Search results for "Transporter"

In response to the paper 'High-protein diet: A barrier to the nephroprotective effects of sodium-glucose co-transporter-2 inhibitors?'

2020

We agree with the paper recently published in your journal regarding the relationship between a high‐protein diet and the possible neutral effect of sodium‐glucose co‐transporter‐2 inhibitors (SGLT2inh),1 but wish to discuss certain nuances.

Impact of Glucose-Lowering Medications on Cardiovascular and Metabolic Risk in Type 2 Diabetes

2020

Type 2 Diabetes Mellitus (T2DM) is associated with a high risk of atherosclerotic cardiovascular (CV) disease. Among the well-known pathophysiologic factors, crucial roles are played by endothelial dysfunction (caused by oxidative stress and inflammation hyperglycemia-linked), increased activity of nuclear factor kB, altered macrophage polarization, and reduced synthesis of resident endothelial progenitor cells. As consequence, a potentially rapid progression of the atherosclerotic disease with a higher propensity to unstable plaque is arguable, finally leading to significantly increased cardiovascular mortality. Main managements are focused on both prevention and early diagnosis, by target…

Membrane Transport of l-Arginine and Cationic Amino Acid Analogs

2000

Publisher Summary This chapter reviews the current knowledge of the mechanisms and regulation of cationic amino acids (CAA) carrier proteins and discusses the potential involvement of each transporter in supplying L-arginine for nitric oxide biosynthesis. The CAA L-arginine, the substrate for nitric oxide synthases (NOSs), is considered a semi-essential amino acid in most mammals. Consequently, mammalian cells must be capable of exchanging CAA with the environment. The bilayer of the plasma membrane is impermeable to polar molecules, and thus, specialized carrier proteins with distinct substrate specificity transport hydrophilic solutes such as amino acids. L-arginine shares the same transp…

O44. Inhibition of CD98-associated amino acid transporters by dinitrosyl iron complexes

2008

C4-dicarboxylate metabolons: Interaction of C4-dicarboxylate transporters of Escherichia coli with cytosolic enzymes

2021

AbstractMetabolons represent the structural organization of proteins for metabolic or regulatory pathways. Here the interaction of enzymes fumarase FumB and aspartase AspA with the C4-DC transporters DcuA and DcuB of Escherichia coli was tested by a bacterial two-hybrid (BACTH) assay in situ, or by co-chromatography (mSPINE). DcuB interacted strongly with FumB and AspA, and DcuA with AspA. The fumB-dcuB and the dcuA-aspA genes encoding the respective proteins are known for their colocalization on the genome and the production of co-transcripts. The data consistently suggest the formation of DcuB/FumB, DcuB/AspA and DcuA/AspA metabolons in fumarate respiration for the uptake of L-malate, or …

CATs, a family of three distinct mammalian cationic amino acid transporters

1996

Three related mammalian carrier proteins that mediate the transport of cationic amino acids through the plasma membrane have been identified in murine and human cells (CAT for cationic amino acid transporter). Models of the CAT proteins in the membrane suggest they have 12 or 14 transmembrane domains connected by short hydrophilic loops and intracellular N- and C-termini. The transport activity of the CAT proteins is sensitive to trans-stimulation and independent of the presence of sodium ions. These features agree with the behaviour of carrier proteins mediating facilitated diffusion. The three CAT proteins, CAT-1, CAT-2A and CAT-2(B) are encoded by two different genes (CAT-1 and CAT-2). C…

Expression, regulation and function of carrier proteins for cationic amino acids.

2001

Different carrier proteins exhibiting distinct transport properties participate in cationic amino acid transport. There are sodium-independent systems, such as b+, y+, y+L and b0,+, and a sodium-dependent system B0,+, most of which have now been identified at the molecular level. In most non-epithelial cells, members of the cationic amino acid transporter (CAT) family mediating system y+ activity seem to be the major entry pathway for cationic amino acids. CAT proteins underlie complex regulation at the transcriptional, post-transcriptional and activity levels. Recent evidence indicates that individual CAT isoforms are necessary for providing the substrate for nitric oxide synthesis, for ex…

Cationic Amino Acid Transporters (CATs)

2002

When the transport properties of mCAT-1 were described in 1991, the y+ carrier and major transporter for cationic amino acids seemed to be discovered. Today, we know that there are at least three different CAT isoforms that mediate y+ activity and the family might be growing. In addition, transport systems for cationic amino acids other than y + have been described and proteins that induce the respective transport activities have been identified. Consequently, the transport of cationic amino acids appears to be a complex process involving many proteins— carriers and possibly also regulatory proteins—whose expression is cell-specific and dependent on a variety of external stimuli. The multit…

How Glutamate Is Managed by the Blood-Brain Barrier

2016

A facilitative transport system exists on the blood brain barrier (BBB) that has been tacitly assumed to be a path for glutamate entry to brain. But glutamate is a non-essential amino acid whose brain content is much greater than plasma, and studies in vivo show that glutamate does not enter brain in material quantities except in those small regions with fenestrated capillaries (circumventricular organs). The situation became understandable when luminal (blood facing) and abluminal (brain facing) membranes were isolated and studied separately. Facilitative transport of glutamate and glutamine exist only on the luminal membranes whereas Na+-dependent transport systems for glutamate, glutamin…

Allelic variants of hexose transporter Hxt3p and hexokinases Hxk1p/Hxk2p in strains ofSaccharomyces cerevisiaeand interspecies hybrids

2015

The transport of sugars across the plasma membrane is a critical step in the utilization of glucose and fructose by Saccharomyces cerevisiae during must fermentations. Variations in the molecular structure of hexose transporters and kinases may affect the ability of wine yeast strains to finish sugar fermentation, even under stressful wine conditions. In this context, we sequenced and compared genes encoding the hexose transporter Hxt3p and the kinases Hxk1p/Hxk2p of Saccharomyces strains and interspecies hybrids with different industrial usages and regional backgrounds. The Hxt3p primary structure varied in a small set of amino acids, which characterized robust yeast strains used for the p…