Abstract
Lung tissue from patients with interstitial lung disease (ILD), adult respiratory distress syndrome (ARDS), and control subjects with no obvious fibrotic lung disease was analyzed for its content of the collagen cross-links hydroxylysinonorleucine (HLNL), dihydroxylysinonorleucine (DHLNL), and hydroxypyridinium (OHP). We observed significant elevations of the DHLNL:HLNL ratio in patients with ARDS, and significant increases in the content of OHP in lungs of patients with ILD. These results are consistent with data from animal models of fibrotic lung disease, suggesting that increases in the DHLNL:HLNL ratio of lung collagen may serve as a marker of an acute fibrotic episode, whereas increased lung collagen OHP content serves as a marker of chronic lung fibrosis. We suggest that the underlying mechanism for the changes in DHLNL content in (pre)fibrotic acutely injured lung tissue and in OHP content in long-term fibrosis may be an increase in the activity of lysyl hydroxylase, a key intracellular enzyme responsible for a specific post-translational modification of collagen.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 307-313 |
| Number of pages | 7 |
| Journal | American Review of Respiratory Disease |
| Volume | 141 |
| Issue number | 2 I |
| State | Published - 1990 |
Fingerprint
ASJC Scopus subject areas
- Pulmonary and Respiratory Medicine
Cite this
Collagen cross-linking in adult patients with acute and chronic fibrotic lung disease. Molecular markers for fibrotic collagen. / Last, Jerold A; King, T. E.; Nerlich, A. G.; Reiser, K. M.
In: American Review of Respiratory Disease, Vol. 141, No. 2 I, 1990, p. 307-313.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Collagen cross-linking in adult patients with acute and chronic fibrotic lung disease. Molecular markers for fibrotic collagen
AU - Last, Jerold A
AU - King, T. E.
AU - Nerlich, A. G.
AU - Reiser, K. M.
PY - 1990
Y1 - 1990
N2 - Lung tissue from patients with interstitial lung disease (ILD), adult respiratory distress syndrome (ARDS), and control subjects with no obvious fibrotic lung disease was analyzed for its content of the collagen cross-links hydroxylysinonorleucine (HLNL), dihydroxylysinonorleucine (DHLNL), and hydroxypyridinium (OHP). We observed significant elevations of the DHLNL:HLNL ratio in patients with ARDS, and significant increases in the content of OHP in lungs of patients with ILD. These results are consistent with data from animal models of fibrotic lung disease, suggesting that increases in the DHLNL:HLNL ratio of lung collagen may serve as a marker of an acute fibrotic episode, whereas increased lung collagen OHP content serves as a marker of chronic lung fibrosis. We suggest that the underlying mechanism for the changes in DHLNL content in (pre)fibrotic acutely injured lung tissue and in OHP content in long-term fibrosis may be an increase in the activity of lysyl hydroxylase, a key intracellular enzyme responsible for a specific post-translational modification of collagen.
AB - Lung tissue from patients with interstitial lung disease (ILD), adult respiratory distress syndrome (ARDS), and control subjects with no obvious fibrotic lung disease was analyzed for its content of the collagen cross-links hydroxylysinonorleucine (HLNL), dihydroxylysinonorleucine (DHLNL), and hydroxypyridinium (OHP). We observed significant elevations of the DHLNL:HLNL ratio in patients with ARDS, and significant increases in the content of OHP in lungs of patients with ILD. These results are consistent with data from animal models of fibrotic lung disease, suggesting that increases in the DHLNL:HLNL ratio of lung collagen may serve as a marker of an acute fibrotic episode, whereas increased lung collagen OHP content serves as a marker of chronic lung fibrosis. We suggest that the underlying mechanism for the changes in DHLNL content in (pre)fibrotic acutely injured lung tissue and in OHP content in long-term fibrosis may be an increase in the activity of lysyl hydroxylase, a key intracellular enzyme responsible for a specific post-translational modification of collagen.
UR - http://www.scopus.com/inward/record.url?scp=0025098828&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0025098828&partnerID=8YFLogxK
M3 - Article
C2 - 2301849
AN - SCOPUS:0025098828
VL - 141
SP - 307
EP - 313
JO - American Journal of Respiratory and Critical Care Medicine
JF - American Journal of Respiratory and Critical Care Medicine
SN - 1073-449X
IS - 2 I
ER -