Animal science)
;
.
Pines, Mark
;
.
Volume :
1156
Co-Authors:
Granot, I., Institute of Animal Science, Agricultural Research Organization, The Volcani Center, Bet Dagan, Israel
Halevy, O., Department of Animal Science, Faculty of Agriculture, The Hebrew University of Jerusalem, Rehovot, Israel
Hurwitz, S., Institute of Animal Science, Agricultural Research Organization, The Volcani Center, Bet Dagan, Israel
Pines, M., Institute of Animal Science, Agricultural Research Organization, The Volcani Center, Bet Dagan, Israel
Facilitators :
From page:
107
To page:
112
(
Total pages:
6
)
Abstract:
The effect of halofuginone - a plant alkaloid used as a coccidiostat in birds - on collagen metabolism was studied in various avian and mammalian cell cultures. In avian skin fibroblasts halofuginone attenuated the incorporation of [3H]proline into collagenase-digestible proteins (CDP) at concentrations as low as 10-11 M, without affecting production of [3H]collagenase-non-digestible proteins (NCDP), cell proliferation or collagen degradation. Halofuginine depressed specifically the expression of α1 gene of collagen type I but not that of collagen type II. This was demonstrated in skin fibroblasts and growth-plate chondrocytes using probes containing inserts sequences corresponding to the α1(I) and α1(II) mRNAs. A slight inhibition of the expression of α2(I) was observed in avian skin fibroblasts but not in growth-plate chondrocytes. The inhibition of gene expression of both polypeptides of collagen type I in skin fibroblasts resulted in a decrease in synthesis, as demonstrated by immunoprecipitation with specific type I collagen antiserum. In primary cultures of mouse skin fibroblasts, avian epiphyseal growth plate chondrocytes and a rat embryo cell line - all of which produce and secrete collagen type I - halofuginone inhibited the incorporation of [3H]proline into CDP, the Rat-1 line being the most sensitive to the drug. These results suggest that halofuginone affects specifically type I collagen synthesis by repressing gene-expression. The need for extremely low concentrations of halofuginone to inhibit collagen type I synthesis, regardless of the tissue or animal species, contributes to the potential usefulness of the substance in studying collagen metabolism. © 1993.
Note:
Related Files :
Animal
animal cell
bird
Cell Division
Coccidiostats
Collagenases
embryo
gene expression
Growth plate
mice
Quinazolines
Show More
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More details
DOI :
10.1016/0304-4165(93)90123-P
Article number:
0
Affiliations:
Database:
Scopus
Publication Type:
article
;
.
Language:
English
Editors' remarks:
ID:
27099
Last updated date:
21/08/2022 07:45
Creation date:
17/04/2018 00:28
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Scientific Publication
Halofuginone: An inhibitor of collagen type I synthesis
1156
Granot, I., Institute of Animal Science, Agricultural Research Organization, The Volcani Center, Bet Dagan, Israel
Halevy, O., Department of Animal Science, Faculty of Agriculture, The Hebrew University of Jerusalem, Rehovot, Israel
Hurwitz, S., Institute of Animal Science, Agricultural Research Organization, The Volcani Center, Bet Dagan, Israel
Pines, M., Institute of Animal Science, Agricultural Research Organization, The Volcani Center, Bet Dagan, Israel
Halofuginone: An inhibitor of collagen type I synthesis
The effect of halofuginone - a plant alkaloid used as a coccidiostat in birds - on collagen metabolism was studied in various avian and mammalian cell cultures. In avian skin fibroblasts halofuginone attenuated the incorporation of [3H]proline into collagenase-digestible proteins (CDP) at concentrations as low as 10-11 M, without affecting production of [3H]collagenase-non-digestible proteins (NCDP), cell proliferation or collagen degradation. Halofuginine depressed specifically the expression of α1 gene of collagen type I but not that of collagen type II. This was demonstrated in skin fibroblasts and growth-plate chondrocytes using probes containing inserts sequences corresponding to the α1(I) and α1(II) mRNAs. A slight inhibition of the expression of α2(I) was observed in avian skin fibroblasts but not in growth-plate chondrocytes. The inhibition of gene expression of both polypeptides of collagen type I in skin fibroblasts resulted in a decrease in synthesis, as demonstrated by immunoprecipitation with specific type I collagen antiserum. In primary cultures of mouse skin fibroblasts, avian epiphyseal growth plate chondrocytes and a rat embryo cell line - all of which produce and secrete collagen type I - halofuginone inhibited the incorporation of [3H]proline into CDP, the Rat-1 line being the most sensitive to the drug. These results suggest that halofuginone affects specifically type I collagen synthesis by repressing gene-expression. The need for extremely low concentrations of halofuginone to inhibit collagen type I synthesis, regardless of the tissue or animal species, contributes to the potential usefulness of the substance in studying collagen metabolism. © 1993.
Scientific Publication
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