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Comparison of angiopoietin-like protein 3 and 4 reveals structural and mechanistic similarities

Gunn, Kathryn H., Gutgsell, Aspen R., Xu, Yongmei, Johnson, Caitlin V., Liu, Jian, Neher, Saskia B.·2021·Journal of Biological Chemistry
DOI 10.1016/j.jbc.2021.100312PMC PMC7949051
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Figure 1 DNA contamination reduces ANGPTL3 inhibition potency.A, schematic of ANGPTL3, highlighting the N-terminal construct used for this work. B, representative ANGPTL3 SEC elution profile following nickel affinity purification. ANGPTL3 protein (280 nm, blue) eluted as two peaks, labeled peak 1 and peak 2. The ANGPTL3 was contaminated with nucleic acid (254 nm, red). C, the ANGPTL3 nucleic acid contaminant from ANGPTL3 peak 1 was visualized on an agarose gel. The contaminant was sensitive to DNase, but not RNase, indicating the contaminant was DNA. D, lipoprotein lipase inhibition with DNA-contaminated ANGPTL3 peak 1 and peak 2 significantly differ. E, an additional MonoQ anion-exchange purification step was performed between the nickel affinity column and SEC. A representative SEC trace shows that the ANGPTL3 DNA contamination was substantially reduced (254 nm, red), allowing better resolution of the ANGPTL3 peak 1 and peak 2 proteins (280 nm, blue). F, ANGPTL3 peak 1 and peak 2 were visualized using SDS-PAGE, showing both peak 1 and peak 2 contain ANGPTL3 (26.8 kDa). G, after removal of DNA, both ANGPTL3 peak 1 and peak 2 inhibit lipoprotein lipase equivalently. SEC, size-exclusion chromatography.
Figure 1 DNA contamination reduces ANGPTL3 inhibition potency.A, schematic of ANGPTL3, highlighting the N-terminal construct used for this work. B, representative ANGPTL3 SEC elution profile following nickel affinity purification. ANGPTL3 protein (280 nm, blue) eluted as two peaks, labeled peak 1 and peak 2. The ANGPTL3 was contaminated with nucleic acid (254 nm, red). C, the ANGPTL3 nucleic acid contaminant from ANGPTL3 peak 1 was visualized on an agarose gel. The contaminant was sensitive to DNase, but not RNase, indicating the contaminant was DNA. D, lipoprotein lipase inhibition with DNA-contaminated ANGPTL3 peak 1 and peak 2 significantly differ. E, an additional MonoQ anion-exchange purification step was performed between the nickel affinity column and SEC. A representative SEC trace shows that the ANGPTL3 DNA contamination was substantially reduced (254 nm, red), allowing better resolution of the ANGPTL3 peak 1 and peak 2 proteins (280 nm, blue). F, ANGPTL3 peak 1 and peak 2 were visualized using SDS-PAGE, showing both peak 1 and peak 2 contain ANGPTL3 (26.8 kDa). G, after removal of DNA, both ANGPTL3 peak 1 and peak 2 inhibit lipoprotein lipase equivalently. SEC, size-exclusion chromatography.CC BY · PubMed Central
Figure 2 ANGPTL3 forms noninterconvertible hexamers and trimers and ANGPTL4 forms a trimer. SEC purified (A) ANGPTL3 peak 1 and (B) ANGPTL3 peak 2 were separately concentrated and reinjected for analysis with SEC–multiangle light scattering. Peak 1 had a molecular weight (MW) of 151 kDa, indicating a hexamer of ANGPTL3 (monomer 26.8 kDa). Peak 2 had a MW of 76 kDa, indicating a trimer of ANGPTL3. The ANGPTL3 trimers and hexamers did not interconvert when reinjected on SEC. Owing to the elution being close together, a small amount of trimer and hexamer can be seen after the peaks were separated and reinjected. C, SEC purified ANGPTL4 was concentrated and injected for SEC–multiangle light scattering analysis. ANGPTL4 resolved as a single peak with a MW of 46 kDa, which indicates a trimer of ANGPTL4 (monomer 15.4 kDa). The UV trace representing protein absorbance at 280 nm is in black and MW is represented in gray. SEC, size-exclusion chromatography.
Figure 2 ANGPTL3 forms noninterconvertible hexamers and trimers and ANGPTL4 forms a trimer. SEC purified (A) ANGPTL3 peak 1 and (B) ANGPTL3 peak 2 were separately concentrated and reinjected for analysis with SEC–multiangle light scattering. Peak 1 had a molecular weight (MW) of 151 kDa, indicating a hexamer of ANGPTL3 (monomer 26.8 kDa). Peak 2 had a MW of 76 kDa, indicating a trimer of ANGPTL3. The ANGPTL3 trimers and hexamers did not interconvert when reinjected on SEC. Owing to the elution being close together, a small amount of trimer and hexamer can be seen after the peaks were separated and reinjected. C, SEC purified ANGPTL4 was concentrated and injected for SEC–multiangle light scattering analysis. ANGPTL4 resolved as a single peak with a MW of 46 kDa, which indicates a trimer of ANGPTL4 (monomer 15.4 kDa). The UV trace representing protein absorbance at 280 nm is in black and MW is represented in gray. SEC, size-exclusion chromatography.CC BY · PubMed Central
Figure 3 ANGPTL3 and ANGPTL4 have elongated structures. Size-exclusion chromatography–small-angle X-ray scattering scattering data as a log-linear plot with inset showing the real-space distance distribution and the filtered average ab initio models determined using DAMMIN for (A) ANGPTL3 hexamer (SASDJK8), (B) ANGPTL3 trimer (SASDJL8), and (C) ANGPTL4 (SASDJM8). Data deposited in the Small Angle Scattering Biological Data Bank (SASBDB) (61).
Figure 3 ANGPTL3 and ANGPTL4 have elongated structures. Size-exclusion chromatography–small-angle X-ray scattering scattering data as a log-linear plot with inset showing the real-space distance distribution and the filtered average ab initio models determined using DAMMIN for (A) ANGPTL3 hexamer (SASDJK8), (B) ANGPTL3 trimer (SASDJL8), and (C) ANGPTL4 (SASDJM8). Data deposited in the Small Angle Scattering Biological Data Bank (SASBDB) (61).CC BY · PubMed Central
Figure 4 ANGPTL3 and ANGPTL4 are both potent LPL inhibitors. Representative IC50 curves were collected with 10 nM LPL, 200 μg/ml VLDL triglycerides, and varying amounts of (A) ANGPTL3 hexamer, (B) ANGPTL3 trimer, or (C) ANGPTL4. IC50 was calculated from three biological replicates and the error from the standard deviation. Data were fit with an exponential decay curve in KaleidaGraph and the IC50 determined from where the curve crossed 50% of the maximum LPL activity without inhibitor. The ANGPTL3 hexamer had the least potent IC50, whereas the IC50s for the ANGPTL3 trimer and ANGPTL4 were similar. Representative Michaelis–Menten curves were collected at 10 nM LPL with varying amounts of VLDL and (D) ANGPTL3 hexamer, (E) ANGPTL3 trimer, and (F) ANGPTL4 as indicated. Analysis of the data showed that the Vmax decreased with increasing inhibitor concentration, and the Km did not change (Fig. S4). These results are consistent with a noncompetitive mechanism of inhibition for both ANGPTL3 and ANGPTL4. The reported Ki is the average of three biological replicates analyzed using a global noncompetitive fit, and the error is the standard deviation between replicates. LPL, lipoprotein lipase; VLDL, very-low-density lipoprotein.
Figure 4 ANGPTL3 and ANGPTL4 are both potent LPL inhibitors. Representative IC50 curves were collected with 10 nM LPL, 200 μg/ml VLDL triglycerides, and varying amounts of (A) ANGPTL3 hexamer, (B) ANGPTL3 trimer, or (C) ANGPTL4. IC50 was calculated from three biological replicates and the error from the standard deviation. Data were fit with an exponential decay curve in KaleidaGraph and the IC50 determined from where the curve crossed 50% of the maximum LPL activity without inhibitor. The ANGPTL3 hexamer had the least potent IC50, whereas the IC50s for the ANGPTL3 trimer and ANGPTL4 were similar. Representative Michaelis–Menten curves were collected at 10 nM LPL with varying amounts of VLDL and (D) ANGPTL3 hexamer, (E) ANGPTL3 trimer, and (F) ANGPTL4 as indicated. Analysis of the data showed that the Vmax decreased with increasing inhibitor concentration, and the Km did not change (Fig. S4). These results are consistent with a noncompetitive mechanism of inhibition for both ANGPTL3 and ANGPTL4. The reported Ki is the average of three biological replicates analyzed using a global noncompetitive fit, and the error is the standard deviation between replicates. LPL, lipoprotein lipase; VLDL, very-low-density lipoprotein.CC BY · PubMed Central
Figure 5 Heparin effects LPL inhibition of ANGPTL3 and ANGPTL4. The activity of LPL was determined in the presence of ANGPTL3 using both (A) DGGR and (B) VLDL as substrates. ANGPTL3 experiences a significant loss of inhibition when incubated with 12-mer heparin, but not 6-mer heparin for both substrates. LPL activity was also tested with ANGPTL4 using (C) DGGR and (D) VLDL substrates. ANGPTL4 is an effective inhibitor with addition of either heparin variant. E, biotinylated 6-mer and 12-mer were used to pull down human LPL, ANGPTL3, and ANGPTL4 and assessed via Western blot. Both LPL and ANGPTL4 bound to the 6-mer and 12-mer, whereas ANGPTL3 only showed binding to the 12-mer. Full blots are shown in Fig. S5. DGGR assays were performed with 2.5 nM LPL, 6 μM ANGPTL, 10 μg/ml heparin, and 10 μM DGGR. VLDL assays were performed with 10 nM LPL, 10 nM ANGPTL, 2 nM heparin, and 200 μg/ml VLDL triglycerides. Data were normalized to the activity of LPL without inhibitor present. Dots represent biological replicates; significance was determined by two-tailed Student’s t test. DGGR, 1,2-Di-O-lauryl-rac-glycero-3-glutaric acid 6′-methylresorufin ester; LPL, lipoprotein lipase; VLDL, very-low-density lipoprotein.
Figure 5 Heparin effects LPL inhibition of ANGPTL3 and ANGPTL4. The activity of LPL was determined in the presence of ANGPTL3 using both (A) DGGR and (B) VLDL as substrates. ANGPTL3 experiences a significant loss of inhibition when incubated with 12-mer heparin, but not 6-mer heparin for both substrates. LPL activity was also tested with ANGPTL4 using (C) DGGR and (D) VLDL substrates. ANGPTL4 is an effective inhibitor with addition of either heparin variant. E, biotinylated 6-mer and 12-mer were used to pull down human LPL, ANGPTL3, and ANGPTL4 and assessed via Western blot. Both LPL and ANGPTL4 bound to the 6-mer and 12-mer, whereas ANGPTL3 only showed binding to the 12-mer. Full blots are shown in Fig. S5. DGGR assays were performed with 2.5 nM LPL, 6 μM ANGPTL, 10 μg/ml heparin, and 10 μM DGGR. VLDL assays were performed with 10 nM LPL, 10 nM ANGPTL, 2 nM heparin, and 200 μg/ml VLDL triglycerides. Data were normalized to the activity of LPL without inhibitor present. Dots represent biological replicates; significance was determined by two-tailed Student’s t test. DGGR, 1,2-Di-O-lauryl-rac-glycero-3-glutaric acid 6′-methylresorufin ester; LPL, lipoprotein lipase; VLDL, very-low-density lipoprotein.CC BY · PubMed Central

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Metadata

Authors
Gunn, K. H., Gutgsell, A. R., Xu, Y., Johnson, C. V., Liu, J., & Neher, S. B.
ORCID
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
2021-01
Volume
296
Pages
100312
ISSN
0021-9258
DOI
10.1016/j.jbc.2021.100312
PMC
PMC7949051
Cited by
12
References
5
Language
en
Licence
Funders
  • American Heart Association (19PRE34370070, 20POST35210031)
  • Office of Science
  • National Institutes of Health (R01-HL094463)
  • Argonne National Laboratory (DE-AC02-06CH11357)
  • U.S. Department of Energy
  • University of North Carolina
  • National Cancer Institute
  • Office of Extramural Research, National Institutes of Health (1R42GM128484, 9 P41 GM103622, P30 GM124169, P30CA016086, R01-HL12565, R01-HL144970)
  • National Institute of General Medical Sciences (S10OD018483)

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