Results 21 to 30 of about 174 (173)

Downregulation of SLC7A7 Triggers an Inflammatory Phenotype in Human Macrophages and Airway Epithelial Cells

Frontiers in Immunology, 2018
Lysinuric protein intolerance (LPI) is a recessively inherited aminoaciduria caused by mutations of SLC7A7, the gene encoding y+LAT1 light chain of system y+L for cationic amino acid transport. The pathogenesis of LPI is still unknown.
Bianca Maria Rotoli, Amelia Barilli, Rossana Visigalli, Filippo Ingoglia, Marco Milioli, Maria Di Lascia, Benedetta Riccardi, Paola Puccini, Valeria Dall’Asta   +8 more
doaj   +1 more source

Important differences in cationic amino acid transport by lysosomal system c and system y+ of the human fibroblast.

Journal of Biological Chemistry, 1987
Superficial similarities led us to extend our designation for the transport of the plasma membrane for cationic amino acids, y+, to the lysosomal system also serving for such amino acids. Further study on the purified lysosomes of human skin fibroblasts leads us now to redesignate the lysosomal system as c (for cationic), rather than y+, to emphasize ...
R L, Pisoni, J G, Thoene, R M, Lemons, H N, Christensen   +3 more
openaire   +2 more sources

Cationic amino acid transport across the blood-brain barrier is mediated exclusively by system y⁺

American Journal of Physiology-Endocrinology and Metabolism, 2006
Cationic amino acid (CAA) transport is brought about by two families of proteins that are found in various tissues: Cat (CAA transporter), referred to as system y+, and Bat [broad-scope amino acid (AA) transporter], which comprises systems b0,+, B0,+, and y+L.
Robyn L, O'Kane, Juan R, Viña, Ian, Simpson, Rosa, Zaragozá, Ashwini, Mokashi, Richard A, Hawkins   +5 more
openaire   +3 more sources

Obligatory amino acid exchange via systems bo,+-like and y+L-like. A tertiary active transport mechanism for renal reabsorption of cystine and dibasic amino acids.

The Journal of biological chemistry, 1996
Mutations in the rBAT gene cause type I cystinuria, a common inherited aminoaciduria of cystine and dibasic amino acids due to their defective renal and intestinal reabsorption (Calonge, M. J., Gasparini, P., Chillarón, J., Chillón, M., Gallucci, M., Rousaud, F., Zelante, L., Testar, X., Dallapiccola, B., Di Silverio, F., Barceló, P., Estivill, X ...
J, Chillarón, R, Estévez, C, Mora, C A, Wagner, H, Suessbrich, F, Lang, J L, Gelpí, X, Testar, A E, Busch, A, Zorzano, M, Palacín   +10 more
openaire   +3 more sources

Cloning and functional expression of a cDNA from rat jejunal epithelium encoding a protein (4F2hc) with system y+L amino acid transport activity [PDF]

Biochemical Journal, 1998
Two different protein families, designated CAT (cationic amino acid transporter) and BAT (broad-specificity amino acid transporter) mediate the plasma membrane transport of cationic amino acids in animal cells. CAT transporters have 12-14 transmembrane domains and are selective for cationic amino acids.
S Y, Yao, W R, Muzyka, J F, Elliott, C I, Cheeseman, J D, Young   +4 more
openaire   +2 more sources

The Binding Specificity of Amino Acid Transport System y + L in Human Erythrocytes is Altered by Monovalent Cations

Journal of Membrane Biology, 1996
System y+L is a broad-scope amino acid transporter which binds and translocates cationic and neutral amino acids. Na+ replacement with K+ does not affect lysine transport, but markedly decreases the affinity of the transporter for L-leucine and L-glutamine.
Angelo,, Irarrázabal,, Devés, Rosa
openaire   +3 more sources

Protein pyrophosphorylation by inositol pyrophosphates — detection, function, and regulation

FEBS Letters, EarlyView.
Protein pyrophosphorylation is an unusual signaling mechanism that was discovered two decades ago. It can be driven by inositol pyrophosphate messengers and influences various cellular processes. Herein, we summarize the research progress and challenges of this field, covering pathways found to be regulated by this posttranslational modification as ...
Sarah Lampe, Tanmay Kumar Mohanty, Rashna Bhandari, Dorothea Fiedler   +3 more
wiley   +1 more source

Inhibition of endothelial cell amino acid transport System y+ by arginine analogs that inhibit nitric oxide synthase

Biochimica et Biophysica Acta (BBA) - Biomembranes, 1997
A variety of N omega-monosubstituted L-arginine analogs are established inhibitors of nitric oxide synthase; in all cases, initial binding is competitive with the substrate L-arginine. The efficacy of such compounds in vivo will depend on their transport into the relevant nitric oxide synthase-containing cells; in fact, inhibition may actually be ...
McDonald, Kelly K, Rouhani, Riaz, Handlogten, Mary E, Block, Edward R, Griffith, Owen W, Allison, R.Donald, Kilberg, Michael S   +6 more
openaire   +2 more sources

The planar cell polarity protein Vangl2 interacts with the PDZ‐domains of Scribble but not with a unique PDZ‐like domain in Inturned

FEBS Letters, EarlyView.
Structural and biochemical characterisations show that the planar cell polarity (PCP) protein Inturned harbours a unique PDZ‐like domain that does not bind canonical PDZ‐binding motifs (PBMs) like that of another PCP protein Vangl2. In contrast, the apical‐basal polarity protein Scribble contains four PDZ domains that bind Vangl2, but one PDZ domain ...
Stephan Wilmes, Jan Brysch, Carmen Gelze, Lilli Meier, Daniel Kümmel   +4 more
wiley   +1 more source

Characterization of blood-brain barrier L-arginine uptake using in situ brain perfusions in a female mouse model

Fluids and Barriers of the CNS
Background L-arginine is a critical determinant of central nervous system (CNS) function through nitric oxide (NO) production. Its uptake from plasma into brain is dependent on carrier-mediated transport across the blood-brain barrier (BBB).
Olivia C. Milam, Cullen P. Wolford, Geoffrey L. Pecar, Joshua J. Applegate, Maxine E. Casto, Dominic J. Gabriele, Austin S. Nestor, Paul R. Lockman   +7 more
doaj   +1 more source