Casein-mediated neutrophil chemotaxis

Epps, Dennis E. Van; Bankhurst, Arthur D.; Williams, Ralph C.

doi:10.1007/bf00918673

Cited by 28 publications

(6 citation statements)

References 9 publications

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“…Patients with persistently raised blood eosinophil counts have a high incidence of endomyocardial fibrosis [Loffler's or eosinophilic endomyocardial disease (Chusid et al, 1975;Parrillo et al, 1979)] and it has been suggested that eosinophils themselves could cause the cardiac injury (Brockington et al, 1970). Initially experiments in vitro to see whether eosinophils could damage antibody-coated cells including heart cells showed little cytotoxicity (van Epps & Bankhurst, 1978) unless complement was also present (Parrillo & Fauci, 1978). However, the presence of degranulated eosinophils in the blood and cardiac tissues of patients with endomyocardial disease supported the suggestion that this disease was caused by eosinophil secretion products released from degranulated eosinophils (Spry & Tai, 1976).…”

mentioning

confidence: 99%

Toxic effects of human eosinophil products on isolated rat heart cells in vitro

Tai¹,

Hayes²,

Clark³

et al. 1982

Biochemical Journal

142

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Rat heart cells and mitochondria were incubated with supernatants from eosinophils or neutrophils that had been stimulated with zymosan-C3b. Supernatants from eosinophils, but not neutrophils, were toxic to rat heart cells in a dose-dependent manner. This was associated with an increased O2 uptake, which was blocked by either 1 mM-cyanide or 100 microM-ouabain. Supernatants from eosinophils, but not neutrophils, caused a decrease in O2 uptake by rat heart mitochondria utilizing pyruvate (+ malate) but not other substrates. The activity of pyruvate dehydrogenase (EC 1.2.4.1) from rat heart was inhibited by Ca2+-free eosinophil supernatants. The activity of oxoglutarate dehydrogenase (EC 1.2.4.2) was also inhibited but not that of lipoamide dehydrogenase (EC 1.6.4.3). Prior incubation with heparin prevented these effects of eosinophil supernatants on heart cells, suggesting that they were caused by eosinophil cationic proteins. Other cationic proteins, including poly-L-lysine and poly-L-arginine were also toxic to rat heart cells, but these reduced O2 uptake. It was concluded that granulocyte secretion products containing eosinophil cationic proteins are toxic to isolated rat heart cells in vitro. This may be due to an initial increase in membrane permeability, which may lead to activation of (Na+ + K+)-dependent ATPase and increased O2 uptake. A second step may involve inhibition of pyruvate dehydrogenase by the same products, leading to a decreased O2 uptake. It is suggested that these mechanisms could contribute to the development of cardiac injury and myocardial disease in clinical situations where many degranulated eosinophils are present.

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mentioning

confidence: 99%

Toxic effects of human eosinophil products on isolated rat heart cells in vitro

Tai¹,

Hayes²,

Clark³

et al. 1982

Biochemical Journal

142

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“…As PMNs are critical players in inflammatory and tumorigenic processes in the colon [5,9,38,39], we investigated the significance of increased LDs and loss of FOXO3 in PMNs' activity. Intraperitoneal PMNs were obtained from wild type (WT) and FOXO3 knock-out (KO) mice following casein injection [40,41]. After PMNs enrichment, the final fraction contained more than 90% PMNs (FACS assessment of surface marker Ly6G), and peritoneal PMNs in FOXO3 KO mice were increased compared to WT.…”

Section: Increased Migratory Activity Of Pmns Is Associated With Elev...mentioning

confidence: 99%

FOXO3 Deficiency in Neutrophils Drives Colonic Inflammation and Tumorigenesis

Ghimire

Iftikhar

Penrose

et al. 2023

IJMS

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Inflammatory bowel disease (IBD), characterized by infiltration of polymorphonuclear neutrophils (PMNs), increases the risk of colon cancer. PMN activation corresponds to the accumulation of intracellular Lipid Droplets (LDs). As increased LDs are negatively regulated by transcription factor Forkhead Box O3 (FOXO3), we aim to determine the significance of this regulatory network in PMN-mediated IBD and tumorigenesis. Affected tissue of IBD and colon cancer patients, colonic and infiltrated immune cells, have increased LDs’ coat protein, PLIN2. Mouse peritoneal PMNs with stimulated LDs and FOXO3 deficiency have elevated transmigratory activity. Transcriptomic analysis of these FOXO3-deficient PMNs showed differentially expressed genes (DEGs; FDR < 0.05) involved in metabolism, inflammation, and tumorigenesis. Upstream regulators of these DEGs, similar to colonic inflammation and dysplasia in mice, were linked to IBD and human colon cancer. Additionally, a transcriptional signature representing FOXO3-deficient PMNs (PMN-FOXO3389) separated transcriptomes of affected tissue in IBD (p = 0.00018) and colon cancer (p = 0.0037) from control. Increased PMN-FOXO3389 presence predicted colon cancer invasion (lymphovascular p = 0.015; vascular p = 0.046; perineural p = 0.03) and poor survival. Validated DEGs from PMN-FOXO3389 (P2RX1, MGLL, MCAM, CDKN1A, RALBP1, CCPG1, PLA2G7) are involved in metabolism, inflammation, and tumorigenesis (p < 0.05). These findings highlight the significance of LDs and FOXO3-mediated PMN functions that promote colonic pathobiology.

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“…In vitro experiments reported caseininduced macrophage and neutrophil migration. [4][5][6] Most proteins are digested into peptides and amino acids when a food protein is taken orally. Previously, it has been reported that YPVEP, produced by digesting β-casein with actinase, derived from actinomycetes, helps migrate mouse macrophages.…”

Section: Introductionmentioning

confidence: 99%

Peptides Derived from Soybean β-Conglycinin Induce the Migration of Human Peripheral Polymorphonuclear Leukocytes

Nagashima

Fujii

Oka

et al. 2023

Biological & Pharmaceutical Bulletin

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Food-derived peptides have various biological activities. When food proteins are ingested orally, they are digested into peptides by endogenous digestive enzymes and absorbed by the immune cell-rich intestinal tract. However, little is known about the effects of food-derived peptides on the motility of human immune cells. In this study, we aimed to understand the effects of peptides derived from a soybean protein β-conglycinin on the motility of human peripheral polymorphonuclear leukocytes. We illustrated that MITL and MITLAIPVNKPGR, produced by digestion using in-vivo enzymes (trypsin and pancreatic elastase) of β-conglycinin, induces the migration of dibutyryl cAMP (Bt 2 cAMP)-differentiated human promyelocytic leukemia 60 (HL-60) cells and human polymorphonuclear leukocytes in a dose-and time-dependent manner. This migration was more pronounced in Bt 2 cAMP-differentiated HL-60 cells; mRNA expression of formyl peptide receptor (FPR) 1 increased significantly than in all-trans-retinoic acid (ATRA)-differentiated HL-60 cells. This migration was inhibited by tert-butoxycarbonyl (Boc)-MLP, an inhibitor of FPR, and by pretreatment with pertussis toxin (PTX). However, the effect was weak when treated with WRW4, a selective inhibitor of the FPR2. We then demonstrated that MITLAIPVNKPGR induced intracellular calcium responses in human polymorphonuclear leukocytes and Bt 2 cAMP-HL60 cells. Furthermore, pre-treatment by fMLP desensitized the calcium response of MITLAIPVNKPGR in these cells. From the above, MITLAIPVNKPGR and MITL derived from soybean β-conglycinin induced polymorphonuclear leukocyte migration via the FPR1-dependent mechanism. We found chemotactic peptides to human polymorphonuclear leukocytes, which are the endogenous enzyme digests of soybean protein.

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Casein-mediated neutrophil chemotaxis

Cited by 28 publications

References 9 publications

Toxic effects of human eosinophil products on isolated rat heart cells in vitro

Toxic effects of human eosinophil products on isolated rat heart cells in vitro

FOXO3 Deficiency in Neutrophils Drives Colonic Inflammation and Tumorigenesis

Peptides Derived from Soybean β-Conglycinin Induce the Migration of Human Peripheral Polymorphonuclear Leukocytes

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