Dataset Information

AML patients samples compared to Healthy Human CD34+ cells (LFQ LC-MSMS)

ABSTRACT: Cryopreserved normal CD34 + bone marrow cells were derived from eight healthy Caucasians (four men and four women; PromoCell GMBH; Heidelberg, Germany), and their age did not differ significantly from the AML patients analysed in the study. The submitted samples have been analyzed together with raw files derived from 50 different AML patient samples (9 patients samples in this project and 41 patient samples in project PXD014997).

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Blood Cell, Bone Marrow

DISEASE(S): Acute Leukemia

SUBMITTER: Frode Selheim

LAB HEAD: Frode Selheim

PROVIDER: PXD058846 | Pride | 2025-05-07

REPOSITORIES: Pride

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Publications

Proteomic Comparison of Acute Myeloid Leukemia Cells and Normal CD34+ Bone Marrow Cells: Studies of Leukemia Cell Differentiation and Regulation of Iron Metabolism/Ferroptosis.

Selheim Frode F Aasebø Elise E Reikvam Håkon H Bruserud Øystein Ø Hernandez-Valladares Maria M

Proteomes 20250217 1

Acute myeloid leukemia (AML) is an aggressive bone marrow malignancy that can be cured only by intensive chemotherapy possibly combined with allogeneic stem cell transplantation. We compared the pretreatment proteomic profiles of AML cells derived from 50 patients at the time of first diagnosis with normal CD34+ bone marrow cells. A comparison based on all AML and CD34+ normal cell populations identified 121 differentially abundant proteins that showed at least 2-fold diffe ...[more]

PMID: 39982321

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Project description:Extraintestinal pathogenic Escherichia coli (ExPEC) have a capacity to cause serious infections of blood, the central nervous system and particularly the urinary tract. Relatively little is known about how ExPEC adapt their cell-wide protein expression to environments with different carbon sources and other required nutrients. We used label-free quantitative (LFQ) proteomic analysis to determine proteomes of five ExPEC strains purified from clinical blood cultures, and compared them with proteomes of reference uropathogenic E. coli strain 536 derived from blood culture and two chemically different solid media. We identified 2,883 proteins in total, and for 90% of the detected proteins described their relative quantitative levels based on LFQ intensity scores. Comparison of anaerobic and aerobic blood cultures revealed significant differences in the levels of 32 proteins out of 1854 shared proteins. A majority of these proteins was associated with acquisition and utilization of metal ions, which are critical either for anaerobic (nickel) or aerobic (iron) respiration. ANOVA analysis of the relative quantitative levels of 1758 proteins shared between the strains identified 47 differentially expressed proteins, including proteins involved in vitamin B6 metabolism, cell motility and virulence. Comparison of strain 536 proteomes derived from blood cultures and solid media showed substantial variation in the relative quantitative levels of 200 proteins, which represented 11% of the common proteins between the conditions. Blood culture condition was characteristic by upregulation of anaerobic fermentative metabolism, cell motility and iron utilization. In a response to the growth on solid media increased levels of proteins functional in aerobic respiration, catabolism of various biochemicals obtained from the media and protection against environmental stresses. The study presents the largest coverage of ExPEC/UPEC proteome to date,with a detail account of ExPEC metabolism under three chemically different environments.

			Action	DRS
	AML-OSvsNS_LF_39.raw	Raw
	AML-OSvsNS_LF_Ctr1.raw	Raw
	AML-OSvsNS_LF_Ctr2.raw	Raw
	AML-OSvsNS_LF_Ctr5.raw	Raw
	AML-OSvsNS_LF_Ctr6.raw	Raw

Dataset Information

AML patients samples compared to Healthy Human CD34+ cells (LFQ LC-MSMS)

Dataset's files

Publications

Proteomic Comparison of Acute Myeloid Leukemia Cells and Normal CD34<sup>+</sup> Bone Marrow Cells: Studies of Leukemia Cell Differentiation and Regulation of Iron Metabolism/Ferroptosis.

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