apolipoprotein A-II; May stabilize HDL (high density lipoprotein) structure by its association with lipids, and affect the HDL metabolism

apolipoprotein A-IV; May have a role in chylomicrons and VLDL secretion and catabolism. Required for efficient activation of lipoprotein lipase by ApoC-II; potent activator of LCAT. Apoa-IV is a major component of HDL and chylomicrons

apolipoprotein A-II; May stabilize HDL (high density lipoprotein) structure by its association with lipids, and affect the HDL metabolism

apolipoprotein B (including Ag(x) antigen)

apolipoprotein A-II; May stabilize HDL (high density lipoprotein) structure by its association with lipids, and affect the HDL metabolism

apolipoprotein C-III; Inhibits lipoprotein lipase and hepatic lipase and decreases the uptake of lymph chylomicrons by hepatic cells. This suggests that it delays the catabolism of triglyceride-rich particles

apolipoprotein A-II; May stabilize HDL (high density lipoprotein) structure by its association with lipids, and affect the HDL metabolism

glypican 1; Cell surface proteoglycan that bears heparan sulfate. Binds, via the heparan sulfate side chains, alpha-4 (V) collagen and participates in Schwann cell myelination (By similarity). May act as a catalyst in increasing the rate of conversion of prion protein PRPN(C) to PRNP(Sc) via associating (via the heparan sulfate side chains) with both forms of PRPN, targeting them to lipid rafts and facilitating their interaction. Required for proper skeletal muscle differentiation by sequestering FGF2 in lipid rafts preventing its binding to receptors (FGFRs) and inhibiting the FGF-med [...]

apolipoprotein A-II; May stabilize HDL (high density lipoprotein) structure by its association with lipids, and affect the HDL metabolism

glypican 2; Cell surface proteoglycan that bears heparan sulfate. May fulfill a function related to the motile behaviors of developing neurons (By similarity)

apolipoprotein A-II; May stabilize HDL (high density lipoprotein) structure by its association with lipids, and affect the HDL metabolism

glypican 3; Cell surface proteoglycan that bears heparan sulfate. Inhibits the dipeptidyl peptidase activity of DPP4. May be involved in the suppression/modulation of growth in the predominantly mesodermal tissues and organs. May play a role in the modulation of IGF2 interactions with its receptor and thereby modulate its function. May regulate growth and tumor predisposition

apolipoprotein A-II; May stabilize HDL (high density lipoprotein) structure by its association with lipids, and affect the HDL metabolism

glypican 4; Cell surface proteoglycan that bears heparan sulfate. May be involved in the development of kidney tubules and of the central nervous system (By similarity)

apolipoprotein A-II; May stabilize HDL (high density lipoprotein) structure by its association with lipids, and affect the HDL metabolism

glypican 5; Cell surface proteoglycan that bears heparan sulfate (By similarity)

apolipoprotein A-II; May stabilize HDL (high density lipoprotein) structure by its association with lipids, and affect the HDL metabolism

heparan sulfate proteoglycan 2; Integral component of basement membranes. Component of the glomerular basement membrane (GBM), responsible for the fixed negative electrostatic membrane charge, and which provides a barrier which is both size- and charge-selective. It serves as an attachment substrate for cells. Plays essential roles in vascularization. Critical for normal heart development and for regulating the vascular response to injury. Also required for avascular cartilage development

apolipoprotein A-II; May stabilize HDL (high density lipoprotein) structure by its association with lipids, and affect the HDL metabolism

lipoprotein lipase; The primary function of this lipase is the hydrolysis of triglycerides of circulating chylomicrons and very low density lipoproteins (VLDL). Binding to heparin sulfate proteogylcans at the cell surface is vital to the function. The apolipoprotein, APOC2, acts as a coactivator of LPL activity in the presence of lipids on the luminal surface of vascular endothelium (By similarity)

apolipoprotein A-II; May stabilize HDL (high density lipoprotein) structure by its association with lipids, and affect the HDL metabolism

low density lipoprotein receptor-related protein 1; Endocytic receptor involved in endocytosis and in phagocytosis of apoptotic cells. Required for early embryonic development. Involved in cellular lipid homeostasis. Involved in the plasma clearance of chylomicron remnants and activated LRPAP1 (alpha 2-macroglobulin), as well as the local metabolism of complexes between plasminogen activators and their endogenous inhibitors. May modulate cellular events, such as APP metabolism, kinase-dependent intracellular signaling, neuronal calcium signaling as well as neurotransmission

apolipoprotein A-II; May stabilize HDL (high density lipoprotein) structure by its association with lipids, and affect the HDL metabolism

syndecan 1; Cell surface proteoglycan that bears both heparan sulfate and chondroitin sulfate and that links the cytoskeleton to the interstitial matrix

apolipoprotein A-II; May stabilize HDL (high density lipoprotein) structure by its association with lipids, and affect the HDL metabolism

syndecan 2; Cell surface proteoglycan that bears heparan sulfate. Regulates dendritic arbor morphogenesis (By similarity)

apolipoprotein A-II; May stabilize HDL (high density lipoprotein) structure by its association with lipids, and affect the HDL metabolism

syndecan 3; Cell surface proteoglycan that may bear heparan sulfate (By similarity). May have a role in the organization of cell shape by affecting the actin cytoskeleton, possibly by transferring signals from the cell surface in a sugar-dependent mechanism

apolipoprotein A-II; May stabilize HDL (high density lipoprotein) structure by its association with lipids, and affect the HDL metabolism

syndecan 4; Cell surface proteoglycan that bears heparan sulfate

apolipoprotein A-IV; May have a role in chylomicrons and VLDL secretion and catabolism. Required for efficient activation of lipoprotein lipase by ApoC-II; potent activator of LCAT. Apoa-IV is a major component of HDL and chylomicrons

apolipoprotein A-II; May stabilize HDL (high density lipoprotein) structure by its association with lipids, and affect the HDL metabolism

apolipoprotein A-IV; May have a role in chylomicrons and VLDL secretion and catabolism. Required for efficient activation of lipoprotein lipase by ApoC-II; potent activator of LCAT. Apoa-IV is a major component of HDL and chylomicrons

apolipoprotein B (including Ag(x) antigen)

apolipoprotein A-IV; May have a role in chylomicrons and VLDL secretion and catabolism. Required for efficient activation of lipoprotein lipase by ApoC-II; potent activator of LCAT. Apoa-IV is a major component of HDL and chylomicrons

apolipoprotein C-III; Inhibits lipoprotein lipase and hepatic lipase and decreases the uptake of lymph chylomicrons by hepatic cells. This suggests that it delays the catabolism of triglyceride-rich particles

apolipoprotein A-IV; May have a role in chylomicrons and VLDL secretion and catabolism. Required for efficient activation of lipoprotein lipase by ApoC-II; potent activator of LCAT. Apoa-IV is a major component of HDL and chylomicrons

amyloid beta (A4) precursor protein

apolipoprotein A-IV; May have a role in chylomicrons and VLDL secretion and catabolism. Required for efficient activation of lipoprotein lipase by ApoC-II; potent activator of LCAT. Apoa-IV is a major component of HDL and chylomicrons

glypican 1; Cell surface proteoglycan that bears heparan sulfate. Binds, via the heparan sulfate side chains, alpha-4 (V) collagen and participates in Schwann cell myelination (By similarity). May act as a catalyst in increasing the rate of conversion of prion protein PRPN(C) to PRNP(Sc) via associating (via the heparan sulfate side chains) with both forms of PRPN, targeting them to lipid rafts and facilitating their interaction. Required for proper skeletal muscle differentiation by sequestering FGF2 in lipid rafts preventing its binding to receptors (FGFRs) and inhibiting the FGF-med [...]