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anti human zip14 (Alomone Labs)

Name: anti human zip14
Brand: Alomone Labs
Rating: 96 (243 reviews)

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Alomone Labs anti human zip14
A Schematic workflow of the high-throughput screening to identify <t>ZIP14</t> inhibitors. B Chemical structure of 1-phenyl-8-(2-phenylethyl)-1,3,8-triazaspiro[4.5]decan-4-one (PPTD).

A Schematic workflow of the high-throughput screening to identify <t>ZIP14</t> inhibitors. B Chemical structure of 1-phenyl-8-(2-phenylethyl)-1,3,8-triazaspiro[4.5]decan-4-one (PPTD).

Anti Human Zip14, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 96/100, based on 243 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/anti human zip14/product/Alomone Labs
Average 96 stars, based on 243 article reviews

anti human zip14 - by Bioz Stars, 2026-03

96/100 stars

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1) Product Images from "Discovery of a Selective Inhibitor of ZIP14 with Therapeutic Potential for Cancer-associated Cachexia"

Article Title: Discovery of a Selective Inhibitor of ZIP14 with Therapeutic Potential for Cancer-associated Cachexia

Journal: bioRxiv

doi: 10.1101/2025.10.23.682519

A Schematic workflow of the high-throughput screening to identify ZIP14 inhibitors. B Chemical structure of 1-phenyl-8-(2-phenylethyl)-1,3,8-triazaspiro[4.5]decan-4-one (PPTD).

Figure Legend Snippet: A Schematic workflow of the high-throughput screening to identify ZIP14 inhibitors. B Chemical structure of 1-phenyl-8-(2-phenylethyl)-1,3,8-triazaspiro[4.5]decan-4-one (PPTD).

Techniques Used: High Throughput Screening Assay

Xenopus oocytes injected either with ( A, B ) human ZIP14 or ( E, F ) human ZIP8 cRNA were incubated with either ( A, E ) ⁶⁵Zn or ( B, F ) ⁵⁵Fe in the presence of ( A, E ) 50 µM or ( B, F ) 10 µM PPTD for 30 min at 22 °C. Radioactivity was measured as described under Methods . Data are normalized against DMSO-treated transporter-expressing controls, and presented as mean ± standard deviation (S.D.) (n=3 independent experiments). Similarly, (C, D) TREx-hZIP14 or (G, H) TREx-hZIP8 cells were treated with Tet (1 μg/mL) for 24 h, followed by incubation either with ( C, G ) ⁵⁴MnCl₂ or (D, H) ¹⁰⁹CdCl₂ in the presence of PPTD at the indicated concentrations for 1 h. Radioactivity was measured as described under Methods . The data (mean + SD) represent results from three independent experiments. Statistical significance was determined using Student’s t -test (A, B, E, F) or one-way ANOVA followed by Dunnett’s post hoc test (C, D, G, H). (* p < 0.05, ** p < 0.01, *** p < 0.005, **** p < 0.001, ***** p < 0.0005).

Figure Legend Snippet: Xenopus oocytes injected either with ( A, B ) human ZIP14 or ( E, F ) human ZIP8 cRNA were incubated with either ( A, E ) ⁶⁵Zn or ( B, F ) ⁵⁵Fe in the presence of ( A, E ) 50 µM or ( B, F ) 10 µM PPTD for 30 min at 22 °C. Radioactivity was measured as described under Methods . Data are normalized against DMSO-treated transporter-expressing controls, and presented as mean ± standard deviation (S.D.) (n=3 independent experiments). Similarly, (C, D) TREx-hZIP14 or (G, H) TREx-hZIP8 cells were treated with Tet (1 μg/mL) for 24 h, followed by incubation either with ( C, G ) ⁵⁴MnCl₂ or (D, H) ¹⁰⁹CdCl₂ in the presence of PPTD at the indicated concentrations for 1 h. Radioactivity was measured as described under Methods . The data (mean + SD) represent results from three independent experiments. Statistical significance was determined using Student’s t -test (A, B, E, F) or one-way ANOVA followed by Dunnett’s post hoc test (C, D, G, H). (* p < 0.05, ** p < 0.01, *** p < 0.005, **** p < 0.001, ***** p < 0.0005).

Techniques Used: Injection, Incubation, Radioactivity, Expressing, Standard Deviation

A Structural predictions of ZIP14-PPTD complexes using both monomeric (left) and dimeric (right) forms of human ZIP14 by AlphaFold3. Magenta circles indicate the predicted PPTD binding sites. Protein models are colored by structure prediction confidence estimated by predicted Local Distance Difference Test (pLDDT) (dark blue, pLDDT >90, light blue, pLDDT of 90-70, yellow, pLDDT of 70-50, orange, pLDDT <50). B Structural overlay of the ZIP14-PPTD and ZIP14-zinc complexes, predicted using AlphaFold3. PPTD and zinc bind in close proximity within the dimerized ZIP14 protein. magenta: PPTD, purple: zinc, blue: His347 and His380 residues. C Prediction of human ZIP14 amino acid residues interacting with PPTD by Protein–Ligand Interaction Profiler and AlphaFold3 (Supplementary Table 5). magenta: PPTD, green dot line: pi-stacking, yellow dot line: salt bridges, gray dot line: hydrophobic interactions, blue line: hydrogen bond. D Asp348 is essential for ZIP14-mediated zinc transport. Xenopus oocytes were injected with human ZIP14 (WT), ZIP14 (D348L), ZIP14 (D348N) cRNA, or water (wi, control). The uptake assay was performed with 10 μM ZnSO 4 including a trace amount of radioactive tracer in the presence of 50 μM PPTD for 30 min at 22 °C. Radioactivity was measured as described under Methods . Statistical analysis was performed by one-way ANOVA followed by Tukey’s multiple comparison test. (*** p < 0.001). All data are shown as mean ± S.E.M. (n= 6 to 9 oocytes).

Figure Legend Snippet: A Structural predictions of ZIP14-PPTD complexes using both monomeric (left) and dimeric (right) forms of human ZIP14 by AlphaFold3. Magenta circles indicate the predicted PPTD binding sites. Protein models are colored by structure prediction confidence estimated by predicted Local Distance Difference Test (pLDDT) (dark blue, pLDDT >90, light blue, pLDDT of 90-70, yellow, pLDDT of 70-50, orange, pLDDT <50). B Structural overlay of the ZIP14-PPTD and ZIP14-zinc complexes, predicted using AlphaFold3. PPTD and zinc bind in close proximity within the dimerized ZIP14 protein. magenta: PPTD, purple: zinc, blue: His347 and His380 residues. C Prediction of human ZIP14 amino acid residues interacting with PPTD by Protein–Ligand Interaction Profiler and AlphaFold3 (Supplementary Table 5). magenta: PPTD, green dot line: pi-stacking, yellow dot line: salt bridges, gray dot line: hydrophobic interactions, blue line: hydrogen bond. D Asp348 is essential for ZIP14-mediated zinc transport. Xenopus oocytes were injected with human ZIP14 (WT), ZIP14 (D348L), ZIP14 (D348N) cRNA, or water (wi, control). The uptake assay was performed with 10 μM ZnSO 4 including a trace amount of radioactive tracer in the presence of 50 μM PPTD for 30 min at 22 °C. Radioactivity was measured as described under Methods . Statistical analysis was performed by one-way ANOVA followed by Tukey’s multiple comparison test. (*** p < 0.001). All data are shown as mean ± S.E.M. (n= 6 to 9 oocytes).

Techniques Used: Binding Assay, Injection, Control, Radioactivity, Comparison

A Comparison of structural simulations of the human ZIP14 (WT)-PPTD complex (upper) and the ZIP14 (S343Y)-PPTD complex (lower). Substitution of Serine 343 with Tyrosine (S343Y) reduces the size of the PPTD-binding pocket within ZIP14, as indicated by the dotted red circle in the mutant structure. magenta: PPTD. B Serine 343 is essential for ZIP14-mediated zinc transport. Xenopus oocytes were injected either with human ZIP14 (WT), ZIP14 (S343Y) cRNA, or water (wi, control). The uptake assay was performed with 10 μM ZnSO 4 including a trace amount of radioactive tracer in the presence of 50 μM PPTD. Radioactivity was measured as described under Methods . All data are shown as mean ± S.E.M. (n= 6 to 9 oocytes). C Structural overlay of five modeled complexes of PPTD bound to human ZIP14 with aspartic acid to leucine substitution at position 443 (D443L). In the four models, PPTD consistently occupies an internal binding region of ZIP14 (indicated by the blue arrow), while one model shows PPTD associating with the protein surface (the red arrow). This variation suggests that the D443L mutation may disrupt the stable binding of PPTD to ZIP14. D Aspartic acid at position 443 contributes to the sensitivity of ZIP14 to PPTD. After preincubation with indicated concentrations of PPTD, Xenopus oocytes injected with cRNA encoding wild-type human ZIP14 (WT) or the D443L mutant were incubated with 10 μM ZnSO 4 including a trace amount of radioactive tracer in the presence of the same concentrations of PPTD for 30 min at 22 °C. The IC₅₀ values for ZIP14 WT and D443L were 8.9 μM and 19.0 μM, respectively. Radioactivity and IC₅₀ values were determined as described under Methods . E The ZIP14 D443L mutant retains transport activity but loses sensitivity to PPTD. Xenopus oocytes were injected with cRNA encoding either wild-type human ZIP14 (WT) or the D443L mutant. The uptake assay was performed with 10 μM ZnSO 4 including a trace amount of radioactive tracer in the presence of 20 μM PPTD. Radioactivity was measured as described under Methods . Statistical analysis was performed using one-way ANOVA followed by Tukey’s multiple comparison test (*** p < 0.001). All data are shown as mean ± S.E.M. (n= 6 to 9 oocytes).

Figure Legend Snippet: A Comparison of structural simulations of the human ZIP14 (WT)-PPTD complex (upper) and the ZIP14 (S343Y)-PPTD complex (lower). Substitution of Serine 343 with Tyrosine (S343Y) reduces the size of the PPTD-binding pocket within ZIP14, as indicated by the dotted red circle in the mutant structure. magenta: PPTD. B Serine 343 is essential for ZIP14-mediated zinc transport. Xenopus oocytes were injected either with human ZIP14 (WT), ZIP14 (S343Y) cRNA, or water (wi, control). The uptake assay was performed with 10 μM ZnSO 4 including a trace amount of radioactive tracer in the presence of 50 μM PPTD. Radioactivity was measured as described under Methods . All data are shown as mean ± S.E.M. (n= 6 to 9 oocytes). C Structural overlay of five modeled complexes of PPTD bound to human ZIP14 with aspartic acid to leucine substitution at position 443 (D443L). In the four models, PPTD consistently occupies an internal binding region of ZIP14 (indicated by the blue arrow), while one model shows PPTD associating with the protein surface (the red arrow). This variation suggests that the D443L mutation may disrupt the stable binding of PPTD to ZIP14. D Aspartic acid at position 443 contributes to the sensitivity of ZIP14 to PPTD. After preincubation with indicated concentrations of PPTD, Xenopus oocytes injected with cRNA encoding wild-type human ZIP14 (WT) or the D443L mutant were incubated with 10 μM ZnSO 4 including a trace amount of radioactive tracer in the presence of the same concentrations of PPTD for 30 min at 22 °C. The IC₅₀ values for ZIP14 WT and D443L were 8.9 μM and 19.0 μM, respectively. Radioactivity and IC₅₀ values were determined as described under Methods . E The ZIP14 D443L mutant retains transport activity but loses sensitivity to PPTD. Xenopus oocytes were injected with cRNA encoding either wild-type human ZIP14 (WT) or the D443L mutant. The uptake assay was performed with 10 μM ZnSO 4 including a trace amount of radioactive tracer in the presence of 20 μM PPTD. Radioactivity was measured as described under Methods . Statistical analysis was performed using one-way ANOVA followed by Tukey’s multiple comparison test (*** p < 0.001). All data are shown as mean ± S.E.M. (n= 6 to 9 oocytes).

Techniques Used: Comparison, Binding Assay, Mutagenesis, Injection, Control, Radioactivity, Incubation, Activity Assay

A Schematic overview of the experimental workflow for PPTD administration to the mouse model of cancer cachexia. B Effects of PPTD administration on body weight loss in the cancer cachexia model. Mice were administered PPTD via drinking water at either 0.1 g/L (low-dose) or 1.0 g/L (high-dose). C PPTD extends survival in the cancer cachexia model. Mice were administered 0.1 g/L (low dose, blue line) or 1.0 g/L (high dose, red line) PPTD through drinking water. Survival was analyzed using the Kaplan-Meier method. Black line: water-treated control group. Survival curves were compared using the Kaplan–Meier method and log-rank test ( p < 0.05 is considered significant). D PPTD delays the onset of cachexia symptoms. Mice were administered 0.1 g/L (low-dose) or 1.0 g/L (high-dose) PPTD via drinking water. The day on which each group first exhibited ≥10% body weight loss or death is shown. Statistical analysis was performed using one-way ANOVA followed by Dunnett’s post hoc test (* p < 0.05). E PPTD improves locomotor activity in a cancer cachexia model. The locomotor of individual mice (n = 3 per group) was recorded on the 16th day of PPTD administration and analyzed using ImageJ (Supplementary Movie 7), as described under Methods . The results are presented as box plots with gray and blue boxes representing the H₂O control group and the PPTD-treated group (0.1 g/L), respectively. Each point represents an individual mouse. Statistical significance was assessed using Welch’s t-test to compare total distances between groups (* p < 0.05). F Working model: Inflammatory stimuli induce ZIP14 expression, promoting metal-induced cytotoxicity that contributes to cancer cachexia (left). The ZIP14 inhibitor PPTD alleviates key features of cancer cachexia (right) and may contribute to improving patients’ quality of life (QOL) (bottom).

Figure Legend Snippet: A Schematic overview of the experimental workflow for PPTD administration to the mouse model of cancer cachexia. B Effects of PPTD administration on body weight loss in the cancer cachexia model. Mice were administered PPTD via drinking water at either 0.1 g/L (low-dose) or 1.0 g/L (high-dose). C PPTD extends survival in the cancer cachexia model. Mice were administered 0.1 g/L (low dose, blue line) or 1.0 g/L (high dose, red line) PPTD through drinking water. Survival was analyzed using the Kaplan-Meier method. Black line: water-treated control group. Survival curves were compared using the Kaplan–Meier method and log-rank test ( p < 0.05 is considered significant). D PPTD delays the onset of cachexia symptoms. Mice were administered 0.1 g/L (low-dose) or 1.0 g/L (high-dose) PPTD via drinking water. The day on which each group first exhibited ≥10% body weight loss or death is shown. Statistical analysis was performed using one-way ANOVA followed by Dunnett’s post hoc test (* p < 0.05). E PPTD improves locomotor activity in a cancer cachexia model. The locomotor of individual mice (n = 3 per group) was recorded on the 16th day of PPTD administration and analyzed using ImageJ (Supplementary Movie 7), as described under Methods . The results are presented as box plots with gray and blue boxes representing the H₂O control group and the PPTD-treated group (0.1 g/L), respectively. Each point represents an individual mouse. Statistical significance was assessed using Welch’s t-test to compare total distances between groups (* p < 0.05). F Working model: Inflammatory stimuli induce ZIP14 expression, promoting metal-induced cytotoxicity that contributes to cancer cachexia (left). The ZIP14 inhibitor PPTD alleviates key features of cancer cachexia (right) and may contribute to improving patients’ quality of life (QOL) (bottom).

Techniques Used: Control, Activity Assay, Expressing

Image Search Results

Journal: bioRxiv

Article Title: Discovery of a Selective Inhibitor of ZIP14 with Therapeutic Potential for Cancer-associated Cachexia

doi: 10.1101/2025.10.23.682519

Figure Lengend Snippet: A Schematic workflow of the high-throughput screening to identify ZIP14 inhibitors. B Chemical structure of 1-phenyl-8-(2-phenylethyl)-1,3,8-triazaspiro[4.5]decan-4-one (PPTD).

Article Snippet: The following primary antibodies were used: anti-human ZIP14 (generated previously ), anti-human ZIP8 (Alomone Labs, #AZT-008), and anti-β-actin (Cell Signaling Technology, #3700S).

Techniques: High Throughput Screening Assay

Journal: bioRxiv

Article Title: Discovery of a Selective Inhibitor of ZIP14 with Therapeutic Potential for Cancer-associated Cachexia

doi: 10.1101/2025.10.23.682519

Figure Lengend Snippet: Xenopus oocytes injected either with ( A, B ) human ZIP14 or ( E, F ) human ZIP8 cRNA were incubated with either ( A, E ) ⁶⁵Zn or ( B, F ) ⁵⁵Fe in the presence of ( A, E ) 50 µM or ( B, F ) 10 µM PPTD for 30 min at 22 °C. Radioactivity was measured as described under Methods . Data are normalized against DMSO-treated transporter-expressing controls, and presented as mean ± standard deviation (S.D.) (n=3 independent experiments). Similarly, (C, D) TREx-hZIP14 or (G, H) TREx-hZIP8 cells were treated with Tet (1 μg/mL) for 24 h, followed by incubation either with ( C, G ) ⁵⁴MnCl₂ or (D, H) ¹⁰⁹CdCl₂ in the presence of PPTD at the indicated concentrations for 1 h. Radioactivity was measured as described under Methods . The data (mean + SD) represent results from three independent experiments. Statistical significance was determined using Student’s t -test (A, B, E, F) or one-way ANOVA followed by Dunnett’s post hoc test (C, D, G, H). (* p < 0.05, ** p < 0.01, *** p < 0.005, **** p < 0.001, ***** p < 0.0005).

Techniques: Injection, Incubation, Radioactivity, Expressing, Standard Deviation

Journal: bioRxiv

Article Title: Discovery of a Selective Inhibitor of ZIP14 with Therapeutic Potential for Cancer-associated Cachexia

doi: 10.1101/2025.10.23.682519

Figure Lengend Snippet: A Structural predictions of ZIP14-PPTD complexes using both monomeric (left) and dimeric (right) forms of human ZIP14 by AlphaFold3. Magenta circles indicate the predicted PPTD binding sites. Protein models are colored by structure prediction confidence estimated by predicted Local Distance Difference Test (pLDDT) (dark blue, pLDDT >90, light blue, pLDDT of 90-70, yellow, pLDDT of 70-50, orange, pLDDT <50). B Structural overlay of the ZIP14-PPTD and ZIP14-zinc complexes, predicted using AlphaFold3. PPTD and zinc bind in close proximity within the dimerized ZIP14 protein. magenta: PPTD, purple: zinc, blue: His347 and His380 residues. C Prediction of human ZIP14 amino acid residues interacting with PPTD by Protein–Ligand Interaction Profiler and AlphaFold3 (Supplementary Table 5). magenta: PPTD, green dot line: pi-stacking, yellow dot line: salt bridges, gray dot line: hydrophobic interactions, blue line: hydrogen bond. D Asp348 is essential for ZIP14-mediated zinc transport. Xenopus oocytes were injected with human ZIP14 (WT), ZIP14 (D348L), ZIP14 (D348N) cRNA, or water (wi, control). The uptake assay was performed with 10 μM ZnSO 4 including a trace amount of radioactive tracer in the presence of 50 μM PPTD for 30 min at 22 °C. Radioactivity was measured as described under Methods . Statistical analysis was performed by one-way ANOVA followed by Tukey’s multiple comparison test. (*** p < 0.001). All data are shown as mean ± S.E.M. (n= 6 to 9 oocytes).

Techniques: Binding Assay, Injection, Control, Radioactivity, Comparison

Journal: bioRxiv

Article Title: Discovery of a Selective Inhibitor of ZIP14 with Therapeutic Potential for Cancer-associated Cachexia

doi: 10.1101/2025.10.23.682519

Figure Lengend Snippet: A Comparison of structural simulations of the human ZIP14 (WT)-PPTD complex (upper) and the ZIP14 (S343Y)-PPTD complex (lower). Substitution of Serine 343 with Tyrosine (S343Y) reduces the size of the PPTD-binding pocket within ZIP14, as indicated by the dotted red circle in the mutant structure. magenta: PPTD. B Serine 343 is essential for ZIP14-mediated zinc transport. Xenopus oocytes were injected either with human ZIP14 (WT), ZIP14 (S343Y) cRNA, or water (wi, control). The uptake assay was performed with 10 μM ZnSO 4 including a trace amount of radioactive tracer in the presence of 50 μM PPTD. Radioactivity was measured as described under Methods . All data are shown as mean ± S.E.M. (n= 6 to 9 oocytes). C Structural overlay of five modeled complexes of PPTD bound to human ZIP14 with aspartic acid to leucine substitution at position 443 (D443L). In the four models, PPTD consistently occupies an internal binding region of ZIP14 (indicated by the blue arrow), while one model shows PPTD associating with the protein surface (the red arrow). This variation suggests that the D443L mutation may disrupt the stable binding of PPTD to ZIP14. D Aspartic acid at position 443 contributes to the sensitivity of ZIP14 to PPTD. After preincubation with indicated concentrations of PPTD, Xenopus oocytes injected with cRNA encoding wild-type human ZIP14 (WT) or the D443L mutant were incubated with 10 μM ZnSO 4 including a trace amount of radioactive tracer in the presence of the same concentrations of PPTD for 30 min at 22 °C. The IC₅₀ values for ZIP14 WT and D443L were 8.9 μM and 19.0 μM, respectively. Radioactivity and IC₅₀ values were determined as described under Methods . E The ZIP14 D443L mutant retains transport activity but loses sensitivity to PPTD. Xenopus oocytes were injected with cRNA encoding either wild-type human ZIP14 (WT) or the D443L mutant. The uptake assay was performed with 10 μM ZnSO 4 including a trace amount of radioactive tracer in the presence of 20 μM PPTD. Radioactivity was measured as described under Methods . Statistical analysis was performed using one-way ANOVA followed by Tukey’s multiple comparison test (*** p < 0.001). All data are shown as mean ± S.E.M. (n= 6 to 9 oocytes).

Techniques: Comparison, Binding Assay, Mutagenesis, Injection, Control, Radioactivity, Incubation, Activity Assay

Journal: bioRxiv

Article Title: Discovery of a Selective Inhibitor of ZIP14 with Therapeutic Potential for Cancer-associated Cachexia

doi: 10.1101/2025.10.23.682519

Figure Lengend Snippet: A Schematic overview of the experimental workflow for PPTD administration to the mouse model of cancer cachexia. B Effects of PPTD administration on body weight loss in the cancer cachexia model. Mice were administered PPTD via drinking water at either 0.1 g/L (low-dose) or 1.0 g/L (high-dose). C PPTD extends survival in the cancer cachexia model. Mice were administered 0.1 g/L (low dose, blue line) or 1.0 g/L (high dose, red line) PPTD through drinking water. Survival was analyzed using the Kaplan-Meier method. Black line: water-treated control group. Survival curves were compared using the Kaplan–Meier method and log-rank test ( p < 0.05 is considered significant). D PPTD delays the onset of cachexia symptoms. Mice were administered 0.1 g/L (low-dose) or 1.0 g/L (high-dose) PPTD via drinking water. The day on which each group first exhibited ≥10% body weight loss or death is shown. Statistical analysis was performed using one-way ANOVA followed by Dunnett’s post hoc test (* p < 0.05). E PPTD improves locomotor activity in a cancer cachexia model. The locomotor of individual mice (n = 3 per group) was recorded on the 16th day of PPTD administration and analyzed using ImageJ (Supplementary Movie 7), as described under Methods . The results are presented as box plots with gray and blue boxes representing the H₂O control group and the PPTD-treated group (0.1 g/L), respectively. Each point represents an individual mouse. Statistical significance was assessed using Welch’s t-test to compare total distances between groups (* p < 0.05). F Working model: Inflammatory stimuli induce ZIP14 expression, promoting metal-induced cytotoxicity that contributes to cancer cachexia (left). The ZIP14 inhibitor PPTD alleviates key features of cancer cachexia (right) and may contribute to improving patients’ quality of life (QOL) (bottom).

Techniques: Control, Activity Assay, Expressing

Primers used in mouse RT-PCR experiments

Journal: Biological Trace Element Research

Article Title: The Role of Zinc on Liver Fibrosis by Modulating ZIP14 Expression Throughout Epigenetic Regulatory Mechanisms

doi: 10.1007/s12011-023-04057-5

Figure Lengend Snippet: Primers used in mouse RT-PCR experiments

Article Snippet: A 50 μL containing 5 × 10 4 cells as the unstained cell group was separated into a separate microcentrifuge tube and the remaining cells were stained with 1 μL of FITC mouse anti-human ZIP14 (MyBioSource, MBS151580) antibody and isotype antibodies respectively to the cells in 100 μL of 5% BSA and 0.05% sodium azide in 1X PBS.

Techniques:

Effects of ZnCl 2 on the accumulation of MTF-1, histone deacetylase 4 to the promoters of ZIP14 promoter. The Sham group received mineral oil only, CCl 4 and CCl 4 + ZnCl 2 group were injected with 10% CCl 4 in mineral oil for 8 weeks. 10 µM ZnCl 2 was only injected to CCl 4 + ZnCl 2 group for two weeks after CCl 4 treatment was completed. The enrichment of A MTF-1, B HDAC4 on the ZIP14 gene was analyzed by ChIP analysis. Genomic DNA extracted from hepatocytes of A control mice and B mice with CCl 4 -induced hepatic fibrosis were immunoprecipitated with anti-MTF-1 and anti-HDAC4. The change in the accumulation of these proteins on the ZIP14 gene was quantified by qPCR. The data were expressed as a percent of input. An asterisk (*) indicates p < 0.05, ** indicates p < 0.01, and *** indicates p < 0.001. All data are represented as the mean ± SD ( n = 4)

Journal: Biological Trace Element Research

Article Title: The Role of Zinc on Liver Fibrosis by Modulating ZIP14 Expression Throughout Epigenetic Regulatory Mechanisms

doi: 10.1007/s12011-023-04057-5

Figure Lengend Snippet: Effects of ZnCl 2 on the accumulation of MTF-1, histone deacetylase 4 to the promoters of ZIP14 promoter. The Sham group received mineral oil only, CCl 4 and CCl 4 + ZnCl 2 group were injected with 10% CCl 4 in mineral oil for 8 weeks. 10 µM ZnCl 2 was only injected to CCl 4 + ZnCl 2 group for two weeks after CCl 4 treatment was completed. The enrichment of A MTF-1, B HDAC4 on the ZIP14 gene was analyzed by ChIP analysis. Genomic DNA extracted from hepatocytes of A control mice and B mice with CCl 4 -induced hepatic fibrosis were immunoprecipitated with anti-MTF-1 and anti-HDAC4. The change in the accumulation of these proteins on the ZIP14 gene was quantified by qPCR. The data were expressed as a percent of input. An asterisk (*) indicates p < 0.05, ** indicates p < 0.01, and *** indicates p < 0.001. All data are represented as the mean ± SD ( n = 4)

Techniques: Histone Deacetylase Assay, Injection, Control, Immunoprecipitation

Changes in mRNA and protein expression of the zinc transporter ZIP14 upon ZnCl 2 treatment in mice with CCl 4 -induced hepatic fibrosis. The Sham group received mineral oil only, CCl 4 and CCl 4 + ZnCl 2 group were injected with 10% CCl 4 in mineral oil for 8 weeks. A 10 µM ZnCl 2 was only injected into the CCl 4 + ZnCl 2 group for two weeks after CCl 4 treatment was completed. A The mRNA expression levels of ZIP14 in were measured by qRT-PCR in hepatocytes. B The protein expression of ZIP14 was measured with flow cytometry and C supported with the immunofluorescence staining with ZIP14 antibody. Hepatocytes were isolated from control (sham) and fibrotic (CCl 4 ) mice were cultured. Transcript levels were normalized to GAPDH. * Indicates p < 0.05, ** indicates p < 0.01. All data are represented as the mean ± SD ( n = 4)

Journal: Biological Trace Element Research

Article Title: The Role of Zinc on Liver Fibrosis by Modulating ZIP14 Expression Throughout Epigenetic Regulatory Mechanisms

doi: 10.1007/s12011-023-04057-5

Figure Lengend Snippet: Changes in mRNA and protein expression of the zinc transporter ZIP14 upon ZnCl 2 treatment in mice with CCl 4 -induced hepatic fibrosis. The Sham group received mineral oil only, CCl 4 and CCl 4 + ZnCl 2 group were injected with 10% CCl 4 in mineral oil for 8 weeks. A 10 µM ZnCl 2 was only injected into the CCl 4 + ZnCl 2 group for two weeks after CCl 4 treatment was completed. A The mRNA expression levels of ZIP14 in were measured by qRT-PCR in hepatocytes. B The protein expression of ZIP14 was measured with flow cytometry and C supported with the immunofluorescence staining with ZIP14 antibody. Hepatocytes were isolated from control (sham) and fibrotic (CCl 4 ) mice were cultured. Transcript levels were normalized to GAPDH. * Indicates p < 0.05, ** indicates p < 0.01. All data are represented as the mean ± SD ( n = 4)

Techniques: Expressing, Injection, Quantitative RT-PCR, Flow Cytometry, Immunofluorescence, Staining, Isolation, Control, Cell Culture

(A) Whole-exome sequencing (WES) was performed on one patient with Hyperostosis Cranialis Interna. Variants were filtered for their absence in dbSNP, by excluding non-coding and synonymous variants and its presence in the linkage region on chromosome 8 (chr8: 21,593,210–28,256,787) after which only two variants remained. (B) Identification of the c.1322T>G mutation in exon 8 of the SLC39A14 ( ZIP14 ) gene by Sanger sequencing. (C) Localization of the p.L441R mutation in the fifth transmembrane domain of ZIP14. (D) 65 Zn uptake experiments demonstrate that WT ZIP14 significantly ( p <0.001) increases 65 Zn uptake when compared to cells transfected with empty vector (Empty V.). L441R and W22X ZIP14 show no sign of 65 Zn uptake from the extracellular space into the cell. (E) FluoZin3-AM experiments demonstrate a significant ( p <0.05) increase in Zn accumulation in cells overexpressing WT ZIP14. Overexpression of L441R ZIP14 results in a stronger ( p <0.001) increase in intracellular Zn accumulation. *: p <0.05; **: p <0.001 by one-way ANOVA.

Journal: PLoS Genetics

Article Title: Conditional mouse models support the role of SLC39A14 (ZIP14) in Hyperostosis Cranialis Interna and in bone homeostasis

doi: 10.1371/journal.pgen.1007321

Figure Lengend Snippet: (A) Whole-exome sequencing (WES) was performed on one patient with Hyperostosis Cranialis Interna. Variants were filtered for their absence in dbSNP, by excluding non-coding and synonymous variants and its presence in the linkage region on chromosome 8 (chr8: 21,593,210–28,256,787) after which only two variants remained. (B) Identification of the c.1322T>G mutation in exon 8 of the SLC39A14 ( ZIP14 ) gene by Sanger sequencing. (C) Localization of the p.L441R mutation in the fifth transmembrane domain of ZIP14. (D) 65 Zn uptake experiments demonstrate that WT ZIP14 significantly ( p <0.001) increases 65 Zn uptake when compared to cells transfected with empty vector (Empty V.). L441R and W22X ZIP14 show no sign of 65 Zn uptake from the extracellular space into the cell. (E) FluoZin3-AM experiments demonstrate a significant ( p <0.05) increase in Zn accumulation in cells overexpressing WT ZIP14. Overexpression of L441R ZIP14 results in a stronger ( p <0.001) increase in intracellular Zn accumulation. *: p <0.05; **: p <0.001 by one-way ANOVA.

Article Snippet: Incubation with primary anti-human ZIP14 antibody (PA5-21077, Thermo Fisher Scientific, 1:200 dilution) was performed at room temperature for 1 hour.

Techniques: Sequencing, Mutagenesis, Transfection, Plasmid Preparation, Over Expression

WT ZIP14 is located on the plasma membrane and in the cytoplasm, whereas L441R ZIP14 is no longer present on the plasma membrane, but clusters in the cytoplasm. A heterozygous model (WT/L441R ZIP14) shows increased expression in the cytoplasm (compared to WT) and some co-localization on the plasma membrane. W22X ZIP14 shows expression in the cytoplasm as well as in the nucleus. Scale bars, 10μm.

Journal: PLoS Genetics

Article Title: Conditional mouse models support the role of SLC39A14 (ZIP14) in Hyperostosis Cranialis Interna and in bone homeostasis

doi: 10.1371/journal.pgen.1007321

Figure Lengend Snippet: WT ZIP14 is located on the plasma membrane and in the cytoplasm, whereas L441R ZIP14 is no longer present on the plasma membrane, but clusters in the cytoplasm. A heterozygous model (WT/L441R ZIP14) shows increased expression in the cytoplasm (compared to WT) and some co-localization on the plasma membrane. W22X ZIP14 shows expression in the cytoplasm as well as in the nucleus. Scale bars, 10μm.

Article Snippet: Incubation with primary anti-human ZIP14 antibody (PA5-21077, Thermo Fisher Scientific, 1:200 dilution) was performed at room temperature for 1 hour.

Techniques: Clinical Proteomics, Membrane, Expressing

(A) Immunohistochemistry of osteoblastoma and giant cell tumor tissue depicts ZIP14 expression in osteoblasts (black line), in giant osteoclast-like cells (arrowheads) and not in osteocytes. Scale bars upper figures, 500μm; scale bars lower figures, 100μm (B) Expression of murine Zip14 ( mZip14 ) during differentiation of KS483 cells to mature mineralizing osteoblasts, indicating stable expression of mZip14 during proliferation (day 4–7) and maturation (day 11–14) of osteoblast differentiation and rising expression during mineralization (day 18–21). (C) In vitro generated osteoclasts from murine calvariae and long bones were cultured on plastic or cortical bone slices, supplemented with M-CSF (M) or M-CSF + RANKL (M+R). qPCR analysis indicates expression of mZip14 in osteoclasts derived from calvariae and long bones.

Journal: PLoS Genetics

Article Title: Conditional mouse models support the role of SLC39A14 (ZIP14) in Hyperostosis Cranialis Interna and in bone homeostasis

doi: 10.1371/journal.pgen.1007321

Figure Lengend Snippet: (A) Immunohistochemistry of osteoblastoma and giant cell tumor tissue depicts ZIP14 expression in osteoblasts (black line), in giant osteoclast-like cells (arrowheads) and not in osteocytes. Scale bars upper figures, 500μm; scale bars lower figures, 100μm (B) Expression of murine Zip14 ( mZip14 ) during differentiation of KS483 cells to mature mineralizing osteoblasts, indicating stable expression of mZip14 during proliferation (day 4–7) and maturation (day 11–14) of osteoblast differentiation and rising expression during mineralization (day 18–21). (C) In vitro generated osteoclasts from murine calvariae and long bones were cultured on plastic or cortical bone slices, supplemented with M-CSF (M) or M-CSF + RANKL (M+R). qPCR analysis indicates expression of mZip14 in osteoclasts derived from calvariae and long bones.

Article Snippet: Incubation with primary anti-human ZIP14 antibody (PA5-21077, Thermo Fisher Scientific, 1:200 dilution) was performed at room temperature for 1 hour.

Techniques: Immunohistochemistry, Expressing, In Vitro, Generated, Cell Culture, Derivative Assay

(A) Calvarial thickness (Calv.Th) and porosity (Calv.Po) measured at the calvariae of Zip14 -/- and Zip14 +/+ mice shows no significant ( p <0.05) differences. (B) 3D reconstruction of calvariae of Zip14 fl/- , Zip14 fl/- ; Runx2-Cre and Zip14 fl/- ; CtsK-Cre mice. (C) Calvarial porosity appears lower in Zip14 fl/- ; Runx2-Cre mice, but no significant ( p <0.05) differences were observed in Zip14 fl/- ; Runx2-Cre and Zip14 fl/- ; CtsK-Cre mice. N = 6 animals/genotype.

Journal: PLoS Genetics

Article Title: Conditional mouse models support the role of SLC39A14 (ZIP14) in Hyperostosis Cranialis Interna and in bone homeostasis

doi: 10.1371/journal.pgen.1007321

Figure Lengend Snippet: (A) Calvarial thickness (Calv.Th) and porosity (Calv.Po) measured at the calvariae of Zip14 -/- and Zip14 +/+ mice shows no significant ( p <0.05) differences. (B) 3D reconstruction of calvariae of Zip14 fl/- , Zip14 fl/- ; Runx2-Cre and Zip14 fl/- ; CtsK-Cre mice. (C) Calvarial porosity appears lower in Zip14 fl/- ; Runx2-Cre mice, but no significant ( p <0.05) differences were observed in Zip14 fl/- ; Runx2-Cre and Zip14 fl/- ; CtsK-Cre mice. N = 6 animals/genotype.

Article Snippet: Incubation with primary anti-human ZIP14 antibody (PA5-21077, Thermo Fisher Scientific, 1:200 dilution) was performed at room temperature for 1 hour.

Techniques:

(A) 3D reconstruction of whole femora (top) and a vertical section of cortical (middle) and trabecular bone (bottom) of Zip14 fl/- controls, Zip14 fl/- ; Runx2-Cre and Zip14 fl/- ; CtsK-Cre mice. Femora of Zip14 fl/- ; Runx2-Cre mice show an increased cortical thickness and decreased midshaft diameter along with a decreased trabecular bone mass. (B) μ CT analysis of cortical (Ct) bone parameters confirms a significantly increased cortical thickness (Ct.Th) and decreased midshaft diameter (Ms.D) of Zip14 fl/- ; Runx2-Cre mice. Both Zip14 fl/- ; Runx2-Cre and Zip14 fl/- ; CtsK-Cre mice have a decreased cortical porosity (Ct.Po). (C) μ CT analysis of trabecular (Tb) bone parameters confirms a significantly decreased trabecular bone volume (BV/TV), number (Tb.N), connecting density (Conn.D) and increased separation (Tb.Sp) in Zip14 fl/- ; Runx2-Cre mice. N = 6 animals/genotype; *: p <0.05; **: p <0.025 by 2-tailed Student’s t-test (compared to Zip14 fl/- mice).

Journal: PLoS Genetics

Article Title: Conditional mouse models support the role of SLC39A14 (ZIP14) in Hyperostosis Cranialis Interna and in bone homeostasis

doi: 10.1371/journal.pgen.1007321

Figure Lengend Snippet: (A) 3D reconstruction of whole femora (top) and a vertical section of cortical (middle) and trabecular bone (bottom) of Zip14 fl/- controls, Zip14 fl/- ; Runx2-Cre and Zip14 fl/- ; CtsK-Cre mice. Femora of Zip14 fl/- ; Runx2-Cre mice show an increased cortical thickness and decreased midshaft diameter along with a decreased trabecular bone mass. (B) μ CT analysis of cortical (Ct) bone parameters confirms a significantly increased cortical thickness (Ct.Th) and decreased midshaft diameter (Ms.D) of Zip14 fl/- ; Runx2-Cre mice. Both Zip14 fl/- ; Runx2-Cre and Zip14 fl/- ; CtsK-Cre mice have a decreased cortical porosity (Ct.Po). (C) μ CT analysis of trabecular (Tb) bone parameters confirms a significantly decreased trabecular bone volume (BV/TV), number (Tb.N), connecting density (Conn.D) and increased separation (Tb.Sp) in Zip14 fl/- ; Runx2-Cre mice. N = 6 animals/genotype; *: p <0.05; **: p <0.025 by 2-tailed Student’s t-test (compared to Zip14 fl/- mice).

Article Snippet: Incubation with primary anti-human ZIP14 antibody (PA5-21077, Thermo Fisher Scientific, 1:200 dilution) was performed at room temperature for 1 hour.

Techniques:

$(A) X-rays of femora and tibiae of a Zip14 fl/- and Zip14 fl/- ; Runx2-Cre mouse. The latter demonstrates with a tibial fracture (arrow), whereas narrowing of the femoral midshaft can be observed as well (arrowhead). (B) Three-point bending analysis indicates that femora of Zip14 fl/- ; Runx2-Cre mice tolerate higher stress levels and are more elastic. Work-to-fracture is also significantly reduced and qBEI analysis indicates significant lower cortical mineralization (Ct.CaMean) of femora of these mice, compared to controls. (C) Representative undecalcified spine (upper row) and tibia sections (bottom row) from Zip14 fl/- , Zip14 fl/- ; Runx2-Cre and Zip14 fl/- ; CtsK-Cre mice stained with von Kossa/van Gieson. Vertebrae of Zip14 fl/- ; Runx2-Cre mice show less trabecular bone, whereas tibiae of these mice show an increased cortical thickness and decreased midshaft diameter compared to Zip14 fl/- controls. (D) Quantification of the bone surface covered by osteoblasts (Ob.S/BS), osteoblast number per bone perimeter (N.Ob/B.Pm), osteoclast surface per bone surface (Oc.S/BS) and osteoclast number per bone perimeter (N.Oc/B.Pm) in the vertebral bodies analyzed using toluidine blue staining. N = 6 animals/genotype; *: p <0.05; **: p <0.025 by 2-tailed Student’s t-test (compared to Zip14 fl/- mice).$

Journal: PLoS Genetics

Article Title: Conditional mouse models support the role of SLC39A14 (ZIP14) in Hyperostosis Cranialis Interna and in bone homeostasis

doi: 10.1371/journal.pgen.1007321

Figure Lengend Snippet: (A) X-rays of femora and tibiae of a Zip14 fl/- and Zip14 fl/- ; Runx2-Cre mouse. The latter demonstrates with a tibial fracture (arrow), whereas narrowing of the femoral midshaft can be observed as well (arrowhead). (B) Three-point bending analysis indicates that femora of Zip14 fl/- ; Runx2-Cre mice tolerate higher stress levels and are more elastic. Work-to-fracture is also significantly reduced and qBEI analysis indicates significant lower cortical mineralization (Ct.CaMean) of femora of these mice, compared to controls. (C) Representative undecalcified spine (upper row) and tibia sections (bottom row) from Zip14 fl/- , Zip14 fl/- ; Runx2-Cre and Zip14 fl/- ; CtsK-Cre mice stained with von Kossa/van Gieson. Vertebrae of Zip14 fl/- ; Runx2-Cre mice show less trabecular bone, whereas tibiae of these mice show an increased cortical thickness and decreased midshaft diameter compared to Zip14 fl/- controls. (D) Quantification of the bone surface covered by osteoblasts (Ob.S/BS), osteoblast number per bone perimeter (N.Ob/B.Pm), osteoclast surface per bone surface (Oc.S/BS) and osteoclast number per bone perimeter (N.Oc/B.Pm) in the vertebral bodies analyzed using toluidine blue staining. N = 6 animals/genotype; *: p <0.05; **: p <0.025 by 2-tailed Student’s t-test (compared to Zip14 fl/- mice).

Article Snippet: Incubation with primary anti-human ZIP14 antibody (PA5-21077, Thermo Fisher Scientific, 1:200 dilution) was performed at room temperature for 1 hour.

Techniques: Staining

(A) Dynamic histomorphometry of the tibial endocortical (Ct) bone surface indicates a significant increase in endosteal mineralizing surface (MS/BS) and bone formation rate (BFR/BS) in Zip14 fl/- ; Runx2-Cre . In Zip14 fl/- ; CtsK-Cre mice a significant increase in MS/BS was detected. (B) Dynamic histomorphometry of trabecular (Tb) bone surface of vertebral bodies (L3-L4) indicates a significant lower MS/BS and BFR/BS in Zip14 fl/- ; CtsK-Cre mice. (C) Measurement of the bone turnover markers procollagen type-I C-terminal peptide (PICP; bone formation) and collagen type 1 cross-linked C-telopeptide (Crosslaps; bone resorption) in serum of 6-month old control ( Zip14 fl/- ), osteoblast-specific knock-in ( Zip14 fl/- ; Runx2-Cre ) and osteoclast-specific knock-in ( Zip14 fl/- ; CtsK-Cre ) mice. (D) Quantification of the serum RANKL and OPG levels and the calculated RANKL/OPG ratio. N = 6 animals/genotype; *: p <0.05; **: p <0.025 by 2-tailed Student’s t-test (compared to Zip14 fl/- mice).

Journal: PLoS Genetics

Article Title: Conditional mouse models support the role of SLC39A14 (ZIP14) in Hyperostosis Cranialis Interna and in bone homeostasis

doi: 10.1371/journal.pgen.1007321

Figure Lengend Snippet: (A) Dynamic histomorphometry of the tibial endocortical (Ct) bone surface indicates a significant increase in endosteal mineralizing surface (MS/BS) and bone formation rate (BFR/BS) in Zip14 fl/- ; Runx2-Cre . In Zip14 fl/- ; CtsK-Cre mice a significant increase in MS/BS was detected. (B) Dynamic histomorphometry of trabecular (Tb) bone surface of vertebral bodies (L3-L4) indicates a significant lower MS/BS and BFR/BS in Zip14 fl/- ; CtsK-Cre mice. (C) Measurement of the bone turnover markers procollagen type-I C-terminal peptide (PICP; bone formation) and collagen type 1 cross-linked C-telopeptide (Crosslaps; bone resorption) in serum of 6-month old control ( Zip14 fl/- ), osteoblast-specific knock-in ( Zip14 fl/- ; Runx2-Cre ) and osteoclast-specific knock-in ( Zip14 fl/- ; CtsK-Cre ) mice. (D) Quantification of the serum RANKL and OPG levels and the calculated RANKL/OPG ratio. N = 6 animals/genotype; *: p <0.05; **: p <0.025 by 2-tailed Student’s t-test (compared to Zip14 fl/- mice).

Article Snippet: Incubation with primary anti-human ZIP14 antibody (PA5-21077, Thermo Fisher Scientific, 1:200 dilution) was performed at room temperature for 1 hour.

Techniques: Control, Knock-In

qRT-PCR analysis of genes encoding inflammatory cytokines ( Il-6 , Tnf ) and osteoblast markers ( Runx2 , Col1a , Ibsp , Bglap ) was performed in primary osteoblasts derived from the long bones and calvariae of Zip14 fl/- mice and Zip14 fl/- ; Runx2-Cre mice at three time points (d 0 , d 14 , d 21 ) during their differentiation. A significant higher expression of Il-6 and Tnf was detected at respectively day 0 and day 14 of differentiating long bone Zip14 fl/- ; Runx2-Cre osteoblasts, compared to long bone Zip14 fl/- osteoblasts. Bglap expression was, on the other hand, significantly lower at day 0 of differentiating long bone Zip14 fl/- ; Runx2-Cre osteoblasts. N = 3 animals/genotype; *: p <0.05; **: p <0.01 by 2-tailed Student’s t-test (compared to Zip14 fl/- mice).

Journal: PLoS Genetics

Article Title: Conditional mouse models support the role of SLC39A14 (ZIP14) in Hyperostosis Cranialis Interna and in bone homeostasis

doi: 10.1371/journal.pgen.1007321

Figure Lengend Snippet: qRT-PCR analysis of genes encoding inflammatory cytokines ( Il-6 , Tnf ) and osteoblast markers ( Runx2 , Col1a , Ibsp , Bglap ) was performed in primary osteoblasts derived from the long bones and calvariae of Zip14 fl/- mice and Zip14 fl/- ; Runx2-Cre mice at three time points (d 0 , d 14 , d 21 ) during their differentiation. A significant higher expression of Il-6 and Tnf was detected at respectively day 0 and day 14 of differentiating long bone Zip14 fl/- ; Runx2-Cre osteoblasts, compared to long bone Zip14 fl/- osteoblasts. Bglap expression was, on the other hand, significantly lower at day 0 of differentiating long bone Zip14 fl/- ; Runx2-Cre osteoblasts. N = 3 animals/genotype; *: p <0.05; **: p <0.01 by 2-tailed Student’s t-test (compared to Zip14 fl/- mice).

Article Snippet: Incubation with primary anti-human ZIP14 antibody (PA5-21077, Thermo Fisher Scientific, 1:200 dilution) was performed at room temperature for 1 hour.

Techniques: Quantitative RT-PCR, Derivative Assay, Expressing

Luciferase reporter assays investigating cAMP-CREB activity, NF-κB activity and NFAT activity by wildtype (WT), L441R and truncated (W22X) ZIP14 in (A) HEK293T cells and (B) Saos-2 cells demonstrate a significant increase in cAMP-CREB and NFAT signaling by L441R ZIP14, compared to WT ZIP14. *: p <0.05; **: p <0.01 by 2-tailed Student’s t-test.

Journal: PLoS Genetics

Article Title: Conditional mouse models support the role of SLC39A14 (ZIP14) in Hyperostosis Cranialis Interna and in bone homeostasis

doi: 10.1371/journal.pgen.1007321

Figure Lengend Snippet: Luciferase reporter assays investigating cAMP-CREB activity, NF-κB activity and NFAT activity by wildtype (WT), L441R and truncated (W22X) ZIP14 in (A) HEK293T cells and (B) Saos-2 cells demonstrate a significant increase in cAMP-CREB and NFAT signaling by L441R ZIP14, compared to WT ZIP14. *: p <0.05; **: p <0.01 by 2-tailed Student’s t-test.

Article Snippet: Incubation with primary anti-human ZIP14 antibody (PA5-21077, Thermo Fisher Scientific, 1:200 dilution) was performed at room temperature for 1 hour.

Techniques: Luciferase, Activity Assay

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1) Product Images from "Discovery of a Selective Inhibitor of ZIP14 with Therapeutic Potential for Cancer-associated Cachexia"

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