| Id |
Subject |
Object |
Predicate |
Lexical cue |
| TextSentencer_T1 |
0-122 |
Sentence |
denotes |
Interaction of a recombinant form of apolipoprotein[a] with human fibroblasts and with the human hepatoma cell line HepG2. |
| TextSentencer_T2 |
123-258 |
Sentence |
denotes |
We have studied the binding, uptake, and degradation of a recombinant form of apolipoprotein[a] (r-apo[a]) using a cultured cell model. |
| TextSentencer_T3 |
259-510 |
Sentence |
denotes |
In HepG2 cells and in human fibroblasts, r-apo[a] complexed with low density lipoprotein(LDL) is bound and internalized via high affinity (Kd = 10 nM) receptors; in both cell types, low affinity (Kd = 200-300 nM) sites also mediate free apo[a] uptake. |
| TextSentencer_T4 |
511-620 |
Sentence |
denotes |
Using competition studies, we found that the high affinity binding component corresponds to the LDL receptor. |
| TextSentencer_T5 |
621-891 |
Sentence |
denotes |
Involvement of the LDL receptor in r-apo[a] uptake by fibroblasts was confirmed using fibroblasts derived from an individual homozygous for familial hypercholesterolemia; in contrast to normal fibroblasts, these cells lacked the high affinity r-apo[a] binding component. |
| TextSentencer_T6 |
892-1066 |
Sentence |
denotes |
Cell association of 125I-labeled r-apo[a] was increased and decreased concomitantly with the up- and down-regulation of the LDL receptor in response to a number of compounds. |
| TextSentencer_T7 |
1067-1379 |
Sentence |
denotes |
The addition of alpha 2-macroglobulin as well as treatment with heparinase, chondroitinase ABC, and sodium chlorate did not decrease total specific binding of r-apo[a], suggesting that neither the low density lipoprotein receptor-related protein nor cell surface proteoglycans are involved in r-apo[a] clearance. |
| TextSentencer_T8 |
1380-1714 |
Sentence |
denotes |
The low affinity binding component present in both fibroblasts and HepG2 cells likely corresponds to the plasminogen receptor, as binding of r-apo[a] to these sites was specifically decreased by the addition of plasminogen or the lysine analogue epsilon-aminocaproic acid, but not by the addition of tissue-type plasminogen activator. |
| TextSentencer_T9 |
1715-1874 |
Sentence |
denotes |
Heparin abolished uptake of r-apo[a] by the LDL receptor component only; this indicates that apo[a] must be associated with LDL to be cleared by this receptor. |
| TextSentencer_T10 |
1875-2032 |
Sentence |
denotes |
In contrast, free apo[a] can be effectively cleared by the plasminogen receptor which may represent a significant route of clearance for free apo[a] in vivo. |
| T1 |
0-122 |
Sentence |
denotes |
Interaction of a recombinant form of apolipoprotein[a] with human fibroblasts and with the human hepatoma cell line HepG2. |
| T2 |
123-258 |
Sentence |
denotes |
We have studied the binding, uptake, and degradation of a recombinant form of apolipoprotein[a] (r-apo[a]) using a cultured cell model. |
| T3 |
259-510 |
Sentence |
denotes |
In HepG2 cells and in human fibroblasts, r-apo[a] complexed with low density lipoprotein(LDL) is bound and internalized via high affinity (Kd = 10 nM) receptors; in both cell types, low affinity (Kd = 200-300 nM) sites also mediate free apo[a] uptake. |
| T4 |
511-620 |
Sentence |
denotes |
Using competition studies, we found that the high affinity binding component corresponds to the LDL receptor. |
| T5 |
621-891 |
Sentence |
denotes |
Involvement of the LDL receptor in r-apo[a] uptake by fibroblasts was confirmed using fibroblasts derived from an individual homozygous for familial hypercholesterolemia; in contrast to normal fibroblasts, these cells lacked the high affinity r-apo[a] binding component. |
| T6 |
892-1066 |
Sentence |
denotes |
Cell association of 125I-labeled r-apo[a] was increased and decreased concomitantly with the up- and down-regulation of the LDL receptor in response to a number of compounds. |
| T7 |
1067-1379 |
Sentence |
denotes |
The addition of alpha 2-macroglobulin as well as treatment with heparinase, chondroitinase ABC, and sodium chlorate did not decrease total specific binding of r-apo[a], suggesting that neither the low density lipoprotein receptor-related protein nor cell surface proteoglycans are involved in r-apo[a] clearance. |
| T8 |
1380-1714 |
Sentence |
denotes |
The low affinity binding component present in both fibroblasts and HepG2 cells likely corresponds to the plasminogen receptor, as binding of r-apo[a] to these sites was specifically decreased by the addition of plasminogen or the lysine analogue epsilon-aminocaproic acid, but not by the addition of tissue-type plasminogen activator. |
| T9 |
1715-1874 |
Sentence |
denotes |
Heparin abolished uptake of r-apo[a] by the LDL receptor component only; this indicates that apo[a] must be associated with LDL to be cleared by this receptor. |
| T10 |
1875-2032 |
Sentence |
denotes |
In contrast, free apo[a] can be effectively cleared by the plasminogen receptor which may represent a significant route of clearance for free apo[a] in vivo. |