Uptake of L-proline by Histoplasma capsulatum

1976 ◽  
Vol 22 (8) ◽  
pp. 1188-1190 ◽  
Author(s):  
Nina Dabrowa ◽  
Dexter H. Howard
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Active Transport ◽  
Transport System ◽  
Histoplasma Capsulatum ◽  
Yeast Cells ◽  
Side Chain ◽  
Simple Diffusion ◽  
Aliphatic Side Chain ◽  
Active Transport System

The uptake and incorporation of L-proline by yeast cells of the dimorphic zoopathogen Histoplasma capsulatum were studied. The amino acid was assimilated in at least two ways: by an active transport system with a Km of 1.7 × 10−5 M and by simple diffusion. The active transport system was stereospecific and severely restricted to neutral aliphatic side-chain amino acids. Certain analogues inhibited L-proline uptake and prevented incorporation of the amino acid into cellular constituents. The inhibition of L-proline uptake by L-leucine was competitive. Since L-leucine and L-proline are seemingly transported by a system with similarcharacteristics, it must be concluded, as originally postulated, that the buckled ring of L-proline, in solution, acts as an aliphatic side chain and that this cyclic amino acid is transported by a system more or less specific for amino acids with neutral aliphatic side chains.

Specificity of the transport system for neutral amino acids in the hamster intestine

1962 ◽  
Vol 202 (5) ◽  
pp. 919-925 ◽  
Author(s):  
Edmund C. C. Lin ◽  
Hiroshi Hagihira ◽  
T. Hastings Wilson
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Transport System ◽  
Side Chain ◽  
Carboxyl Group ◽  
Amino Group ◽  
Methyl Group ◽  
Neutral Amino Acids ◽  
Active Transport System ◽  
Everted Sacs

The specificity of the active transport system for neutral amino acids has been studied with everted sacs of hamster intestine. Amino acids with modifications or replacements of the carboxyl, amino, or α-hydrogen groups were poorly transported and were poor inhibitors of the transport of other l-amino acids. The carboxyl group must remain free, the amino group must not be in the tertiary or quaternary state, and the α-hydrogen can not be replaced by a methyl group without serious effect on the transport rate. It was concluded that the l-amino acids were distinguished from the d-isomers by the interaction of the carrier with the carboxyl group, the amino group, and the α-hydrogen. The side chain of the amino acid must be nonpolar but there is relatively little restriction on its structure.

Specificity of L-Alanine Transport in the Spine Epithelium of Paracentrotus Lividus (Echinoidea)

1978 ◽  
Vol 58 (2) ◽  
pp. 425-440 ◽  
Author(s):  
M. E. de Burgh
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Active Transport ◽  
Marine Invertebrates ◽  
Paracentrotus Lividus ◽  
Arenicola Marina ◽  
Nereis Virens ◽  
Alanine Transport ◽  
Active Transport System ◽  
Digestive Glands

In many marine invertebrates the presence of an active transport system for the epithelial absorption of amino acids has been conclusively demonstrated (Stephens, 1968. 1972; West, de Burgh & Jeal, 1977). It has been observed by several authors that inhibition of uptake of a given amino acid can occur in the presence of other amino acids, in a manner analogous to that observed in vertebrate gut absorption systems. Some examples are the work of Chapman & Taylor (1969) on whole Nereis virens, Ferguson (1968) on the digestive glands of Echinaster spinulosus, Ferguson (1971) on whole asteroids, Bamford & Stewart (1973 a, b) on Arenicola marina gut, and Bamford & McCrea (1975) on the gill of Cerastoderma edule.

Construction of Bacterial Cells with an Active Transport System for Unnatural Amino Acids

2019 ◽  
Vol 8 (5) ◽  
pp. 1195-1203 ◽  
Author(s):  
Wooseok Ko ◽  
Rahul Kumar ◽  
Sanggil Kim ◽  
Hyun Soo Lee
Keyword(s):  
Amino Acids ◽  
Active Transport ◽  
Transport System ◽  
Unnatural Amino Acids ◽  
Bacterial Cells ◽  
Active Transport System

Some Observations On Platelet Amino Acid Transport Systems

1981 ◽  
Author(s):  
U T Yardimci ◽  
A Özbilen ◽  
O N Ulutin
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Active Transport ◽  
Amino Acid Transport ◽  
Acid Group ◽  
Transport Systems ◽  
Acid Transport ◽  
Amino Acid Group ◽  
Active Transport System ◽  
Group Transport

We have studied the transport systems for amino acids in platelets. Na+/K+ dependent active transport systems were found to be responsible for the transport of amino acids through the platelet membrane (Km’s being at uM ranges). We have also isolated the binding proteins for amino acids from platelet membranes as the carriers involved in these active transport systems by cold osmotic shock procedure. Each amino acid besides being transported by a specific active transport system may be subject to transport by group amino acid transport systems.Group amino acid transport systems are classified by countertransport experiments as follows: Neutral amino acid group transport systems: IA: glycine, alanine, serine, threonine IB: valine, leucine, isoleucine, serine,threonine IC: cysteine, methionine, proline Basic amino acid group transport systems: lie: lysine IIB: histidine, arginine Acidic amino acid group transport systems: III A: Aspartic acid, glutamic acid Aromatic amino acid group transport systems: IVC: Phenylalanine,tyrosine, histidine, proline.

scholarly journals STRUCTURAL DETERMINANTS REQUIRED FOR IDENTIFICATION OF ACC TRANSPORT-RELATED MEMBRANE PROTEINS

HortScience ◽  
1995 ◽  
Vol 30 (2) ◽  
pp. 190c-190
Author(s):  
Robert A. Saftner
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Membrane Proteins ◽  
Transport System ◽  
Ethylene Biosynthesis ◽  
Side Chain ◽  
Structural Determinants ◽  
Amino Acid Analogs ◽  
Photoaffinity Probes ◽  
Kinetics Of

The ethylene precursor, 1 -aminocyclopropane- 1 -carboxylic acid (ACC), is actively transported across the tonoplast of plant cells, impacting cellular compartmentation of ACC and ethylene biosynthesis. To identify potential photoaffinity probes for identifying ACC transport-related membrane proteins, the effects of over 70 ACC and other amino acid analogs on ACC uptake into isolated maize vacuoles were investigated. Only relatively nonpolar, neutral amino acid stereoisomers of L-configuration were strong inhibitors of ACC transport. Group additions, substitutions, or deletions at the carboxyl, (x-amino and the Pro-(R) methylene, or hydrogen moieties essentially eliminated transport inhibition, whereas side-chain substitutions remained antagonistic. The kinetics of ACC and neutral L-amino acid analogs tested were competitive. The results indicate that the ACC transport system can be classified as a neutral L-amino acid carrier having a relatively high affinity for ACC and other nonpolar amino acids. The results also suggest that the carrier interacts with the carboxyl, alpha-amino, and Pro-(R) groups and the side chain of substrate amino acids. Based on these findings, potential photoaffinity probes of the ACC transport system have been identified.

On the structural organization of biological pumps and channels

1984 ◽  
Vol 42 ◽  
pp. 138-141
Author(s):  
G. Zampighi ◽  
M. Kreman
Keyword(s):  
Active Transport ◽  
Transport System ◽  
Plasma Membranes ◽  
Transport Proteins ◽  
Molecular Organization ◽  
Passive Transport ◽  
Concentration Gradients ◽  
Cell Functions ◽  
Natural Concentration ◽  
Active Transport System

The plasma membranes of most animal cells contain transport proteins which function to provide passageways for the transported species across essentially impermeable lipid bilayers. The channel is a passive transport system which allows the movement of ions and low molecular weight molecules along their concentration gradients. The pump is an active transport system and can translocate cations against their natural concentration gradients. The actions and interplay of these two kinds of transport proteins control crucial cell functions such as active transport, excitability and cell communication. In this paper, we will describe and compare several features of the molecular organization of pumps and channels. As an example of an active transport system, we will discuss the structure of the sodium and potassium ion-activated triphosphatase [(Na+ +K+)-ATPase] and as an example of a passive transport system, the communicating channel of gap junctions and lens junctions.

scholarly journals Actions of external hypertonic urea, ADH, and theophylline on transcellular and extracellular solute permeabilities in frog skin.

1975 ◽  
Vol 65 (5) ◽  
pp. 599-615 ◽  
Author(s):  
L J Mandel
Keyword(s):  
Linear Relationship ◽  
Active Transport ◽  
Transport System ◽  
Frog Skin ◽  
Open Circuit Potential ◽  
Open Circuit ◽  
Solute Permeability ◽  
Parallel Lines ◽  
Paracellular Pathways ◽  
Active Transport System

Increases in transepithelial solute permeability were elicited in the frog skin with external hypertonic urea, theophylline, and vasopressin (ADH). In external hypertonic urea, which is known to increase the permeability of the extracellular (paracellular) pathway, the unidirectional transepithelial fluxes of Na (passive), K, Cl, and urea increased substantially while preserving a linear relationship to each other. The same linear relationship was also observed for the passive Na and urea fluxes in regular Ringer and under stimulation with ADH or 10 mM theophylline, indicating that their permeation pathway was extracellular. A linear relationship between Cl and urea fluxes could be demonstrated if the skins were separated according to their open circuit potentials; parallel lines were obtained with increasing intercepts on the Cl axis as the open circuit potential decreased. The slopes of the Cl vs. urea lines were not different from that obtained in external hypertonic urea, indicating that this relationship described the extracellular movement of Cl. The intercept on the ordinate was interpreted as the contribution from the transcellular Cl movement. In the presence of 0.5 mM theophylline or 10 mU/ml of ADH, mainly the transcellular movement of Cl increased, whereas 10 mM theophylline caused increases in both transcellular and extracellular Cl fluxes. These and other data were interpreted in terms of a possible intracellular control of the theophylline-induced increase in extracellular fluxes. The changes in passive solute permeability were shown to be independent of active transport. The responses of the active transport system, the transcellular and paracellular pathways to theophylline and ADH could be explained in terms of the different resulting concentrations of cyclic 3'-5'-AMP produced by each of these substances in the tissue.

The immunosuppressant FK506 inhibits amino acid import in Saccharomyces cerevisiae

1993 ◽  
Vol 13 (8) ◽  
pp. 5010-5019 ◽  
Author(s):  
J Heitman ◽  
A Koller ◽  
J Kunz ◽  
R Henriquez ◽  
A Schmidt ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Amino Acids ◽  
Amino Acid ◽  
Cyclosporin A ◽  
Secretory Pathway ◽  
Yeast Cells ◽  
Amino Acid Transporters ◽  
Yeast Saccharomyces Cerevisiae ◽  
Eukaryotic Microorganisms

The immunosuppressants cyclosporin A, FK506, and rapamycin inhibit growth of unicellular eukaryotic microorganisms and also block activation of T lymphocytes from multicellular eukaryotes. In vitro, these compounds bind and inhibit two different types of peptidyl-prolyl cis-trans isomerases. Cyclosporin A binds cyclophilins, whereas FK506 and rapamycin bind FK506-binding proteins (FKBPs). Cyclophilins and FKBPs are ubiquitous, abundant, and targeted to multiple cellular compartments, and they may fold proteins in vivo. Previously, a 12-kDa cytoplasmic FKBP was shown to be only one of at least two FK506-sensitive targets in the yeast Saccharomyces cerevisiae. We find that a second FK506-sensitive target is required for amino acid import. Amino acid-auxotrophic yeast strains (trp1 his4 leu2) are FK506 sensitive, whereas prototrophic strains (TRP1 his4 leu2, trp1 HIS4 leu2, and trp1 his4 LEU2) are FK506 resistant. Amino acids added exogenously to the growth medium mitigate FK506 toxicity. FK506 induces GCN4 expression, which is normally induced by amino acid starvation. FK506 inhibits transport of tryptophan, histidine, and leucine into yeast cells. Lastly, several genes encoding proteins involved in amino acid import or biosynthesis confer FK506 resistance. These findings demonstrate that FK506 inhibits amino acid import in yeast cells, most likely by inhibiting amino acid transporters. Amino acid transporters are integral membrane proteins which import extracellular amino acids and constitute a protein family sharing 30 to 35% identity, including eight invariant prolines. Thus, the second FK506-sensitive target in yeast cells may be a proline isomerase that plays a role in folding amino acid transporters during transit through the secretory pathway.

scholarly journals Amino acids whose intracellular levels change most during aging alter chronological lifespan of fission yeast

2020 ◽  
Author(s):  
Charalampos Rallis ◽  
Michael Mülleder ◽  
Graeme Smith ◽  
Yan Zi Au ◽  
Markus Ralser ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Fission Yeast ◽  
Yeast Cells ◽  
Total Amino Acid ◽  
Wild Type ◽  
Chronological Lifespan ◽  
Biomarkers Of Aging ◽  
Concentration Changes ◽  
Amino Acid Levels

AbstractAmino acid deprivation or supplementation can affect cellular and organismal lifespan, but we know little about the role of concentration changes in free, intracellular amino acids during aging. Here, we determine free amino-acid levels during chronological aging of non-dividing fission yeast cells. We compare wild-type with long-lived mutant cells that lack the Pka1 protein of the protein kinase A signalling pathway. In wild-type cells, total amino-acid levels decrease during aging, but much less so in pka1 mutants. Two amino acids strongly change as a function of age: glutamine decreases, especially in wild-type cells, while aspartate increases, especially in pka1 mutants. Supplementation of glutamine is sufficient to extend the chronological lifespan of wild-type but not of pka1Δ cells. Supplementation of aspartate, on the other hand, shortens the lifespan of pka1Δ but not of wild-type cells. Our results raise the possibility that certain amino acids are biomarkers of aging, and their concentrations during aging can promote or limit cellular lifespan.

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