scholarly journals Solubilization of lipids from hamster bile-canalicular and contiguous membranes and from human erythrocyte membranes by conjugated bile salts

1987 ◽  
Vol 242 (3) ◽  
pp. 825-834 ◽  
Author(s):  
J M Graham ◽  
T C Northfield

We have demonstrated in vitro the efficacy of the taurine-conjugated dihydroxy bile salts deoxycholate and chenodeoxycholate in solubilizing both cholesterol and phospholipid from hamster liver bile-canalicular and contiguous membranes and from human erythrocyte membrane. On the other hand, the dihydroxy bile salt ursodeoxycholate and the trihydroxy bile salt cholate solubilize much less lipid. The lipid solubilization by the four bile salts correlated well with their hydrophobicity: glycochenodeoxycolate, which is more hydrophobic than the tauro derivative, also solubilized more lipid. All the dihydroxy bile salts have a threshold concentration above which lipid solubilization increases rapidly; this correlates approximately with the critical micellar concentration. The non-micelle-forming bile salt dehydrocholate solubilized no lipid at all up to 32 mM. All the dihydroxy bile acids are much more efficient at solubilizing phospholipid than cholesterol. Cholate does not show such a pronounced discrimination. Lipid solubilization by chenodeoxycholate was essentially complete within 1 min, whereas that by cholate was linear up to 5 min. Maximal lipid solubilization with chenodeoxycholate occurred at 8-12 mM; solubilization by cholate was linear up to 32 mM. Ursodeoxycholate was the only dihydroxy bile salt which was able to solubilize phospholipid (although not cholesterol) below the critical micellar concentration. This similarity between cholate and ursodeoxycholate may reflect their ability to form a more extensive liquid-crystal system. Membrane specificity was demonstrated only inasmuch as the lower the cholesterol/phospholipid ratio in the membrane, the greater the fractional solubilization of cholesterol by bile salts, i.e. the total amount of cholesterol solubilized depended only on the bile-salt concentration. On the other hand, the total amount of phospholipid solubilized decreased with increasing cholesterol/phospholipid ratio in the membrane.

1972 ◽  
Vol 27 (03) ◽  
pp. 594-609 ◽  
Author(s):  
A. M Engel ◽  
B Alexander

SummaryCertain purified bile salts, individually or in a mixture, profoundly affect - either inhibiting or enhancing - the esterolytic activities of thrombin, trypsin, and plasmin, the clotting activity of thrombin, and caseinolysis by trypsin. They also promote SK-induced fibrinolysis and impair FI clottability. These effects are directly related to bile salt concentration but not to the critical micellar concentration.A very unusual effect was observed with deoxycholate and FI : besides inhibiting FI clottability, the salt induces spontaneous gelation. In addition, it binds strongly to the protein, as has been already reported for another plasma protein, albumin, and to a lesser degree, to alpha- and beta-globulins.Noteworthy is the fact that activation of pancreatic juice trypsinogen by thrombin also was increased by prior thrombin exposure to the salts. On the other hand, thrombin-induced platelet aggregation was slightly inhibited by the bile salt mixture, which, when added to PRP moderately inhibited the ADP-induced aggregation. No effect was observed on the conversion of F II in plasma via the thromboplastic mechanism when deoxycholate, or cholate, or glycocholate was added to the system.It is postulated that the bile salt mixture enhances SK-induced fibrinolysis by direct action, either on SK, or on the SK-activator complex, attributable to the detergent properties of the salts.The physiologic and pathologic implications of our results with respect to hemostasis and pancreatitis are discussed.


1987 ◽  
Vol 253 (6) ◽  
pp. G730-G736 ◽  
Author(s):  
R. E. Honkanen ◽  
J. S. Patton

Bile salt absorption was examined in vitro using entire small intestines from the killifish Fundulus heteroclitus. Intestines were everted over a glass rod and incubated in solutions containing 10 nM to 20 mM bile salts. After rinsing and correcting for the adherent fluid space, uptake rates and bile salt concentrations in the tissue were determined. The distal intestine contained a Na+-dependent active transport system for bile salt uptake with an apparent Vmax for taurocholate and cholate of 1.4 and 2.3 nmol.min-1.mg dry wt-1 (Km = 117 and 357 microM), respectively. At low concentrations (10 nM to 500 microM), absorption occurred almost exclusively (greater than 84%) in the distal intestine. However, at concentrations of 1 mM and above, bile salt absorption in the middle and proximal regions equaled that in the distal intestine. Thus, although an active transport system makes the distal intestine more efficient in absorbing bile salts, passive absorption appears to account for a significant amount of bile salt uptake at concentrations above the critical micellar concentration. The presence of oleic acid did not significantly affect bile salt uptake.


1974 ◽  
Vol 77 (1) ◽  
pp. 64-70 ◽  
Author(s):  
Gustav Wägar

ABSTRACT Whether the short-term regulation of thyroidal protein synthesis by TSH occurs at the transcriptional or the translational level was tested by measuring the effect of actinomycin D (act D) on the TSH-induced stimulation of L-14C-leucine incorporation into the thyroidal proteins of rats. TSH was injected 6 h before the rats were killed. The thyroid glands were then removed and incubated in vitro in the presence of L-14C-leucine for 2 h. The pronounced stimulation of leucine incorporation in the TSH-treated animals was depressed as compared with controls but still significant even when the animals had been pre-treated with 100 μg act D 24 and 7 h before sacrifice. On the other hand, act D strongly decreased incorporation of 3H-uridine into RNA. Short-term regulation of thyroidal protein synthesis by TSH appears to be partly but not wholly dependent on neosynthesis of RNA. Hence regulation may partly occur at the translation level of protein synthesis.


1987 ◽  
Vol 52 (9) ◽  
pp. 2317-2325 ◽  
Author(s):  
Jan Hlaváček ◽  
Jan Pospíšek ◽  
Jiřina Slaninová ◽  
Walter Y. Chan ◽  
Victor J. Hruby

[8-Neopentylglycine]oxytocin (II) and [8-cycloleucine]oxytocin (III) were prepared by a combination of solid-phase synthesis and fragment condensation. Both analogues exhibited decreased uterotonic potency in vitro, each being about 15-30% that of oxytocin. Analogue II also displayed similarly decreased uterotonic potency in vivo and galactogogic potency. On the other hand, analogue III exhibited almost the same potency as oxytocin in the uterotonic assay in vivo and in the galactogogic assay.


1997 ◽  
Vol 62 (11) ◽  
pp. 1804-1814 ◽  
Author(s):  
Marie Stiborová ◽  
Hana Hansíková

Tulip bulbs (Tulipa fosteriana, L.) contain peroxidases catalyzing the oxidation of the xenobiotics N-nitrosodimethylamine (NDMA) and N-nitroso-N-methylaniline (NMA). Three anionic (A1, A2, A3) and four cationic (B, C, D, E) peroxidases were purified from this tissue, partially characterized and used for kinetic studies. Demethylation of NDMA and NMA producing formaldehyde is catalyzed by one anionic (A1) and three cationic (C, D, E) peroxidases. The oxidation of NDMA by tulip peroxidases exhibits the Michaelis-Menten kinetics. The apparent Michaelis constant and the maximal velocity values for this substrate were determined. On the other hand, non-Michaelian kinetics for the NMA oxidation were observed with tulip peroxidases. The most abundant cationic peroxidase (peroxidase C) was used for detailed enzymatic studies. In addition to formation of formaldehyde, methylaniline, aniline, 4-aminophenol and phenol were found to be metabolites formed from NMA. Phenol was formed presumably by N-demethylation via a benzenediazonium ion, while methylaniline, aniline and 4-aminophenol were products of denitrosation of the substrate. The efficiencies of plant peroxidases to oxidize NDMA and NMA in vitro are compared with those of cytochromes P450 and discussed.


Blood ◽  
1978 ◽  
Vol 51 (3) ◽  
pp. 539-547 ◽  
Author(s):  
DH Chui ◽  
SK Liao ◽  
K Walker

Abstract Erythroid progenitor cells in +/+ and Sl/Sld fetal livers manifested as burst-forming units-erythroid (BFU-E) and colony-forming units- erythroid (CFU-E) were assayed in vitro during early development. The proportion of BFU-E was higher as mutant than in normal fetal livers. On the other hand, the proportion of CFU-E was less in the mutant than in the normal. These results suggest that the defect in Sl/Sld fetal hepatic erythropoiesis is expressed at the steps of differentiation that effect the transition from BFU-E to CFU-E.


1917 ◽  
Vol 25 (4) ◽  
pp. 557-580 ◽  
Author(s):  
Carroll G. Bull

Streptococci cultivated from the tonsils of thirty-two cases of poliomyelitis were used to inoculate various laboratory animals. In no case was a condition induced resembling poliomyelitis clinically or pathologically in guinea pigs, dogs, cats, rabbits, or monkeys. On the other hand, a considerable percentage of the rabbits and a smaller percentage of some of the other animals developed lesions due to streptococci. These lesions consisted of meningitis, meningo-encephalitis, abscess of the brain, arthritis, tenosynovitis, myositis, abscess of the kidney, endocarditis, pericarditis, and neuritis. No distinction in the character or frequency of the lesions could be determined between the streptococci derived from poliomyelitic patients and from other sources. Streptococci isolated from the poliomyelitic brain and spinal cord of monkeys which succumbed to inoculation with the filtered virus failed to induce in monkeys any paralysis or the characteristic histological changes of poliomyelitis. These streptococci are regarded as secondary bacterial invaders of the nervous organs. Monkeys which have recovered from infection with streptococci derived from cases of poliomyelitis are not protected from infection with the filtered virus, and their blood does not neutralize the filtered virus in vitro. We have failed to detect any etiologic or pathologic relationship between streptococci and epidemic poliomyelitis in man or true experimental poliomyelitis in the monkey.


2012 ◽  
Vol 16 (01) ◽  
pp. 114-121 ◽  
Author(s):  
Tapan K. Saha ◽  
Yutaka Yoshikawa ◽  
Hirouki Yasui ◽  
Hiromu Sakurai

We prepared [meso-tetrakis(4-carboxylatophenyl)porphyrinato]oxovanadium(IV) tetrasodium, ([VO(tcpp)]Na4), and investigated its in vitro insulin-mimetic activity and in vivo metallokinetic feature in healthy rats. The results were compared with those of previously proposed insulin-mimetic oxovanadium(IV)porphyrin complexes and oxovanadium(IV) sulphate. The in vitro insulin-mimetic activity and bioavailability of [VO(tcpp)]Na4 were considerably better than those of [meso-tetrakis (1-methylpyridinium-4-yl)porphyrinato]oxovanadium(IV)(4+) tetraperchlorate ([VO(tmpyp)](ClO4)4) and oxovanadium(IV) sulphate. On the other hand, [VO(tcpp)]Na4 and [meso-tetrakis(4-sulfonatophenyl) porphyrinato]oxidovanadate(IV)(4-)([VO(tpps)]) showed very similar in vitro insulin-mimetic activity and in vivo metallokinetic feature in healthy rats. In particular, the order of in vitro insulin-mimetic activity of the complexes was determined to be: [VO(tcpp)]Na4 ≈ [VO(tpps)] > ([VO(tmpyp)](ClO4)4 > oxovanadium(IV) sulphate.


1994 ◽  
Vol 298 (3) ◽  
pp. 599-604 ◽  
Author(s):  
E G Lee ◽  
S J Marciniak ◽  
C M MacLean ◽  
J M Edwardson

We have developed a system in which the fusion of pancreatic plasma membranes with zymogen granules can be studied in vitro. We show here that pancreatic plasma membranes fuse not only with pancreatic zymogen granules but also with parotid secretory granules. In contrast, parotid membranes fuse only with parotid granules and not with pancreatic granules. The extent of fusion is insensitive to Ca2+ for all combinations of plasma membranes and granules. Guanosine 5′-[gamma-thio]triphosphate (GTP[S]), on the other hand, stimulates fusion of pancreatic membranes with both pancreatic granules and parotid granules, but inhibits fusion between parotid membranes and parotid granules.


Sign in / Sign up

Export Citation Format

Share Document