Biomedical subjects

H Vorum

Publications and source records attributed to H Vorum.

59 records · Page 4Linked to original sources

PubMed1988

Characteristics of D-alanine transport by luminal membrane vesicles from pars convoluta and pars recta of rabbit proximal tubule.

Uptake of D-alanine against a concentration gradient has been shown to occur with isolated luminal-membrane vesicles from pars convoluta or pars recta of rabbit proximal tubule. Renal D-alanine transport systems, displaying the following characteristics, were shown: (1) In vesicles from pars convoluta, the uptake of D-alanine was mediated by both Na+-dependent and Na+-independent transport processes. It was found that an inwardly directed H+-gradient could drive the transport of D-alanine into the vesicles both in the presence and absence of Na+. Thus, in addition to Na+, the transport of D-alanine is influenced by the H+-gradient. (2) In vesicles from pars recta, the transient accumulation of D-alanine was strictly dependent on Na+, since no 'overshoot' was ever observed in the absence of Na+. Although the Na+-dependent uptake of D-alanine was stimulated at acid pH, H+ did not substitute for Na+, as it apparently does in pars convoluta, but instead potentiated the Na+ effect. (3) Addition of L-alanine to vesicle preparations, both from pars convoluta and from pars recta, specifically inhibited renal uptake of D-alanine. A comparison between the transport characteristics of D- and L-alanine indicated that these two isomers of alanine probably share common transport systems located along the proximal tubule of rabbit kidney.

Alanine↗

PubMed1988

Mechanism of transport of L-alanine by luminal-membrane vesicles from pars recta of rabbit proximal tubule.

The characteristics of renal transport of L-alanine by luminal-membrane vesicles from proximal straight tubules (pars recta) of rabbit kidney were investigated. The following picture emerges from transport studies. Two electrogenic and Na+ requiring systems confined to this region of the nephron exist for the transport of L-alanine. In addition to Na+, the transport of L-alanine was influenced by H+. However, H+ does not substitute for Na+, but instead potentiates the Na+ effect. Modification of histidyl residues of the intact luminal-membrane vesicles by diethylpyrocarbonate (DEP), completely abolished the transient renal accumulation of L-alanine. Substrate and Na+-protection experiments suggest that histidyl residues may be at or close to the active site of the L-alanine transporter in membrane vesicles from pars recta.

Alanine↗

PubMedDate not supplied

Fatty acid-binding protein from human heart localized in native and denaturing two-dimensional gels.

A group of low molecular weight fatty acid-binding cytosolic proteins, FABPc, with high abundance in heart, liver, skeletal muscle, intestine and adipose tissue, are anticipated to play a role in long-chain fatty acid metabolism in these tissues. Recently, a FABPc with Mr 15 kDa has been purified from human heart muscle and found to be present in levels 2-4% of cytosolic proteins of human heart myocytes. In the present study two-dimensional gel electrophoresis under native and denaturing conditions has been used to characterize FABPc from human heart and this protein is found to be a major protein of human heart myocytes. The pI of FABPc from human heart was found to be about 5.3 under native conditions and about 6.5 in the presence of 9 M urea.

Carrier Proteins↗

PubMedDate not supplied

Fatty acid binding to serum albumin in type I insulin-dependent diabetes mellitus.

Equilibria of binding of long-chain fatty acids to albumin in sera from type I diabetic patients and healthy adults were studied by dialysis exchange rate determinations and described by, p*, the reserve albumin concentration for binding of fatty acid, C*/p*, the total availability of fatty acids, where C* is the total concentration of non-esterified fatty acid, and L*, the fatty acid binding property of albumin, which is L* = p*/P + 0.05 C*/P, where P is the albumin concentration. Studies in samples from 81 diabetic patients and 99 healthy adults showed that availability of fatty acids increased with increasing fatty acid concentrations, equally in the two groups. Some diabetics had higher fatty acid concentrations, and thus higher fatty acid availabilities, than the normals. It is shown that the fatty acid binding property of serum albumin is individually variable, ranging about the same mean value in normal and diabetic persons but with a larger variation in the latter. The fatty acid binding property of albumin in serum, L*, and sixteen clinical parameters were measured in 42 of the 81 diabetic patients. Regression analysis indicated that L* was correlated to serum cholesterol concentration (probability of 0-hypothesis, p = 0.01) and to serum triglyceride concentration (p = 0.05). Values of L* were slightly correlated to age, age on diagnosis, duration, Body Mass Index (BMI), diastolic blood pressure, albumin excretion rate, serum creatinine concentration, and serum non-esterified fatty acid concentration with p-values varying from 0.10 to 0.50. For sex, retinopathy, hemoglobin A1c, systolic blood pressure, daily insulin dose, and blood glucose concentration no correlation to L* was found, p-values ranging from 0.56 to 0.96. Non-enzymatic glycosylation of serum albumin did not decrease binding affinity for fatty acid in vitro.

Adult↗

PubMedDate not supplied

Valproate competes with palmitate for binding to serum albumin.

Addition of sodium valproate (VPA) to a buffered solution of human serum albumin (HSA) or to serum reduces binding affinity for palmitate. A maximal pharmacologic VPA concentration, 700 microM, added to a 300-microM albumin solution, reduces the reserve albumin concentration for binding of palmitate by a factor of 0.64. One possible site model explaining these findings may be that VPA competes strongly with one among three palmitate molecules, bound to albumin with high affinity, and induces a weaker displacement of a second palmitate.

Binding, Competitive↗