scholarly journals Urinary excretion of isomers of biliverdin after destruction in vivo of haemoproteins and haemin

1985 ◽  
Vol 229 (2) ◽  
pp. 477-483 ◽  
Author(s):  
K Hirota ◽  
S Yamamoto ◽  
H A Itano
Keyword(s):  
Urinary Excretion ◽  
Mammalian Species ◽  
Fold Increase ◽  
The Other ◽  
Chemical Degradation ◽  
Isomeric Composition ◽  
Other Hand ◽  
Biliverdin Ix ◽  
Physiological Values

The amount and isomeric composition of urinary biliverdin in rabbits were analysed by h.p.l.c. Physiological values were maintained after the injection of haemin. On the other hand, when haemoglobins from several mammalian species were injected into rabbits, the excretion of biliverdin-IX alpha and biliverdin-IX beta were increased 6-18-fold and 32-66-fold respectively over physiological excretion. Injection of myoglobin resulted in a 44-fold increase in excretion of the IX alpha-isomer. Coupled oxidation with ascorbate of haemoglobin and myoglobin by oxygen produced mainly the IX alpha- and IX beta-isomers from haemoglobin and the IX alpha-isomer from myoglobin. The destruction of part of the haem from injected haemoproteins by non-enzymic chemical degradation would account for the observed respective increases in the excretion of biliverdin isomers. The excretion of biliverdin isomers after the injection of phenylhydrazine into rabbits was similar to that after the injection of haemoglobin.

Oxytocin analogues with non-coded amino acid residues in position 8: [8-Neopentylglycine]oxytocin and [8-cycloleucine]oxytocin

1987 ◽  
Vol 52 (9) ◽  
pp. 2317-2325 ◽  
Author(s):  
Jan Hlaváček ◽  
Jan Pospíšek ◽  
Jiřina Slaninová ◽  
Walter Y. Chan ◽  
Victor J. Hruby
Keyword(s):  
Amino Acid ◽  
Solid Phase Synthesis ◽  
Solid Phase ◽  
The Other ◽  
Amino Acid Residues ◽  
Phase Synthesis ◽  
Other Hand ◽  
Fragment Condensation

[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.

In vitro insulin-mimetic activity and in vivo metallokinetic feature of oxovanadium(IV)porphyrin complexes in healthy rats

2012 ◽  
Vol 16 (01) ◽  
pp. 114-121 ◽  
Author(s):  
Tapan K. Saha ◽  
Yutaka Yoshikawa ◽  
Hirouki Yasui ◽  
Hiromu Sakurai
Keyword(s):  
The Other ◽  
Insulin Mimetic ◽  
Other Hand ◽  
Better Than

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.

scholarly journals Seminal vesicle proteins SVS3 and SVS4 facilitate SVS2 effect on sperm capacitation

Reproduction ◽  
2016 ◽  
Vol 152 (4) ◽  
pp. 313-321 ◽  
Author(s):  
Naoya Araki ◽  
Natsuko Kawano ◽  
Woojin Kang ◽  
Kenji Miyado ◽  
Kaoru Yoshida ◽  
...  
Keyword(s):  
Seminal Vesicle ◽  
Reproductive Tract ◽  
Female Reproductive Tract ◽  
The Other ◽  
Sperm Capacitation ◽  
Other Hand ◽  
Sperm Membrane ◽  
Vesicle Secretion ◽  
Mammalian Spermatozoa

Mammalian spermatozoa acquire their fertilizing ability in the female reproductive tract (sperm capacitation). On the other hand, seminal vesicle secretion, which is a major component of seminal plasma, inhibits the initiation of sperm capacitation (capacitation inhibition) and reduces the fertility of the capacitated spermatozoa (decapacitation). There are seven major proteins involved in murine seminal vesicle secretion (SVS1-7), and we have previously shown that SVS2 acts as both a capacitation inhibitor and a decapacitation factor, and is indispensable forin vivofertilization. However, the effects of SVSs other than SVS2 on the sperm have not been elucidated. Since mouseSvs2–Svs6genes evolved by gene duplication belong to the same gene family, it is possible that SVSs other than SVS2 also have some effects on sperm capacitation. In this study, we examined the effects of SVS3 and SVS4 on sperm capacitation. Our results showed that both SVS3 and SVS4 are able to bind to spermatozoa, but SVS3 alone showed no effects on sperm capacitation. On the other hand, SVS4 acted as a capacitation inhibitor, although it did not show decapacitation abilities. Interestingly, SVS3 showed an affinity for SVS2 and it facilitated the effects of SVS2. Interaction of SVS2 and spermatozoa is mediated by the ganglioside GM1 in the sperm membrane; however, both SVS3 and SVS4 had weaker affinities for GM1 than SVS2. Therefore, we suggest that separate processes may cause capacitation inhibition and decapacitation, and SVS3 and SVS4 act on sperm capacitation cooperatively with SVS2.

scholarly journals Albumin Enhances Caspofungin Activity against Aspergillus Species by Facilitating Drug Delivery to Germinating Hyphae

2015 ◽  
Vol 60 (3) ◽  
pp. 1226-1233 ◽  
Author(s):  
Petros Ioannou ◽  
Aggeliki Andrianaki ◽  
Tonia Akoumianaki ◽  
Irene Kyrmizi ◽  
Nathaniel Albert ◽  
...  
Keyword(s):  
Drug Delivery ◽  
Cell Culture ◽  
Antifungal Agents ◽  
Fold Increase ◽  
Culture Conditions ◽  
The Other ◽  
Related Factors ◽  
Content Type

The modestin vitroactivity of echinocandins againstAspergillusimplies that host-related factors augment the action of these antifungal agentsin vivo. We found that, in contrast to the other antifungal agents (voriconazole, amphotericin B) tested, caspofungin exhibited a profound increase in activity against variousAspergillusspecies under conditions of cell culture growth, as evidenced by a ≥4-fold decrease in minimum effective concentrations (MECs) (P= 0. 0005). Importantly, the enhanced activity of caspofungin againstAspergillusspp. under cell culture conditions was strictly dependent on serum albumin and was not observed with the other two echinocandins, micafungin and anidulafungin. Of interest, fluorescently labeled albumin bound preferentially on the surface of germinatingAspergillushyphae, and this interaction was further enhanced upon treatment with caspofungin. In addition, supplementation of cell culture medium with albumin resulted in a significant, 5-fold increase in association of fluorescently labeled caspofungin withAspergillushyphae (P< 0.0001). Collectively, we found a novel synergistic interaction between albumin and caspofungin, with albumin acting as a potential carrier molecule to facilitate antifungal drug delivery toAspergillushyphae.

The Influence of 17-Oxo- and 17-Hydroxy-16,17-secoestratriene Derivatives on Estrogen Receptor

2006 ◽  
Vol 71 (4) ◽  
pp. 532-542 ◽  
Author(s):  
Suzana Jovanović-Šanta ◽  
Julijana Petrović ◽  
Marija Sakač ◽  
Zorica Žakula ◽  
Esma Isenović ◽  
...  
Keyword(s):  
Estrogen Receptor ◽  
Estrogen Receptors ◽  
Estrogenic Activity ◽  
Total Loss ◽  
The Other ◽  
Binding Parameters ◽  
Antiestrogenic Activity ◽  
Other Hand

Since many of newly synthesised D-secoestratriene derivatives showed antiestrogenic effect, with almost a total loss of estrogenic activity, we studied the effects of some of these compounds on estrogen receptors (ER), the translocation of the estrogen-ER complexes formed in presence of competing substances into the nucleus, as well as the binding of these complexes to DNA. The results of uterotrophic effects of analysed derivatives are in agreement with the influence of these compounds on activity and binding parameters of estrogen receptors. Namely, compounds that show relatively high antiestrogenic activity predominantly increase Kd and inhibit translocation to nuclei of radioactive complexes formed in their presence. On the other hand, compounds that do not significantly change binding parameters of estrogen receptors do not show antiestrogenic effect in in vivo experiments.

scholarly journals Interplay between MPIase, YidC, and PMF during Sec-independent insertion of membrane proteins

2021 ◽  
Vol 5 (1) ◽  
pp. e202101162
Author(s):  
Yuta Endo ◽  
Yuko Shimizu ◽  
Hanako Nishikawa ◽  
Katsuhiro Sawasato ◽  
Ken-ichi Nishiyama
Keyword(s):  
Membrane Proteins ◽  
Molecular Basis ◽  
Terminal Region ◽  
Integral Membrane Proteins ◽  
The Other ◽  
Other Hand ◽  
Model Protein

Integral membrane proteins with the N-out topology are inserted into membranes usually in YidC- and PMF-dependent manners. The molecular basis of the various dependencies on insertion factors is not fully understood. A model protein, Pf3-Lep, is inserted independently of both YidC and PMF, whereas the V15D mutant requires both YidC and PMF in vivo. We analyzed the mechanisms that determine the insertion factor dependency in vitro. Glycolipid MPIase was required for insertion of both proteins because MPIase depletion caused a significant defect in insertion. On the other hand, YidC depletion and PMF dissipation had no effects on Pf3-Lep insertion, whereas V15D insertion was reduced. We reconstituted (proteo)liposomes containing MPIase, YidC, and/or F0F1-ATPase. MPIase was essential for insertion of both proteins. YidC and PMF stimulated Pf3-Lep insertion as the synthesis level increased. V15D insertion was stimulated by both YidC and PMF irrespective of the synthesis level. These results indicate that charges in the N-terminal region and the synthesis level are the determinants of YidC and PMF dependencies with the interplay between MPIase, YidC, and PMF.

99mTc-Aprotinin: Comparison with 99mTc-DMSA in Normal and Diseased Kidneys

1984 ◽  
Vol 22 (01) ◽  
pp. 22-26
Author(s):  
R. Saponaro ◽  
G. Villa ◽  
F. Lunghi ◽  
C. Aprile
Keyword(s):  
Renal Function ◽  
Urinary Excretion ◽  
Kidney Failure ◽  
Clearance Rate ◽  
The Other ◽  
Blood Clearance ◽  
Liver Uptake ◽  
Other Hand ◽  
Failure Correlation

SummaryAprotinin (A) and DMSA labelled with 99mTc were compared in patients with normal (NK, n = 12) and diseased kidneys (CRF, n = 13) by means of quantitative serial scans and measurements of blood clearance and urinary excretion. Serial scans only were obtained in additional 13 patients. Scan quality in the NK patients was essentially equal: faster blood clearances, reduced urinary excretions and higher fixations of A in the target compensated for the increased liver uptake. On the other hand, the scan quality in the CRF patients was definitely superior with A, allowing detection of residual functioning parenchyma also in severe kidney failure. Correlation between the net kidney uptake 6 hrs p.i. and the separate hippuran clearance rate was better with A than with DMSA, indicating the feasibility of A in evaluating relative renal function.

Fibrinolytic Properties of Proteases Derived from Human, Dog and Rabbit Leukocytes

1963 ◽  
Vol 10 (02) ◽  
pp. 379-389 ◽  
Author(s):  
Henry Gans
Keyword(s):  
Plasminogen Activator ◽  
Proteolytic Activity ◽  
Human Cell ◽  
Fold Increase ◽  
The Other ◽  
Human Leukocytes ◽  
Plasminogen Activator Activity ◽  
Other Hand

SummaryIntact and disintegrated human, dog and rabbit leukocytes were studied for their ability to lyse fibrin. It was noted that broken-up rabbit leukocytes fail to lyse bovine or rabbit fibrin. Human and dog leukocytes, on the other hand, readily lyse bovine fibrin.Prior incubation at pH 1 and pH 8 resulted in maximally active human cell preparations. Similar results were obtained with dog cells upon prior incubation at pH 4 and pH 8. Loss of activity was noted upon prior incubation for 15 minutes at 56° C. Adsorption of human leukocytes with celite and charcoal resulted in a 2 and 21/2 fold increase in activity.The noted lysis was found to result from proteolytic activity as well as from plasminogen activator activity. The results to these studies suggest that autolysis of relatively few leukocytes will produce a rapid breakdown of considerable amounts of fibrin.

scholarly journals In vivo phosphorylation of regulatory light chain of myosin II during mitosis of cultured cells

1994 ◽  
Vol 124 (1) ◽  
pp. 129-137 ◽  
Author(s):  
Y Yamakita ◽  
S Yamashiro ◽  
F Matsumura
Keyword(s):  
Light Chain ◽  
Myosin Ii ◽  
Mitotic Arrest ◽  
Regulatory Light Chain ◽  
The Other ◽  
Other Hand ◽  
Mlc Phosphorylation ◽  
Phosphate Incorporation ◽  
Mitotic Cells

Phosphorylation of the regulatory light chain of myosin II (MLC) controls the contractility of actomyosin in nonmuscle and muscle cells. It has been reported that cdc2 phosphorylates MLC in vitro at Ser-1 or Ser-2 and Thr-9 which protein kinase C phosphorylates (Satterwhite, L. L., M. J. Lohka, K. L. Wilson, T. Y. Scherson, L. K. Cisek, J. L. Corden, and T. D. Pollard. 1992 J. Cell Biol. 118:595-605). We have examined in vivo phosphorylation of MLC during mitosis and after the release of mitotic arrest. Phosphate incorporation of MLC in mitotic cells is found to be 6-12 times greater than that in nonmitotic cells. Phosphopeptide maps have revealed that the MLC from mitotic cells is phosphorylated at Ser-1 and/or Ser-2 (Ser-1/2), but not at Thr-9. MLC is also phosphorylated to a much lesser extent at Ser-19 which myosin light chain kinase phosphorylates. On the other hand, MLC of nonmitotic cells is phosphorylated at Ser-19 but not at Ser-1/2. The extent of phosphate incorporation is doubled at 30 min after the release of mitotic arrest when some cells start cytokinesis. Phosphopeptide analyses have revealed that the phosphorylation at Ser-19 is increased 20 times, while the phosphorylation at Ser-1/2 is decreased by half. This high extent of MLC phosphorylation at Ser-19 is maintained for another 30 min and gradually decreased to near the level of interphase cells as cells complete spreading at 180 min. On the other hand, phosphorylation at Ser-1/2 is decreased to 18% at 60 min, and is practically undetectable at 180 min after the release of mitotic arrest. The stoichiometry of MLC phosphorylation has been determined by quantitation of phosphorylated and unphosphorylated forms of MLC separated on 2D gels. The molar ratio of phosphorylated MLC to total MLC is found to be 0.16 +/- 0.06 and 0.31 +/- 0.05 in interphase and mitotic cells, respectively. The ratio is increased to 0.49 +/- 0.05 at 30 min after the release of mitotic arrest. These results suggest that the change in the phosphorylation site from Ser-1/2 to Ser-19 plays an important role in signaling cytokinesis.

scholarly journals In vitro Multiplication of Iraca palm (Carludovica palmata Ruíz & Pavón)

2020 ◽  
Vol 73 (1) ◽  
pp. 9039-9046
Author(s):  
Rodrigo Alberto Hoyos Sanchez ◽  
Diego Chicaíza Finley ◽  
Juan Carlos Zambrano Arteaga
Keyword(s):  
Root Formation ◽  
The Other ◽  
Naphthaleneacetic Acid ◽  
Multiplication Rate ◽  
In Vitro Multiplication ◽  
Commercial Interest ◽  
Other Hand ◽  
Number Of Shoots

Carludovica palmata Ruíz & Pavón is a plant that belongs to the Cyclanthaceae family. Its commercial interest is related to the production of fibers for the manufacture of handicrafts, mainly the Panama hat, so it is important to study its propagation. This investigation aimed to determine the effect of 6-benzylaminopurine (BAP) in the formation of new shoots and 1-naphthaleneacetic acid (NAA) in the formation of roots, as well as the adaptation in greenhouse conditions of Carludovica palmata Ruíz & Pavón. In order to find the optimal multiplication rate, 0.5 cm length explants were planted in glass jars with 15 mL of semisolid MS with different concentrations of BAP and cultured under in vitro conditions for 90 days. The multiplication parameters in this stage were number of shoots per explant (NSE), length of shoots (LS), and length of roots (LR) as multiplication parameters. In a similar procedure, the number of roots per explant (NRE), length of roots (LR), and length of plantlets (LP) was determined using different concentrations of NAA. Finally, different substrates were evaluated for the adaptation of plantlets of C. palmata produced in vitro, under greenhouse conditions for 80 days. The highest multiplication rate (17±3 shoots per explant) was obtained with 2.0 mg L-1 of BAP. Root formation occurred efficiently in all treatments, without significant statistical differences between them. On the other hand, the use of substrate soil-t15 was the best treatment for the growth of C. palmata under greenhouse conditions. From the results obtained, it is concluded that C. palmata can be efficiently multiplied under in vitro conditions and did not present problems during the in vivo rooting process.

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