scholarly journals Plasma proteomic profiles of healthy and mastitic cows – host responses to bovine mastitis

2013 ◽  
Vol 56 (1) ◽  
pp. 980-987 ◽  
Author(s):  
L.L. Niu ◽  
C.H. Wei ◽  
L.X. Du
Keyword(s):  
Dairy Cows ◽  
Acute Phase Proteins ◽  
Bovine Mastitis ◽  
Economic Loss ◽  
Differentially Expressed ◽  
Host Responses ◽  
Common Disease ◽  
Differentially Expressed Proteins ◽  
Proteomic Profiling ◽  
Two Dimensional Gel Electrophoresis

Abstract. Mastitis is the most common disease in dairy cows and has resulted in a tremendous economic loss in dairy industry. In the present study, differentially expressed proteins (DEP) were identified among healthy, moderate and severe mastitic cows by proteomic profiling. The health status of cows was closely determined by the somatic cell count (SCC). Differentially expressed proteins were resolved using the two-dimensional gel electrophoresis (2-DE) with the pH 4–7 non-linear DryStrips. Subsequently, 8 protein spots, which altered more than 3-fold, were isolated and identified with the matrix-assisted laser desorption/ionisation-time of flight mass spectrometry (MALDI TOF/TOF MS). The identified spots were split into four proteins: α-2-HS-glycoprotein, serum albumin, transthyretin (TTR) and haptoglobin, respectively. Compared with the healthy cows, the expression of haptoglobin was up-regulated in mastitic cows, and the others were down-regulated. Moreover, the proteomic data were consistent with the results of Western blot. All of the identified DEPs were acute phase proteins, which acted together and represented the consequence of serial cascades after mastitic infection. More importantly, the α-2-HS-glycoprotein was novel identified corresponding to the bovine mastitis in Chinese Holstein dairy cows. Taken together, our results indicate that the host responses may play an important role in the pathogenesis of mastitis and provide the potential diagnostic indicator of the underlying mastitis in dairy cows.

scholarly journals Quantitative analysis of proteomic profiling in constipation colon biopsies

2020 ◽  
Author(s):  
Chen Ye ◽  
Qiyi Chen ◽  
Di Zhao ◽  
Hongliang Tian ◽  
Xueying Zhang ◽  
...  
Keyword(s):  
Signaling Pathways ◽  
Pathway Analysis ◽  
Expression Profiles ◽  
Human Colon ◽  
Quantitative Information ◽  
Differentially Expressed ◽  
Spectrometric Analysis ◽  
Common Disease ◽  
Differentially Expressed Proteins ◽  
Proteomic Profiling

Abstract Background Chronic constipation is a common disease and between 2% and 27% of people are suffering from it in the world. Rare studies explore the diversity of genetic polymorphisms and cell metabolisms in constipation. This study provided a first analysis of constipation-related proteomic data. Methods To help elucidate the potential mechanisms responsible for constipation, proteomic profiling of human colon biopsy specimens was performed. Dysregulated proteins in disease tissues compared with normal tissues were characterized from the expression profiles by Liquid chromatography–mass spectrometry and Tandem Mass Tag proteomic methodology and further subjected to pathway analysis to identify altered biological processes and signaling pathways. Results A total of 5,208 proteins were identified, of which 4,522 had quantitative information. All the differentially expressed proteins displayed fold change greater than 1.3 were considered as dysregulated. Specifically, 42 proteins were up-regulated and 23 proteins were down-regulated in constipation samples. Bioinformatics analysis showed that most of the differentially expressed proteins were involved in the cellular process, single-organism process, metabolic process, biological regulation and response to stimulus. Pathway analysis of dysregulated proteins in constipation showed that the up-regulated proteins mainly participated in drug metabolism-cytochrome P450. Conclusions The TMT method followed by mass spectrometric analysis was applied to study the biopsy proteomic profiling alterations in constipation patients. Our results clearly proved that different protein profiles and signaling pathways were involved in constipation patients.

Proteomic analysis of the effects of lutein on mammary gland metabolism in dairy cows

2018 ◽  
Vol 85 (2) ◽  
pp. 152-156
Author(s):  
Caihong Wang ◽  
Chong Wang ◽  
Jianxin Liu ◽  
Hongyun Liu
Keyword(s):  
Blood Flow ◽  
Mammary Gland ◽  
Fatty Acid ◽  
Dairy Cows ◽  
Control Diet ◽  
Differentially Expressed ◽  
Acid Oxidation ◽  
Differentially Expressed Proteins ◽  
Proteomic Approach ◽  
Increased Blood Flow

The aim of the research reported in this Research Communication was to identify differentially expressed proteins in dairy cows with normal and lutein diet and to elucidate the mechanisms of lutein-induced effects on bovine mammary gland metabolism using a comparative proteomic approach. Thirty-three differentially expressed proteins were identified from mammary gland of control diet-fed and lutein diet-fed dairy cows. Among these proteins, 15 were upregulated and 18 were downregulated in the lutein group. Functional analysis of the differentially expressed proteins showed that increased blood flow, depressed glycolysis, enhanced lactose anabolism, decreased fatty acid oxidation and up-regulated beta lactoglobulin expression were connected with lutein addition. These results suggested that the increased blood flow, reduced glucose catabolism, enhanced capacity for milk lactose synthesis, depressed fatty acid catabolism and increased expression of antioxidantion related protein may be the prime factors contributing to the increased milk production and enhanced immune status in lutein-fed dairy cows. This study provides molecular mechanism of dietary lutein in regulating lactation of dairy cows.

scholarly journals Proteomic profiling reveals differentially expressed proteins associated with amylose accumulation during rice grain filling

BMC Genomics ◽  
2020 ◽  
Vol 21 (1) ◽  
Author(s):  
Hengdong Zhang ◽  
Jiana Chen ◽  
Shuanglü Shan ◽  
Fangbo Cao ◽  
Guanghui Chen ◽  
...  
Keyword(s):  
Amylose Content ◽  
Starch Synthesis ◽  
Grain Filling ◽  
Adenosine Diphosphate ◽  
Differentially Expressed ◽  
Rice Grain ◽  
Rice Cultivars ◽  
Differentially Expressed Proteins ◽  
Proteomic Profiling ◽  
Rice Grains

Abstract Background Amylose accumulation in rice grains is controlled by genetic and environmental factors. Amylose content is a determinant factor of rice quality in terms of cooking and eating. Great variations in amylose content in indica rice cultivars have been observed. The current study was to identify differentially expressed proteins in starch and sucrose metabolism and glycolysis/gluconeogenesis pathways and their relationships to amylose synthesis using two rice cultivars possess contrasting phenotypes in grain amylose content. Results Synthesis and accumulation of amylose in rice grains significantly affected the variations between rice cultivars in amylose contents. The high amylose content cultivar has three down-regulated differentially expressed proteins, i.e., LOC_Os01g62420.1, LOC_Os02g36600.1, and LOC_Os08g37380.2 in the glycolysis/gluconeogenesis pathway, which limit the glycolytic process and decrease the glucose-1-phosphate consumption. In the starch and sucrose metabolic pathway, an up-regulated protein, i.e., LOC_Os06g04200.1 and two down-regulated proteins, i.e., LOC_Os05g32710.1 and LOC_Os04g43360.1 were identified (Figure 4). Glucose-1-phosphate is one of the first substrates in starch synthesis and glycolysis that are catalyzed to form adenosine diphosphate glucose (ADPG), then the ADPG is catalyzed by granule-bound starch synthase I (GBSS I) to elongate amylose. Conclusions The results indicate that decreasing the consumption of glucose-1-phosphate in the glycolytic process is essential for the formation of ADPG and UDPG, which are substrates for amylose synthesis. In theory, amylose content in rice can be regulated by controlling the fate of glucose-1-phosphate.

Acute Lymphoblastic Leukemia Is a Bcl-2 Dependent Disease: Proteomic Profiling and Pre-Clinical Efficacy Of a Selective Bcl-2 Antagonist ABT-199

Blood ◽  
2013 ◽  
Vol 122 (21) ◽  
pp. 3919-3919 ◽  
Author(s):  
Marina Konopleva ◽  
Juliana M Benito ◽  
Karine G. Harutyunyan ◽  
Isabel Marzo ◽  
LaKiesha Debose ◽  
...  
Keyword(s):  
Family Members ◽  
Burkitt’S Lymphoma ◽  
Black Box ◽  
Burkitt's Lymphoma ◽  
Differentially Expressed ◽  
Bimolecular Fluorescence Complementation ◽  
Differentially Expressed Proteins ◽  
Proteomic Profiling ◽  
Two Samples ◽  
Apoptotic Proteins

Abstract The expression of Bcl-2 family proteins is perturbed in multiple types of cancers, including leukemias, and is associated with disease progression and resistance to chemotherapy. ABT-199 (GDC-0199) is a new BH3 mimetic that was developed to specifically target Bcl-2 while sparing Bcl-XL, hence avoiding thrombocytopenia intrinsic to 1st generation BH3 mimetics like ABT-737 (Souers et al., Nat Med, 2013). In this study, we report proteomic profiling of Bcl-2 family members in a large series of ALL patients (pts) and pre-clinical activity of ABT-199. Expression of 20 pro- and anti-apoptotic proteins was studied in 186 newly diagnosed ALL using reverse phase protein arrays (RPPA). Supervised clustering demonstrated distinct differences in 11 proteins in ALL with different cytogenetic and FAB characteristics (Fig. 1, p<0.005, false discovery rate <0.2%). Among these, pts with Burkitt's leukemia/lymphoma (n=9) expressed low levels of Bcl-2 and Bax while maintaining high expression of Bim, caspases and PARP. In contrast, t(4;11) pts expressed higher levels of Bcl-2, Bax and Bim. No significant differences in Bcl-XL or Mcl-1 levels were found in different ALL subtypes. Figure 1 RPPA profiling of apoptosis regulators in ALL. Heatmap of differentially expressed proteins based on cytogenetics and immunophenotype. Black box, Burkitt's leukemia; red box, t(4;11). Figure 1. RPPA profiling of apoptosis regulators in ALL. Heatmap of differentially expressed proteins based on cytogenetics and immunophenotype. Black box, Burkitt's leukemia; red box, t(4;11). The potential of ABT-199 to disrupt interactions between Bcl-2 and different pro-apoptotic proteins was studied using Bimolecular Fluorescence Complementation (BiFC, J Biol Chem 288:4935, 2013). The coding sequences for human Bcl-2, Bim, Bak, Bax and Noxa were subcloned into BiFC plasmids containing Venus fragments and transfected into HeLa cells. Approximately 60-70% of transfected cells were positive for Venus fluorescence due to association between Bcl-2 and Bim, Noxa, Bax or Bak. ABT-199 (2.5 µM, 24 hrs) significantly reduced Venus signal, indicating an inhibition of the interactions of Bcl-2 with these proteins, most potently with the multidomain proteins Bax and Bak (95%±18% and 85%±15% inhibition, respectively). ABT-199 rapidly induced apoptotic cell death in ALL cell lines and in primary ALL samples. Pre-B ALL cells (Nalm-6, REH, SEMK2 and RS4;11) were sensitive to ABT-199 and ABT-737 (IC50 0.007-1.4µM (199) and 0.035-0.7µM (737)). Notably, ABT-199 was more cytotoxic than ABT-737 against MLL-rearranged SEMK2 and RS4;11 cells, consistent with the notion of the greater Bcl-2 dependency of these cells. Lentiviral silencing of Bcl-XL sensitized REH cells to apoptosis by ABT-199 and ABT-737. T-ALL cells (PF-382, MOLT-4, P-12) expressed lower levels of Bcl-2 and were uniformly less sensitive to ABT-199 compared to ABT-737 (IC50 3.7±1.1µM vs 0.7±0.3µM, p=0.01). Burkitt's lymphoma cells Ramos and Raji had low Bcl-2 and high Mcl-1 expression, and were resistant to both agents (IC50>4µM). Next, the cytotoxic activity of ABT-199 was tested against a panel of 12 genetically diverse primary ALL samples, including 6 from pts with relapsed or refractory disease. Ten out of twelve samples (83%) were exquisitely sensitive to both agents, with IC50 values of 0.0001-0.14µM for ABT-199 and 0.0004-0.3µM for ABT-737. One of the four Ph+ samples was resistant to both agents, and one of the two T-ALL was less sensitive to ABT-199 compared to ABT-737. Two samples with t(4;11) were highly sensitive to ABT-199. All primary ALL samples tested (n=7) expressed high levels of Bcl-2, and no significant correlation between sensitivity and expression of Bcl-2 family members was found. Importantly, three human-derived xenografts from pediatric pre-B-ALL samples (1345, 1809, 0398) were very sensitive to ABT-199 (IC50 3nM, 0.1nM and 2.3nM, respectively). Finally, anti-leukemia activity of ABT-199 was tested in MLL-rearranged patient-derived xenograft NSG mice. Treatment with ABT-199 at 100mg/kg/d by oral gavage days 13-23 significantly reduced leukemia tumor burden as determined by bioluminescence imaging (average 70% reduction in BLI signal in 4 ABT-treated mice compared to 4 control animals at 9 weeks, p=0.03). In summary, proteomic profiling and patterns of sensitivity to Bcl-2 inhibition indicate that ALL, with exception of Burkitt's lymphoma, represents a Bcl-2 dependent disease. These results provide strong rationale for introducing ABT-199, which recently showed impressive efficacy in CLL trials, into the clinical armamentarium of ALL therapy. Disclosures: Konopleva: AbbVie, Inc: Research Funding. Leverson:AbbVie, Inc.: Employment, Equity Ownership.

Proteomic profile of primary isolated rat mesangial cells in high-glucose culture condition and decreased expression of PSMA6 in renal cortex of diabetic ratsThis paper is one of a selection of papers published in this special issue entitled “Second International Symposium on Recent Advances in Basic, Clinical, and Social Medicine” and has undergone the Journal's usual peer review process.

2010 ◽  
Vol 88 (4) ◽  
pp. 635-648 ◽  
Author(s):  
Zhiguo Li ◽  
Haojun Zhang ◽  
Xi Dong ◽  
Frank J. Burczynski ◽  
Patrick Choy ◽  
...  
Keyword(s):  
Diabetic Nephropathy ◽  
High Glucose ◽  
Gel Electrophoresis ◽  
Renal Cortex ◽  
Mesangial Cells ◽  
Diabetic Rats ◽  
Differentially Expressed ◽  
Differentially Expressed Proteins ◽  
Two Dimensional Gel Electrophoresis ◽  
Isolated Rat

Diabetic nephropathy (DN) is one of the most important complications of diabetic patients and is characterized histologically by an accumulation of extracellular matrix (ECM) protein in the glomerular mesangium. Therefore, mesangial cells likely play an important role in the development of diabetic nephropathy. Here, we employed proteomic techniques to investigate the protein profile of rat mesangial cells under high-glucose culture conditions. Primary isolated rat glomerular mesangial cells were cultured under different concentrations of glucose (5.4 mmol·L–1 for normal control and 30 mmol·L–1 for high glucose) for 0, 8, 16, and 72 h, as well as for 25 days. Cellular total proteins were isolated from these cells and employed for two-dimensional gel electrophoresis (2-DE). Differentially expressed proteins were identified by matrix-assisted laser desorption – ionization time-of-flight mass spectrometry (MALDI-TOF-MS) and some of these proteins were documented in rat models of diabetes by Western blot. Rat mesangial cells were successfully isolated in the laboratory and their proliferation rates were significantly inhibited by high glucose. Two-dimensional gel electrophoresis analyses revealed 28 differentially expressed protein spots between the normal and high-glucose groups. After MALDI-TOF-MS analysis, all 28 protein spots were successfully identified with the peptide mass fingerprint (PMF) method. Representatively, SOD1, PCBP1 and PSMA6 were validated by Western blot analysis following protein extractions from the normal and high-glucose groups. Abundance of these proteins was consistent with that found in 2-DE. Moreover, expression of SOD1, PCBP1, and PSMA6 in renal cortex was further examined in two rat models of diabetes (streptozotocin-induced and spontaneous OLETF diabetic models). Abundance of SOD1 and PCBP1 proteins did not show any significant difference between normal control and diabetic rats. However, abundance of the PSMA6 protein was significantly reduced in the renal cortex of both STZ-induced and spontaneous OLETF diabetic rats. Proteomic analysis identified 28 differentially expressed proteins in primary isolated rat mesangial cells between normal and high glucose treatments. Expression of one identified protein was found to be consistent with expression in the renal cortex of two rat diabetic models. Therefore, identification of protein expression patterns in mesangial cells can be employed to develop a therapeutic target for treatment of diabetic nephropathy.

scholarly journals Yeasts as a causative agent of bovine mastitis in Greece

2018 ◽  
Vol 54 (2) ◽  
pp. 105 ◽  
Author(s):  
E. BOURTZI-HATZOPOULOU (Ε. ΜΠΟΥΡΤΖΗ-ΧΑΤΖΟΠΟΥΛΟΥ) ◽  
A. ZDRAGAS (Α. ΖΔΡΑΓΚΑΣ) ◽  
E. PETRIDOU (Ε. ΠΕΤΡΙΔΟΥ) ◽  
G. FILIOUSIS (Γ. ΦΙΛΙΟΥΣΗΣ)
Keyword(s):  
Mammary Gland ◽  
Dairy Cows ◽  
Bovine Mastitis ◽  
Economic Loss ◽  
Geotrichum Candidum ◽  
Clinical Mastitis ◽  
Antibacterial Treatment ◽  
Northern Greece ◽  
Milk Samples ◽  
Mastitic Milk

The aim of this study was to isolate fungi from mastitic milk of dairy cows and to identify fungal microorganisms involved in bovine mastitis. A total of 608 milk samples from clinical mastitis quarters from 580 animals in Northern Greece were collected, during the years 1997-2001. Antibacterial treatment was administrated to 50% of the sampled animals. Forty two (42) fungi were isolated and identified using mycological media and methods. From the 42 fungi isolates, 38 were yeasts and 4 moulds. The yeasts isolated were classified into the genera Candida, Geotrichum, Rhodotorula. From the thirty four (34) Candida species, 14 were identified as G tropicalis and 6 as G krusei. Furthermore, 4 isolates were classified as G pseudotropicalis, 4 as G albicans, 3 as G parapsilosis and 3 as G rugosa. Geotrichum candidum and Rhodotorula spp. were represented with 2 isolates. The isolated moulds were classified into the genus Aspergillus. Fungi were isolated in pure culture from 38 milk samples and in mixed culturewith bacteria from 4. In 510 samples only bacteria were cultured, while in 56 samples no growth of microorganism was observed. The results of the present study indicate that a level of 6.9% of mycotic mastitis is significant and yeasts are apparently implicated in mammary gland pathology causing economic loss.

scholarly journals Improving Sperm Cryopreservation With Type III Antifreeze Protein: Proteomic Profiling of Cynomolgus Macaque (Macaca fascicularis) Sperm

2021 ◽  
Vol 12 ◽  
Author(s):  
Bingbing Chen ◽  
Shengnan Wang ◽  
Briauna Marie Inglis ◽  
Hao Ding ◽  
Angbaji Suo ◽  
...  
Keyword(s):  
Molecular Mechanism ◽  
Sperm Motility ◽  
Cynomolgus Macaque ◽  
Antifreeze Protein ◽  
Differentially Expressed ◽  
Differentially Expressed Proteins ◽  
Proteomic Profiling ◽  
Freezing And Thawing ◽  
Proteomic Change ◽  
Acrosomal Integrity

Antifreeze protein III (AFP III) is used for the cryopreservation of germ cells in various animal species. However, the exact mechanism of its cryoprotection is largely unknown at the molecular level. In this study, we investigated the motility, acrosomal integrity, and mitochondrial membrane potential (MMP), as well as proteomic change, of cynomolgus macaque sperm after cryopreservation. Sperm motility, acrosomal integrity, and MMP were lower after cryopreservation (p &lt; 0.001), but significant differences in sperm motility and MMP were observed between the AFP-treated sperm sample (Cryo+AFP) and the non-treated sample (Cryo–AFP) (p &lt; 0.01). A total of 141 and 32 differentially expressed proteins were, respectively, identified in cynomolgus macaque sperm cryopreserved without and with 0.1 μg/ml AFP III compared with fresh sperm. These proteins were mainly involved in the mitochondrial production of reactive oxygen species (ROS), glutathione (GSH) synthesis, and cell apoptosis. The addition of AFP III in the sperm freezing medium resulted in significant stabilization of cellular molecular functions and/or biological processes in sperm, as illustrated by the extent of proteomic changes after freezing and thawing. According to the proteomic change of differentially expressed proteins, we hypothesized a novel molecular mechanism for cryoprotection that AFP III may reduce the release of cytochrome c and thereby reduce sperm apoptosis by modulating the production of ROS in mitochondria. The molecular mechanism that AFP III acts with sperm proteins for cellular protection against cryoinjuries needs further study.

Comparative Proteomic Analysis Reveals Novel Biomarkers for Gastric Cancer in South Indian Tamil Population

2021 ◽  
Vol 24 ◽  
Author(s):  
Ananthi Sivagnanam ◽  
Balasankar Thangasamy ◽  
Vignesh Nagarajan ◽  
Subeksha Govindarajan Ravi ◽  
Jeevitha Chithra Madhesh ◽  
...  
Keyword(s):  
Gastric Cancer ◽  
Early Detection ◽  
Zinc Finger Protein ◽  
Critical Role ◽  
Differentially Expressed ◽  
Differentially Expressed Proteins ◽  
Serum Samples ◽  
Two Dimensional Gel Electrophoresis ◽  
South Indian ◽  
Novel Biomarkers

Background: Gastric cancer (GC) remains a major global health problem due to a poor understanding of its progression at the molecular level and a lack of early detection or diagnosis. Early detection is highly crucial for improving prognosis. The incidence of GC is very high in countries like India due to the limitations among the established biomarkers for GC owing to poor sensitivity and specificity. Objective: To identify the novel biomarkers from serum samples obtained from GC patients when compared with healthy subjects. Methods: Serum samples from GC patients were analyzed by two-dimensional gel electrophoresis (2DGE) coupled with tandem mass spectrometry (MS), including both matrix-assisted laser desorption/ionization-time of flight (MALDI-ToF) and liquid chromatography-MS (LC-MS/MS) analysis. Identified proteins were further analyzed by gene ontology and protein interaction studies. Results: A total of 73 protein spots were detected in 2DGE image analysis. Among them, seven differentially-expressed proteins were identified using MS analyses, which included serotransferrin/transferrin, albumin, ceruloplasmin, C-reactive protein (CRP), fibrinogen γ-chain (FGG), and two unreported novel proteins, immunoglobulin kappa constant (IgκC) region and Homo sapiens zinc finger protein 28 (ZNF28) homolog. Among these proteins, serotransferrin, albumin, ceruloplasmin, FGG, and ZNF28 were down-regulated in GC samples (p < 0.05), while IgκC region and CRP were up-regulated significantly. Conclusion: Most of the differentially expressed proteins were involved in angiogenesis, plasminogen-activating cascade, and blood coagulation pathways which are known to play a critical role in gastric tumorigenesis. Our current results provide a panel of candidate biomarkers for GC with novel biomarkers which were not reported earlier.

scholarly journals Proteomic profiling of von Hippel–Lindau syndrome and multiple endocrine neoplasia type 2 pheochromocytomas reveals different expression of chromogranin B

2007 ◽  
Vol 14 (2) ◽  
pp. 463-471 ◽  
Author(s):  
Frederieke M Brouwers ◽  
Sven Gläsker ◽  
Amanda F Nave ◽  
Alexander O Vortmeyer ◽  
Irina Lubensky ◽  
...  
Keyword(s):  
Multiple Endocrine Neoplasia ◽  
Multiple Endocrine Neoplasia Type ◽  
Differentially Expressed ◽  
Differentially Expressed Proteins ◽  
Proteomic Profiling ◽  
Chromogranin B ◽  
Von Hippel Lindau ◽  
Endocrine Neoplasia ◽  
Von Hippel Lindau Syndrome

Pheochromocytomas are catecholamine-producing tumors that can occur in the context of von Hippel–Lindau syndrome (VHL) and multiple endocrine neoplasia type 2 (MEN2). Pheochromocytomas in these two syndromes differ in histopathological features, catecholamine metabolism, and clinical phenotype. To further investigate the nature of these differences, we compared the global protein expressions of 8 MEN2A-associated pheochromocytomas with 11 VHL-associated pheochromocytomas by two-dimensional gel electrophoresis proteomic profiling followed by sequencing and identification of differentially expressed proteins. Although both types of pheochromocytoma shared similarities in their protein expression patterns, the expression of several proteins was distinctly different between VHL- and MEN2A-associated pheochromocytomas. We identified several of these differentially expressed proteins. One of the proteins with higher expression in MEN2-associated tumors was chromogranin B, of which the differential expression was confirmed by western blot analysis. Our results expand the evidence for proteomic differences between these two tumor entities, and suggest that VHL-associated pheochromocytomas may be deficient in fundamental machinery for catecholamine storage. In light of these new findings, as well as existing evidence for differences between both types of pheochromocytomas, we propose that these tumors may have different developmental origins.

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