Journal: JACC: Basic to Translational Science

Article Title: PCSK9 Modulates the Secretion But Not the Cellular Uptake of Lipoprotein(a) Ex Vivo

doi: 10.1016/j.jacbts.2016.06.006

Figure Lengend Snippet: PCSK9 Treatment Increases Apo(a) Secretion From Primary Human Hepatocytes: An Effect Blocked by Alirocumab Cells were treated with increasing concentrations of recombinant PCSK9 with or without alirocumab for 72 h. ApoB100 (A) and apo(a) (B) were quantified in the culture medium by enzyme-linked immunosorbent assay and liquid chromatography-tandem mass spectrometry, respectively. *p < 0.05 vs. control (no PCSK9). **p < 0.05 vs. same dose of PCSK9 without alirocumab, using 1-way analysis of variance on rank-transformed values with post-hoc Newman-Keuls test. Histograms represent the mean ± SEM of 3 independent experiments from 2 hepatocyte donors. Abbreviations as in Figure 1 .

Article Snippet: The culture medium was collected, spun to get rid of cell debris, and assessed for apoB100 concentration with the EA 7001-1 sandwich enzyme-linked immunosorbent assay (ELISA) kit (Assaypro, St Charles, Missouri), and for apo(a) concentration by ELISA with the EL3001-1 sandwich ELISA kit (Assaypro) as well as by liquid chromatography-tandem mass spectrometry (LC-MS/MS).

Techniques: Recombinant, Enzyme-linked Immunosorbent Assay, Liquid Chromatography, Mass Spectrometry, Control, Transformation Assay

Journal: Proceedings of the National Academy of Sciences of the United States of America

Article Title: Recruitment of APOL1 kidney disease risk variants to lipid droplets attenuates cell toxicity.

doi: 10.1073/pnas.1820414116

Figure Lengend Snippet: Fig. 1. APOL1 is a lipid droplet-associated protein that can alter lipid droplet number and size. (A and B) Fluorescence micrographs of human primary podocytes transiently transfected with untagged APOL1 (G0, G1, or G2) (A) or with RFP-tagged APOL1 (B). Lipid droplets were labeled with BODIPY 493/503 (green) and nuclei with DAPI. (Scale bar, 10 μm.) (C and D) Percentage of human primary podocytes containing APOL1-positive LDs (C) (as in A) or APOL1-RFP–positive LDs (D) (as in B). Data from each group represent >50 podocytes from three independent experiments. Data are presented as means ± SD. ***P < 0.001; ns, non- significant. (E) Number of LDs per cell in APOL1-RFP–expressing human primary podocytes. Data from three independent experiments, each with at least 30 cells per group, are presented as means ± SD. ***P < 0.001; ns, nonsignificant. (F) Cross-sectional area (number of pixels) of human primary podocytes transfected with APOL1-RFP, quantified from pooled cells from three separate experiments for each group with untransfected (UT) n = 545, G0 n = 131, G1 n = 48, and G2 n = 75 presented as means ± SD. *P < 0.05, ***P < 0.001. (G) Distribution of lipid droplet diameters in untransfected human primary podocytes or podocytes transfected with APOL1-RFP (G0, G1, G2). (H) Indirect immunofluorescence of human primary podocytes transfected with APOL1-FLAG (G0-FLAG and G2-FLAG) and labeled with BODIPY 493/503 and DAPI. (Scale bar, 10 μm.) (I) Immunoblot analysis of purified APOL1-FLAG; 1% Nonidet P-40 lysates from human primary podocytes transfected 16 to 18 h previously with Apol1-FLAG (G0, G2) or empty vector were incubated with anti-FLAG agarose and eluted with 3× FLAG peptide. (J) APOL1-FLAG solid-phase lipid binding. Affinity-purified APOL1-FLAG (G0, G2) or 3× FLAG peptide (negative control) were used in a lipid overlay assay. APOL1- FLAG (G0) bound strongly to PI(4)P, PI(4,5)P2, and PI(3,4,5)P3 and less strongly to PPA and CL. APOL1-FLAG (G2) bound more strongly to PS and CL than to PI(4,5)P2 or PI(3,4,5)P3. One of two experiments with identical results performed with one of two immunopurified preparations of recombinant APOL1. 3-SGC, 3-sulfogalactosylceramide; Blank, solvent blank; Chol, cholesterol; CL, cardiolipin; DAG, diacylglycerol; PPA, phosphatidic acid; PC, phosphati- dylcholine; PE, phosphatidylethanolamine; PG, phosphatidylglycerol; PI(4)P, phosphatidylinositol (4)-phosphate; PI(4,5)P2, phosphatidylinositol (4,5)-bisphos- phate; PI, phosphatidylinositol; PI(3,4,5)P3, phosphatidylinositol (3–5)-trisphosphate; PS, phosphatidylserine; SPH, sphingomyelin; TG, triglyceride.

Article Snippet: APOL1 cDNA was purchased from OriGene.

Techniques: Fluorescence, Transfection, Labeling, Expressing, Immunofluorescence, Western Blot, Purification, Plasmid Preparation, Incubation, Binding Assay, Affinity Purification, Negative Control, Overlay Assay, Recombinant, Solvent

Journal: Proceedings of the National Academy of Sciences of the United States of America

Article Title: Recruitment of APOL1 kidney disease risk variants to lipid droplets attenuates cell toxicity.

doi: 10.1073/pnas.1820414116

Figure Lengend Snippet: Fig. 2. Differential localization of wild-type (G0) APOL1 to LDs and its risk variants (G1, G2) primarily to the ER. (A) SR-SIM micrographs of representative primary human podocytes transiently transfected with APOL1-RFP, labeled for perilipin-2 (light blue), and with BODIPY 493/503 and DAPI (blue). [Scale bars, 10 μm and 2 μm (Insets).] (B) SR-SIM micrographs of primary human podocytes transiently transfected with APOL1-GFP, labeled for mitochondria (MitoTracker in red), ER (calnexin in magenta), and DAPI (blue). [Scale bars, 10 μm and 2 μm (Insets).] (C) Colocalization analysis of APOL1-GFP with MitoTracker Red (mitochondria) or calnexin (endoplasmic reticulum). Data are presented as means ± SD. *P < 0.05. (D and E) Yellow arrow indicating colocalization of APOL1- RFP with GFP-Rab7. Airyscan micrographs of live primary human podocytes coexpressing APOL1-RFP (G0) with GFP-Rab7 and mito-BFP (D) or with GFP- PLIN2 and BFP-KDEL (E). [Scale bars, 10 μm and 2 μm (Insets).] See SI Appendix, Fig. S3 for time frame still images. See also Movies S1 and S2.

Article Snippet: APOL1 cDNA was purchased from OriGene.

Techniques: Transfection, Labeling

Journal: Proceedings of the National Academy of Sciences of the United States of America

Article Title: Recruitment of APOL1 kidney disease risk variants to lipid droplets attenuates cell toxicity.

doi: 10.1073/pnas.1820414116

Figure Lengend Snippet: Fig. 3. Treatment with oleic acid can enrich APOL1(G0)-RFP on LDs and redistribute risk variants G1 and G2 from a reticular pattern to LDs. SR-SIM mi- crographs of representative human primary podocytes transiently transfected with APOL1-GFP and treated with vehicle (fatty acid-free BSA) (A) or oleic acid (0.8 mM) (B), and then labeled with BODIPY 665/676 and DAPI. (Scale bars, 10 μm.)

Article Snippet: APOL1 cDNA was purchased from OriGene.

Techniques: Transfection, Labeling

Journal: Proceedings of the National Academy of Sciences of the United States of America

Article Title: Recruitment of APOL1 kidney disease risk variants to lipid droplets attenuates cell toxicity.

doi: 10.1073/pnas.1820414116

Figure Lengend Snippet: Fig. 4. Treatment of T-Rex-293 cells with oleic acid reduces cellular toxicity and autophagic flux. (A) Bright-field phase-contrast micrographs of represen- tative APOL1 T-Rex-293 cells stably expressing empty vector (EV), G0, G1, or G2 pretreated with vehicle (fatty acid-free BSA), 1 mM oleic acid, or 1 mM palmitic acid for 3 h and then induced for 18.5 h with tetracycline (10 ng/mL) to express APOL1. (Scale bar, 50 μm.) (B) Quantitation of T-Rex-293 cells stably expressing an empty vector or APOL1 variants G0, G1, or G2 treated with BSA, 1 mM OA, or 1 mM PA and induced to express APOL1 with tetracycline (10 ng/mL) for 16 h. ***P < 0.001. (C) Cell cytotoxicity/viability after 22-h treatment with tetracycline (10 ng/mL). Data from two independent experiments, each with eight experimental replicates, are presented as means ± SD. ***P < 0.001; ns, nonsignificant. (D) Immunoblot of APOL1-FLAG, LC3, and vinculin from whole-cell lysates prepared after 22-h induction with tetracycline (10 ng/mL) and treatment with 1 mM OA or 1 mM PA. (E) Quantitation of band intensities by den- sitometry from two independent experiments for LC3I and LC3II mean densities (from C) displayed as a ratio (means ± SD).

Article Snippet: APOL1 cDNA was purchased from OriGene.

Techniques: Stable Transfection, Expressing, Plasmid Preparation, Quantitation Assay, Western Blot

Journal: Proceedings of the National Academy of Sciences of the United States of America

Article Title: Recruitment of APOL1 kidney disease risk variants to lipid droplets attenuates cell toxicity.

doi: 10.1073/pnas.1820414116

Figure Lengend Snippet: Fig. 5. Coexpression of APOL1 (G0) with its risk variants (G1 or G2) promotes G1/G2 accumulation on LDs and reduces cell death. (A) Diagram illustrating predicted localization of APOL1-RFP (red) or APOL1-GFP (green) variants to the LD or ER. (B) Immunoblot of whole-cell lysates from human primary podocytes transiently cotransfected with the indicated APOL1-RFP and APOL1-GFP variant DNAs in equal amounts. (C) Airyscan micrographs of human primary podocytes cotransfected with the indicated variants of APOL1-RFP (red), APOL1-GFP (green), and BODIPY 665/676 (blue). Merged images in magenta when overlapped with APOL1-RFP, APOL1-GFP, and BODIPY 665/676. (Scale bar, 10 μm.) (D) Quantitation of human primary podocytes containing detectable LDs positive for APOL1-RFP (G0, G1, G2) when cotransfected with the indicated APOL1-GFP variants. Data from three independent experiments per group, each with ≥50 cells analyzed, are presented as means ± SD. ***P < 0.001; ns, nonsignificant. (E) Number of LDs per cell in human primary podocytes cotransfected with APOL1-RFP and APOL1-GFP. Data presented from at least 25 cells per group are presented as means ± SD. ***P < 0.001; ns, nonsignificant. (F) Cross-sectional area of human primary podocytes cotransfected with APOL1-RFP and APOL1-GFP; quantified for each group, G0-RFP/G0-GFP n = 56, G0-RFP/G2-GFP n = 46, and G2-RFP/G2-GFP n = 65, presented as means ± SD. *P < 0.05, ***P < 0.001. (G) Quantitation from bright-field images using five fields from two representative experiments of tetracycline-inducible transgenic APOL1 T-Rex-293 cells stably expressing empty vector (C-terminal MYC and FLAG tags), G0 (APOL1-G0-T-Rex-293), G1 (APOL1-G1-T-Rex-293), or G2 (APOL1-G2-T-Rex-293) cells transfected with plasmids encoding RFP (control plasmid), G0-RFP (G0), or G2-RFP (G2) 4 h before induction of tetracycline (10 ng/mL)- inducible APOL1 for 16 h. **P < 0.01, ***P < 0.001. (H) Immunoblot of APOL1 T-Rex-293 whole-cell lysates after transient transfection with APOL1-FLAG (G0, G2) or empty vector 4 h before tetracycline (10 ng/mL) induction for 18 h and cell collection at 22 h. (I) Quantitation of cytotoxicity/viability of APOL1 T-Rex-293 cells transiently transfected with APOL1-FLAG (G0, G2) or empty vector for 4 h before tetracycline induction for 18 h. Data from three independent experiments, each with eight experimental replicates, are presented as means ± SD. ***P < 0.001, *P < 0.05; ns, nonsignificant.

Article Snippet: APOL1 cDNA was purchased from OriGene.

Techniques: Western Blot, Variant Assay, Quantitation Assay, Transgenic Assay, Stable Transfection, Expressing, Plasmid Preparation, Transfection, Control

Journal: Proceedings of the National Academy of Sciences of the United States of America

Article Title: Recruitment of APOL1 kidney disease risk variants to lipid droplets attenuates cell toxicity.

doi: 10.1073/pnas.1820414116

Figure Lengend Snippet: Fig. 6. Model for APOL1-mediated cytotoxicity and its reduction by ma- neuvers promoting LD formation and enlargement. Under normal physio- logic conditions, podocytes express low levels of APOL1 and do not cause cytotoxicity. Innate immune activation by environmental stress or viral in- fection are thought to up-regulate APOL1. Accumulating levels of G1 and G2 may reach a threshold level causing burden on organelles such as the ER and mitochondria, possibly via communication via mitochondrial-associated membranes. Excess APOL1 will activate cell stress pathways including stress- activated protein kinases, ER stress pathways, and mitochondrial oxidation pathways. LD formation might (partially or totally) relieve stress pathways caused by excessive APOL1 risk variant accumulation in the ER. 1: For G0, APOL1 can be efficiently diverted away from the ER to the LD (a relatively inert reservoir for lipophilic proteins) and the podocyte can process APOL1 to levels below a threshold causing toxicity. APOL1 directed to lipid droplets can interact with other organelles, including endosomes and mitochondria, which may aid the processing, transport, and metabolism of APOL1. 2: Coover- expression of wild-type APOL1 can recruit APOL1 risk variants to lipid drop- lets. 3: Treatment with OA can increase LD size and number, acting as shuttles to sequester toxic APOL1 risk variant polypeptides away from the ER.

Article Snippet: APOL1 cDNA was purchased from OriGene.

Techniques: Activation Assay, Variant Assay, Expressing

Journal: bioRxiv

Article Title: Germline Targeted Baboon Apolipoprotein L-1 Protects Mice Against African Trypanosomes

doi: 10.1101/2025.09.23.676901

Figure Lengend Snippet: Pictured above the phylogenetic tree and haplotype table is a schematic of the five protein-coding exons of APOL1 in primates (NC, non-coding; PC, protein-coding). All of the observed polymorphisms were present in exons 2, 3, and 5. Only the sites that are polymorphic between the baboon individuals are shown. Each observed haplotype is depicted separately, with haplotypes grouped by their phylogeny (left). Polymorphisms that do not match the reference sequence (Panu2.0) are red, while reference-matching sites are black. The genetic coordinates of each site in the reference sequence are listed below the table, and polymorphic sites that encode missense mutations (relative to the reference sequence Panu 2.0) are highlighted by the encoded amino acid change above the table. H38V (*) is intentionally located between two SNPs because the amino acid change is encoded by two adjacent polymorphisms. The ‘No Indels’ and asterisks at the right refer to , wherein the amino acid changes, starting at amino acid position 300, encoded by the different Indel patterns are clarified.

Article Snippet: An anti-human APOL1 antibody (ProteinTech, 11486-2-AP) was used for the detection of human, gorilla, or the chimeric APOL1.

Techniques: Sequencing

Journal: bioRxiv

Article Title: Germline Targeted Baboon Apolipoprotein L-1 Protects Mice Against African Trypanosomes

doi: 10.1101/2025.09.23.676901

Figure Lengend Snippet: (A) Illustration of the putative domain architecture of APOL1 (determined using JPred4), highlighting the location of the polymorphic sites that differentiate the consensus sequences of the various species. APOL1 has an N-terminal signal peptide (aqua) that directs the protein to the endoplasmic reticulum during translation, four predicted membrane spanning helices (JPred4, red), and a C-terminal leucine zipper motif (green). (B) Only the polymorphic amino acids that define the consensus sequences are listed, meaning that every non-listed amino acid position is identical between all species consensus sequences. However, more rare polymorphic sites specific to certain subgroups are listed in . Sites that differ from the consensus among the different species are highlighted in red. Positions 169 and 385 in P. ursinus APOL1 cannot be assigned given the low number of individuals (n=2), so both possible variants are listed.

Article Snippet: An anti-human APOL1 antibody (ProteinTech, 11486-2-AP) was used for the detection of human, gorilla, or the chimeric APOL1.

Techniques: Membrane

Journal: bioRxiv

Article Title: Germline Targeted Baboon Apolipoprotein L-1 Protects Mice Against African Trypanosomes

doi: 10.1101/2025.09.23.676901

Figure Lengend Snippet: (A) UV absorbance chromatograms of the final size exclusion chromatography step of three different baboon recombinant APOL1 (rAPOL1) protein purifications. (B) Coomassie stained gels of the purified Papio rAPOL1 proteins. Expected size: 42 kDa (C) 24-hour trypanolysis assay showing the lytic capacity of 1,250 ng/ml of each of the indicated rAPOL1 proteins against T. b. brucei and T. b. gambiense . Reproducible data from multiple assays were combined to generate this graph (error bars represent mean +/− SD of three experimental replicates).

Article Snippet: An anti-human APOL1 antibody (ProteinTech, 11486-2-AP) was used for the detection of human, gorilla, or the chimeric APOL1.

Techniques: Size-exclusion Chromatography, Recombinant, Staining, Purification

Journal: bioRxiv

Article Title: Germline Targeted Baboon Apolipoprotein L-1 Protects Mice Against African Trypanosomes

doi: 10.1101/2025.09.23.676901

Figure Lengend Snippet: (A) 24-hour trypanolysis assay showing the lytic capacity of serially diluted P. hamadryas and P. cynocephalus rAPOL1 proteins against T. b. brucei parasites. IC50 P. hamadryas 113.7 ng/ml, P. cynocephalus 217.9 ng/ml. (B) Individual baboon plasma samples reveal the range of concentrations of APOL1. The band intensities compared to a serially diluted sample of rAPOL1 via pixel counts using FIJI (NIH). (C) 24-hour trypanolysis assay showing the lytic capacity of serially diluted P. hamadryas and P. cynocephalus rAPOL1 under control conditions (solid line) and when the endosomal system has been neutralized (dotted lines) using 20 mM NH4Cl treatment of the parasites 30 minutes prior to APOL1 treatment. IC50 P. hamadryas 96.04 ng/ml, + NH4Cl 666.4 ng/ml, P. cynocephalus 146.0 ng/ml, + NH4Cl 1525 ng/ml.

Article Snippet: An anti-human APOL1 antibody (ProteinTech, 11486-2-AP) was used for the detection of human, gorilla, or the chimeric APOL1.

Techniques: Clinical Proteomics, Control

Journal: bioRxiv

Article Title: Germline Targeted Baboon Apolipoprotein L-1 Protects Mice Against African Trypanosomes

doi: 10.1101/2025.09.23.676901

Figure Lengend Snippet: (A) Schematic illustrating the planar lipid bilayer. Two compartments containing 1 ml buffered KCl (bilayer buffer; see methods) are separated by a phospholipid and cholesterol bilayer. The side of the bilayer that APOL1 is added to is referred to as the “Cis” side, while the opposite side is the “Trans” side. The experimenter sets the voltage (blue line, to mimic a membrane potential) and alters the pH on each side of the membrane by adding pre-calibrated volumes of KOH or HCl to the continuously stirred solutions. Formation of ion-permeant channels in the bilayer is read in the form of an electrical current (I, red line). A table summarizing the pHs at which each protein can insert and open is on the right. (B-E) The voltage (in millivolts) is shown in blue in the lower traces, and the current output (in picoamperes, pA) is shown in red in the upper traces. The green boxes indicate neutral pH, prior to acidification. The orange boxes show acidification. The purple boxes indicate neutralization after acidification. (B) The channel forming capacity of H. sapiens . (C) The channel forming capacity of P. hamadryas APOL1 at Cis (black) and Trans (purple) pH values. Ion fluxes (20-50 pA) are detected at pH 7.2 prior to Cis acidification (green box). (D) The channel forming capacity of P. cynocephalus APOL1 at different Cis pH values. In contrast to (B) P. hamadryas , there is no detectable ion flux in this region (pH 7.4-6.3, green box) prior to Cis acidification (pH 6.0, orange box), whereupon there is increasing ion flux. (E) The channel forming capacities of P. cynocephalus APOL1 and P. hamadryas APOL1 at neutral pH on the same bilayer. During the period marked with the black bar (labelled as ‘Perfuse’) the cis compartment was perfused with chamber buffer (pH 7.2) to remove non-membrane-associated protein.

Article Snippet: An anti-human APOL1 antibody (ProteinTech, 11486-2-AP) was used for the detection of human, gorilla, or the chimeric APOL1.

Techniques: Membrane, Neutralization

Journal: bioRxiv

Article Title: Germline Targeted Baboon Apolipoprotein L-1 Protects Mice Against African Trypanosomes

doi: 10.1101/2025.09.23.676901

Figure Lengend Snippet: Total HDL lipoproteins were isolated from human and baboon plasma. The HDLs were either treated with vehicle control or PNGase F before electrophoresis under reducing conditions. The molecular mass of baboon APOL1 and both human and baboon HPR decrease significantly after PNGase F treatment, indicating that the proteins are N -glycosylated. The red asterisk in the left panel highlights an APOL1 C-terminal cleavage product that often accumulates during sample collection.

Article Snippet: An anti-human APOL1 antibody (ProteinTech, 11486-2-AP) was used for the detection of human, gorilla, or the chimeric APOL1.

Techniques: Isolation, Clinical Proteomics, Control, Electrophoresis

Journal: bioRxiv

Article Title: Germline Targeted Baboon Apolipoprotein L-1 Protects Mice Against African Trypanosomes

doi: 10.1101/2025.09.23.676901

Figure Lengend Snippet: (A-B) Schematics of the targeting constructs used to insert the genomic baboon APOL1 locus into the mouse genome. The construct in panel B was generated by making two substitutions (*) in the construct shown in panel A (E150Q and L180M). (C) Ethidium bromide-stained agarose gel showing the results of gene-specific PCRs of cDNA synthesized from RNA derived from liver homogenates of a wild-type mouse and a germline transgenic mouse expressing P. anubis APOL1 from the ROSA26 locus. (D-F) Kaplan-Meier survival curves of mice infected with 5000 T. b. brucei (427-SRA) parasites intraperitoneally (i.p.). (D) Heterozygous or homozygous transgenic mice expressing either P. hamadryas APOL1 from the Myh9 locus or P. anubis APOL1 from the ROSA26 locus compared to wild-type counterparts. (E) P. anubis APOL1 and human APOA-I- expressing mice compared to wild-type counterparts. (F) P. anubis APOL1 -expressing mice expressing P. hamadryas HPR by HGD compared to APOL1 or HPR alone (p = 0.09; Log-rank test).

Article Snippet: An anti-human APOL1 antibody (ProteinTech, 11486-2-AP) was used for the detection of human, gorilla, or the chimeric APOL1.

Techniques: Construct, Generated, Staining, Agarose Gel Electrophoresis, Synthesized, Derivative Assay, Transgenic Assay, Expressing, Infection

Journal: bioRxiv

Article Title: Germline Targeted Baboon Apolipoprotein L-1 Protects Mice Against African Trypanosomes

doi: 10.1101/2025.09.23.676901

Figure Lengend Snippet: (A) Schematic of the targeting construct used to insert a single copy of the P. hamadryas APOL1 cDNA into the ROSA26 locus of the mouse genome. bGH is bovine growth hormone. (B) Anti-baboon APOL1 western blot of serially diluted baboon P. hamadryas ( P. ham ) plasma and transgenic (Tg) homozygous (HOM) and heterozygous (HET) mouse plasma samples. (C) Anti-baboon APOL1 western blot of purified baboon HDL and transgenic mouse HDL samples. (D) Kaplan-Meier curve showing the survival of P. hamadryas APOL1 transgenic heterozygous mice compared to wild type counterparts infected with 5000 T. b. brucei Lister-427 parasites i.p. (* p = 0.01; Log-rank test). (E) Weight gain in heterozygous and homozygous APOL1 transgenic mice compared to wild type counterparts as a function of time post-birth (error bars represent the mean +/− the SD for each group each week). (F) Hematoxylin and eosin-stained kidney tissue slices focused on a glomerulus from adult wild type and APOL1 HET transgenic mice. Images represent three mice from each group. Images were captured using a light microscope with 40X magnification.

Article Snippet: An anti-human APOL1 antibody (ProteinTech, 11486-2-AP) was used for the detection of human, gorilla, or the chimeric APOL1.

Techniques: Construct, Western Blot, Clinical Proteomics, Transgenic Assay, Purification, Infection, Staining, Light Microscopy

Journal: bioRxiv

Article Title: Germline Targeted Baboon Apolipoprotein L-1 Protects Mice Against African Trypanosomes

doi: 10.1101/2025.09.23.676901

Figure Lengend Snippet: (A-B) The calculated number of parasites per milligram of perfused (all blood removed) tissue in wild type (WT) C57 BL/6N-J mice (A) or heterozygous (HET) P. hamadryas APOL1 -transgenic mice (B) after DNA isolation and qPCR using primers specific to T. congolense Cathepsin L (housekeeping gene) compared to a standard curve of a known number of parasites. Each number denotes 1 individual mouse. D.P.I.; Days Post-Infection.

Article Snippet: An anti-human APOL1 antibody (ProteinTech, 11486-2-AP) was used for the detection of human, gorilla, or the chimeric APOL1.

Techniques: Transgenic Assay, DNA Extraction, Infection

Journal: bioRxiv

Article Title: Germline Targeted Baboon Apolipoprotein L-1 Protects Mice Against African Trypanosomes

doi: 10.1101/2025.09.23.676901

Figure Lengend Snippet: (A) Schematic of the targeting construct used to insert the P. hamadryas APOL1 and HPR cDNAs into the ROSA26 locus of the mouse genome with APOL1 expression driven by a ubiquitin promoter and HPR by an albumin (alb) promoter. bGH is bovine growth hormone. (B) Western blot showing the relative concentration of HPR in the plasma of heterozygous (HET) and homozygous (HOM) transgenic mice compared to a representative baboon plasma sample using an anti-human Hp antibody that cross-reacts with human and primate HPR. (C) Parasitemia over time showing the number of parasites per mL of blood in transgenic mice inoculated with 5000 pleomorphic T. b. brucei (AnTat DRF) parasites by i.p. on day 0. The graph shows the parasitemia in each individual mouse of each genotype (number of mice per genotype, including wild type, in parentheses). Parasitemia was counted by light microscopy; the limit of detection is approximately 3-5 x 10 6 parasites per mL (p/mL). The P. hamadryas APOL1/HPR Alb HET cohort are represented schematically as 1, though we did not detect parasites in these mice. (D) Kaplan-Meier survival curve of wild-type and HET transgenic mice inoculated with 5000 T. b. rhodesiense (KETRI 243) parasites i.p. (**** p < 0.0001; Log-rank test). (E) Schematic of the targeting construct used to insert the P. hamadryas APOL1 and HPR cDNAs into the ROSA26 locus of the mouse genome with APOL1 and HPR expression both driven by a ubiquitin (ubq) promoter. (F) Western blot showing relative APOL1 concentration in plasma of HET transgenic mice compared to a representative baboon plasma sample, using an APOL1 antibody specific for baboon APOL1. (F) T. b. brucei (AnTat DRF) parasite challenge in mice WT, HET and HOM for APOL1 and HPR both on ubiquitin promoters in the same scheme as outlined in C. (G) Kaplan-Meier survival curve of WT, HET, and HOM infected with T. b. rhodesiense (KETRI 243) in the same scheme as (D) (*** p = 0.0010; Log-rank test).

Article Snippet: An anti-human APOL1 antibody (ProteinTech, 11486-2-AP) was used for the detection of human, gorilla, or the chimeric APOL1.

Techniques: Construct, Expressing, Ubiquitin Proteomics, Western Blot, Concentration Assay, Clinical Proteomics, Transgenic Assay, Light Microscopy, Infection

Journal: bioRxiv

Article Title: Germline Targeted Baboon Apolipoprotein L-1 Protects Mice Against African Trypanosomes

doi: 10.1101/2025.09.23.676901

Figure Lengend Snippet: (A) Illustration of the putative domain architecture of APOL1 (determined using JPred4 [9]) from human APOL1, gorilla APOL1, baboon APOL1, and the chimeric APOL1 genes, which encode the first 360 amino acids of either the human ( Hum360 ) or gorilla ( Gor360 ) APOL1 protein fused to the C-terminus of the P. hamadryas APOL1 protein (the C-terminal 36 amino acids). The junction between human/gorilla and baboon occurs at the C-terminal end of the 4 th putative membrane spanning region, such that all chimeras encode the baboon C-terminal leucine zipper motif. (B) Kaplan-Meier survival curve of mice expressing chimeric APOL1 or human APOL1 by hydrodynamic gene delivery (HGD) inoculated with 5000 T. b. rhodesiense KETRI 243 parasites i.p. (*** p = 0.0001; Log-rank test). (C) Kaplan-Meier survival curve of WT and HET mice expressing chimeric APOL1 (Hum360) on a ubiquitin promoter, inoculated with 5000 T. b. rhodesiense KETRI 243 parasites i.p. (** p = 0.0035; Log-rank test). (D) Kaplan-Meier survival curve of mice expressing chimeric APOL1 (Gor360) or human APOL1 and HPR (ubiquitin promoters) by HGD inoculated with 5000 T. vivax IL1392 parasites i.p. (ns, p = 0.4302; Log-rank test). Experiment was repeated with a second isolate, with similar results.

Article Snippet: An anti-human APOL1 antibody (ProteinTech, 11486-2-AP) was used for the detection of human, gorilla, or the chimeric APOL1.

Techniques: Membrane, Expressing, Ubiquitin Proteomics

Journal: bioRxiv

Article Title: Germline Targeted Baboon Apolipoprotein L-1 Protects Mice Against African Trypanosomes

doi: 10.1101/2025.09.23.676901

Figure Lengend Snippet: (A) The mice expressing either HPR, or APOL1 and HPR, or the APOL1 chimeras via HGD in various experiments were assayed for protein production by western blot of 0.75 µL of plasma collected 2 days-post vector injection by HGD (the same day as parasite infection) to confirm that the data could be interpreted without consideration of poor protein expression. (B) Trypanosoma vivax (IL1392) identity was confirmed by PCR from DNA extracted from blood of infected and uninfected mice, using established primers. The expected band size was 200 bp, indicated with an asterisk.

Article Snippet: An anti-human APOL1 antibody (ProteinTech, 11486-2-AP) was used for the detection of human, gorilla, or the chimeric APOL1.

Techniques: Expressing, Western Blot, Clinical Proteomics, Plasmid Preparation, Injection, Infection

Journal: Cell Death Discovery

Article Title: APOA2-mediated endothelial mesenchymal transition and cancer lipid metabolism reprogramming confers antiangiogenic drug resistance through TGF-β

doi: 10.1038/s41420-026-02984-5

Figure Lengend Snippet: a MRI images, changes in AFP, and quantification of tumor volume in representative HCC-resistant patients before and after apatinib treatment. Scale bars, 10 cm. b MRI images, changes in AFP, and quantification of tumor thrombus volume in representative HCC-sensitive patients before and after apatinib treatment. Scale bars, 10 cm. c The GO pathway analysis of differential genes was enriched, with APOA2 ranking first in the small molecule metabolic process. d The KEGG pathway analysis of differential genes was enriched, with APOA2 ranking first in the PPAR signaling pathway. e Intensity of APOA2 IHC staining in 10 paired HCC patient tissues (sensitive vs resistant). Scale bars, 50 µm. f Predicted network diagram of the interactions between APOA2 and VEGFR2.

Article Snippet: Primary APOA2 antibody (Proteintech, 16845-1-AP, CHN) was diluted at 1:50, while mouse/rabbit linker (Santa Cruz, sc2357, USA) was diluted at 1:100.

Techniques: Immunohistochemistry

Journal: Cell Death Discovery

Article Title: APOA2-mediated endothelial mesenchymal transition and cancer lipid metabolism reprogramming confers antiangiogenic drug resistance through TGF-β

doi: 10.1038/s41420-026-02984-5

Figure Lengend Snippet: After the evaluation of acquired drug resistance, the HCC-bearing mice were divided into 3 groups: (C)control ( n = 7), (R)resistant ( n = 7), and (S)sensitive ( n = 24). a Quantification of subcutaneous tumor mass and volume in the three groups. Numbers 1–7 represent control group, 1–7 for resistance group, and 1–7 for sensitivity group. * p < 0.05, ns, not significant. b . Representative images of CD31 immunofluorescence staining of tumor tissue. The upper part of the image is a comprehensive view of CD31 staining of the entire tumor tissue section, while the bottom part shows CD31 staining under magnification. CD31 + microvessel signals were randomly quantified from 12 fields ( n = 7 mice in each group), Scale bars, 50 µm. * p < 0.05, ns, not significant. c and d . Western blotting of APOA2, VEGFR2, and P-VEGFR2 in tumor tissue ( n = 4). e Representative images of APOA2 IHC staining intensity of tumor tissue, Scale bars, 100 µm. The upper part of the image is a comprehensive view of APOA2 staining of the entire tumor tissue section, while the bottom part shows APOA2 staining under magnification. Scale bars, 100 µm. * p < 0.05, ns, not significant.

Article Snippet: Primary APOA2 antibody (Proteintech, 16845-1-AP, CHN) was diluted at 1:50, while mouse/rabbit linker (Santa Cruz, sc2357, USA) was diluted at 1:100.

Techniques: Control, Immunofluorescence, Staining, Western Blot, Immunohistochemistry

Journal: Cell Death Discovery

Article Title: APOA2-mediated endothelial mesenchymal transition and cancer lipid metabolism reprogramming confers antiangiogenic drug resistance through TGF-β

doi: 10.1038/s41420-026-02984-5

Figure Lengend Snippet: a Representative images of HCC cell lines overexpressing APOA2. Scale bars, 100 µm. Western blotting verified the protein levels of APOA2, VEGFR2, and P-VEGFR2 in 4 cell lines. b – d Subcutaneous tumor, tumor volume and tumor mass quantification, along with tumor growth curve of each group ( n = 6). e – g Characterization of tumor inhibition rate in each group. *** p < 0.001, **** p < 0.0001, ns not significant.

Article Snippet: Primary APOA2 antibody (Proteintech, 16845-1-AP, CHN) was diluted at 1:50, while mouse/rabbit linker (Santa Cruz, sc2357, USA) was diluted at 1:100.

Techniques: Western Blot, Inhibition

Journal: Cell Death Discovery

Article Title: APOA2-mediated endothelial mesenchymal transition and cancer lipid metabolism reprogramming confers antiangiogenic drug resistance through TGF-β

doi: 10.1038/s41420-026-02984-5

Figure Lengend Snippet: a – f The experiment comprised two groups: control (Control) and APOA2 overexpression (APOA2). a , d Colony formation assay conducted on MHCC97H and SMMC7721 cells ( n = 3), b , e Representative images from EdU assay performed on MHCC97H and SMMC7721 cells, with EdU signals quantified from 12 fields ( n = 6), Scale bars, 50 µm. c , f CCK8 assay results of MHCC97H and SMMC7721 cells. g The experiment comprised 4 groups: control group receiving solvent and apatinib (Control + Vehicle vs Control + Apatinib), and the APOA2 overexpression group receiving solvent and apatinib (APOA2+Vehicle vs APOA2+Apatinib). Representative images of Ki67 and cleaved-caspase 3 immunofluorescence staining of tumor tissue, with Ki67+ and cleaved-caspase 3+ signals quantified from 12 fields ( n = 6). Scale bars, 100 µm. * p < 0.05, ns not significant.

Article Snippet: Primary APOA2 antibody (Proteintech, 16845-1-AP, CHN) was diluted at 1:50, while mouse/rabbit linker (Santa Cruz, sc2357, USA) was diluted at 1:100.

Techniques: Control, Over Expression, Colony Assay, EdU Assay, CCK-8 Assay, Solvent, Immunofluorescence, Staining

Journal: Cell Death Discovery

Article Title: APOA2-mediated endothelial mesenchymal transition and cancer lipid metabolism reprogramming confers antiangiogenic drug resistance through TGF-β

doi: 10.1038/s41420-026-02984-5

Figure Lengend Snippet: a Representative bright-field images of tubular formation in HUVECs cultured with conditioned media from MHCC97H and SMCC7721 (overexpressing APOA2 or not). Scale bar, 400 µm. b Representative images of EdU assay conducted on HUVECs cultured with conditioned media from MHCC97H and SMCC7721 (overexpressing APOA2 or not), with EdU signals quantified from 12 fields ( n = 6). Scale bars, 100 µm. c Representative images of migration of HUVECs cultured with conditioned media from MHCC97H and SMCC7721 (overexpressing APOA2 or not), Scale bars, 100 µm. * p < 0.05, ns not significant.

Article Snippet: Primary APOA2 antibody (Proteintech, 16845-1-AP, CHN) was diluted at 1:50, while mouse/rabbit linker (Santa Cruz, sc2357, USA) was diluted at 1:100.

Techniques: Cell Culture, EdU Assay, Migration

Journal: Cell Death Discovery

Article Title: APOA2-mediated endothelial mesenchymal transition and cancer lipid metabolism reprogramming confers antiangiogenic drug resistance through TGF-β

doi: 10.1038/s41420-026-02984-5

Figure Lengend Snippet: a Volcano plot of differentially expressed proteins between the APOA2 overexpression group and the control group, with a fold change ≥ 1.5 and adjusted p < 0.01 ( n = 3). Gray denotes no significant difference, blue indicates low expression, and red indicates high expression. The volcano plot labels the five highest expressed proteins and five lowest expressed proteins. b Histogram of 5 highest expressed proteins and 5 lowest expressed proteins ( n = 3). c Enrichment analysis of KEGG pathways for differentially expressed proteins between the APOA2 overexpression group and the control group. d Histogram showing levels of TGF-β ligand, receptor, and signaling pathway-related protein in proteomics (n = 3). e Pearson correlation analysis of five highly expressed proteins and TGF-β in HCC. f Relative mRNA levels of TGF-β in HCC cells and tumor tissues with or without overexpressing APOA2 analyzed by real-time quantitative PCR ( n = 6). g ELISA detection of TGF-β in HCC cell (with or without overexpressing APOA2) medium and serum of HCC-bearing mice (with or without overexpressing APOA2). h Western blotting detecting the protein levels of TGF-βR1, TGF-βR2, P-TGFβR1 and P-TGFβR2 in HCC cells and tumor tissues with or without overexpressing APOA2. * p < 0.05, ns, not significant.

Article Snippet: Primary APOA2 antibody (Proteintech, 16845-1-AP, CHN) was diluted at 1:50, while mouse/rabbit linker (Santa Cruz, sc2357, USA) was diluted at 1:100.

Techniques: Over Expression, Control, Expressing, Real-time Polymerase Chain Reaction, Enzyme-linked Immunosorbent Assay, Western Blot

Journal: Cell Death Discovery

Article Title: APOA2-mediated endothelial mesenchymal transition and cancer lipid metabolism reprogramming confers antiangiogenic drug resistance through TGF-β

doi: 10.1038/s41420-026-02984-5

Figure Lengend Snippet: a Enrichment analysis of GO pathways for differentially expressed proteins between APOA2 overexpression and the control group, with a fold change ≥ 1.5 and adjusted p -value < 0.01. b Glucose consumption in MHCC97H cells in the designated group ( n = 6). c Lactate production in MHCC97H cells in the designated group ( n = 6). d Mito Fuel Flex test revealed dependence on the oxidation of glucose, glutamine, or FA in MHCC97H cells in the designated group ( n = 6). e BODIPY-FA uptake in MHCC97H cells in the designated group. f β-oxidation assay in MHCC97H cells in the designated group ( n = 6). g Intracellular ATP levels in MHCC97H cells in the designated group ( n = 6). * p < 0.05, ns not significant.

Article Snippet: Primary APOA2 antibody (Proteintech, 16845-1-AP, CHN) was diluted at 1:50, while mouse/rabbit linker (Santa Cruz, sc2357, USA) was diluted at 1:100.

Techniques: Over Expression, Control, Oxidation Assay

Journal: Acta Pharmaceutica Sinica. B

Article Title: Acteoside ameliorates hepatocyte ferroptosis and hepatic ischemia-reperfusion injury via targeting PCBP2

doi: 10.1016/j.apsb.2025.03.002

Figure Lengend Snippet: The hepatocyte specific knockout of PCBP2 interferes the therapeutic effects of ACT. (A) The particle size, (B) PDI, zeta potential and EE (%) of LNPs-si-PCBP2. (C) The stability of LNPs-si-PCBP2 in PBS and cell culture media. (D) The release behaviors of free si-RNA and LNPs-si-PCBP2. (E) Flow chart of ApoE-LNPs animal experiment. (F) The content of Fe 3+ , Fe 2+ , Cys and GSH in mouse livers. Statistical significance: ∗∗ P < 0.01, ∗∗∗ P < 0.001, compared with the sham group ( n = 6). Representative images of (G) H & E staining (scale bar = 40 μm), (H) PPB staining (scale bar = 40 μm), (I) immunofluorescence staining for PCBP2/SLC3A2/SLC7A11 (scale bar = 40 μm), (J) immunofluorescence staining for HMGB1 (scale bar = 40 μm) and (K) CD68 (scale bar = 40 μm) in mouse livers. (L) The Relative mRNA levels of slc3a2 , slc7a11 , p300 , hmgb1 and F4/80 were measured by qPCR and further normalized with hprt1 in mouse livers. Statistical significance: ∗ P < 0.05, ∗∗ P < 0.01, ∗∗∗ P < 0.001, compared with the sham group ( n = 6).

Article Snippet: The purified apolipoprotein E (ApoE) (MedChemExpress, NJ, USA) was then incubated with iminothiolane hydrochloride (2-IT) at a molar ration 1:2 and dissolved in phosphate-buffered saline at 25 °C for 90 min.

Techniques: Knock-Out, Zeta Potential Analyzer, Cell Culture, Staining, Immunofluorescence

Journal: The Journal of Biological Chemistry

Article Title: Effect of phospholipid transfer protein on plasma sphingosine-1-phosphate

doi: 10.1016/j.jbc.2024.107837

Figure Lengend Snippet: Lipid and PLTP activity measurements in A apo m -KO mice . A, strategy for Apom -KO mouse preparation. Three-month-old mice (male and female) on chow diet were used. B, plasma (0.2 μl) was separated by 4 to 15% SDS gel electrophoresis and immunoblotted with polyclonal antibodies against apoM. Ponceau S staining was used as a loading control . C, plasma cholesterol measurement. D, plasma PLTP activity measurement. E, plasma S1P measurement. The above mice were then put on the Western diet for 2 weeks and the following were measured. F, plasma cholesterol. G, PLTP activity. H, plasma S1P. Values are the mean ± SD, n = 4 to 5, ∗ p < 0.01. PLTP, plasma phospholipid transfer protein; S1P, sphingosine-1-phosphate.

Article Snippet: Plasma (0.2 μl) was separated by 4 to 15% SDS gel electrophoresis and immunoblotted with polyclonal antibodies against apoM (Proteintech, Catalog #:12817-1-AP) and apoA-I (Proteintech, Catalog #:14427-1-AP).

Techniques: Activity Assay, Clinical Proteomics, SDS-Gel, Electrophoresis, Staining, Control, Western Blot

Journal: The Journal of Biological Chemistry

Article Title: Effect of phospholipid transfer protein on plasma sphingosine-1-phosphate

doi: 10.1016/j.jbc.2024.107837

Figure Lengend Snippet: S1P and apoM measurement in Alb-KO mice . Three-month-old Alb -KO- male mice on chow diet were used. A, Western blot analyses of plasma albumin and apoM. B, plasma S1P measurement. C, PLTP activity measurement. Values are the mean ± SD, n = 3. Alb -KO, albumin gene knockout mice; PLTP, plasma phospholipid transfer protein; S1P, sphingosine-1-phosphate.

Article Snippet: Plasma (0.2 μl) was separated by 4 to 15% SDS gel electrophoresis and immunoblotted with polyclonal antibodies against apoM (Proteintech, Catalog #:12817-1-AP) and apoA-I (Proteintech, Catalog #:14427-1-AP).

Techniques: Western Blot, Clinical Proteomics, Activity Assay, Gene Knockout

Journal: The Journal of Biological Chemistry

Article Title: Effect of phospholipid transfer protein on plasma sphingosine-1-phosphate

doi: 10.1016/j.jbc.2024.107837

Figure Lengend Snippet: Lipid and apolipoprotein measurement in inducible Pltp - KO mice . Three-month-old mice (male and female) on chow diet were used. A, plasma PLTP activity measurement. B, FPLC for evaluating plasma cholesterol distribution. HDL and non-HDL fractions were labeled. C, Western blot analyses for plasma apoA-I and apoM (male). The intensity of each band, measured by Image-Pro Plus version 4.5 software, was used for quantification. For apoA-I: 100 ± 7% WT versus 55 ± 6% Pltp -KO, p < 0.01; for apoM: 100 ± 15% WT versus 44 ± 5% Pltp -KO, p < 0.01. D, plasma cholesterol measurement. E, plasma phospholipid measurement. F, plasma S1P measurement (male). Three-month-old mice (male and female) on the Western diet for 2 weeks were used. G, plasma cholesterol measurement. H, plasma phospholipid measurement. I, plasma S1P measurement (male). Values are the mean ± SD, n = 5, ∗∗ p < 0.01. FPLC, fast protein liquid chromatography; PKO, Pltp -KO mice; PLTP, plasma phospholipid transfer protein; S1P, sphingosine-1-phosphate.

Article Snippet: Plasma (0.2 μl) was separated by 4 to 15% SDS gel electrophoresis and immunoblotted with polyclonal antibodies against apoM (Proteintech, Catalog #:12817-1-AP) and apoA-I (Proteintech, Catalog #:14427-1-AP).

Techniques: Clinical Proteomics, Activity Assay, Labeling, Western Blot, Software, Fast Protein Liquid Chromatography

Journal: The Journal of Biological Chemistry

Article Title: Effect of phospholipid transfer protein on plasma sphingosine-1-phosphate

doi: 10.1016/j.jbc.2024.107837

Figure Lengend Snippet: Plasma lipid measurement in experimental and WT mice . WT, Apom -KO (MKO), inducible Pltp -KO (PKO), and inducible Pltp -KO/germline Apom -KO (dKO) mice on chow diet were used. A, plasma cholesterol measurement in male mice. B, plasma phospholipid measurement in male mice. C, plasma S1P measurement in male mice. D, plasma S1P measurement in female mice. Values are the mean ± SD, n = 4. Columns labeled with different lowercase letters are statistically different, p < 0.01. dKO, double KO; PLTP, plasma phospholipid transfer protein; S1P, sphingosine-1-phosphate.

Article Snippet: Plasma (0.2 μl) was separated by 4 to 15% SDS gel electrophoresis and immunoblotted with polyclonal antibodies against apoM (Proteintech, Catalog #:12817-1-AP) and apoA-I (Proteintech, Catalog #:14427-1-AP).

Techniques: Clinical Proteomics, Labeling

Journal: The Journal of Biological Chemistry

Article Title: Effect of phospholipid transfer protein on plasma sphingosine-1-phosphate

doi: 10.1016/j.jbc.2024.107837

Figure Lengend Snippet: PLTP activity, lipid, and apoM measurements in germline Pltp - transgenic mice . Three-month-old Pltp -Tg and WT male mice on chow diet were used. A , PLTP activity measurement. B, plasma cholesterol measurement. C, plasma phospholipid measurement. D, plasma S1P measurement. E, Western blot analyses for plasma apoM. The intensity of each band was used for quantification: 100 ± 5% WT versus 95 ± 15% Pltp -Tg. Values are the mean ± SD, n = 4. ∗ p < 0.05, ∗∗ p < 0.01. PLTP, plasma phospholipid transfer protein; S1P, sphingosine-1-phosphate.

Article Snippet: Plasma (0.2 μl) was separated by 4 to 15% SDS gel electrophoresis and immunoblotted with polyclonal antibodies against apoM (Proteintech, Catalog #:12817-1-AP) and apoA-I (Proteintech, Catalog #:14427-1-AP).

Techniques: Activity Assay, Transgenic Assay, Clinical Proteomics, Western Blot

Journal: The Journal of Biological Chemistry

Article Title: Effect of phospholipid transfer protein on plasma sphingosine-1-phosphate

doi: 10.1016/j.jbc.2024.107837

Figure Lengend Snippet: Lipid and apolipoprotein measurements in AAV- Pltp and AAV-null mice . Two-month-old WT male mice (C57BL/6) were injected with AAV-PLTP and AAV-null (i.v., 2 × 10 11 per 100 ul). Three weeks later, lipid and apolipoprotein levels were measured. A, PLTP activity measurement. B, plasma cholesterol measurement. C, plasma phospholipid measurement. D, Western blot analyses for plasma apoA-I and apoM. The intensity of each band was used for quantification. For apoA-I: 100 ± 10% WT versus 65 ± 15% AAV-PLTP, p < 0.05; for apoM: 100 ± 8% WT versus 52 ± 15% AAV-PLTP, p < 0.01. E, plasma S1P measurement. Values are the mean ± SD, n = 4 to 5. ∗∗ p < 0.01. AAV, adenovirus-associated virus; PLTP, plasma phospholipid transfer protein; S1P, sphingosine-1-phosphate.

Article Snippet: Plasma (0.2 μl) was separated by 4 to 15% SDS gel electrophoresis and immunoblotted with polyclonal antibodies against apoM (Proteintech, Catalog #:12817-1-AP) and apoA-I (Proteintech, Catalog #:14427-1-AP).

Techniques: Injection, Activity Assay, Clinical Proteomics, Western Blot, Virus