Premium
Transforming growth factor β 1 influences lysyl hydroxylation of collagen I and reduces steady‐state levels of lysyl hydroxylase mRNA in human osteoblast‐Iike celIs *
Author(s) -
SEITZER U.,
BÄTGE B.,
ACIL Y.,
MÜLLER P. K.
Publication year - 1995
Publication title -
european journal of clinical investigation
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.164
H-Index - 107
eISSN - 1365-2362
pISSN - 0014-2972
DOI - 10.1111/j.1365-2362.1995.tb01974.x
Subject(s) - hydroxylation , osteoblast , chemistry , endocrinology , medicine , messenger rna , growth factor , transforming growth factor , lysyl oxidase , enzyme , biology , biochemistry , gene , in vitro , receptor
. Transforming growth factor β 1 (TGF‐β 1 ) is an osteotropic growth factor that is found in substantial concentration in bone. The authors studied the influence of TGF‐β 1 on the modification of lysine residues of collagen I. The degree of lysyl hydroxylation and lysyl glycosylation of newly synthesized collagen as well as steady‐state levels of mRNA for both lysyl hydroxylase and collagens I and 111 were determined in human osteoblast‐like cells in vitro . In normal human osteoblasts lysyl hydroxylation was decreased by TGF‐β 1 particularly in the collagen α 2 ‐chain. This effect was paralleled by an increase in lysyl residues, whereas glycosylation was not affected. The mRNA for lysyl hydroxylase was reduced by one‐third under the influence of TGF‐β 1 . Additionally, the mRNAs for both procollagen I α‐chains were stimulated by TGF‐β 1 , whereas proα1 (111)‐mRNA showed a decrease. Changes in the local regulatory activity of TGF‐β 1 may play a role in matrix maturation such as collagen type production and lysyl hydroxylation, the latter being altered in various pathological conditions, e.g. in generalized osteopenia.