Glucose and cationic amino acid transporter expression in growing chickens (Gallus gallus domesticus)

Humphrey, Brooke; Stephensen, Charles B.; Calvert, C. C.; Klasing, Kirk C.

doi:10.1016/j.cbpb.2004.06.016

Cited by 64 publications

(24 citation statements)

References 40 publications

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“…Primer sequences (Table1) for genes of interest were either derived from published sources or designed using Primer3 Software (Rozen and Skaletsky, 2000) as previously described (Humphrey et al, 2004). The primers were designed to span introns to prevent contamination with genomic DNA and preliminary experiments confirmed that the primer pairs each only produced one product of predicted size.…”

Section: Relative Qrt-pcrmentioning

confidence: 99%

Mobilization of ectopic yolk in Gallus domesticus: a novel reverse lipid transport process

Cornax

Walzem

Larner

et al. 2013

Journal of Experimental Biology

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SUMMARYIn many oviparous animals, bursting type atresia of ovarian follicles occurs during the reproductive cycle, resulting in the escape of yolk into the extracellular compartment. In birds, this ectopic yolk is rapidly cleared by an unknown process that involves the appearance of yolk-engorged macrophage-like cells. To study this unique type of lipid transport, we injected young male chickens intra-abdominally with egg yolk. Absorption of egg yolk from the body cavity markedly increased the triacylglyceride-rich fraction (TRL) of plasma lipoproteins and was coincident with increased levels of plasma triacylglycerides (TAGs) but not non-esterified fatty acids (NEFAs). Thus, the transport of yolk lipids from the abdominal cavity appears to occur in lipoproteins and be more similar to the transport of hepatic TAGs to the periphery via lipoproteins than to transport of adipose TAGs to the periphery via NEFAs released by the action of lipases. When macrophages were exposed to yolk in vitro, they quickly phagocytized yolk; however, it is unclear whether this level of phagocytosis contributes significantly to total yolk clearance. Instead, the chicken macrophage may function more as a facilitator of yolk clearance through the modification of yolk lipoproteins and the regulation of the local and systemic immune response to ectopic yolk. Yolk appears to be anti-inflammatory in nature. Yolk did not increase levels of the inflammatory cytokines IL-1, IL-6 and IFNγ either in vivo or in vitro; in fact, yolk dampened many inflammatory changes caused by lipopolysaccharide (LPS). Conversely, LPS-induced inflammation retarded yolk clearance from the abdominal cavity and plasma TAG levels.

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Section: Relative Qrt-pcrmentioning

confidence: 99%

Mobilization of ectopic yolk in Gallus domesticus: a novel reverse lipid transport process

Cornax

Walzem

Larner

et al. 2013

Journal of Experimental Biology

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“…The annealing temperature for analyzing CD25 was 56˚C, CTLA-4 was 55˚C, and LAG-3 was 57˚C. Fold change from the reference was calculated (26) as ES (Ct sample)/ER (Ct reference), in which ES and ER are the sample and reference PCR amplification efficiencies as determined by LinRegPCR program (27) and Ct is the threshold cycle. The reference group was the CD4 2 CD25 2 group for CD25 mRNA analysis and the CD4 + CD25…”

Section: Mrna Analysesmentioning

confidence: 99%

Regulatory T Cell Properties of Chicken CD4+CD25+ Cells

Shanmugasundaram

Selvaraj

2011

The Journal of Immunology

114

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Chicken CD4+CD25+ cells were characterized for mammalian regulatory T cells’ suppressive and cytokine production properties. Anti-chicken CD25 mAb was produced in mice and conjugated with a fluorescent tag. The specificity of the Ab against chicken CD25 was confirmed by evaluating Con A-induced CD25 upregulation in thymocytes and by quantifying the CD25 mRNA content of positive and negative cells identified by anti-chicken CD25 Ab. The percentage of CD4+CD25+ cells, expressed as a percentage of CD4+ cells, in thymus and blood was ∼3–7%, in spleen was 10%, and in cecal tonsil, lung, and bone marrow was ∼15%. Bursa had no detectable CD4+CD25+ cells. CD25+ cells were mostly CD4+ in the thymus, whereas in every other organ studied, CD25+ cells were distributed between CD4+ and CD4− cells. Chicken thymic CD4+CD25+ cells did not proliferate in vitro in the absence of recombinant chicken IL-2 (rCIL-2). In the presence of rCIL-2, PMA plus ionomycin or Con A stimulated CD4+CD25+ cell proliferation, whereas anti-CD3 plus CD28 did not stimulate CD4+CD25+ cell proliferation. Naive CD4+CD25+ cells had 29-fold more IL-10 mRNA and 15-fold more TGF-β mRNA than the naive CD4+CD25− cells. Naive CD4+CD25+ had no detectable IL-2 mRNA. Both naive and PMA plus ionomycin-stimulated thymic CD4+CD25+ cells suppressed naive T cell proliferation. The suppressive properties were partially contact dependent. Supplementing CD4+CD25+ cell coculture with rCIL-2 reversed the suppressive properties of CD4+CD25+ cells. Chicken CD4+CD25+ cells have suppressive properties similar to that of mammalian regulatory T cells.

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“…Chicken CAT-1 mRNA is found in the bursa, thymus, skeletal muscle and liver, but not in the heart or spleen [24]. In mammals, CAT-1 is found in nearly all tissues except hepatocytes [25].…”

Section: Arginine Metabolismmentioning

confidence: 93%

“…In mammals, CAT-1 is found in nearly all tissues except hepatocytes [25]. Chicken CAT-3 has a slightly lower affinity than CAT-1 and is found in the bursa, thymus, heart and pectoralis [24]. The mammalian CAT-3 is expressed in the thymus, brain, uterus and testis [25].…”

Section: Arginine Metabolismmentioning

confidence: 99%

“…Primary macrophages isolated from tissue and primary monocytes isolated from blood exhibit similar responses when activated. Both types of cell isolates produce reactive nitrogen species, actively phagocytose, synthesize cytokines and increase major histocompatibility II expression [23,24]. Many specialized macrophages, or macrophage-like cells, exist in numerous tissues including alveolar macrophages in the lungs, Kupffer cells in the liver, microglial cells in the nervous tissue and osteoclasts in bone [25,26].…”

Section: Macrophagesmentioning

confidence: 99%

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Nitric oxide synthesis by chicken macrophages results in coordinated changes of multiple arginine transporters

Moulds¹

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Macrophages metabolize arginine (ARG) to nitric oxide (NO) via inducible nitric oxide synthase (iNOS). In mammals, macrophage NO synthesis is dependent upon CAT‐2B mediated ARG uptake; however, in avian macrophages the transporter(s) coordinating ARG uptake for NO synthesis are unknown. Therefore, HD‐11 cells were cultured in complete media with 0 (control) or 1μg/ml E. coli lipopolysaccharide (LPS) to determine any changes in the ARG transporter(s) involved in ARG uptake for NO production. At 24 and 48 h of culture, media nitrite concentrations were measured and ARG transporter systems and iNOS mRNA abundance were measured by quantitative real‐time PCR. LPS increased nitrite 18‐fold and 76‐fold at 24 and 48 h, respectively, compared to control (P<0.05). LPS increased iNOS mRNA 8.5‐fold compared to control at 48 h (P<0.05). CAT‐2B mRNA was not detected in control or LPS treated HD‐11 cells. LPS increased the mRNA abundance of ARG importers CAT‐2A by 1.6‐fold and b0,+ by 3.7‐fold at 48 h. LPS induced mRNA expression of ARG importers CAT‐1 and CAT‐3 at 48 h. LPS decreased the mRNA abundance of the ARG exporter y+LAT1 by 71% at 48 h. Unlike mammals, avian macrophages appear to utilize a number of ARG transport systems to increase ARG uptake for NO production. Funding: California Agricultural Research Initiative

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Glucose and cationic amino acid transporter expression in growing chickens (Gallus gallus domesticus)

Cited by 64 publications

References 40 publications

Mobilization of ectopic yolk in Gallus domesticus: a novel reverse lipid transport process

Mobilization of ectopic yolk in Gallus domesticus: a novel reverse lipid transport process

Regulatory T Cell Properties of Chicken CD4+CD25+ Cells

Nitric oxide synthesis by chicken macrophages results in coordinated changes of multiple arginine transporters

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