Early changes in phosphatidylcholine metabolism in human acute promyelocytic leukemia cells stimulated to differentiate by phorbol ester

Pa, Cassileth; Suholet, D; Cooper, Ronald H.

doi:10.1182/blood.v58.2.237.bloodjournal582237

Cited by 4 publications

(5 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Cells of the myelomonocytic cell lines THP‐1 and HL‐60 were cultured in RPMI supplemented with the additives used for monocytes and 10% FCS. The differentiation of these cells into MAC‐like cells was triggered by 10 −7 m 1α,25‐dihydroxyvitamin D 3 or 10 −8 m phorbol myristate acetate (PMA) for up to 2 days 30–33 …”

Section: Methodsmentioning

confidence: 99%

Inverse regulation of the ADAM‐family members, decysin and MADDAM/ADAM19 during monocyte differentiation

et al. 2003

View full text Add to dashboard Cite

SUMMARYTwo members of the ADAM (a disintegrin and metalloprotease)-family, MADDAM and decysin, were described as dendritic cell (DC) maturation markers. We are interested in monocyte differentiation and investigated in particular the expression pattern of both genes during the differentiation of human monocytes into DC and macrophages (MAC). Both genes are weakly expressed in freshly isolated monocytes. In immature DC decysin mRNA was absent, even after induction of the terminal differentiation of DC by CD40L or tumour necrosis factor-a (TNF-a). Only in DC maturated by lipopolysaccharide (LPS) strong signals of decysin mRNA were detected. However, MADDAM mRNA was expressed in immature DC and the expression was markedly increased after induction of the terminal DC differentiation by various stimuli. In contrast, MAC showed a high constitutive decysin mRNA expression, but expressed no MADDAM mRNA. On protein level similar results of MADDAM expression were obtained. Stimulation of MAC by LPS did not induce MADDAM mRNA expression, while decysin mRNA expression was strongly increased. Further investigations revealed that the well-known inducer of MAC differentiation, 1a,25-dihydroxyvitamin D 3 up-regulated decysin mRNA expression during the differentiation of primary monocytes and myelomonocytic THP-1 cells into MAC. In vivo decysin mRNA expression was only detected in human colon, but not in other tissues we examined. Accordingly, isolated intestinal MAC expressed decysin mRNA. In conclusion, decysin and MADDAM mRNA expression were regulated in an opposite way during monocyte differentiation: MADDAM mRNA and protein was mainly detected in DC, whereas decysin mRNA expression was mainly found in MAC. Therefore only MADDAM, but not decysin is a suitable marker for human monocyte-derived DC.

show abstract

Section: Methodsmentioning

confidence: 99%

Inverse regulation of the ADAM‐family members, decysin and MADDAM/ADAM19 during monocyte differentiation

et al. 2003

View full text Add to dashboard Cite

show abstract

“…It is long known that phorbol esters stimulate PC synthesis in cultured human promyelocytic leukemia cells [39]. Since PMA was used to differentiate THP-1 cells in our studies, we surmise that these cells would maintain on-going synthesis of PC and GPLs, and that M1-like induction by LPS+IFN enhances the synthesis and also the breakdown of PC and GPLs [40].…”

Section: Significant Changes Of Gpls Spls and Tags In M1 And M2 States By Fatp4 Inactivation In Thp-1mentioning

confidence: 70%

“…Remarkably, FATP4 KD caused strong increases in PC, PE, PI, PS, and SM levels observed at M0 and M2 but not M1 state (Figures 3A,B). This suggests that FATP4 deficiency may provide fatty acids directed for the on-going PMA-activated PC synthesis [39] resulting in increased levels of these GPLs under basal M0 and anti-inflammatory M2-like conditions.…”

Section: Significant Changes Of Gpls Spls and Tags In M1 And M2 States By Fatp4 Inactivation In Thp-1mentioning

confidence: 99%

FATP4 inactivation in cultured macrophages attenuates M1- and ER stress-induced cytokine release via a metabolic shift towards triacylglycerides

Zhang

Gan-Schreier

et al. 2021

Biochemical Journal

View full text Add to dashboard Cite

Fatty acid transport protein 4 (FATP4) belongs to a family of acyl-CoA synthetases which activate long-chain fatty acids into acyl-CoAs subsequently used in specific metabolic pathways. Patients with FATP4 mutations and Fatp4-null mice show thick desquamating skin and other complications, however, FATP4 role on macrophage functions has not been studied. We here determined whether the levels of macrophage glycerophospholipids, sphingolipids including ceramides, triacylglycerides, and cytokine release could be altered by FATP4 inactivation. Two in vitro experimental systems were studied: FATP4 knockdown in THP-1-derived macrophages undergoing M1 (LPS + IFNγ) or M2 (IL-4) activation and bone marrow-derived macrophages (BMDMs) from macrophage-specific Fatp4-knockout (Fatp4M−/−) mice undergoing tunicamycin (TM)-induced endoplasmic reticulum stress. FATP4-deficient macrophages showed a metabolic shift towards triacylglycerides and were protected from M1- or TM-induced release of pro-inflammatory cytokines and cellular injury. Fatp4M−/− BMDMs showed specificity in attenuating TM-induced activation of inositol-requiring enzyme1α, but not other unfolded protein response pathways. Under basal conditions, FATP4/Fatp4 deficiency decreased the levels of ceramides and induced an up-regulation of mannose receptor CD206 expression. The deficiency led to an attenuation of IL-8 release in THP-1 cells as well as TNF-α and IL-12 release in BMDMs. Thus, FATP4 functions as an acyl-CoA synthetase in macrophages and its inactivation suppresses the release of pro-inflammatory cytokines by shifting fatty acids towards the synthesis of specific lipids.

show abstract

“…The contribution of each of these two pathways to the biosynthesis of PC appears to be balanced in a compensatory fashion. The stimulation of the synthesis of PC via the CDP-choline pathway in HL-60 cells (Cassileth, Suholet and Cooper 1981), rat brain synaptosomes (Prasad and Edwards, unpublished observations), and Saccharomyces cerevisiae (Waechter, Steiner and Lester 1969) has been shown to inhibit the transmethylation pathway whereas the inhibition of the transmethylation pathway by 3-deazaadenosine has been shown to increase choline incorporation into rat or hamster liver PC (Chiang, Im and Cantoni 1980). Whether these opposing directions in PC synthesis are independently triggered events or are the cell's response to maintain homeostatic integrity of PC compartments or pools is uncertain.…”

Section: Discussionmentioning

confidence: 99%

Regulation of Phosphatidylcholine Biosynthesis by the Methylation Pathway in Rat Pituitary Gland

Prasad¹,

Edwards²

1984

Horm Metab Res

View full text Add to dashboard Cite

Rat pituitary extracts catalyze methylation of phosphatidylethanolamine to phosphatidylcholine using S-adenosyl-L-methionine as the methyl donor. In vitro incubation of hemipituitaries with 1 mM 2-methylaminoethanol led to a dose dependent decrease in phosphatidylethanolamine methyltransferase activity as well as the incorporation of the radioactivity from [3H-methyl]-L-methionine into phosphatidyl-choline. The inhibitory effect of 2-methylaminoethanol was selective for phospholipids methylation since protein carboxymethyltransferase and catechol-o-methyltransferase activities were not affected.

show abstract

Early changes in phosphatidylcholine metabolism in human acute promyelocytic leukemia cells stimulated to differentiate by phorbol ester

Cited by 4 publications

References 0 publications

Inverse regulation of the ADAM‐family members, decysin and MADDAM/ADAM19 during monocyte differentiation

Inverse regulation of the ADAM‐family members, decysin and MADDAM/ADAM19 during monocyte differentiation

FATP4 inactivation in cultured macrophages attenuates M1- and ER stress-induced cytokine release via a metabolic shift towards triacylglycerides

Regulation of Phosphatidylcholine Biosynthesis by the Methylation Pathway in Rat Pituitary Gland

Contact Info

Product

Resources

About