PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
8682650-6	1996	Assuming that a) heparinase treatment abolished the heparan-sulfate pathway, and that b) the degradation remaining in heparin-treated cultures represents nonspecific values, it appears that heparan sulfate contributes about 61%, 83% and 95% of total LPL degradation, whereas the LRP pathway contributes 39%, 17% and less than 5% of LPL degradation in MEF, PEA-10 and PEA-13 cells, respectively.	Heparitin Sulfate	190-205	lipoprotein lipase	Mus musculus	250-253	
8682650-6	1996	Assuming that a) heparinase treatment abolished the heparan-sulfate pathway, and that b) the degradation remaining in heparin-treated cultures represents nonspecific values, it appears that heparan sulfate contributes about 61%, 83% and 95% of total LPL degradation, whereas the LRP pathway contributes 39%, 17% and less than 5% of LPL degradation in MEF, PEA-10 and PEA-13 cells, respectively.	Heparitin Sulfate	190-205	lipoprotein lipase	Mus musculus	332-335	
8682650-7	1996	In addition, the data indicate that LPL interaction with heparan sulfate and the LRP pathways is independent of each other.	Heparitin Sulfate	57-72	lipoprotein lipase	Mus musculus	36-39	
11129947-1	2000	Altered lipoprotein lipase regulation associated with diabetes leading to the development of hypertriglyceridemia might be attributed to possible changes in content and the fine structure of heparan sulfate and its associated lipoprotein lipase.	Heparitin Sulfate	191-206	lipoprotein lipase	Mus musculus	8-26	
11129947-1	2000	Altered lipoprotein lipase regulation associated with diabetes leading to the development of hypertriglyceridemia might be attributed to possible changes in content and the fine structure of heparan sulfate and its associated lipoprotein lipase.	Heparitin Sulfate	191-206	lipoprotein lipase	Mus musculus	226-244	
11129947-2	2000	Adipocyte cell surface is the primary site of synthesis of lipoprotein lipase and the enzyme is bound to cell surface heparan sulfate proteoglycans via heparan sulfate side chains.	Heparitin Sulfate	118-133	lipoprotein lipase	Mus musculus	59-77	
11129947-2	2000	Adipocyte cell surface is the primary site of synthesis of lipoprotein lipase and the enzyme is bound to cell surface heparan sulfate proteoglycans via heparan sulfate side chains.	Heparitin Sulfate	152-167	lipoprotein lipase	Mus musculus	59-77	
11129947-9	2000	Heparan sulfate from adipocytes cultured in low glucose conditions binds to lipoprotein lipase by the same order of magnitude as that derived from high glucose conditions.	Heparitin Sulfate	0-15	lipoprotein lipase	Mus musculus	76-94	
11129947-11	2000	In conclusion, it is possible that the reduction in heparan sulfate in diabetes could contribute to the decreased levels of heparan sulfate associated lipoprotein lipase, leading to diabetic hypertriglyceridemia.	Heparitin Sulfate	52-67	lipoprotein lipase	Mus musculus	151-169	
8682650-0	1996	Heparan sulfate-dependent and low density lipoprotein receptor-related protein-dependent catabolic pathways for lipoprotein lipase in mouse embryonic fibroblasts.	Heparitin Sulfate	0-15	lipoprotein lipase	Mus musculus	112-130	
8682650-1	1996	Heparan sulfate and low density lipoprotein receptor related protein (LRP) have been shown to participate in the uptake and degradation of the enzyme lipoprotein lipase (LPL).	Heparitin Sulfate	0-15	lipoprotein lipase	Mus musculus	150-168	
8682650-1	1996	Heparan sulfate and low density lipoprotein receptor related protein (LRP) have been shown to participate in the uptake and degradation of the enzyme lipoprotein lipase (LPL).	Heparitin Sulfate	0-15	lipoprotein lipase	Mus musculus	170-173	
35229724-6	2022	The GPIHBP1-bound LPL was trapped on the abluminal surface of ECs by electrostatic interactions between the large basic patch on the surface of LPL and negatively charged heparan sulfate proteoglycans (HSPGs) on the surface of ECs.	Heparitin Sulfate	171-186	lipoprotein lipase	Mus musculus	18-21