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1.
Arq. neuropsiquiatr ; 73(2): 140-146, 02/2015. tab, graf
Article in English | LILACS | ID: lil-741179

ABSTRACT

The objective of this article is to highlight some of the most important pioneering books specifically focused on the neurological examination and their authors. During the XIX Century, Alexander Hammond, William Gowers and Charles Mills pioneered the neurological literature, followed in the XX Century by Aloysio de Castro, Monrad-Krohn, Derek Denny-Brown, Robert Wartenberg, Gordon Holmes, and Russel DeJong. With determination and a marked sense of observation and research, they competently developed and spread the technique and art of the neurological exam.


O objetivo deste artigo é destacar alguns dos primeiros e mais importantes livros-texto interessados em difundir o ensino do exame neurológico e seus autores. Durante o século XIX, Alexander Hammond, William Gowers e Charles Mills foram pioneiros na literatura neurológica, seguidos por Aloysio de Castro, Monrad-Krohn, Derek Denny-Brown, Robert Wartenberg, Gordon Holmes e Russel DeJong no século XX. Com determinação, grande senso de observação e pesquisa, eles competentemente disseminaram a técnica e a arte de se realizar o exame neurológico.


Subject(s)
Animals , Female , Pregnancy , Betamethasone/pharmacology , Gestational Age , Glucocorticoids/pharmacology , Hydroxysteroid Dehydrogenases/analysis , Placenta/enzymology , Blotting, Northern , Blotting, Western , Fetal Blood/chemistry , Hydrocortisone/blood , Hydroxysteroid Dehydrogenases/genetics , Labor, Obstetric/physiology , Papio , RNA, Messenger/analysis
2.
Rev. bras. enferm ; 67(6): 881-885, Nov-Dec/2014.
Article in English | LILACS, BDENF | ID: lil-732816

ABSTRACT

Interdisciplinary collaboration is widely recognized and considered essential for optimizing the development of knowledge and practice. However, interdisciplinarity is commonly accepted as an unquestioned good; rarely examined as both a source of benefit as well as difficulty for nursing and other disciplines. The aim of this article is to critically examine the opportunities and challenges that interdisciplinarity can provide for research in nursing and other disciplines. Based on a North American perspective, I describe the emergence of uni-disciplinary nursing research and the knowledge exchanges that occurred between nursing and other disciplines. I discuss the rise of interdisciplinary research, outline several examples of nursing participation in interdisciplinarity, and highlight the prominent benefits and difficulties associated with interdisciplinary research. I argue that authentic collaboration is required to conduct meaningful interdisciplinary research and describe how this can be promoted.


Colaboração interdisciplinar é amplamente reconhecida e considerada essencial para a otimização do desenvolvimento do conhecimento e prática. No entanto, a interdisciplinaridade é comumente aceita como um bem inquestionável, raramente examinado tanto como uma fonte de benefícios, bem como dificuldade para a enfermagem e outras disciplinas. O objetivo deste artigo é analisar criticamente as oportunidades e desafios que a interdisciplinaridade pode oferecer para a pesquisa em enfermagem e outras disciplinas. Com base em uma perspectiva norte-americana, descreve-se o surgimento de pesquisas em enfermagem unidisciplinar e as trocas de conhecimento que ocorreram entre a enfermagem e outras disciplinas. Discute-se a ascensão da pesquisa interdisciplinar, delineiam-se vários exemplos de participação da enfermagem na interdisciplinaridade, e destacam-se os benefícios proeminentes e dificuldades associadas com a pesquisa interdisciplinar. Defende-se que a colaboração autêntica é necessária para conduzir a pesquisa interdisciplinar significativa e descreve-se como isso pode ser promovido.


La colaboración interdisciplinaria es ampliamente reconocida y considerada esencial para optimizar el desarrollo del conocimiento y la práctica. Sin embargo, la interdisciplinariedad es comúnmente aceptada como un bien incuestionable; rara vez examinada tanto como una fuente de beneficio, así como de dificultad para la enfermería y otras disciplinas. El objetivo de este artículo es examinar críticamente las oportunidades y desafíos que la interdisciplinariedad puede proporcionar para la investigación en enfermería y otras disciplinas. Sobre la base de una perspectiva norteamericana, describe-se el surgimiento de la investigación en enfermería unidisciplinaria y los intercambios de conocimientos que se produjeron entre la enfermería y otras disciplinas. Se discute el aumento de la investigación interdisciplinaria, esbozan-se varios ejemplos de la participación de enfermería en la interdisciplinariedad, y destacan-se los beneficios y las dificultades asociadas con la investigación interdisciplinaria. Argumenta-sé que se requiere auténtica colaboración para llevar a cabo la investigación interdisciplinaria significativa y describe-se la forma en que esto puede ser promovido. .


Subject(s)
Humans , Female , Catechol O-Methyltransferase/biosynthesis , /biosynthesis , Placenta/enzymology , Pregnancy/metabolism , Steroid Hydroxylases/biosynthesis , Xenobiotics/pharmacology , Butylated Hydroxyanisole/pharmacology , Carcinogens , Coumarins/pharmacology , Enzyme Induction , Naphthols/pharmacology , Pregnancy Trimester, First
3.
São Paulo med. j ; 129(6): 387-391, Dec. 2011. ilus, tab
Article in English | LILACS | ID: lil-611806

ABSTRACT

CONTEXT AND OBJECTIVE: Preeclampsia is a multi-systemic disease and one of the most frequent severe health problems during pregnancy. Binding of insulin triggers phosphorylation and activates cytoplasmic substrates such as phosphatidylinositol 3 kinase (PI3K). Phosphorylation of membrane phosphoinositide 2 (PIP2) to phosphoinositide 3 (PIP3) by PI3K starts Akt/PKB activation. Defects in phosphorylation of the insulin receptor and its substrates have an important role in insulin resistance. Studies have shown that insulin resistance is associated with preeclampsia and its pathophysiology. The aim here was to investigate insulin stimulation of the Akt/PKB pathway in the placenta, in normal and preeclampsia parturients. DESIGN AND SETTING: Cross-sectional study in a tertiary public university hospital. METHODS: Placentas were collected from 12 normal and 12 preeclampsia patients. These were stimulated and analyzed using Western blot to quantify the Akt/PKB phosphorylation. RESULTS: The insulin stimulation was confirmed through comparing the stimulated group (1.14 ± 0.10) with the non-stimulated group (0.91 ± 0.08; P < 0.001). The phosphorylation of Akt/PKB did not differ between the placenta of the normal patients (1.26 ± 0.16) and those of the preeclampsia patients (1.01 ± 0.11; P = 0.237). CONCLUSIONS: In vitro insulin stimulation of the human placenta has been well established. There was no difference in Akt/PKB phosphorylation, after stimulation with insulin, between placentas of normal and preeclampsia patients. Nevertheless, it cannot be ruled out that the Akt/PKB signaling pathway may have a role in the pathophysiology of preeclampsia, since the substrates of Akt/PKB still need to be investigated.


CONTEXTO E OBJETIVO: Pré-eclâmpsia (PE) é uma doença multissistêmica das mais frequentes e graves durante a gestação. A ligação da insulina inicia a fosforilação e ativação de substratos citoplasmáticos, tais como fosfatidil-inositol 3 quinase (PI3K). A fosforilação do fosfoinositol 2 (PIP2) da membrana em fosfoinosiltol 3 (PIP3) pela PI3K inicia a ativação da Akt/PKB. Defeitos na fosforilação do receptor de insulina e seus substratos têm papel importante na resistência à insulina. Estudos demonstraram que resistência à insulina está associada com pré-eclâmpsia e sua patofisiologia. O objetivo foi investigar a via de estimulação com insulina da Akt/PKB em placenta de parturientes normais e com pré-eclampsia. TIPO DE ESTUDO E LOCAL: Estudo do tipo transversal em um hospital universitário público de nível terciário. MÉTODOS: Vinte e quatro placentas (12 normais, 12 com PE) foram coletadas, estimuladas e analisadas por Western blot para quantificar a fosforilação da Akt/PKB. RESULTADOS: A estimulação com insulina foi confirmada comparando os grupos estimulados (1,14 ± 0,10) e não estimulados (0.91 ± 0.08; P < 0.001). A fosforilação de Akt/PKB não foi diferente na placenta de pacientes normais (1,26 ± 0,16) e com PE (1,01 ± 0,11; P = 0,237). CONCLUSÕES: A estimulação in vitro da placenta humana com insulina foi bem estabelecida. Não houve diferença na fosforilação da Akt/PKB após estimulação em placentas de pacientes normais e PE. Contudo, não é possível descartar a participação desta via de sinalização na patofisiologia da PE, uma vez que os substratos da Akt/PKB ainda precisam ser investigados.


Subject(s)
Adult , Female , Humans , Pregnancy , Insulin/pharmacology , Placenta/drug effects , Pre-Eclampsia/enzymology , Proto-Oncogene Proteins c-akt/metabolism , Blotting, Western , Case-Control Studies , Cross-Sectional Studies , Enzyme Activation , Insulin Resistance/physiology , Phosphorylation , Placenta/enzymology , Signal Transduction
4.
DMJ-Dohuk Medical Journal. 2009; 3 (2): 52-66
in English | IMEMR | ID: emr-119442

ABSTRACT

Disruption of normal placental morphology and function might correlate with several pregnancy disorders as preeclampsia and preterm labor. Many studies tried to localize placental alkaline phosphatase, and placental acid phosphatase in placentas of mothers with complicated pregnancy and try to find out whether the changes in their pattern have a direct bearing on functional and morphological integrity of the placental tissue and on the fetal growth and development. This study aims to find the difference in localization or intensity of placental alkaline phosphatase, and placental acid phosphatase in a group of preterm preeclarnpsia and in placentae of normotensive preterm ones, compared with normotensive term mothers. This study examined placentae obtained from 61 singleton pregnant women and it was performed over a period of three months started form 1[st] April 2008 till 30 [th] June 2008 and conducted at Al-Batool Maternity Teaching hospital in Mosul city in northern Iraq. Smokers, Rh negative mothers, and cases of diabetes mellitus were excluded. The study sample was divided into 3 groups after recording of medical reports of the history and clinical examination and accurate assignment of gestational age. Group 1: This group consisted of 25 normotensive women who delivered at term [between 38 and 42 weeks' gestation]. Group2: This group consisted of 23 normotensive women who delivered before 37 weeks' gestation spontaneously. Group3: This group consisted of 13 women with positive history of blood pressure equal to 140/90 mm Hg after 20 weeks of gestation and proteinuria 300 mg/ 24 hrs or [3]1+ dipstick and delivered before 37 weeks' gestation. All placental sections of the three study groups were stained using alkaline phosphatase stain [Gomori's method-cobalt] and acid phosphatase stain [Gomori's method-lead] and submitted for light microscopic examination in Laboratory of Postgraduate Studies at the Department of Anatomy, Histology and Embryology in Mosul College of Medicine. This study revealed that most sections obtained from normotensive term group showed discrete localization of acid phosphatase P-ACP in all cellular elements of the placenta. Placental sections obtained from cases of preterm preeclampsia [group 3] and those obtained from spontaneous preterm labor [group 2] showed more intense acid phosphatase activity which was arranged in focal distribution. On the other hand, most sections obtained from normotensive term group revealed that alkaline phosphatase P-ALP was localized mostly in the syncytiotrophoblast, moderate reaction of the maternal deciduas, while villous stroma showed weak activity. Sections obtained from placentas of group 2 and group 3 women showed that very strong alkaline phosphatase activity expressed in syncytiotrophoblast, moderate to intense alkaline phosphatase activity in villous stroma and maternal deciduas. The present study demonstrated that the placental tissue in cases of preterm preeclampsia and in cases of spontaneous prematurity exhibits changes in the activity patterns


Subject(s)
Humans , Female , Placenta/enzymology , Phosphoric Monoester Hydrolases , Pregnancy Complications , Pregnancy , Infant, Premature , Alkaline Phosphatase , Acid Phosphatase
5.
J Vector Borne Dis ; 2007 Jun; 44(2): 116-21
Article in English | IMSEAR | ID: sea-117916

ABSTRACT

BACKGROUND & OBJECTIVES: Early gestational malaria is more deleterious than late gestational infection. Still the pathophysiology of maternofoetal organ--the placenta in malaria remains almost unexplored during early gestation. Present study dealing with oxidoreductases in early gestational placenta during maternal malarial infection of Plasmodium cynomolgi bastianellii in rhesus monkeys was anticipated to provide a better insight into the functional impairment of this organ leading to foetal abnormalities. METHODS: Three control and four experimental monkeys (Macaca mulatta) were quarantined for one month prior to experimentation. Experimental monkeys at 2- 2 1/2 months of gestation were inoculated with P. cynomolgi bastianellii. On attaining first peak of parasitaemia the placentae were collected from anesthetised animals. The snap-frozen, cryostat sections were subjected to histochemical localisation for 3 (or 17) beta-hydroxysteroid dehydrogenase (beta-HSD) [3 (or 17) beta-hydroxysteroid: NAD (P+) oxidoreductase, EC 1.1.1.51 hydroxysteroid dehydrogenases] and NADPH-tetrazolium reductase [NADPH: (acceptor) oxidoreductase, EC 1.6.99.1 NADPH-TR]. Comparative microscopy of control and malaria infected placental sections was performed and analysed. RESULTS: A localised decrease in both the enzymes was observed in syncytiotrophoblast layer of malaria infected monkey placenta. The areas showing morphological damage of syncytiotrophoblast were also depicting gross reduction in NADPH-TR activity. INTERPRETATION & CONCLUSION: The altered enzymatic activities [3 (or 17) beta-HSD and NADPH-TR] in malaria infected early gestational monkey placenta have been discussed in the light of placental function. It could be concluded by present studies that these alterations would affect the cellular metabolism especially steroidogenesis and detoxification process which in turn would affect the normal development of the foetus as well as maintenance of gestation.


Subject(s)
Animals , Disease Models, Animal , Female , Macaca mulatta , Malaria/enzymology , Oxidoreductases/metabolism , Placenta/enzymology , Plasmodium cynomolgi/pathogenicity , Pregnancy , Pregnancy Complications, Parasitic/enzymology
6.
Journal of Sabzevar School of Medical Sciences. 2007; 14 (3): 159-164
in Persian | IMEMR | ID: emr-83571

ABSTRACT

Alkaline Phosphatase [EC: 3.1.3.1] is synthesized by kidney, liver, bone, Intestine and placenta. This enzyme is a glycoprotein and dimmer 4 Zn+2 and Mn+2 in each dimmer. It hydrolyzes mono ester phosphate to organic compound and phosphate_in alkaline medium. The purpose of this research is to compare this enzyme with placental alkaline phosphatase. Human Molehydatiform was purified by folds of precipitation of bybutanol, acetone, Amoniumm sulphate, Sephadex G200, affinity chromatography and preparative electrophoresis. Human Molehydatiform was purified 611.8 times. We obtained specific activity, optimum temperature and optimum Ph equaling to 611.8 U/mg, 40 centigrade degrees and 10.4 respectively. Purified Human Molehydatiform Alkalie phosphatase is different from Human placental Alkaline phosphatase due to optimum pH and optimum temperature


Subject(s)
Humans , Alkaline Phosphatase/chemistry , Alkaline Phosphatase/physiology , Placenta/enzymology , Pregnancy , Hydatidiform Mole/enzymology
7.
J Vector Borne Dis ; 2005 Dec; 42(4): 135-40
Article in English | IMSEAR | ID: sea-118024

ABSTRACT

BACKGROUND & OBJECTIVES: Early gestational malaria is found to be more fatal than late gestational infection but the pathophysiology of early gestational placenta, the maternofoetal organ responsible for maintenance of pregnancy, remains unexplored. Present study dealing with hydrolytic enzymes in early gestational placenta of rhesus monkeys during Plasmodium cynomolgi infection was anticipated to provide a better insight into the functional impairment of this organ during early gestational maternal malaria. METHODS: Experimental monkeys (Macaca multtta) at 2-2 1/2 months of pregnancy were inoculated with P. cynomolgi bastianelli. After attaining first peak of parasitaemia the animals were anesthetised and placentae were collected for histochemical studies. The snap-frozen, cryostat sections were subjected to histochemical reactions for acid phosphatase and alkaline phosphatase. RESULTS: The placental syncytiotrophoblast showed a loss in alkaline phosphatase activity, while the trophoblast layers and phagocytic cells of the maternal blood showed increased acid phosphatase activity during early gestational malarial infection. Morphological damage to the placental tissue whenever occurred was associated with altered Alk pase activity. INTERPRETATION & CONCLUSION: The altered distribution of Ac pase and Alk pase in malaria infected early gestational placenta has been discussed in the light of placental function. It could be concluded by present studies that these malaria induced changes in hydrolytic enzyme activities in monkey placenta have a direct bearing on functional and morphological integrity of the placental tissue. These changes are apparently responsible for early gestational foetal death and abortions as reported in literature.


Subject(s)
Acid Phosphatase/metabolism , Alkaline Phosphatase/metabolism , Animals , Disease Models, Animal , Female , Immunohistochemistry , Macaca mulatta , Malaria/complications , Placenta/enzymology , Plasmodium cynomolgi , Pregnancy , Pregnancy Complications, Parasitic/enzymology
8.
Article in English | IMSEAR | ID: sea-37711

ABSTRACT

Chemoprevention is considered a rational strategy for dietary approaches to prevention of cancer. Multiple lines of evidence suggest that many of our dietary principles are able to intervene in the multistage carcinogenesis process and phytic acid (inositol hexaphosphate, IP6), a phytochemical present in a variety of plant species, has been shown to prevent various cancers, including those of the mammary gland, colon and liver. However, the mechanism of chemoprevention by IP6 has not been fully elucidated. In the present study, we examined the effects of inositol and/or IP6 supplementation on rat hepatocarcinogenesis initiated by diethylnitrosamine (DEN) and promoted by partial hepatectomy (PH). Supplementation with either inositol or IP6, or their combination, starting one week prior to administration of DEN, resulted in a significant decrease in both the area and the number of placental glutathione S-transferase positive (GST-P+) foci, a preneoplastic marker for DEN-initiated hepatocarcinogenesis. The administration of inositol and/or IP6 in drinking water caused marked enhancement in the glutathione S-transferase (GST) activity. In addition, the production of thiobarbituric acid reactive substances and the catalase activity were significantly reduced in rats supplemented with inositol and /or IP6. Based on these findings, it is likely that the chemopreventive effects of inositol and/or IP6 on rat hepatocarcinogenesis initiated by DEN and promoted by PH are associated with induction of GST activity and suppression of lipid peroxidation.


Subject(s)
Administration, Oral , Analysis of Variance , Animals , Diethylnitrosamine , Glutathione Transferase/metabolism , Inositol/administration & dosage , Inositol Phosphates/administration & dosage , Liver/drug effects , Liver Neoplasms, Experimental/chemically induced , Male , Placenta/enzymology , Rats , Rats, Sprague-Dawley
9.
Rev. Soc. Bras. Med. Trop ; 38(supl.2): 87-91, 2005. graf, ilus
Article in Spanish | LILACS | ID: lil-444167

ABSTRACT

Trypanosoma cruzi induces changes in the protein pattern of human placenta syncytiotrophoblast. Placental alkaline phosphatase (PLAP) is a glycoenzyme anchored to the membrane by a glycosyl-phosphatidylinositol molecule. PLAP activity and its presence was altered by the parasite in cultures of human placental villi and HEp2 cells with T.cruzi. The cells treated before the cultures with agents which affect PILAP or glycosyl-phosphatidylinositol (antibodies, PL-C, genistein, lithium) presented less parasitic invasion than the control ones. It was also observed a modification in the pattern of actine filaments of the host cells infected. We concluded that PLAP would participate in the process of T. cruzi invasion into placental syncitiotrophoblast cells, by a mechanism that involves hydrolysis of the glycosyl-phosphatidylinositol molecules, the activation of tyrosine kinase proteins, the increase of cytosolic calcium and the rearrangement of actine filaments of the host cells.


Subject(s)
Animals , Female , Humans , Pregnancy , Chagas Disease/enzymology , Alkaline Phosphatase/metabolism , Placenta/enzymology , Trypanosoma cruzi/physiology , Analysis of Variance , Cell Culture Techniques , Chagas Disease/immunology , Chagas Disease/parasitology , Alkaline Phosphatase/analysis , Glycosylphosphatidylinositols/metabolism , Immunohistochemistry , Biomarkers , Placenta/parasitology , Trophoblasts/enzymology , Trophoblasts/parasitology , Chorionic Villi/enzymology , Chorionic Villi/parasitology
10.
Experimental & Molecular Medicine ; : 160-166, 2003.
Article in English | WPRIM | ID: wpr-10316

ABSTRACT

The enzyme complex 3b-hydroxysteroid dehydrogenase/delta(5)-delta(4)-isomerase (3beta-HSD) is involved in the biosynthesis of all classes of active steroids. The expression of 3beta-HSD in human uterine endometrium during the menstrual cycle and decidua was examined in an effort to understand its role during ova implantation. 3beta-HSD was weakly expressed in the glandular epithelium of the proliferative phase and moderately expressed in the glandular epithelium of secretory phase of the endometrium. In the decidua of the ectopic pregnancy, 3beta-HSD was strongly expressed. The human uterine endometrial 3beta-HSD was identified as being the same type as the placental 3beta-HSD by RT-PCR and sequence analysis. In addition to the expression of 3beta-HSD, P450scc was expressed in the decidua of the ectopic pregnancy. These results suggest that pregnenolone might be synthesized from cholesterol by P450scc de novo and then, it is converted to progesterone by 3beta-HSD in the uterine endometrium. The data implies that the endometrial 3beta-HSD can use not only the out-coming pregnenolone from the adrenal gland but also the self- made pregnenolone to produce progesterone. The de novo synthesis of progesterone in the endometrium might be a crucial factor for implantation and maintenance of pregnancy.


Subject(s)
Female , Humans , Pregnancy , Cholesterol/chemistry , Cholesterol Side-Chain Cleavage Enzyme/biosynthesis , Decidua/enzymology , Endometrium/enzymology , Gene Expression/physiology , Menstrual Cycle/physiology , Multienzyme Complexes/biosynthesis , Placenta/enzymology , Pregnenolone/biosynthesis , Progesterone/biosynthesis , Progesterone Reductase/biosynthesis , Steroid Isomerases/biosynthesis
12.
Rev. Fac. Cienc. Méd. (Córdoba) ; 57(1): 115-9, 2000. ilus, tab
Article in Spanish | LILACS | ID: lil-279415

ABSTRACT

En el plasma humano pueden encontrarse las isoenzimas ósea, hepática e intestinal de fosfatasa alcalina (EC 3.1.3.1). En el plasma de mujeres embarazadas, durante el último trimestre de gestación puede encontrarse otra isoenzima, la fosfatasa alcalina placentaria. Además, en extractos butanólicos de tejido placentario se ha encontrado una isoenzima unida a membrana, la fosfatasa alcalina placentaria de alto peso molecular. En suero de mujeres embarazadas se ha determinado la actividad de fosfatasa alcalina placentaria soluble pero, hasta el momento, no se ha detectado la presencia de la isoenzima de alto peso molecular. En nuestro laboratorio hemos desarrollado un método que permite la detección de fosfatasa alcalina de alto peso molecular en el pellet de plasma centrifugado a 100.000xg. Utilizando el mencionado método hemos determinado la actividad de fosfatasa alcalina placentaria de alto peso molecular en plasma de mujeres embarazadas durante el último trimestre de gestación


Subject(s)
Humans , Female , Pregnancy , Alkaline Phosphatase/blood , Placenta/enzymology , Pregnancy/blood , Alkaline Phosphatase/isolation & purification , Alkaline Phosphatase/metabolism , Molecular Weight , Pregnancy Trimester, Third
14.
Experimental & Molecular Medicine ; : 30-35, 1999.
Article in English | WPRIM | ID: wpr-56321

ABSTRACT

C-Terminal carboxyl methylation of a human placental 23 kDa protein catalyzed by membrane-associated methyltransferase has been investigated. The 23 kDa protein substrate methylated was partially purified by DEAE-Sephacel, hydroxyapatite and Sephadex G-100 gel filtration chromatographies. The substrate protein was eluted on Sephadex G-100 gel filtration chromatography as a protein of about 29 kDa. In the absence of Mg2+, the methylation was stimulated by guanine nucleotides (GTP, GDP and GTPgammaS), but in the presence of Mg2+, only GTPgammaS stimulated the methylation which was similar to the effect on the G25K/rhoGDI complex. AFC, an inhibitor of C-terminal carboxyl methylation, inhibited the methylation of human placental 23 kDa protein. These results suggests that the substrate is a small G protein different from the G25K and is methylated on C-terminal isoprenylated cysteine residue. This was also confirmed by vapor phase analysis. The methylated substrate protein was redistributed to membrane after in vitro methylation, suggesting that the methylation of this protein is important for the redistribution of the 23 kDa small G protein for its putative role in intracellular signaling.


Subject(s)
Female , Humans , Pregnancy , Cysteine/metabolism , GTP-Binding Proteins/metabolism , Guanine Nucleotides/pharmacology , Methylation , Placenta/metabolism , Placenta/enzymology , Pregnancy Proteins/metabolism , Protein Methyltransferases/metabolism
15.
Indian J Cancer ; 1997 Jun; 34(2): 73-6
Article in English | IMSEAR | ID: sea-50952

ABSTRACT

Placental alkaline phosphatase (PLAP) has been shown to be a reliable tumor marker in the management of patients with seminoma. Radioimmunoassay (RIA) and Enzyme linked immunoassay (ELISA) procedures were compared for PLAP levels in serum of seminoma patients. The statistical analysis showed excellent correlationship between the two. It is evident from the results that performance of ELISA in terms of sensitivity specificity, precision, accuracy and reproducibility is equivalent to or better than RIA.


Subject(s)
Alkaline Phosphatase/analysis , Case-Control Studies , Enzyme-Linked Immunosorbent Assay , Female , Humans , Male , Placenta/enzymology , Pregnancy , Radioimmunoassay , Seminoma/enzymology , Testicular Neoplasms/enzymology , Biomarkers, Tumor/blood
16.
Rev. Fac. Cienc. Méd. (Córdoba) ; 55(1/2): 5-8, 1997. tab, graf
Article in English | LILACS | ID: lil-231895

ABSTRACT

The Kinetic properties of plasma placental alkaline phosphatase patients with Chagas' disease were studied. When Cl2 Mg was used as activator the same increase of activity (17-20 per cent) was found in the chagasic and non chagasic groups. The enzyme was not inhibited by F-ion in any of the groups. No significant differences were detected between the two groups (chagasic and non chagasic) when the enzyme was treated with inhibitors such as EDTA and L-phenylamine. However, when the CN- ion was used, the enzyme of the normal pregnant women followed a Michaelian curve, whereas in the chagasic group a sigmoideal plot was observed. Thus, the Hill coefficient was 1.1 for the normal group and over 1.5 for the chagasic.


Subject(s)
Adult , Female , Humans , Pregnancy , Alkaline Phosphatase/blood , Chagas Disease/enzymology , Edetic Acid , Placenta/enzymology , Pregnancy Complications, Parasitic/enzymology , Alkaline Phosphatase/drug effects , Alkaline Phosphatase/metabolism , Chagas Disease/blood , Edetic Acid , Enzyme Inhibitors/pharmacology , Enzyme Reactivators/pharmacology , Pregnancy Complications, Parasitic/blood , Pregnancy Trimester, Third
17.
Braz. j. med. biol. res ; 29(5): 589-97, May 1996. tab, graf
Article in English | LILACS | ID: lil-182541

ABSTRACT

ATP-diphosphohydrolase (apyrase, EC 3.6.1.5) has both ATPase and ADPase activity that are stimulated by bivalent metais, with Ca2+ being the most effective. The possible physiological function of this enzyme, associated with placental and renal microvilli, is related to the extracellular metabolism of nucleotides. A comparison of the biochemical properties of human placenta and rat kidney apyrase is presented, showing similaiities in Mr, bivalent metal stimulation, nucleotide nonspecificity, insensitivity towards specifjc ATPase inhibitors, and lack of essential sulfhydryl and aliphatic hydroxyl groups. We describe the treatment of membrane preparations from both tissues with different detergents and the isoelectric focusing of the solubilized proteins to partially purify apyrase. An ectoenzyme localization is assigned both in microvillus membranes and in the vasculature on the basis of organ perfusion experiments with nucleotides in the presence of antibodies. Placental and kidney microvillus membranes inhibited ADP-induced platelet aggregation, in agreement with an extracellular role. Initial studies on enzyme regulation suggested the existence of at least two types of modulatory proteins: an activating protein in the cytosol of both tissues, and an inhibitory protein associated with placental microsomes. Possible hormonal regulation was investigated in kidneys using in vivo estradiol treatment, but only slight changes in total apyrase activity were observed.


Subject(s)
Humans , Animals , Rats , Apyrase/metabolism , Kidney/enzymology , Placenta/enzymology , Platelet Aggregation , Apyrase/chemistry , Estradiol/pharmacology
18.
An. Fac. Med. (Perú) ; 57(4): 265-7, 1996. tab
Article in Spanish | LILACS | ID: lil-208451

ABSTRACT

La preeclampsia es una de las patologías más frecuente en el embarazo. La placenta juega un papel importanteen el desarrollo del cuadro. En el presente trabajo realizamos un estudio de las actividades de dos enzimas reguladoras [fosfofructoquinasa I (C.E.2.7.1.11) y glucosa 6-P deshidrogenasa (C.E.1.1.149)] en el metabolismo de los carbohidratos en el tejido placentario normal y en el preeclámptico a término. Se halla una marcada disminución de las actividades de ambas enzinas en los tejidos patológicos. Se discute los posibles mecanismos.


Subject(s)
Humans , Male , Female , Placenta/enzymology , Placenta/metabolism , Pre-Eclampsia/diagnosis , Pre-Eclampsia/enzymology , Pre-Eclampsia/therapy , Glucose Dehydrogenases , Glucose Dehydrogenases/therapeutic use , Maternal-Fetal Exchange
19.
Indian J Exp Biol ; 1994 Nov; 32(11): 800-3
Article in English | IMSEAR | ID: sea-60374

ABSTRACT

Role of fatty acid binding proteins (FABPs) in modulating inhibition of human placental malate dehydrogenase by palmitoyl-CoA and oleate has been studied. Activity of human placental cytosolic malate dehydrogenase is detected throughout the gestation, showing a peak at midgestation (20-25 weeks). Inhibition (50%) of the enzyme activity is obtained by 20 microM palmitoyl-CoA or 35 microM oleate. FABPs enhance the activity of malate dehydrogenase in absence of palmitoyl-CoA or oleate and also protect against palmitoyl-CoA or oleate inhibition. Such a modulatory effect of FABP may be due to the binding of long chain fatty acyl-CoA or fatty acid rather than a direct effect of FABPs on the enzyme.


Subject(s)
Carrier Proteins/pharmacology , Fatty Acid-Binding Proteins , Fatty Acids/pharmacology , Female , Gestational Age , Humans , Malate Dehydrogenase/metabolism , Neoplasm Proteins , Placenta/enzymology , Pregnancy , Tumor Suppressor Proteins
20.
Medicentro ; 10(1): 59-68, ene.-jun. 1994. tab, ilus
Article in Spanish | LILACS | ID: lil-168730

ABSTRACT

Se estudio "in vitro" la actividad enzimatica de la beta galactosidasa acida, glucosa 6 fosfatasa y succinico deshidrogenasa para determinar si se afectaban en presencia de aspirina, cafeina y diazepam en homogeneizado total de placenta humana. Se utilizaron dosis de 10, 50 y 100 /ml de cada farmaco, y se determino si existia diferencia significativa en ausencia de los farmacos y en presencia de los mismos mediante la prueba t de Student para series apareadas. En todas las concentraciones de los tres farmacos la beta galactosidasa acida presento un aumento altamente significativo. La glucosa 6 fosfatasa y la succinico deshidrogenasa tuvieron una disminucion altamente significativa, aunque en esta ultima la disminucion fue solosignificativa con la dosis mas pequena. Se concluye que la presencia de aspirina, cafeina y diazepam produce alteraciones en la actividad de las enzimas estudiadas que pueden provocar trastornos del metabolismo placentario


Subject(s)
Humans , Female , Aspirin/pharmacokinetics , Caffeine/pharmacokinetics , Diazepam/pharmacokinetics , Galactosidases/drug effects , Glucose-6-Phosphatase/drug effects , In Vitro Techniques , Placenta/enzymology , Placenta/metabolism , Succinate Dehydrogenase/drug effects
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