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PubMed1997

Influence of ischemia and reperfusion on the course of brain tissue swelling and blood-brain barrier permeability in a rodent model of transient focal cerebral ischemia.

Brain swelling is a serious complication associated with focal ischemia in stroke and severe head injury. Experimentally, reperfusion following focal cerebral ischemia exacerbates the level of brain swelling. In this study, the permeability of the blood-brain barrier has been investigated as a possible cause of reperfusion-related acute brain swelling. Blood-brain barrier disruption was investigated using Evans Blue dye and [14C]aminoisobutyric acid autoradiography in a rodent model of reversible middle cerebral artery (MCA) occlusion. Acute brain swelling and cerebral blood flow (CBF) during ischemia and reperfusion were analyzed from double-label CBF autoradiograms after application of the potent vasoconstrictor peptide endothelin-1 to the MCA. Ischemia was apparent within ipsilateral MCA territory, 5 min after endothelin-1 application to the exposed artery. Reperfusion, examined at 30 min and 1, 2, and 4 h, was gradual but incomplete within this time frame in the core of middle cerebral artery territory and associated with significant brain swelling. Ipsilateral hemispheric swelling increased over time to a maximum (>5%) at 1-2 h after endothelin-1 but was not associated with a significant increase in the ipsilateral transfer constant for [14C]aminoisobutyric acid over this time frame. These results indicate that endothelin-1 induced focal cerebral ischemia is associated with an acute but reversible hemispheric swelling during the early phase of reperfusion which is not associated with a disruption of the blood-brain barrier.

Aminoisobutyric Acids↗
PubMed1979

Amino acid transport in normal and Rous sarcoma virus-transformed chicken embryo fibroblasts.

A study was made of the transport of a variety of amino acids by uninfected and Rous sarcoma virus-infected chicken embryo fibroblasts. Following a period of amino acid starvation, transformed, but not normal cells, showed increased levels of transport for alpha-aminoisobutyric acid, proline and alanine, three amino acids which are transported primarily by the A transport system. There was no starvation-induced increase in the transport of leucine, phenylalanine, lysine, or cycloleucine. In the absence of starvation, normal and transformed cells exhibited comparable rates of amino acid transport. Cycloheximide was able to block the increase in uptake. The enhanced uptake was characterized by an increase in Vmax for transport and little change in Km. The data demonstrate that an alteration in the regulation of the A amino acid transport system is an early event in malignant transformation by Rous sarcoma virus. However, since this alteration in made manifest only following a period of starvation, our findings suggest that increased amino acid uptake does not play a role in generating the other manifestations of the transformed state seen in cell culture.

Amino Acids↗
PubMed1987

Effects of succinylacetone on amino acid uptake in the rat kidney.

Infants with hereditary tyrosinemia also have a renal Fanconi syndrome and excrete succinylacetone (SA). We have studied the effects of SA on rat renal tubular amino acid transport in vivo and in vitro using isolated renal tubules. Injection of SA produces increased clearance of several amino acids in the intact animal. In vitro SA causes a reversible inhibition of alpha-aminoisobutyric acid uptake, resulting from depressed low- and high-affinity transport systems. Addition of glutamate, succinate, or glucose, alone or in combination, did not restore transport. These observations suggest the usefulness of SA in the production of a physiologic animal model for the study of the human Fanconi syndrome.

Amino Acids↗
PubMed1991

Effects of cyclic adenosine 3',5'-monophosphate on amino acid transport and incorporation into protein in the rat aorta.

To assess the effects of cyclic AMP on amino acid transport and incorporation into aortic tissue protein, rat aortic rings were incubated with the cyclic AMP analog, N6-monobutyryl cyclic AMP (MBcAMP), the phosphodiesterase inhibitor, 3-isobutyl-1-methylxanthine (MIX), and radiolabeled amino acids. Subsequently, the aortic rings were homogenized in 5% trichloroacetic acid (TCA) and processed for liquid scintillation counting. Radioactivity present in the TCA supernatant following centrifugation was used to estimate amino acid transport. TCA-precipitable radioactivity was used as a measure of amino acid incorporation into protein. MBcAMP induced an increase in the uptake of [3H]alpha-aminoisobutyric acid into aortic rings and an increase in the incorporation of radiolabeled proline and leucine into TCA-precipitable protein. Similar effects were observed with low concentrations of MIX (0.025-0.25 mM); however, at higher concentrations of MIX, there was an attenuation of the effect or frank inhibition. Maximum stimulation of transport was observed within 90-120 min of the addition of MIX or MBcAMP to the incubation medium, whereas the effect on amino acid incorporation was not detectable until after 12 h of exposure to MIX or MBcAMP. The effects of cyclic AMP on transport were observed in both the tunica media and the tunica adventitia, whereas the effects on amino acid incorporation into protein were observed only in the tunica media. These data are consistent with a possible role for cyclic AMP in promoting changes in the tunica media that could lead to the development of vascular hypertrophy.

1-Methyl-3-isobutylxanthine↗
PubMed1988

Metformin enhances certain insulin actions in cultured rat hepatoma cells.

The effect of the oral antidiabetic agent metformin on insulin regulation of glycogen metabolism, tyrosine-aminotransferase activity, and [1-14C]aminoisobutyric acid uptake was studied in H4IIE cultured rat hepatoma cells. Metformin enhanced both basal (from 0.213 +/- 0.016 to 0.262 +/- 0.024 nmol/mg protein, p less than 0.01) and insulin stimulated [3H] glucose incorporation into glycogen in a time-dependent and dose-dependent manner. A small effect of metformin was seen at 1 mumol/l, and its greatest effects were obtained at 10 mumol/l. At the same concentrations, metformin did not influence basal tyrosine-aminotransferase activity but it potentiated insulin stimulated tyrosine-aminotransferase activity (+29.2 +/- 1.4%, p less than 0.01) and prevented the loss of tyrosine-aminotransferase responsiveness to insulin in H4IIE cells desensitised by a previous exposure to insulin. In contrast, metformin had no effect on basal or insulin-stimulated [1-14C]aminoisobutyric acid uptake. Over the concentrations of metformin that enhanced insulin action in H4IIE cells, the drug had no significant effect on insulin binding to its receptor. These studies suggest, therefore, that metformin may influence cellular metabolism by potentiating certain insulin actions through mechanisms that may be beyond insulin receptor binding.

Aminoisobutyric Acids↗
PubMed1995

A novel proline, glycine: K+ symporter in midgut brush-border membrane vesicles from larval Manduca sexta.

Alkali-cation-dependent uptake of proline and glycine into brush-border membrane vesicles from the midgut of the larval tobacco hornworm Manduca sexta was investigated using rapid filtration assays. Uptake of both amino acids was by electrophoretic symport, with K+ being the favored cation at pH 10. Counterflow accumulation of proline was elicited by glycine and vice versa, suggesting that the two amino acids are transported by a common symporter, which we designate the pro, gly: K+ symporter. L-alpha-Aminoisobutyric acid was the only other amino acid that elicited the accumulation of both proline and glycine. D-Proline was not symported; L-proline, glycine and L-alpha-aminoisobutyric acid appear to be the only substrates of the pro, gly: K+ symporter. Neutral amino acids with relatively short sidechains elicit glycine accumulation, suggesting that glycine may also be symported by the well-established neutral amino acid system. Since proline does not utilize the broad-spectrum, neutral system, its symport appears to be exclusively through the pro, gly: K+ symporter. Proline symport was found mainly in posterior midgut vesicles, suggesting that the pro, gly: K+ symporter may be localized in this region of the midgut.

Animals↗
PubMed1987

Measurement of insulin-like growth factor I (IGF-I) responsiveness of fibroblasts of children with short stature: identification of a patient with IGF-I resistance.

Somatomedins are important mediators of GH action on skeletal tissues. A possible cause of growth failure, therefore, is impaired somatomedin (Sm) responsiveness of the target tissues. To investigate Sm responsiveness, we studied fibroblasts from 11 normal-statured individuals and 9 patients with short stature. Five of the short patients had normal serum GH and normal or increased Sm levels and, therefore, are considered possibly to be Sm resistant. The other short patients include 2 with Laron-type dwarfism and 2 with GH resistance of undefined type. As a measure of Sm responsiveness, we determined the ability of insulin-like growth factor I (IGF-I; Sm-C) to stimulate uptake of [3H]alpha-aminoisobutyric acid by fibroblasts. The mean ED50 of the 11 normal fibroblast cell lines was 3.2 +/- 0.9 (+/- SD) ng/ml. Fibroblasts from 8 of the 9 short-statured patients had ED50 values within the normal range. This included 2 fibroblast lines isolated from children with Laron-type dwarfism. Fibroblasts from 1 patient, however, were significantly less sensitive to IGF-I in 9 separate assays, with an ED50 of 10.7 +/- 1.8 ng/ml. Fibroblasts from the mother of the patient had an ED50 of 5.0 +/- 1.4 ng/ml, and fibroblasts from the father had an ED50 of 4.3 +/- 0.7 ng/ml, both above the normal mean. Measurements of [125I]IGF-I binding by suspended fibroblasts from this patient and her parents failed to demonstrate significant abnormalities in either the number of binding sites or the affinity of binding. We conclude that the ability of IGF-I to stimulate [3H]alpha-aminoisobutyric acid uptake by human fibroblasts provides a useful method of identifying short children with Sm resistance. Of five patients with clinical evidence of possible Sm resistance, fibroblasts from one consistently were hyporesponsive to IGF-I. Cells from two patients with Laron-type dwarfism were normally responsive to IGF-I.

Aminoisobutyric Acids↗
PubMed2000

Transplacental pharmacokinetics and fetal distribution of 2', 3'-didehydro-3'-deoxythymidine (d4T) and its metabolites in late-term rhesus macaques.

BACKGROUND: The overall goal of human immunodeficiency virus (HIV) therapy during pregnancy is to maintain maternal health and reduce the probability of vertical transmission during gestation and delivery, while keeping toxicity risks low. Azidothymidine (AZT) is currently recommended for pregnant women infected with HIV; however, many pregnant women are unable to tolerate AZT because of toxicity. In the present study, the placental transfer and fetal accumulation of the anti-HIV compound 2',3'-didehydro-3'-deoxythymidine (d4T) and its active (triphosphorylated) and inactive (thymine and beta-aminoisobutyric acid) metabolites were examined at steady state in late-term rhesus macaques. METHODS: On the day of the hysterotomy, the mother was administered an intravenous loading dose of d4T, followed by a 3-hr steady-state intravenous infusion that also included [(3)H]d4T as a tracer. After 3 hr of infusion, the fetus was delivered by cesarean section under halothane/N(2)O anesthesia. Plasma, amniotic fluid, and tissues were analyzed for d4T and its inactive metabolites by HPLC; tissue samples were analyzed for d4T and active (phosphorylated) metabolites by strong anion-exchange HPLC. RESULTS: Maternal steady-state plasma concentrations of d4T were 1-2 microg/ml, with a fetal-to-maternal plasma ratio of 0.85 +/- 0.09. The fetal tissue distribution of radioactivity was highest in the kidney and lowest in the brain. D4T, thymine, and beta-aminoisobutyric acid were detected in all fetal tissues examined. CONCLUSIONS: Our data indicate that d4T readily crosses the placenta and is present in the fetus as parent compound or its inactive metabolites after maternal infusion. Although fetal plasma concentrations of d4T were similar to clinical d4T concentrations, no phosphorylated metabolites were detected. Teratology 62:93-99, 2000. Published 2000 Wiley-Liss, Inc.

Aminoisobutyric Acids↗
PubMed1978

Osmotic effects of membrane permeability in a marine bacterium.

When cells of Alteromonas haloplanktis 214 (ATCC 19855) were preloaded with alpha-[(14)C]aminoisobutyric acid or the K(+) in the cells was labeled with (42)K by incubation in a buffered salt solution containing 0.05 M MgSO(4), 0.01 M KCl, and 0.3 M NaCl, the cells retained their radioactivity when resuspended in the same salt solution. When NaCl was omitted from the solution, 80 to 90% of the radioactivity was lost from the cells. Cells suspended at intermediate concentrations of NaCl also lost radioactivity. New steady-state levels of the intracellular solutes were established within 15 s of suspending the cells; the percentage of radioactivity retained at each level decreased proportionately as the osmolality of the NaCl in the suspending solution decreased. With minor variations in effectiveness, MgCl(2), LiCl, and sucrose could substitute for NaCl on an equiosmolal basis for the retention of radioactivity by the cells. KCl, RbCl, and CsCl were appreciably less effective as replacements for NaCl, particularly when their osmolalities in the suspending solutions were low. The amount of alpha-[(14)C]aminoisobutyric acid taken up by the cells at the steady-state level increased to a maximum as the NaCl concentration in the suspending medium increased to 0.3 M. At suboptimal levels of NaCl, either LiCl or sucrose could substitute for NaCl in increasing the steady-state levels. The results obtained indicate that the porosity of the cytoplasmic membrane of this organism is determined by the difference between the osmotic pressure of the cytoplasm and the suspending medium. The lesser effectiveness of K(+), Rb(+), and Cs(+) than Na(+), Li, or Mg(2+) in permitting the retention of solutes by the cells is attributed to the greater penetrability of the hydrated ions of the former group through the dilated pores of a stretched cytoplasmic membrane.

Aminoisobutyric Acids↗
PubMed1983

[Effect of insulin on amino acid transport and protein synthesis in the skeletal muscle of the normal mouse and the insulin-resistant mouse].

The uptake of alpha-aminoisobutyric acid (AIB) and protein synthesis were studied in soleus muscles isolated from lean and goldthioglucose-obese mice (GTG-obese mice) in both basal and insulin-stimulated conditions. Insulin stimulated AIB influx by increasing the apparent Vmax of transport; this effect was partially dependent on new protein synthesis. In muscles of GTG-obese mice, the basal (i.e. non-insulin-stimulated) influx of AIB was decreased. Furthermore, the effect of insulin in obese mice was altered in two ways; the absolute value of the maximally insulin-stimulated AIB influx was lower than in the muscles of lean controls, and the dose response of insulin-stimulated AIB influx was shifted to the right (half-maximally effective concentration: EC50 approximately equal to 1.7 nM) compared to that observed in the muscles of lean animals (EC50 approximately equal to 0.7 nM). On the contrary, protein synthesis was similar in control and GTG-obese mice in both basal and insulin-stimulated conditions. It is concluded that in the muscles of obese mice a) amino acid transport per se is altered, b) the sensitivity of this process to the stimulatory effect of insulin is markedly diminished and c) protein synthesis is unchanged.

Amino Acids↗
PubMed1980

Inhibition of protein synthesis in intact HeLa cells by Shigella dysenteriae 1 toxin.

Shiga toxin purified to near homogeneity from cell lysates of Shigella dysenteriae 1 inhibited protein and deoxyribonucle acid syntheses in intact HeLa cells. Inhibition was dependent on toxin concentration and time of incubation. A minimal latent period of 30 min was observed with saturating doses of toxin. Ribonucleic acid synthesis, uptake of alpha-aminoisobutyric acid, and maintenance of intracellular K+ concentrations were not affected until well after maximal inhibition of protein and deoxyribonucleic acid syntheses. The inhibitory effect of toxin was sensitive to heat inactivation and was prevented by antibody neutralization. Several cytotoxic components were separated by polyacrylamide gel electrophoresis of the purified toxin preparations; all inhibited protein and deoxyribonucleic acid syntheses equally.

Aminoisobutyric Acids↗
PubMed1982

Distribution of two model amino acids from cerebrospinal fluid to brain and blood.

Ventriculocisternal perfusions of anesthetized rabbits were performed for 1-3 h with solutions containing radioactively labeled alpha-aminoisobutyric acid (AIB), cycloleucine (CYCL), and sucrose. Serial brain samples were taken at the conclusion of the perfusion period and assayed for radioactivity. Tissue concentration profiles were constructed from these data; tissue distribution spaces and diffusion coefficients (Dt) plus brain capillary transfer constants were estimated from the profiles. The Dt of sucrose was somewhat larger at 1 h than at 2 and 3 h. Tissue distribution spaces of 300-400% were found with AIB after 3 h. Inclusion of 5 mM AIB in the perfusate produced markedly lower tracer AIB spaces. The tissue distribution spaces of CYCL ranged from 100 to 400% and depended on the concentration of CYCL in the perfusate. A brain-to-blood transfer half time of 7.5 min was measured for CYCL. These findings demonstrate that sizable cellular uptake of CYCL and AIB occurs, that these processes are concentration dependent, and that the rates of influx and efflux across brain capillaries are similar.

Amino Acids↗
PubMed1987

Effect of exogenous gangliosides on amino acid uptake and Na+, K+-ATPase activity in superior cervical and nodose ganglia of rats.

The effects of some gangliosides on active uptake of nonmetabolizable alpha-aminoisobutyric acid (AIB) and Na+, K+-ATPase and Ca2+, Mg2+-ATPase activities in superior cervical ganglia (SCG) and nodose ganglia (NG) excised from adult rats were examined during aerobic incubation at 37 degrees C for 2 h. In NG, amino acid uptake was greatly accelerated with the addition of galactosyl-N-acetylgalactosaminyl-[N-acetylneuraminyl]-galactosylgluc osyl ceramide (GM1) (85%) and also with N-acetylgalactosaminyl-[N-acetylneuraminyl]-galactosylglucosyl ceramide (GM2) or [N-acetylneuraminyl]-galactosyl-N-acetylgalactosaminyl-[N-acetyl- neuraminyl]-galactosylglucosyl ceramide (GD1a) (43% each) compared with a nonaddition control at a 5 nM concentration. Under identical conditions, Na+, K+-ATPase activity was strongly stimulated with GM1 (180%) and GD1a (93%), whereas Ca2+, Mg2+-ATPase activity showed no change. In SCG, on the other hand, AIB uptake was apparently inhibited (-27%) by addition of GM1, with a slight decrease in Na+, K+-ATPase but no change in Ca2+, Mg2+-ATPase activity in the tissue. Both asialo-GM1, in which N-acetylneuraminic acid is deficient, and Forssman glycolipid, which is not present in nervous tissue, failed to produce any significant increase in both SCG and NG not only in amino acid uptake, but also in Na+, K+-ATPase activity. A kinetic study of active AIB uptake showed that GM1 ganglioside produced an increase in Km with no change in Vmax in SCG, whereas it caused a decrease in Km with a slight increase in Vmax in NG. Treatment of NG and SCG with neuraminidase from Vibrio cholerae, an enzyme that split off sialic acid from polysialoganglioside, leaving GM1 intact, caused little inhibition of the amino acid uptake.(ABSTRACT TRUNCATED AT 250 WORDS)

Amino Acids↗
PubMed1982

Inhibition of placental amino acid uptake in rats following acute and chronic ethanol exposure.

The effects of acute and chronic maternal ethanol consumption on in vitro placental uptake of alpha-aminoisobutyric acid (AIB), cycloleucine, L-alanine (Ala), L-leucine (Leu), and L-lysine (Lys) were determined. Ethanol (4 g/kg. po) administered 2 hr prior to sacrifice, reduced (p less than 0.05) placental villous net uptake of cycloleucine and Ala by 29%. Prior chronic ethanol consumption depressed (p less than 0.05) placental uptake of AIB (38%), cycloleucine (45%), Ala (35%), Leu (25%), and Lys (34%). In vitro exposure of previously untreated villous fragments for 2 hr to 2 mg/ml of ethanol reduced (p less than 0.05) the net uptake of AIB and cycloleucine by 24% and 31%, respectively, whereas the minimum concentration of acetaldehyde required to cause a significant inhibition was 310 microM for AIB and 465 microM for cycloleucine. Ethanol (3 mg/ml) had no effect on AIB or cycloleucine net uptake if sodium was omitted from the incubation media. The efflux of AIB (10(-6)M) and cycloleucine (10(-6)M) from villous tissue was unaffected (p less than 0.05) by either ethanol (3 mg/ml) or acetaldehyde (600 microM) and obeyed first order kinetics. It was concluded that acute, and especially chronic, maternal ethanol consumption can depress the placental uptake of a variety of amino acids in the rat and, in the acute setting, the effect was on a sodium-dependent system involved in amino acid influx into placental cells.

Acetaldehyde↗
PubMed1996

Uptake of neutral alpha- and beta-amino acids by human proximal tubular cells.

The transport characteristics of amino acids in primary cell cultures from the proximal tubule of human adults (AHKE cells) were examined, using alpha-aminoisobutyric acid (AIB) and beta-alanine as representatives of alpha- and beta-amino acids, respectively. The Na(+)-gradient dependent influx of AIB occurred by a single, saturable transport system, whereas the Na(+)-gradient dependent uptake data for beta-alanine could be described in terms of two-independent transport components as well as one-transport one-leak model with identical kinetic constants for the high-affinity system. Competition experiments revealed that all the neutral amino acids tested reduced the uptake of AIB, whereas there was no effect of taurine, L-aspartic acid, and L-arginine. By contrast, the influx of beta-alanine was only drastically reduced by beta-amino acids, whereas the inhibition by neutral alpha-amino acids was relatively low. Nor did L-arginine and L-aspartic acid affect the uptake of beta-alanine into AHKE cells. Comparison with the results obtained for normal (NHKE) and immortalized (IHKE) embryonic cells suggested an unaltered expression of the types of transport carriers for neutral alpha- and beta-amino acids in the embryonic and AHKE cells. However, the uptake capacity of the above-mentioned transport proteins was relatively smaller in the embryonic kidney compared with the adult human kidney, which may explain, at least partly, the phenomenon of physiologic amino aciduria in neonates.

Adult↗
PubMed1992

Characterization of sodium-dependent amino acid transport activity during liver regeneration.

Liver regeneration occurs after removal of or damage to a portion of the liver; it leads to restoration of the original liver mass. The activities of three sodium-dependent amino acid transporters--system A, system N and system ASC--were determined during a 5-day period of liver regeneration in the rat. Seventy-percent hepatectomy or laparotomy was performed in pairs of rats; these rats' livers were removed at different time points after surgery. Transport activity was determined through measurement of the Na(+)-dependent uptake of tritiated amino acids by isolated hepatic plasma membrane vesicles. System A activity, as measured by the Na(+)-dependent uptake of 2-aminoisobutyric acid, is increased in the regenerating liver 2 to 24 hr after surgery compared with that of controls. Kinetic analysis of 2-(methylamino)isobutyric acid uptake showed a 100% increase in the maximum velocity of system A transport in the hepatectomized animals with no change in the Michaelis constant, suggesting an increase in the number of system A transport proteins in the plasma membrane of regenerating liver. During liver regeneration, no changes were noted in the transport activities of system N and system ASC as measured by the uptake of glutamine and cysteine, respectively, in the presence of 2-(methylamino)isobutyric acid. Our work suggests that system A performs a unique role in the secondary active transport of its substrate neutral amino acids to meet the metabolic demands of regenerating liver.

Amino Acid Transport Systems↗
PubMed1983

Effects of insulin and glucagon on amino acid transport into the liver and opercular muscle of the eel in vitro.

Effects of insulin and glucagon on amino acid transport in vitro into liver slices and the opercular muscle of the eel were studied using a labeled nonmetabolizable amino acid analog, alpha-[1-14C]aminoisobutyric acid (AIB). Addition of insulin (0.1 IU/ml) to the medium increased the radioactivity in the deproteinized fractions of both the liver slices and opercular muscle, indicating an accelerated movement of this amino acid analog into these tissues. Glucagon (5 micrograms/ml) also enhanced the entry of [14C]AIB into the liver slices; however, treatment of opercular muscle with glucagon did not alter the radioactivity in the deproteinized fraction. These findings clearly indicate that the entry of amino acids into eel tissues independent of protein synthesis can be altered by insulin and glucagon.

Aminoisobutyric Acids↗
PubMed1979

Tissue resistance to insulin stimulation of amino acid uptake in acutely uremic rats.

Peripheral tissue resistance to insulin-mediated glucose uptake occurs in uremia. A similar resistance also may exist to insulin-mediated amino acid uptake. The present study examined the effect of insulin on the uptake or distribution ratios (DR) of alpha-aminoisobutyric acid (AIBA) attained in the tissues of rats made acutely uremic by bilateral nephrectomy. Both uremic and control rats concentrated equally AIBA in the gastrocnemius muscle in the absence of insulin (DR = 2.82 +/- 0.39 in controls, 2.52 +/- 0.40 in uremics). Compared to control rats, the diaphragm and liver of uremic rats, in the absence of insulin, had higher concentrations of AIBA. Insulin had the expected effect of increasing the uptake in the gastrocnemius, diaphragm, and liver of control rats but had no effect on uptake in the gastrocnemius muscle of uremic rats (DR = 5.82 +/- 0.78 in controls, 3.07 +/- 0.60 in uremics). The effect of insulin on the distribution ratio of AIBA in diaphragm and liver or uremic rats was less than it was in control rats. Uremia is associated with inhibition of insulin-mediated amino acid uptake as well as peripheral resistance to glucose utilization.

Amino Acids↗