| Id |
Subject |
Object |
Predicate |
Lexical cue |
| T1 |
0-115 |
Sentence |
denotes |
Disparities in the interaction of rat and human lipoproteins with cultured rat fibroblasts and smooth muscle cells. |
| T2 |
116-172 |
Sentence |
denotes |
Requirements for homology for receptor binding activity. |
| T3 |
173-320 |
Sentence |
denotes |
This study characterizes the interactions of various rat and human lipoproteins with the lipoprotein cell surface receptors of rat and human cells. |
| T4 |
321-612 |
Sentence |
denotes |
Iodinated rat very low density lipoproteins (VLDL), rat chylomicron remnants, rat low density lipoproteins (LDL), and rat high density lipoproteins containing predominantly apoprotein E (HDL1) bound to high affinity cell surface receptors of cultured rat fibroblasts and smooth muscle cells. |
| T5 |
613-755 |
Sentence |
denotes |
Rat VLDL and chylomicron remnants were most avidly bound; the B-containing LDL and the E-containing HDL1 displayed lesser but similar binding. |
| T6 |
756-910 |
Sentence |
denotes |
Rat HDL (d = 1.125 to 1.21) exhibited weak receptor binding; however, after recentrifugation to remove apoprotein E, they were devoid of binding activity. |
| T7 |
911-1244 |
Sentence |
denotes |
Competitive binding studies at 4 degrees C confirmed these results for normal lipoproteins and indicated that VLDL (B-VLDL), LDL, and HDLc (cholesterol-rich HDL1) isolated from hypercholesterolemic rats had increased affinity for the rat receptors compared with their normal counterparts, the most pronounced change being in the LDL. |
| T8 |
1245-1386 |
Sentence |
denotes |
The cell surface receptor pathway in rat fibroblasts and smooth muscle cells resembled the system described for human fibroblasts as follows: |
| T9 |
1387-1957 |
Sentence |
denotes |
1) lipoproteins containing either the B or E apoproteins interacted with the receptors; 2) receptor binding activity was abolished by acetoacetylation or reductive methylation of a limited number of lysine residues of the lipoproteins; 3) receptor binding initiated the process of internalization and degradation of the apo-B- and apo-E-containing lipoproteins; 4) the lipoprotein cholesterol was re-esterified as determined by [14C]oleate incorporation into the cellular cholesteryl esters; and 5) receptor-mediated uptake (receptor number) was lipoprotein cholesterol. |
| T10 |
1958-2110 |
Sentence |
denotes |
An important difference between rat and human fibroblasts was the inability of human LDL to interact with the cell surface receptors of rat fibroblasts. |
| T11 |
2111-2171 |
Sentence |
denotes |
Rat lipoproteins did, however, react with human fibroblasts. |
| T12 |
2172-2268 |
Sentence |
denotes |
Furthermore, the rat VLDL were the most avidly bound of the rat lipoproteins to rat fibroblasts. |
| T13 |
2269-2412 |
Sentence |
denotes |
When the direct binding of 125I-VLDL was subjected to Scatchard analysis, the very high affinity of rat VLDL was apparent (Kd = 1 X 10(-11) M). |
| T14 |
2413-2537 |
Sentence |
denotes |
Moreover, compared with data for rat LDL, the data suggested each VLDL particle bound to four to nine lipoprotein receptors. |
| T15 |
2538-2629 |
Sentence |
denotes |
This multiple receptor binding could explain the enhanced binding affinity of the rat VLDL. |
| T16 |
2630-2805 |
Sentence |
denotes |
The Scatchard plot of rat 125I-VLDL revealed a biphasic binding curve in rat and human fibroblast cells and in rat smooth muscle cells, suggesting two populations of rat VLDL. |
| T17 |
2806-2935 |
Sentence |
denotes |
These results indicate that rat cells have a receptor pathway similar to, but not identical with, the LDL pathway of human cells. |
| T18 |
2936-3121 |
Sentence |
denotes |
Since human LDL bind poorly to rat cell receptors on cultured rat fibroblasts and smooth muscle cells, metabolic studies using human lipoproteins in rats must be interpreted cautiously. |
| T1 |
0-115 |
Sentence |
denotes |
Disparities in the interaction of rat and human lipoproteins with cultured rat fibroblasts and smooth muscle cells. |
| T2 |
116-172 |
Sentence |
denotes |
Requirements for homology for receptor binding activity. |
| T3 |
173-320 |
Sentence |
denotes |
This study characterizes the interactions of various rat and human lipoproteins with the lipoprotein cell surface receptors of rat and human cells. |
| T4 |
321-612 |
Sentence |
denotes |
Iodinated rat very low density lipoproteins (VLDL), rat chylomicron remnants, rat low density lipoproteins (LDL), and rat high density lipoproteins containing predominantly apoprotein E (HDL1) bound to high affinity cell surface receptors of cultured rat fibroblasts and smooth muscle cells. |
| T5 |
613-755 |
Sentence |
denotes |
Rat VLDL and chylomicron remnants were most avidly bound; the B-containing LDL and the E-containing HDL1 displayed lesser but similar binding. |
| T6 |
756-910 |
Sentence |
denotes |
Rat HDL (d = 1.125 to 1.21) exhibited weak receptor binding; however, after recentrifugation to remove apoprotein E, they were devoid of binding activity. |
| T7 |
911-1244 |
Sentence |
denotes |
Competitive binding studies at 4 degrees C confirmed these results for normal lipoproteins and indicated that VLDL (B-VLDL), LDL, and HDLc (cholesterol-rich HDL1) isolated from hypercholesterolemic rats had increased affinity for the rat receptors compared with their normal counterparts, the most pronounced change being in the LDL. |
| T8 |
1245-1386 |
Sentence |
denotes |
The cell surface receptor pathway in rat fibroblasts and smooth muscle cells resembled the system described for human fibroblasts as follows: |
| T9 |
1387-1957 |
Sentence |
denotes |
1) lipoproteins containing either the B or E apoproteins interacted with the receptors; 2) receptor binding activity was abolished by acetoacetylation or reductive methylation of a limited number of lysine residues of the lipoproteins; 3) receptor binding initiated the process of internalization and degradation of the apo-B- and apo-E-containing lipoproteins; 4) the lipoprotein cholesterol was re-esterified as determined by [14C]oleate incorporation into the cellular cholesteryl esters; and 5) receptor-mediated uptake (receptor number) was lipoprotein cholesterol. |
| T10 |
1958-2110 |
Sentence |
denotes |
An important difference between rat and human fibroblasts was the inability of human LDL to interact with the cell surface receptors of rat fibroblasts. |
| T11 |
2111-2171 |
Sentence |
denotes |
Rat lipoproteins did, however, react with human fibroblasts. |
| T12 |
2172-2268 |
Sentence |
denotes |
Furthermore, the rat VLDL were the most avidly bound of the rat lipoproteins to rat fibroblasts. |
| T13 |
2269-2412 |
Sentence |
denotes |
When the direct binding of 125I-VLDL was subjected to Scatchard analysis, the very high affinity of rat VLDL was apparent (Kd = 1 X 10(-11) M). |
| T14 |
2413-2537 |
Sentence |
denotes |
Moreover, compared with data for rat LDL, the data suggested each VLDL particle bound to four to nine lipoprotein receptors. |
| T15 |
2538-2629 |
Sentence |
denotes |
This multiple receptor binding could explain the enhanced binding affinity of the rat VLDL. |
| T16 |
2630-2805 |
Sentence |
denotes |
The Scatchard plot of rat 125I-VLDL revealed a biphasic binding curve in rat and human fibroblast cells and in rat smooth muscle cells, suggesting two populations of rat VLDL. |
| T17 |
2806-2935 |
Sentence |
denotes |
These results indicate that rat cells have a receptor pathway similar to, but not identical with, the LDL pathway of human cells. |
| T18 |
2936-3121 |
Sentence |
denotes |
Since human LDL bind poorly to rat cell receptors on cultured rat fibroblasts and smooth muscle cells, metabolic studies using human lipoproteins in rats must be interpreted cautiously. |
