The DOI matches its Crossref record; 31 of the 31 references it cites were found in a registry or an index; none of the 6 sources its claims cite is checked for support yet.
Low density lipoprotein receptor internalizes low density and very low density lipoproteins that are bound to heparan sulfate proteoglycans via lipoprotein lipase
Open accessAbstract
It has previously been shown that lipoprotein lipase (LPL) enhances the binding of low density lipoproteins (LDL) and very low density lipoproteins (VLDL) to HepG2 cells and fibroblasts, up to 80-fold. This increase in binding is LDL receptor-independent and is due to a bridging of LPL between extracellular heparan sulfate proteoglycans (HSPG) and the lipoproteins. In the present paper, we show that preincubation of the cells with LPL, followed by washing prior to the binding experiment, increased binding to the same extent as occurs when the binding is performed in the presence of LPL. This indicates that the formation of a complex of LPL with the lipoproteins is not a prerequisite of binding. Binding curves and Scatchard analyses reveal that both the number of binding sites and the affinity of the binding are increased 20-30-fold by the addition of 3.4 micrograms/ml LPL. The addition of LPL also resulted in an enhanced uptake and subsequent lysosomal degradation of both LDL and VLDL when compared with binding, although to a lesser extent (up to 25-fold when measured after 5 h at 37 degrees C). Strikingly, enhanced uptake did not occur in LDL receptor-negative fibroblasts. In addition, down-regulation of the LDL receptor activity by preincubation of the cells for 48 h with either LDL or beta-VLDL resulted in a parallel decrease in the uptake of LPL-mediated HSPG-bound LDL, whereas the LPL-mediated binding itself was not diminished. These observations indicate that the uptake of LPL-mediated HSPG-bound LDL and VLDL mainly proceeds via the LDL receptor. Binding of labeled LDL to the cells at 4 degrees C for 2 h followed by a chase period at 37 degrees C revealed that in absolute terms, the initial rate of internalization of HSPG-bound LDL is comparable with that of LDL receptor-bound LDL (0.58 and 0.44 ng/min/mg of cell protein, respectively). We conclude that in LDL receptor-positive cells, the LPL-mediated binding of LDL and VLDL to HSPG is followed by internalization of the lipoproteins mainly through the rapid process of the classical LDL receptor recycling system, whereas only a minor portion is internalized via the much slower process of HSPG uptake.
Overview
AI snapshot
Written from the paper’s full text.
TL;DR
LPL bridges LDL and VLDL to cell-surface heparan sulfate proteoglycans (HSPG), and the major portion of these HSPG-bound lipoproteins is subsequently internalized via the classical LDL receptor rather than by slow HSPG uptake. The paper concludes that LPL-mediated binding is LDL receptor-independent, but LPL-mediated uptake and lysosomal degradation are mainly LDL receptor-dependent.
Key findings
- Preincubating cells with LPL followed by washing increased LDL binding as much as adding LPL during the binding assay, indicating that LPL–lipoprotein complex formation is not required for enhanced binding.
- Binding curves and Scatchard analyses showed that LPL increased both the number of binding sites and binding affinity about 20–30-fold; the abstract reports this with 3.4 pg/ml LPL, and Fig. 2 reports an approximately 20-fold higher maximum LDL binding after preincubation with 1.7 pg/ml LPL.
- LPL enhanced uptake and lysosomal degradation of LDL and VLDL, though less than binding: the abstract states up to 25-fold after 5 h at 37 °C, while Fig. 3 reports internalization increases of 6-fold for LDL and 23-fold for VLDL after 4 h with heat-inactivated LPL.
- Down-regulation of LDL receptor activity decreased uptake of LPL-mediated HSPG-bound LDL in parallel with reduced LDL receptor-bound LDL uptake, while LPL-mediated binding itself was not diminished; the initial internalization rate of HSPG-bound LDL was comparable to LDL receptor-bound LDL (0.58 versus 0.44 ng/min/mg cell protein).
Methods
- Cultured HepG2 cells, normal fibroblasts, and LDL receptor-negative fibroblasts from a patient with homozygous familial hypercholesterolemia were used; LDL, VLDL, and β-VLDL were isolated by ultracentrifugation, iodinated, and incubated with cells in the presence or absence of bovine LPL from skimmed milk or heat-inactivated LPL.
- Binding was measured at 0–4 °C with 10 µg/ml ¹²⁵I-labeled lipoprotein; uptake, intracellular content, and degradation were measured at 37 °C, with trypsin treatment to separate surface-bound from internalized lipoprotein, and with heparinase, chloroquine, or NH₄Cl treatments as indicated.
- Main analyses included binding curves, Scatchard plots, degradation assays, LDL receptor down-regulation by preincubation with LDL or β-VLDL, and chase experiments to measure internalization rates.
Limitations
- The paper states that the relevance of these cell-culture data to the in vivo fate of lipoproteins is still unclear, and that most experiments used LPL concentrations more than 100 times the physiological range of 8–25 ng/ml, although 25 ng/ml LPL still increased LDL binding about 1.5-fold.
- The discussion notes discrepancies with other studies, attributing them to differences in measuring total cell association versus discriminating bound and internalized lipoprotein, different sampling times, and expressing internalization as percent of total radioactivity rather than absolute ng/min/mg cell protein.
- The text itself contains an apparent inconsistency: the abstract says enhanced uptake did not occur in LDL receptor-negative fibroblasts, whereas the discussion says internalization was increased considerably in those cells but was much less efficient than in control fibroblasts.
Model-written summary. Check it against the paper before relying on it.
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- Findingown data
LPL-mediated binding of LDL is already evident at more physiological concentrations of LPL (ng/ml range).
“In Fig. lB, it is shown that the LPL-mediated binding of LDL is already evident at more physiological concentrations of LPL (ng/ml range).”
Quote in the paperNot a substantial claim - Findingown data§ Low Density Lipoprotein Receptor Internalizes Low Density and Very Low Density Lipoproteins That Are Bound to Heparan Sulfate Proteoglycans via Lipoprotein Lipase*
Preincubation of cells with LPL followed by washing prior to the binding experiment increased binding to the same extent as occurs when binding is performed in the presence of LPL.
“In the present paper, we show that preincubation of the cells with LPL, followed by washing prior to the binding experiment, increased binding to the same extent as occurs when the binding is performed in the presence of LPL.”
Quote in the paperSubstantial claim - Findingown data
Treatment of cells with heparinase inhibited LPL-mediated binding and internalization of both LDL and VLDL.
“Fig, 3 shows that besides the inhibition of the LPLmediated binding of LDL and VLDL, treatment of the cells with heparinase also resulted in inhibition of the LPL-mediated internalization of both lipoproteins.”
Quote in the paperSubstantial claim - Findingown data§ Low Density Lipoprotein Receptor Internalizes Low Density and Very Low Density Lipoproteins That Are Bound to Heparan Sulfate Proteoglycans via Lipoprotein Lipase*
Initial rate of internalization of HSPG-bound LDL is comparable with that of LDL receptor-bound LDL (0.58 and 0.44 ng/min/mg of cell protein, respectively).
“Binding of labeled LDL to the cells at 4”
Quote in the paperSubstantial claim - Findingown data
Parallel results were obtained for the uptake of LPL-mediated HSPG-bound LDL (50 and 45% of the control value, respectively).
“Strikingly, parallel results were obtained for the uptake of LPL-mediated HSPG-bound LDL (50 and 45% of the control value, respectively) (D).”
Quote in the paperSubstantial claim
- Findingown data
In LDL receptor-negative fibroblasts, internalization of LDL and VLDL did not reach the same order of magnitude as that measured for receptor-positive fibroblasts.
“However, in contrast to the binding, the internalization of LDL and VLDL in receptornegative fibroblasts did not reach the same order of magnitude as that measured for receptor-positive fibroblasts.”
Quote in the paperSubstantial claim - Findingown data§ Low Density Lipoprotein Receptor Internalizes Low Density and Very Low Density Lipoproteins That Are Bound to Heparan Sulfate Proteoglycans via Lipoprotein Lipase*
Both the number of binding sites and the affinity of binding are increased 20-30-fold by the addition of 3.4 pg/ml LPL.
“Binding curves and Scatchard analyses reveal that both the number of binding sites and the affinity of the binding are increased 20-30-fold by the addition of 3.4 pg/ml LPL.”
Quote in the paperSubstantial claim - Findingown data
LPL-mediated binding of lipoproteins is not suppressed by preincubation of the cells with lipoproteins.
“We found that the LPL-mediated binding of lipoproteins is not suppressed by preincubation of the cells with lipoproteins (Fig. 5).”
Quote in the paperSubstantial claim - Findingown data§ Low Density Lipoprotein Receptor Internalizes Low Density and Very Low Density Lipoproteins That Are Bound to Heparan Sulfate Proteoglycans via Lipoprotein Lipase*
Addition of LPL resulted in enhanced uptake and subsequent lysosomal degradation of both LDL and VLDL compared with binding, although to a lesser extent (up to 25-fold when measured after 5 h at 37C).
“The addition of LPL also resulted in an enhanced uptake and subsequent lysosomal degradation of both LDL and VLDL when compared with binding, although to a lesser extent (up to 25-fold when measured after 5 h at 37”
Quote in the paperSubstantial claim - Findingown data
Uptake of HSPG-bound LDL is suppressed parallel to the down-regulation of the LDL receptor activity.
“However, we also found that in contrast to the binding, the uptake of HSPG-bound LDL is suppressed parallel to the down-regulation of the LDL receptor activity (Fig. 5, C and D).”
Quote in the paperSubstantial claim - Findingown data
Preincubation of cells with beta-VLDL or LDL resulted in decreased internalization of LDL receptor-bound 125I-LDL (40 and 25% of the control value, respectively).
“Preincubation of the cells with P-VLDL or LDL also resulted in a decreased internalization of LDL receptor-bound lZ5I-LDL (40 and 25% of the control value, respectively) (C).”
Quote in the paperSubstantial claim - Findingown data
Degradation of LDL and VLDL is lysosomal both in the absence and in the presence of LPL.
“Furthermore, our results show that the degradation of LDL and VLDL is lysosomal both in the absence and in the presence of LPL, which is similar to the results obtained by Williams et al. (18) with respect to LDL and Lp(a).”
Quote in the paperNot a substantial claim0 of 1 sources checked- cites [18]
Couldn’t be matched to a paper in Crossref, so it can’t be checked.
- Interpretationown data
At least part of the lipoproteins that are bound via LPL to HSPG are subsequently internalized and degraded.
“These results indicate, therefore, that at least part of the lipoproteins that are bound via LPL to HSPG are subsequently internalized and degraded as well.”
Quote in the paperSubstantial claim - Interpretationreasoning
In LDL receptor-negative fibroblasts, the total amount of HSPG-bound lipoprotein is internalized via the slow process of HSPG uptake.
“In LDL receptornegative fibroblast, the total amount of HSPG-bound lipoprotein is internalized via this slow process of HSPG uptake.”
Quote in the paperSubstantial claim - Interpretationown data§ Low Density Lipoprotein Receptor Internalizes Low Density and Very Low Density Lipoproteins That Are Bound to Heparan Sulfate Proteoglycans via Lipoprotein Lipase*
Uptake of LPL-mediated HSPG-bound LDL and VLDL mainly proceeds via the LDL receptor.
“These observations indicate that the uptake of LPL-mediated HSPG-bound LDL and VLDL mainly proceeds via the LDL receptor.”
Quote in the paperSubstantial claim - Interpretationown data§ Low Density Lipoprotein Receptor Internalizes Low Density and Very Low Density Lipoproteins That Are Bound to Heparan Sulfate Proteoglycans via Lipoprotein Lipase*
Formation of a complex of LPL with the lipoproteins is not a prerequisite of binding.
“This indicates that the formation of a complex of LPL with the lipoproteins is not a prerequisite of binding.”
Quote in the paperSubstantial claim - Interpretationown data
The LDL receptor is involved in the uptake of lipoproteins following the binding of these lipoproteins via an LPL-mediated bridging between lipoproteins and HSPG.
“From these results, we conclude that the LDL receptor is involved in the uptake of lipoproteins following the binding of these lipoproteins via an LPL-mediated bridging between lipoproteins and HSPG.”
Quote in the paperSubstantial claim - Interpretationown data
Internalization of HSPG-bound LDL, if expressed as nanograms of LDL/min/mg of cell protein, is as fast as the internalization of LDL bound to the classical LDL receptor (in the absence of LPL).
“These results also indicate that the internalization of HSPG-bound LDL, if expressed as nanograms of LDL/min/mg of cell protein, is as fast as the internalization of LDL bound to the classical LDL receptor (in the absence of LPL).”
Quote in the paperSubstantial claim - Interpretationown data
The LDL receptor is indeed involved in the internalization of LPL-mediated HSPG-bound lipoproteins.
“This sustains our conclusion that the LDL receptor is indeed involved in the internalization of LPL-mediated HSPG-bound lipoproteins.”
Quote in the paperSubstantial claim
- It may state two separate claims as one. 10
- The quote only partly states this claim. 1
- Probably not a substantial claim. 2
It may state two separate claims as one.
Findingown dataMost LDL receptor-bound LDL has been internalized within 10-15 min, which is in accordance with the recycling time reported earlier for the classical LDL receptor.
“As shown in Fig. 6, most of the LDL receptor-bound LDL has been internalized within 10-15 min, which is in accordance with the recycling time reported earlier for the classical LDL receptor (28).”
Quote in the paperSubstantial claim0 of 1 sources checked- cites [28]
Couldn’t be matched to a paper in Crossref, so it can’t be checked.
It may state two separate claims as one.
Findingown dataIn the presence of heat-inactivated LPL, binding of LDL and VLDL is enhanced (about 14- and 31-fold for LDL and VLDL, respectively) and internalization is increased to a lesser extent (6- and 23-fold for LDL and VLDL, respectively).
“In Fig. 3, it is shown that in the presence of heat-inactivated LPL, not only the binding of LDL and VLDL is enhanced (about 14and 31-fold for LDL and VLDL, respectively) but also the internalization (expressed as the amount of intracellular plus degraded lipoprotein) is increased, although to a lesser extent (6-and 23-fold for LDL and VLDL, respectively).”
Quote in the paperSubstantial claimIt may state two separate claims as one.
Findingown data§ Low Density Lipoprotein Receptor Internalizes Low Density and Very Low Density Lipoproteins That Are Bound to Heparan Sulfate Proteoglycans via Lipoprotein Lipase*Down-regulation of LDL receptor activity by preincubation of cells for 48 h with either LDL or beta-VLDL resulted in a parallel decrease in uptake of LPL-mediated HSPG-bound LDL, whereas LPL-mediated binding itself was not diminished.
“In addition, down-regulation of the LDL receptor activity by preincubation of the cells for 48 h with either LDL or 8-VLDL resulted in a parallel decrease in the uptake of LPL-mediated HSPG-bound LDL, whereas the LPL-mediated binding itself was not diminished.”
Quote in the paperSubstantial claimIt may state two separate claims as one.
Premisecitation§ Low Density Lipoprotein Receptor Internalizes Low Density and Very Low Density Lipoproteins That Are Bound to Heparan Sulfate Proteoglycans via Lipoprotein Lipase*The increase in binding is LDL receptor-independent and is due to bridging of LPL between extracellular HSPG and lipoproteins.
“This increase in binding is LDL receptor-independent and is due to a bridging of LPL between extracellular heparan sulfate proteoglycans (HSPG) and the lipoproteins.”
Quote in the paperSubstantial claim0 of 1 sources checked- cites [15]
Couldn’t be matched to a paper in Crossref, so it can’t be checked.
It may state two separate claims as one. The quote only partly states this claim.
Interpretationown data§ Low Density Lipoprotein Receptor Internalizes Low Density and Very Low Density Lipoproteins That Are Bound to Heparan Sulfate Proteoglycans via Lipoprotein Lipase*At 37C, most of the LPL-mediated binding and LPL-mediated internalization of LDL and VLDL could be inhibited by heparinase, indicating that the LPL-mediated increases in both binding and internalization are dependent on the presence of HSPG on the plasma membrane.
“At 37”
Quote in the paperSubstantial claimIt may state two separate claims as one.
Interpretationown dataAlthough LPL-mediated binding of LDL and VLDL occurs via HSPG, the major part of the subsequent internalization of these lipoproteins is mediated via the LDL receptor.
“Thus, although the LPL-mediated binding of LDL and VLDL occurs via HSPG, the major part of the subsequent internalization of these lipoproteins is mediated via the LDL receptor.”
Quote in the paperSubstantial claimProbably not a substantial claim.
Premisecitation§ Low Density Lipoprotein Receptor Internalizes Low Density and Very Low Density Lipoproteins That Are Bound to Heparan Sulfate Proteoglycans via Lipoprotein Lipase*LPL enhances the binding of LDL and VLDL to HepG2 cells and fibroblasts up to 80-fold.
“It has previously been shown that lipoprotein lipase (LPL) enhances the binding of low density lipoproteins (LDL) and very low density lipoproteins (VLDL) to HepG2 cells and fibroblasts, up to 80-fold.”
Quote in the paperSubstantial claim0 of 1 sources checked- cites [15]
Couldn’t be matched to a paper in Crossref, so it can’t be checked.
It may state two separate claims as one.
PremisecitationTrypsin removes both cell-bound lipoproteins and cell-bound lipoprotein lipase.
“Trypsin removes both cell-bound lipoproteins and cell-bound lipoprotein lipase (26).”
Quote in the paperSubstantial claim0 of 1 sources checked- cites [26]
Couldn’t be matched to a paper in Crossref, so it can’t be checked.
Probably not a substantial claim.
PremisecitationLDL receptor-negative fibroblasts were obtained from a patient with homozygous familial hypercholesterolemia.
“LDL receptornegative fibroblasts were obtained from a patient with homozygous familial hypercholesterolemia (25).”
Quote in the paperSubstantial claim0 of 1 sources checked- cites [25]
Couldn’t be matched to a paper in Crossref, so it can’t be checked.
It may state two separate claims as one.
Interpretationown data§ Low Density Lipoprotein Receptor Internalizes Low Density and Very Low Density Lipoproteins That Are Bound to Heparan Sulfate Proteoglycans via Lipoprotein Lipase*In LDL receptor-positive cells, LPL-mediated binding of LDL and VLDL to HSPG is followed by internalization mainly through the rapid process of the classical LDL receptor recycling system, whereas only a minor portion is internalized via the much slower process of HSPG uptake.
“We conclude that in LDL receptor-positive cells, the LPL-mediated binding of LDL and VLDL to HSPG is followed by internalization of the lipoproteins mainly through the rapid process of the classical LDL receptor recycling system, whereas only a minor portion is internalized via the much slower process of HSPG uptake.”
Quote in the paperSubstantial claimIt may state two separate claims as one.
InterpretationreasoningIn normal cells, the uptake of LPL-mediated HSPG-bound LDL continues up to 60 min, indicating that the LDL-receptor recycling system is saturated during 4-6 LDL receptor cycles and is consequently the rate-limiting step in this process.
“The fact that in normal cells the uptake of LPL-mediated HSPG-bound LDL continues up to 60 min indicates that the LDL-receptor recycling system is saturated during 4-6 LDL receptor cycles and, consequently, the rate-limiting step in this process.”
Quote in the paperSubstantial claimIt may state two separate claims as one.
Interpretationown dataLPL-mediated HSPG-bound LDL and VLDL are taken up and directed to the lysosomes for degradation.
“From these results, we conclude that the LPL-mediated HSPG-bound LDL and VLDL are also taken up and directed to the lysosomes for degradation.”
Quote in the paperSubstantial claim
The authors state this as an assumption.
The LRP binds only apoE-containing lipoproteins.
“while the LRP is assumed to bind only apoE-containing lipoproteins.”
The authors state this as an assumption.
The LRP contains no heparan sulfate side chains.
“whereas the LRP is assumed to contain no heparan sulfate side chains.”
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
LPL is known to facilitate the uptake of lipoproteins in the liver.
“LPL is known to facilitate the uptake of lipoproteins in the liver (127–130).”
From Regulation of lipoprotein metabolism by ANGPTL3, ANGPTL4, and ANGPTL8 (2021) · cites this paper as [130]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
Each contradiction between two passages listed here was confirmed by an independent check.
Abstract denies uptake increase in receptor-negative fibroblasts
MajorThe abstract says enhanced uptake did not occur in LDL receptor-negative fibroblasts, but the discussion says LPL considerably increased their internalization of both LDL and VLDL.
“Strikingly, enhanced uptake did not occur in LDL receptornegative fibroblasts.”
“we also show that in LDL receptor-negative fibroblasts, the internalization of LDL and VLDL is increased considerably upon incubation of the cells with LPL (Fig. 4).”
Conflicting preincubation times for receptor down-regulation
MinorThe abstract gives a 48-hour preincubation with LDL or β-VLDL, whereas the description of the down-regulation experiment gives 24 hours.
“down-regulation of the LDL receptor activity by preincubation of the cells for 48 h with either LDL or 8-VLDL”
“the cells were first incubated with HSA alone, DMEM/HSA supplemented with 200 pg/ml rat P-VLDL, or DMEM/HSA supplemented with 300 pg/ml human LDL, as indicated, at 37 "C for a period of 24 h.”
Citations
Cites
PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENT
Lowry, O. H., Rosebrough, N., Farr, A. L., & Randall, R. (1951) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)52451-6 · Cited by 316,200
Bilheimer, D. W., Eisenberg, S., & Levy, R. I. (1972) · Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism · doi:10.1016/0005-2760(72)90034-3 · Cited by 1,822
Separation of plasma lipoproteins by density-gradient ultracentrifugation
Redgrave, T. G., Roberts, D., & West, C. E. (1975) · Analytical Biochemistry · doi:10.1016/0003-2697(75)90488-1 · Cited by 1,101
Herz, J., Hamann, U., Rogne, S., Myklebost, O., Gausepohlꝉ, H., & Stanley, K. K. (1988) · The EMBO Journal · doi:10.1002/j.1460-2075.1988.tb03306.x · Cited by 955
A stable, radioactive substrate emulsion for assay of lipoprotein lipase
Nilsson‐Ehle, P., & Schotz, M. C. (1976) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)41752-3 · Cited by 841
The LDL–receptor–related protein, LRP, is an apolipoprotein E-binding protein
Beisiegel†, U., Weber, W. T., Ihrke, G., Herz, J., & Stanley, K. K. (1989) · Nature · doi:10.1038/341162a0 · Cited by 680
Kowal, R. C., Herz, J., Goldstein, J. L., Esser, V., & Brown, M. S. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.15.5810 · Cited by 595
Strickland, D. K., Ashcom, J. D., Williams, S., Burgess, W. H., Migliorini, M., & Argraves, W. S. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)38172-9 · Cited by 558
Lipoprotein receptors in the liver. Control signals for plasma cholesterol traffic.
Brown, M. S., & Goldstein, J. L. (1983) · Journal of Clinical Investigation · doi:10.1172/jci111044 · Cited by 545
Beisiegel, U., Weber, W., & Bengtsson-Olivecrona, G. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.19.8342 · Cited by 468
Windler, E. E. T., Kovanen, P. T., Chao, Y. S., Brown, M. S., Havel, R. J., & Goldstein, J. L. (1980) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)70487-6 · Cited by 456
Williams, K. J., Fless, G. M., Petrie, K. A., Snyder, M. L., Brocia, R. W., & Swenson, T. L. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)42208-9 · Cited by 205
O’Brien, K. D., Gordon, D., Deeb, S. S., Ferguson, M. S., & Chait, A. (1992) · Journal of Clinical Investigation · doi:10.1172/jci115747 · Cited by 203
Rumsey, S. C., Obunike, J. C., Arad, Y., Deckelbaum, R. J., & Goldberg, I. J. (1992) · Journal of Clinical Investigation · doi:10.1172/jci116018 · Cited by 192
Kita, T., Goldstein, J. L., Brown, M. S., Watanabe, Y., Hornick, C. A., & Havel, R. J. (1982) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.79.11.3623 · Cited by 167
Felts, J. M., Itakura, H., & Thomas Crane, R. (1975) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(75)90524-0 · Cited by 137
Secretion and Degradation of Lipoprotein Lipase in Cultured Adipocytes
Cisar, L. A., Hoogewerf, A. J., Cupp, M. S., Rapport, C. A., & Bensadoun, A. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)94253-5 · Cited by 109
Mulder, M., Lombardi, P., Jansen, H., van Berkel, T. J. C., Frants, R. R., & Havekes, L. M. (1992) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(92)91664-c · Cited by 93
Self-citationvan Dijk, M. C. M., Ziere, G. J., BOERS, W., Linthorst, C., Bijsterbosch, M. K., & van Berkel, T. J. C. (1991) · Biochemical Journal · doi:10.1042/bj2790863 · Cited by 91
Lipoprotein lipase and hepatic lipase
Olivecrona, T., & Bengtsson-Olivecrona, G. (1990) · Current Opinion in Lipidology · doi:10.1097/00041433-199006000-00005 · Cited by 86
Association of plasma lipoproteins with postheparin lipase activities.
Goldberg, I. J., Kandel, J. J., Blum, C. B., & Ginsberg, H. N. (1986) · Journal of Clinical Investigation · doi:10.1172/jci112744 · Cited by 85
Windler, E. E. T., Greeve, J., Daerr, W. H., & Greten, H. (1988) · Biochemical Journal · doi:10.1042/bj2520553 · Cited by 67
Identification and characterization of the endothelial cell surface lipoprotein lipase receptor.
Saxena, U., Klein, M. G., & Goldberg, I. J. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)47402-4 · Cited by 65
Vijayagopal, P., Srinivasan, S. R., Radhakrishnamurthy, B., & Berenson, G. S. (1992) · Arteriosclerosis and Thrombosis A Journal of Vascular Biology · doi:10.1161/01.atv.12.2.237 · Cited by 58
Eisenberg, S., Friedman, G., & Vogel, T. (1988) · Arteriosclerosis An Official Journal of the American Heart Association Inc · doi:10.1161/01.atv.8.5.480 · Cited by 53
Friedman, G., Chajek‐Shaul, T., Olivecrona, T., Stein, O. T., & Stein, Y. (1982) · Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism · doi:10.1016/0005-2760(82)90016-9 · Cited by 40
Bihain, B. E., Deckelbaum, R. J., Yen, F. T., Gleeson, A. M., Carpentier, Y., & Witte, L. D. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)71494-4 · Cited by 39
Owens, R. T., & Wagner, W. D. (1991) · Arteriosclerosis and Thrombosis A Journal of Vascular Biology · doi:10.1161/01.atv.11.6.1752 · Cited by 33
Interaction of β‐very‐low‐density lipoproteins with rat liver cells
Harkes, L., van DUIJNE, A., & van Berkel, T. J. C. (1989) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1989.tb14639.x · Cited by 27
The binding of human lipoprotein lipase treated VLDL by the human hepatoma cell line HepG2
Mulder, M. T., de Wit, E., & Havekes, L. M. (1991) · Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism · doi:10.1016/0005-2760(91)90287-r · Cited by 22
Self-citationCharacterisation of the LDL receptor in Epstein-Barr virus transformed lymphocytes
Lombardi, M. P., de Wit, E., Frants, R. R., & Havekes, L. M. (1990) · Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism · doi:10.1016/0005-2760(90)90227-o · Cited by 6
Self-citation
Flagged first, then by citations
Research works printed but not linked: 5
- De Water, 1992, Biochem. J., 281, 62
- Tajima, 1984, J. Biol. Chem., 96, 1753
- Olivecrona, 1989, Curr. Opin. Lipid., 1, 112
- Villeli, 1991, Med. Sei. Res., 19, 111
- Vilaro, 1988, Am. J. Physiol., 254, G711
Cited by
Sorted by citations
The Response-to-Retention Hypothesis of Early Atherogenesis
Williams, K. J., & Tabas, I. (1995) · Arteriosclerosis, Thrombosis, and Vascular Biology · doi:10.1161/01.atv.15.5.551 · Cited by 1,413
Lipoprotein lipase and lipolysis: central roles in lipoprotein metabolism and atherogenesis
Goldberg, I. J. (1996) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)37569-6 · Cited by 1,021
Mahley, R. W., & Ji, Z.-S. (1999) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)33334-4 · Cited by 693
Biochemistry and pathophysiology of intravascular and intracellular lipolysisPreprint
Young, S. G., & Zechner, R. (2013) · Genes & Development · doi:10.1101/gad.209296.112 · Cited by 367
More to “heparin” than anticoagulation
Lindahl, U., Lidholt, K., Spillmann, D., & Kjellén, L. (1994) · Thrombosis Research · doi:10.1016/0049-3848(94)90136-8 · Cited by 340
Kato, M., Wang, H., Bernfield, M. R., Gallagher, J. T., & Turnbull, J. E. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)32250-0 · Cited by 196
Rensen, P. C. N., Herijgers, N., Netscher, M. H., Meskers, S. C. J., Eck, M. V., & van Berkel, T. J. C. (1997) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)37190-x · Cited by 163
Morita, S. (2015) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.b15-00716 · Cited by 160
Kaplan, M., & Aviram, M. (1999) · Clinical Chemistry and Laboratory Medicine (CCLM) · doi:10.1515/cclm.1999.118 · Cited by 159
Regulation of lipoprotein metabolism by ANGPTL3, ANGPTL4, and ANGPTL8
Sylvers-Davie, K. L., & Davies, B. S. J. (2021) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00195.2021 · Cited by 154
Salinelli, S., Lo, J.-Y., Mims, M. P., Zsigmond, E., Smith, L. C., & Chan, L. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.36.21906 · Cited by 153
Merkel, M., Kako, Y., Radner, H., Cho, I. S., Ramasamy, R., Brunzell, J. D., Goldberg, I. J., & Breslow, J. L. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.23.13841 · Cited by 152
Babaev, V. R., Patel, M., Semenkovich, C. F., Fazio, S., & Linton, M. F. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m002423200 · Cited by 151
Kashyap, V. S., Santamarina-Fojo, S., Brown, D. R., Parrott, C. L., Applebaum-Bowden, D. M., Meyn, S. M., Talley, G. D., Paigen, B. J., Maeda, N., & Brewer, H. B. (1995) · Journal of Clinical Investigation · doi:10.1172/jci118200 · Cited by 147
Lipoprotein lipase hydrolysis of retinyl ester. Possible implications for retinoid uptake by cells
Blaner, W. S., Obunike, J. C., Kurlandsky, S. B., Al-Haideri, M. T., Piantedosi, R., Deckelbaum, R. J., & Goldberg, I. J. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)89425-5 · Cited by 136
Lipoprotein lipase: From gene to atherosclerosis
Li, Y., He, P.-P., Zhang, D.-W., Zheng, X.-L., Cayabyab, F. S., Yin, W.-D., & Tang, C.-K. (2014) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2014.10.016 · Cited by 109
Jukema, J. W., Boven, A. J. V., Groenemeijer, B. E., Zwinderman, A. H., Reiber, J. H. C., Bruschke, A. V. G., Henneman, J. A., Molhoek, G. P., Bruin, T., Jansen, H., et al. (1996) · Circulation · doi:10.1161/01.cir.94.8.1913 · Cited by 123
Self-citationColeman, T., Seip, R. L., Gimble, J. M., Lee, D., Maeda, N., & Semenkovich, C. F. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.21.12518 · Cited by 113
The emergence of mouse models of atherosclerosis and their relevance to clinical research
Smith, J. D., & Breslow, J. L. (1997) · Journal of Internal Medicine · doi:10.1046/j.1365-2796.1997.00197.x · Cited by 108
Ji, Z. S., Sanan, D. A., & Mahley, R. W. (1995) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)39892-8 · Cited by 106
Lipoprotein Lipase in the Brain and Nervous System
Wang, H., & Eckel, R. H. (2012) · Annual Review of Nutrition · doi:10.1146/annurev-nutr-071811-150703 · Cited by 105
Merkel, M., Heeren, J., Dudeck, W., Rinninger, F., Radner, H., Breslow, J. L., Goldberg, I. J., Zechner, R., & Greten, H. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m107914200 · Cited by 105
Plasma and vessel wall lipoprotein lipase have different roles in atherosclerosis
Clee, S. M., Bissada, N., Miao, F., Miao, L., Marais, A. D., Henderson, H. E., Steures, P., McManus, J., McManus, B., LeBoeuf, R. C., et al. (2000) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)32399-3 · Cited by 101
The Importance of Lipoprotein Lipase Regulation in Atherosclerosis
Kumari, A., Kristensen, K. K., Ploug, M., & Winther, A.-M. L. (2021) · Biomedicines · doi:10.3390/biomedicines9070782 · Cited by 100
Ando, Y., Shimizugawa, T., Takeshita, S., Ono, M., Shimamura, M., Koishi, R., & Furukawa, H. (2003) · Journal of Lipid Research · doi:10.1194/jlr.m300031-jlr200 · Cited by 100
Baculovirus capsid display: a novel tool for transduction imaging
Kukkonen, S. P., Airenne, K. J., Marjomäki, V., Laitinen, O. H., Lehtolainen, P., Kankaanpää, P., Mähönen, A. J., Räty, J. K., Nordlund, H. R., Oker‐Blom, C., et al. (2003) · Molecular Therapy · doi:10.1016/j.ymthe.2003.07.009 · Cited by 98
Shimo-Nakanishi, Y., Urabe, T., Hattori, N., Watanabe, Y., Nagao, T., Yokochi, M., Hamamoto, M., & Mizuno, Y. (2001) · Stroke · doi:10.1161/01.str.32.7.1481 · Cited by 96
Kusano, Y., Oguri, K., Nagayasu, Y., Munesue, S., Ishihara, M., Saiki, I., Yonekura, H., Yamamoto, H., & Okayama, M. (2000) · Experimental Cell Research · doi:10.1006/excr.2000.4802 · Cited by 96
Medh, J. D., Bowen, S. L., Fry, G. L., Ruben, S., Andracki, M., Inoue, I., Lalouel, J.-M., Strickland, D. K., & Chappell, D. A. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.29.17073 · Cited by 89
Shakibaei, M., & Frevert, U. (1996) · The Journal of Experimental Medicine · doi:10.1084/jem.184.5.1699 · Cited by 84
Living up to a name: the role of the VLDL receptor in lipid metabolism
Tacken, P. J., Hofker, M. H., Havekes, L. M., & van Dijk, K. W. (2001) · Current Opinion in Lipidology · doi:10.1097/00041433-200106000-00006 · Cited by 83
Self-citationFunctional variants in the lipoprotein lipase gene and risk of cardiovascular disease
Hokanson, J. E. (1999) · Current Opinion in Lipidology · doi:10.1097/00041433-199910000-00003 · Cited by 82
Hokanson, J. E. (1997) · International Journal of Clinical & Laboratory Research · doi:10.1007/bf02827239 · Cited by 80
Role of thyroglobulin endocytic pathways in the control of thyroid hormone release
Marinò, M., & McCluskey, R. T. (2000) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.2000.279.5.c1295 · Cited by 79
Rinninger, F., Kaiser, T., Mann, W. A., Meyer, N., Greten, H., & Beisiegel†, U. (1998) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)32514-1 · Cited by 78
Sullivan, C. J., Teal, T. H., Luttrell, I. P., Tran, K., Peters, M. A., & Wessells, H. (2005) · Physiological Genomics · doi:10.1152/physiolgenomics.00112.2005 · Cited by 76
Cell surface heparan sulfate proteoglycans and lipoprotein metabolism
Kolset, S. O., & Salmivirta, M. (1999) · Cellular and Molecular Life Sciences · doi:10.1007/s000180050031 · Cited by 76
Cellular differences in lipoprotein lipase-mediated uptake of low density lipoproteins.
Obunike, J. C., Edwards, I. J., Rumsey, S. C., Curtiss, L. K., Wagner, W. D., Deckelbaum, R. J., & Goldberg, I. J. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)36808-4 · Cited by 76
Metabolism in two breeds of geese with moderate or large overfeeding induced liver-steatosis
Davail, S., Guy, G. G., André, J., Hermier, D., & Hoo-Paris, R. (2000) · Comparative Biochemistry and Physiology Part A Molecular & Integrative Physiology · doi:10.1016/s1095-6433(00)00190-2 · Cited by 75
Seo, T., Al-Haideri, M. T., Treskova, E., Worgall, T. S., Kako, Y., Goldberg, I. J., & Deckelbaum, R. J. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m910327199 · Cited by 75
Pfohl, M., Schreiber, I., Liebich, H. M., Häring, H. U., & Hoffmeister, H. M. (1999) · Atherosclerosis · doi:10.1016/s0021-9150(98)00242-1 · Cited by 72
Nishitsuji, K., Hosono, T., Uchimura, K., & Michikawa, M. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.172106 · Cited by 65
New aspects on the role of plasma lipases in lipoprotein catabolism and atherosclerosis
Beisiegel†, U. (1996) · Atherosclerosis · doi:10.1016/0021-9150(95)05792-7 · Cited by 71
Omega-3 Triglycerides Modify Blood Clearance and Tissue Targeting Pathways of Lipid Emulsions
Qi, K., Seo, T., Al-Haideri, M. T., Worgall, T. S., Vogel, T., Carpentier, Y., & Deckelbaum, R. J. (2002) · Biochemistry · doi:10.1021/bi015770h · Cited by 70
Receptor-mediated mechanisms of lipoprotein remnant catabolism
Chappell, D. A., & Medh, J. D. (1998) · Progress in Lipid Research · doi:10.1016/s0163-7827(98)00017-4 · Cited by 70
Genetic polymorphisms: importance for response to HMG-CoA reductase inhibitors
der Zee, A. H. M., Klungel, O. H., Stricker, B. H. C., Verschuren, W. M. M., Kastelein, J. J. P., Leufkens, H. G. M., & de Boer, A. (2002) · Atherosclerosis · doi:10.1016/s0021-9150(01)00725-0 · Cited by 70
Gianturco, S. H., Ramprasad, M. P., Song, R., Li, R., Brown, M. L., & Bradley, W. A. (1998) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.18.6.968 · Cited by 70
Hormonal and metabolic responses to overfeeding in three genotypes of ducks
Davail, S., Rideau, N., Guy, G., André, J., Hermier, D., & Hoo-Paris, R. (2003) · Comparative Biochemistry and Physiology Part A Molecular & Integrative Physiology · doi:10.1016/s1095-6433(02)00365-3 · Cited by 68
Salah, D., Bohnet, K., Gueguen, R., Siest, G., & Visvikis‐Siest, S. (1997) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)37215-1 · Cited by 68
Goti, D., Balázs, Z., Panzenboeck, U., Hrzenjak, A., Reicher, H., Wagner, E., Zechner, R., Malle, E., & Sattler, W. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m203989200 · Cited by 65
Bijvoet, S. M., Gagné, S., Moorjani, S., Gagné, C., Henderson, H., Fruchart, J., Dallongeville, J., Alaupovic, P., Prins, M. H., Kastelein, J. J. P., et al. (1996) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)37605-7 · Cited by 65
Megalin (gp330) Is an Endocytic Receptor for Thyroglobulin on Cultured Fisher Rat Thyroid Cells
Marinò, M., Zheng, G., & McCluskey, R. T. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.18.12898 · Cited by 64
Ma, Y., Henderson, H., Min, L. I. U., Zhang, H., Forsythe, I. J., Clarke-Lewis, I., Hayden, M. R., & Brunzell, J. D. (1994) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)39951-x · Cited by 64
Bultel-Brienne, S., Lestavel, S., Pilon, A., Laffont-Proust, I., Tailleux, A., Fruchart, J., Siest, G., & Barthelemy-Clavey, V. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m201943200 · Cited by 63
Kim, M., Kewalramani, G., Puthanveetil, P., Lee, V., Kumar, U., An, D., Abrahani, A., & Rodrigues, B. B. (2007) · Diabetes · doi:10.2337/db07-0832 · Cited by 62
Krapp, A., Zhang, H., Ginzinger, D. G., Liu, M. S., Lindberg, A., Olivecrona, G., Hayden, M. R., & Beisiegel†, U. (1995) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)39717-0 · Cited by 62
Ma, Y., Bao, J., Zhao, X., Shen, H., Lv, J., Ma, S., Zhang, X., Li, Z., Wang, S., Wang, Q., et al. (2013) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m112.026864 · Cited by 60
Avramoglu, R. K., Cianflone, K., & Sniderman, A. D. (1995) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)41088-0 · Cited by 60
The Modification of Serum Lipids after Acute Coronary Syndrome and Importance in Clinical Practice
Balcı, B. (2012) · Current Cardiology Reviews · doi:10.2174/157340311799960690 · Cited by 59
Localization of Lipoprotein Lipase in the Diabetic Heart
Sambandam, N., Abrahani, M. A., Pierre, E. S., Al-Atar, O., Cam, M. C., & Rodrigues, B. B. (1999) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.19.6.1526 · Cited by 58
Wilsie, L. C., Chanchani, S., Navaratna, D., & Orlando, R. A. (2005) · Lipids in Health and Disease · doi:10.1186/1476-511x-4-2 · Cited by 57
Fernandez‐Borja, M., Bellido, D., Vilella, E., Olivecrona, G., & Vilaró, S. (1996) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)37591-x · Cited by 57
Hendriks, W. L., van der Boom, H., VARK, L. C. V., & Havekes, L. M. (1996) · Biochemical Journal · doi:10.1042/bj3140563 · Cited by 57
Self-citationShimano, H., Namba, Y., Ohsuga, J.-I., Kawamura, M., Yamamoto, K., Shimada, M., Gotoda, T., Harada, K., Yazaki, Y., & Yamada, N. (1994) · Journal of Clinical Investigation · doi:10.1172/jci117218 · Cited by 57
Teratani, T., Tomita, K., Furuhashi, H., Sugihara, N., Higashiyama, M., Nishikawa, M., Irie, R., Takajo, T., Wada, A., Horiuchi, K., et al. (2019) · Hepatology Communications · doi:10.1002/hep4.1383 · Cited by 56
Association of lipoprotein lipase gene polymorphisms with coronary artery disease
Anderson, J. L., King, G. J., Bair, T. L., Elmer, S. P., Muhlestein, J. B., Habashi, J., Mixson, L. A., & Carlquist, J. F. (1999) · Journal of the American College of Cardiology · doi:10.1016/s0735-1097(98)00677-9 · Cited by 56
Lipoprotein Lipase Can Function as a Monocyte Adhesion Protein
Obunike, J. C., Paka, S., Pillarisetti, S., & Goldberg, I. J. (1997) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.17.7.1414 · Cited by 54
The lipoprotein lipase S447X polymorphism and plasma lipids
Lee, J., Tan, C. S., Chia, K., Tan, C., Chew, S., Ordovás, J. M., & Tai, E. S. (2004) · Journal of Lipid Research · doi:10.1194/jlr.m400016-jlr200 · Cited by 52
Talmud, P. J., Bujac, S. R., Hall, S., Miller, G. J., & Humphries, S. E. (2000) · Atherosclerosis · doi:10.1016/s0021-9150(99)00309-3 · Cited by 51
Mann, C. J., Khallou‐Laschet, J., Chevreuil, O., Troussard, A. A., Guermani, L. M., Launay, K., Delplanque, B., Yen, F. T., & Bihain, B. E. (1995) · Biochemistry · doi:10.1021/bi00033a014 · Cited by 50
Mulder, M., Koopmans, G., Wassink, G., Mansouri, G. A., Simard, M.-L., Havekes, L. M., Prickaerts, J., & Blokland, A. (2007) · Neuroscience Research · doi:10.1016/j.neures.2007.07.004 · Cited by 49
Self-citationWei, R., Han, C., Deng, D., Ye, F., Gan, X., Liu, H., Li, L., Xu, H., & Wei, S. (2020) · British Poultry Science · doi:10.1080/00071668.2020.1812527 · Cited by 48
Hu, L., van der Hoogt, C. C., Santo, S. M. S. E., Out, R., Kypreos, K. E., van Vlijmen, B. J. M., van Berkel, T. J. C., Romijn, J. A., Havekes, L. M., van Dijk, K. W., et al. (2008) · Journal of Lipid Research · doi:10.1194/jlr.m800130-jlr200 · Cited by 48
Self-citationMutations in the Gene for Lipoprotein Lipase
Pimstone, S. N., Gagné, S., Gagné, C., Lupien, P. J., Gaudet, D., Williams, R. R., Kotze, M. J., Reymer, P. W. A., Defesche, J. C., Kastelein, J. J. P., et al. (1995) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.15.10.1704 · Cited by 44
Anagnostopoulou, K. K., Kolovou, G. D., Kostakou, P. M., Mihas, C. C., Hatzigeorgiou, G., Marvaki, C., Degiannis, D., Mikhailidis, D. P., & Cokkinos, D. V. (2009) · Lipids in Health and Disease · doi:10.1186/1476-511x-8-24 · Cited by 43
Chappell, D. A., Fry, G. L., Waknitz, M. A., Muhonen, L. E., & Pladet, M. W. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)74418-4 · Cited by 43
Seo, T., & Clair, R. W. S. (1997) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)37243-6 · Cited by 43
Lipoprotein lipase-facilitated uptake of LDL is mediated by the LDL receptor
Loeffler, B., Heeren, J., Blaeser, M., Radner, H., Kayser, D., Aydin, B., & Merkel, M. (2006) · Journal of Lipid Research · doi:10.1194/jlr.m600292-jlr200 · Cited by 42
Chen, W., Srinivasan, S. R., Elkasabany, A., Ellsworth, D. L., Boerwinkle, E., & Berenson, G. S. (2001) · Atherosclerosis · doi:10.1016/s0021-9150(01)00508-1 · Cited by 42
Shimada, M., Ishibashi, S., Gotoda, T., Kawamura, M., Yamamoto, K., Inaba, T., Harada, K., Ohsuga, J.-I., Perrey, S., Yazaki, Y., et al. (1995) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.15.10.1688 · Cited by 42
Zsigmond, E., Scheffler, E., Forte, T. M., Potenz, R., Wu, W., & Chan, L. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)32233-0 · Cited by 42
A role for lipoprotein lipase during synaptic remodeling in the adult mouse brain
Blain, J., Paradis, E., Gaudreault, S. B., Champagne, D. L., Richard, D., & Poirier, J. (2004) · Neurobiology of Disease · doi:10.1016/j.nbd.2003.12.001 · Cited by 41
Identification of a Heparin-binding Region of Rat Thyroglobulin Involved in Megalin Binding
Marinò, M., Friedlander, J. A., McCluskey, R. T., & Andrews, D. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.43.30377 · Cited by 41
Finkelstein, J. M., Heemels, M.-T., Shadan, S., & Weiss, U. K. (2014) · Nature · doi:10.1038/510047a · Cited by 41
van Barlingen, H. H. J. J., de Jong, H., Erkelens, D. W., & de Bruin, T. W. A. (1996) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)37573-8 · Cited by 40
Tai, E. S., Adiconis, X., Ordovás, J. M., Carmena-Ramón, R., Real, J., Corella, D., Ascaso, J. F., & Carmena, R. (2002) · Clinical Genetics · doi:10.1034/j.1399-0004.2003.630108.x · Cited by 39
Makoveichuk, E., Lõokene, A., & Olivecrona, G. (1998) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1998.9596 · Cited by 39
Lipoprotein lipase (EC3.1.1.34) targeting of lipoproteins to receptors
Beisiegel†, U., & Heeren, J. (1997) · Proceedings of The Nutrition Society · doi:10.1079/pns19970073 · Cited by 39
Huff, M. W., Miller, D. B., Wolfe, B. M. J., Connelly, P. W., & Sawyez, C. G. (1997) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)37416-2 · Cited by 39
Morita, S. (2003) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/s1388-1981(02)00365-7 · Cited by 38
Halvorsen, B. L., Une, K., Kulseth, M. A., Drevon, C. A., Christiansen, E. N., & Kolset, S. O. (1998) · Biochemical Journal · doi:10.1042/bj3310743 · Cited by 38
Macrophage plasma membrane chondroitin sulfate proteoglycan binds oxidized low-density lipoprotein
Kaplan, M., & Aviram, M. (2000) · Atherosclerosis · doi:10.1016/s0021-9150(99)00287-7 · Cited by 37
Vassiliou, G., & Stanley, K. K. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)36588-2 · Cited by 37
Windler, E. E. T., Greeve, J. C., Robenek, H., Rinninger, F., Greten, H., & Jäckle, S. (1996) · Hepatology · doi:10.1053/jhep.1996.v24.pm0008690403 · Cited by 36
Abu‐Amero, K. K., Wyngaard, C. A., Al-Boudari, O. M., Kambouris, M., & Dzimiri, N. (2003) · Archives of Pathology & Laboratory Medicine · doi:10.5858/2003-127-0597-loaoll · Cited by 35
Extracellular Matrices of the Avian Ovarian Follicle
Hummel, S., Osanger, A., Bajari, T. M., Balasubramani, M., Halfter, W. M., Nimpf, J., & Schneider, W. J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m312694200 · Cited by 35
Changes in cholesterol and its precursors during the first days after major trauma
Bakalář, B., Hyspler, R., Pachl, J., & Zadák, Z. (2003) · Wiener klinische Wochenschrift · doi:10.1007/bf03040502 · Cited by 34
Medh, J. D., Fry, G. L., Bowen, S. L., Ruben, S., Wong, H., & Chappell, D. A. (2000) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)31980-5 · Cited by 34
André, J., Guy, G., Gontier, K., Bernadet, M. D., Davail, B., Hoo-Paris, R., & Davail, S. (2007) · Comparative Biochemistry and Physiology Part A Molecular & Integrative Physiology · doi:10.1016/j.cbpa.2007.09.006 · Cited by 33
Qi, K., Seo, T., Jiang, Z.-F., Carpentier, Y., & Deckelbaum, R. J. (2006) · Journal of Nutrition · doi:10.1093/jn/136.11.2766 · Cited by 33
Metadata
- Authors
- Mulder, M., Lombardi, P., Jansen, H., van Berkel, T. J., Frants, R. R., & Havekes, L. M.
- Affiliations
- Netherlands Organisation for Applied Scientific Research (NL)
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1993-05
- Volume
- 268
- Issue
- 13
- Pages
- 9369-9375
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1525062280
- Cited by
- 214
- References
- 31
- Citations by year
- 2025: 3 · 2024: 1 · 2023: 1 · 2022: 1 · 2021: 5 · 2020: 2 · 2019: 1 · 2018: 1 · 2017: 2 · 2016: 1 · 2015: 5 · 2014: 5 · 2013: 6 · 2012: 5
- FWCI
- 15.93
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- TNO Repository (submittedVersion)
- Repository hosted by TU Delft Library (TU Delft) (submittedVersion)
- Data Archiving and Networked Services (DANS) (submittedVersion, other-oa)
- Topics
- Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Lipid metabolism and disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Cholesterol and Lipid Metabolism
- Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Lipoproteins and Cardiovascular Health
- Keywords
- heparan sulfate proteoglycans, lipoprotein lipase, low-density lipoprotein, VLDL, LDL receptor, receptor internalization, lipoprotein uptake, lysosomal degradation, LDL receptor recycling, receptor down-regulation, hepatic lipoprotein metabolism, fibroblasts, HepG2 cells, lipoprotein binding
- MeSH terms
- Animals, Biological Transport, Cattle, Female, Fibroblasts, Heparan Sulfate, Carcinoma, Hepatocellular, Humans, Kinetics, Lipoprotein Lipase, Lipoproteins, LDL, Lipoproteins, VLDL, Liver Neoplasms, Milk, Models, Biological, Polysaccharide-Lyases, Protein Binding, Proteoglycans, Receptors, LDL, Tumor Cells, Cultured, Heparin Lyase, Heparan Sulfate Proteoglycans
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
A language model drew the claims from the paper on 2026-11-10, under version 3 of the claim definition (model deepseek-v4.1-flash, prompt extract-v3).
A second model labelled each claim on 2026-11-10 (model jev-1.13-20260917, definition revision gold-guideline-v0.2).
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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