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1.
Sci Rep ; 13(1): 20464, 2023 11 22.
Artigo em Inglês | MEDLINE | ID: mdl-37993605

RESUMO

Unmet needs for contraception in India have declined over time but the rate has not been uniform among women across geographies and socio-economic strata. Identifying the characteristics of women in communities where unmet need is still high is important to devise appropriate strategies to ensure access and uptake of modern contraceptive methods. The current study examined whether there was a national decline in unmet need over time and if regional disparities exist in unmet need. Demographic variations in unmet need based on factors such as maternal age, education, religion, caste, wealth index quintile, family size, and access to antenatal care (ANC) were also documented. Our approach was to document the prevalence of total unmet need for family planning and unmet need for spacing among married Indian women and quantify variability based on socio-economic and demographic drivers within a hierarchal framework, thus providing both macro and micro perspectives. We used data from the fourth and fifth rounds of the National Family Health Survey (NFHS) collected from all the States and Union Territories (UTs) in India. Quantile regression analysis and multilevel regression techniques were used to understand the predictors for the total unmet need for family planning and the unmet need for spacing. Results show a considerable decline in the prevalence of unmet need for family planning in India from NFHS-4 to 5 (from 12.9 to 9.3%) in the last six6 years. The north-eastern states show a significant reduction in unmet need for family planning in Manipur (17.8%), Nagaland (13.5%), and followed by Sikkim (9.1%). The predictors such as years of schooling, place of residence, caste, religion, wealth quintile, number of antenatal care (ANC) visits, and children ever born have a significant association with unmet needs for family planning and spacing among married women in India. There is a significant association between years of schooling with the total unmet needs for family planning at (q25) quantiles and the unmet need for spacing at (q25, q50) quantiles. Results reveal that the demand for unmet need for spacing and limiting was the highest among the women in the age categories 15-19 (17.8%) and 20-24 (17.3%). The demand for limiting was the highest (6.8%) among Muslim women. Across wealth quantile categories, the overall unmet demand (11.4%) for spacing and limiting was the highest among the women in the lowest socioeconomic groups. We conclude that greater access to frontline health workers among young wives, and significant investment in education in general, will continue to reduce the unmet needs for family planning in India.


Assuntos
Anticoncepção , Serviços de Planejamento Familiar , Criança , Feminino , Humanos , Gravidez , Índia , Casamento , Características da Família
2.
Andrology ; 7(5): 748-757, 2019 09.
Artigo em Inglês | MEDLINE | ID: mdl-31033221

RESUMO

BACKGROUND: The epididymis is the hallmark of all vertebrate species practicing internal fertilization. While the functions of the epididymis are well documented in laboratory rodents and some domestic animals, the structure and functions of the epididymis in humans remain poorly documented. OBJECTIVES: Using human tissues obtained with the collaboration of our local organ transplantation program, the histology, cell types, and three-dimensional organization of the excurrent duct were investigated. Microarrays were performed to determine the gene expression pattern along the human epididymis. MATERIALS AND METHODS: The histology of longitudinal sections of the proximal epididymis was described, and immunohistochemistry using specific antibodies was used to characterize cell types of the efferent duct and caput epididymis epithelia. The epididymis was divided into eight segments permitting gene profiling by microarray and gene ontology analysis. RESULTS: The proximal region of the human epididymis is formed exclusively by efferent ducts. These ducts form a complex histological structure particularly at the junction of the efferent ducts and caput epididymis. The efferent ducts exhibit a specific cellular signature when compared with the adjacent epididymis tubule. Efferent duct gene expression is not segmented and is dedicated to cilium differentiation and movement. The gene expression pattern of the caput segment is homogeneous and specialized in defense and immune responses and fertilization. DISCUSSION: In murine species, the epididymis is segmented into the initial segment, caput, corpus, and cauda regions, whereas in humans, the proximal region is formed by efferent ducts. The caput tubules have their own histological organization with a well-defined gene expression pattern. The distal corpus and cauda epididymis are distinct by a limited number of differentially expressed genes. CONCLUSIONS: Knowledge of epididymis functions and structure obtained using laboratory species should be extrapolated to humans with caution.


Assuntos
Epididimo/anatomia & histologia , Epididimo/fisiologia , Epitélio/fisiologia , Diferenciação Celular/fisiologia , Epididimo/citologia , Células Epiteliais/fisiologia , Humanos , Masculino , Transcriptoma/genética
3.
Endocrinology ; 140(7): 3318-27, 1999 Jul.
Artigo em Inglês | MEDLINE | ID: mdl-10385429

RESUMO

During epididymal transit, mammalian spermatozoa acquire new surface proteins that are necessary for gamete interaction. We have previously described a 34-kDa human epididymal sperm protein, P34H, that has been shown to be involved in sperm-zona pellucida interaction. In the present study, we report the cloning and characterization of the full-length complementary DNA encoding human P34H. The predicted amino acid sequence revealed 65% identity with P26h, the hamster counterpart of the P34H. The deduced P34H amino acid sequence revealed a 71% similarity with a pig lung tetrameric carbonyl reductase, a member of the short chain dehydrogenase/ reductase family proteins. Northern blot analysis revealed that P34H messenger RNA (mRNA) was highly expressed in the human epididymis, principally in the corpus region. A single 912-bp P34H transcript was detected. In situ hybridization experiments showed that the P34H mRNA was predominantly expressed in the proximal and distal sections of the corpus epididymidis. The staining was restricted to the principal cells of the epididymal epithelium. The localization of P34H mRNA was in agreement with the appearance of P34H protein along the male reproductive tract. Western blot analysis revealed that recombinant P34H expressed by a yeast expression system, is antigenically related to the native P34H sperm protein. Based on its pattern of expression and its function in one of the key steps leading to fertilization, P34H can be considered as a marker of epididymal sperm maturation in humans.


Assuntos
Oxirredutases do Álcool , Epididimo/metabolismo , Proteínas/metabolismo , Adulto , Sequência de Aminoácidos/genética , Animais , Antígenos/imunologia , Sequência de Bases/genética , Northern Blotting , Western Blotting , Moléculas de Adesão Celular/imunologia , Moléculas de Adesão Celular/metabolismo , Cricetinae , DNA Complementar/genética , DNA Complementar/isolamento & purificação , Humanos , Hibridização In Situ , Masculino , Mesocricetus , Dados de Sequência Molecular , Proteínas/genética , Proteínas/imunologia , RNA Mensageiro/metabolismo , Proteínas Recombinantes , Desidrogenase do Álcool de Açúcar , Testículo/metabolismo
4.
Brain Res ; 923(1-2): 71-81, 2001 Dec 27.
Artigo em Inglês | MEDLINE | ID: mdl-11743974

RESUMO

Unilateral epidural applications of nickel solution to motor cortex were followed in about 1 h by contralateral forelimb myoclonus. In rats which displayed frequent myoclonal jerking during the 45-min 2-deoxyglucose (2-DG) uptake and clearing period, autoradiographic analysis showed that glucose utilization at the nickel implant site was greater in the supragranular and infragranular layers than in the granular layer (in normal cortex, activity is greatest in the granular layer), and was also greater in the substantia nigra and other subcortical centers. The same cortical and most of the subcortical changes in 2-DG uptake were also observed when metabolic activity was assessed 1 h after myoclonus had stopped, indicating that it may not have been the seizure activity itself that had altered metabolic activity, but some process engendered by the seizures - possibly a tissue response to excitotoxic damage. In fact, rats which displayed infrequent myoclonus showed negligible increases in cortical and subcortical uptake. These results do not support an earlier claim that increased glucose consumption is the metabolic signature of the interictal activity produced by seizure-inducing metals. Indeed, the findings raise the possibility that tissue damage is responsible for interictal hypermetabolism when it is observed in animal models of epilepsy.


Assuntos
Antimetabólitos/farmacocinética , Encéfalo/metabolismo , Desoxiglucose/farmacocinética , Epilepsias Mioclônicas/metabolismo , Animais , Radioisótopos de Carbono , Epilepsias Mioclônicas/induzido quimicamente , Glucose/metabolismo , Masculino , Neurotoxinas/metabolismo , Níquel , Ratos , Ratos Long-Evans , Convulsões/induzido quimicamente , Convulsões/metabolismo
5.
Epilepsy Res ; 27(1): 13-28, 1997 Apr.
Artigo em Inglês | MEDLINE | ID: mdl-9169287

RESUMO

Nine days after insertion of a pure cobalt metal rod into the visual cortex, regions of increased 2-DG uptake are observed both in relatively normal Nissl-staining tissue lying around the implant site and in the connecting dorsal lateral geniculate nucleus of the thalamus. These hypermetabolic regions have been claimed to be the metabolic 'signatures' of tissue made epileptogenic by the cobalt. The present study showed, however, that while the 'dark patches' develop following posterior cortex implants, they do not appear after anterior cortex cobalt implants. Moreover, the dark patches were not detectable after cortical implants of other seizure-inducing metals such as antimony and nickel. These new findings indicate that the dark patches occur too idiosyncratically to make them the metabolic 'signatures' of tissue made epileptic by cobalt.


Assuntos
Química Encefálica/efeitos dos fármacos , Cobalto/farmacologia , Convulsivantes/farmacologia , Desoxiglucose/metabolismo , Metais/farmacologia , Córtex Visual/fisiologia , Animais , Autorradiografia , Cobalto/administração & dosagem , Convulsivantes/administração & dosagem , Implantes de Medicamento , Masculino , Metais/administração & dosagem , Ratos , Tálamo/efeitos dos fármacos , Tálamo/metabolismo , Tálamo/patologia , Córtex Visual/efeitos dos fármacos , Córtex Visual/patologia
6.
Artigo em Francês | MEDLINE | ID: mdl-1624725

RESUMO

All babies born in a University maternity unit over a period of four months had bacteriological swabs taken in the labour ward. This was to see whether a list of criteria in the history for bacterial infection of the newborn could be relied on. The criteria were: premature rupture of the membranes (before labour had started at all), rupture of the membranes for more than 12 hours, stained liquor, prematurity, fetal tachycardia of more than 160 per minute or abnormal rhythm of the heartbeat, an Apgar score of less than 7 after 1 minute, maternal genital or urinary tract infection (not cured) in month before delivery, maternal temperature above 38 degrees C in labour. During the study there were: 570 live births of which 222 (39%) were at risk of infection according to the above list of criteria, 35 had bacterial colonies present and 4 were definitely infected. More cultures from the placenta, the gastric fluid and the skin came back positive when there was a recognised risk of infection. Both the clinical and bacteriological results show that the risk was 5.24 of colonisation when the risk of infection had been recognised. These prospective results when checked against the retrospective results already obtained in the same department, suggest that this kind of screening for infection is worthwhile without being too expensive, and one can rely on the history to screen for neonatal bacterial infection.


Assuntos
Infecções Bacterianas/epidemiologia , Anamnese/normas , Índice de Apgar , Infecções Bacterianas/etiologia , Infecções Bacterianas/microbiologia , Feminino , Sofrimento Fetal/complicações , Ruptura Prematura de Membranas Fetais/complicações , França/epidemiologia , Frequência Cardíaca Fetal , Hospitais Universitários , Humanos , Recém-Nascido , Programas de Rastreamento/normas , Trabalho de Parto Prematuro/complicações , Gravidez , Complicações Infecciosas na Gravidez , Estudos Prospectivos , Reprodutibilidade dos Testes , Fatores de Risco , Taquicardia/complicações , Infecções Urinárias/complicações
7.
Chronic Dis Inj Can ; 34(2-3): 169-70, 2014 Jul.
Artigo em Inglês, Francês | MEDLINE | ID: mdl-24991780

RESUMO

As a result of a number of factors, the treatment of insulin-dependent diabetes has moved away from using insulin of beef or pork origin to using recombinant (biosynthetic) insulin preparations. However, some people with type 1 diabetes can manage their diabetes better using animal-sourced insulin. Despite dwindling options and decreased production, animal-sourced insulin (and pork insulin in particular) is still available on the Canadian market. This communication describes the actions taken by Health Canada with respect to the availability of animal insulin.


TITRE: Communication courte -- Le rôle de l'insuline d'origine animale dans le traitement du diabète de type 1 et sa disponibilité RÉSUMÉ: En raison d'un certain nombre de facteurs, on traite désormais davantage le diabète insulinodépendant au moyen de préparations d'insuline recombinante (biosynthétique) qu'au moyen d'insuline d'origine bovine et porcine. Cependant, certaines personnes atteintes du diabète de type 1 parviennent à mieux prendre leur diabète en charge à l'aide d'insuline d'origine animale. Malgré la disponibilité de plus en plus réduite de l'insuline d'origine animale et le déclin de sa production, on peut encore s'en procurer sur le marché canadien, en particulier l'insuline porcine. Cette communication décrit les mesures prises par Santé Canada relativement à la disponibilité de l'insuline d'origine animale.


Assuntos
Diabetes Mellitus Tipo 1/tratamento farmacológico , Hipoglicemiantes/uso terapêutico , Insulina Regular de Porco/uso terapêutico , Animais , Canadá , Humanos , Hipoglicemiantes/provisão & distribuição , Insulina Regular de Porco/provisão & distribuição , Medicina Estatal , Suínos
8.
Mol Reprod Dev ; 59(4): 431-41, 2001 Aug.
Artigo em Inglês | MEDLINE | ID: mdl-11468780

RESUMO

We have previously described a hamster sperm glycoprotein, P26h, which is implicated in the cascade of events occurring during the interaction between mature spermatozoa and the oocyte's zona pellucida. The P26h is acquired on the acrosomal cap of the spermatozoon during its maturation arising within the epididymis. Lately, using a polyclonal antiserum raised against P26h, a 34 kDa protein, P34H, has been identified on the acrosomal cap of the human spermatozoon. The cloning and sequencing of the cDNA encoding P34H has revealed a 65% similarity between the P34H and P26h amino acid sequences. Considering that P26h shows total immunocontraceptive properties in the hamster, it is of relevant importance to have an animal model phylogenetically closer to the human. Using the Cynomolgus monkey, we searched for a protein autologous to the human P34H. A 31 kDa protein, the P31m, localized on the acrosomal cap of the monkey spermatozoon has been identified by a Western blot analysis and by immunohistochemical techniques using an anti-hamster P26h antiserum. Northern blot analysis showed increasing high levels of the P31m mRNA through the epididymis and at lower levels in the testis. In situ hybridization showed the presence of the P31m mRNA in the principal cells of the epididymis. The cloning and sequencing of the cDNA encoding the P31m showed a high homology of 97% identity between the P31m and P34H nucleotidic sequences. This study clearly demonstrates that the monkey P31m is the homologous protein of the hamster P26h and of the human P34H. Mol. Reprod. Dev. 59: 431-441, 2001.


Assuntos
Acrossomo/química , Macaca fascicularis/metabolismo , Sequência de Aminoácidos , Animais , Sequência de Bases , Epididimo/química , Epididimo/metabolismo , Humanos , Immunoblotting , Imuno-Histoquímica , Hibridização In Situ , Masculino , Dados de Sequência Molecular , RNA Mensageiro/genética , RNA Mensageiro/metabolismo , Alinhamento de Sequência , Testículo/química , Testículo/metabolismo , Ducto Deferente/química , Ducto Deferente/metabolismo
9.
Biol Reprod ; 65(1): 79-86, 2001 Jul.
Artigo em Inglês | MEDLINE | ID: mdl-11420226

RESUMO

P26h is a hamster sperm protein of 26 kDa that has been previously characterized as a surface protein covering the acrosome acquired during epididymal transit. P26h is involved in sperm-egg interactions. Recently, it has been shown that the P26h transcript is highly expressed in the testis, and the P26h cDNA has been cloned from a hamster testicular cDNA library. Herein we report the production of a fusion protein (maltose binding protein-P26h) with the whole P26h cDNA encoding sequence and the production of a polyclonal antiserum against it. In Western blots, this antiserum recognized both the P26h extracted from cauda epididymal spermatozoa and the MBP-P26h. We also determined the age of appearance of P26h and which germ cell types express P26h mRNA and its translational product. Northern blots and in situ hybridization analysis showed that P26h transcripts appear at 3 wk of age, within the first round of spermatogenesis in the golden hamster. In situ hybridization showed that P26h transcripts are expressed in spermatocytes and round spermatids, whereas immunostaining revealed the presence of P26h in the cytoplasm of round spermatids and elongated spermatids. P26h was undetectable in testicular spermatozoa. Both in situ hybridization and immunostaining showed P26h expression to be dependent of the testicular cell type and the epithelium cycle. The implications for P26h in sperm-egg interaction and the testicular origin of P26h are discussed.


Assuntos
Oxirredutases do Álcool/biossíntese , Moléculas de Adesão Celular/biossíntese , Espermatogênese/fisiologia , Testículo/metabolismo , Animais , Northern Blotting , Western Blotting , Cricetinae , Epididimo/metabolismo , Fertilização in vitro , Células Germinativas/metabolismo , Imuno-Histoquímica , Hibridização In Situ , Masculino , Mesocricetus , RNA Mensageiro/biossíntese , RNA Mensageiro/isolamento & purificação , Proteínas Recombinantes de Fusão/química , Espermátides/metabolismo , Transcrição Gênica
10.
Biol Reprod ; 64(2): 720-7, 2001 Feb.
Artigo em Inglês | MEDLINE | ID: mdl-11159378

RESUMO

Sperm surface proteins involved in fertilization can be added or modified during epididymal transit. P34H, a human epididymal-sperm protein, appears on the sperm acrosomal cap in the distal caput-proximal corpus epididymis. In previous studies, it was shown that P34H is present on spermatozoa in men of proven fertility, is absent in 50% of men presenting with idiopathic infertility, and that a high proportion of men with normospermic vasovasectomy produce spermatozoa deficient in this sperm surface protein. P34H mRNA was expressed in the principal cells of the epididymis of normal men, predominantly in the corpus region. Recently, results coming from the assisted reproductive technologies have questioned the importance of the human epididymis in sperm maturation. In order to understand the effect of obstruction on the physiological state of the human epididymis and its function in sperm maturation, we have analyzed the expression of P34H mRNA at the level of the vas deferens and along the epididymis of normal and vasectomized men. In situ hybridization experiments showed that obstruction of the vas deferens alters the pattern of P34H mRNA expression compared with the tract of normal tissues. The P34H transcript was detected in the proximal caput epididymis of vasectomized men at a much higher intensity than that observed in the same region of normal tissues, being restricted to the principal cells of the epididymal epithelium. Compared with the normal duct, the lumen of vasectomized men was distended throughout the duct and the height of the epithelium was maximal in the caput. P34H mRNA was detectable in vas deferens, was not affected by vasectomy, and a 912-base pair P34H transcript was restricted to the epithelial cells of the vas deferens. Thus, using P34H as a marker, these results show that vasectomy alters the pattern of gene expression along the human epididymis, and suggest that the vas deferens can be a major contributor to sperm maturation in certain situations.


Assuntos
Ductos Ejaculatórios/metabolismo , Epididimo/fisiologia , Biossíntese de Proteínas , Proteínas , RNA Mensageiro/biossíntese , Vasectomia , Adulto , Biomarcadores , Northern Blotting , Humanos , Hibridização In Situ , Técnicas In Vitro , Masculino , Maturação do Esperma/fisiologia , Desidrogenase do Álcool de Açúcar , Transcrição Gênica , Ducto Deferente/metabolismo
11.
Mol Reprod Dev ; 51(3): 265-73, 1998 Nov.
Artigo em Inglês | MEDLINE | ID: mdl-9771646

RESUMO

A bovine oviductal fluid catalase (OFC) which preferentially binds to the acrosome surface of some mammalian spermatozoa has recently been purified. The objectives of this study were to clone the OFC, obtain the full-length cDNA and protein sequence and determine which characteristics of the proteins are associated with the binding of the enzyme to sperm surface. Northern blot analysis revealed low levels of catalase mRNA in bovine oviducts and uterus compared to the liver and kidney. Screening of a cDNA library from the cow oviduct permit to obtain a full-length cDNA of 2282 bp, with an open reading frame of 1581 bp coding for a deduced protein of 526 amino acids (59,789 Da). The deduced protein contained four potential N-glycosylation sites and many potential O-glycosylation sites. The OFC protein exhibited high identity with catalase from other bovine tissues, likewise with catalases from human fibroblast and kidney, and with rat liver catalase. The homology of amino acid sequence of OFC with bovine liver catalase was about 99%. However the OFC possess an extended carboxyl terminus of 20 amino acids not present on the liver catalase. This result is supported by a lower mobility of the OFC compared to the liver catalase when both proteins are submitted on SDS-PAGE.


Assuntos
Catalase/genética , DNA Complementar/genética , Tubas Uterinas/enzimologia , Sequência de Aminoácidos , Animais , Sequência de Bases , Catalase/metabolismo , Bovinos , Clonagem Molecular , Feminino , Humanos , Masculino , Dados de Sequência Molecular , RNA Mensageiro/análise , RNA Mensageiro/genética , Ratos , Alinhamento de Sequência
12.
Mol Reprod Dev ; 52(2): 225-33, 1999 Feb.
Artigo em Inglês | MEDLINE | ID: mdl-9890754

RESUMO

We have previously identified a hamster sperm protein, P26h, proposed to be involved in the interaction between spermatozoa and the egg's zona pellucida. In this study we investigated the mechanism of P26h accumulation on hamster spermatozoa during epididymal maturation. Immunocytochemical studies showed an accumulation of P26h on the acrosomal cap of hamster spermatozoa during epididymal transit. To document the anchoring mechanism of P26h, cauda epididymal spermatozoa were exposed to different treatments. High-salt buffered solutions were unable to remove P26h from the surface of intact spermatozoa. P26h was released in a dose-dependent manner when live spermatozoa were treated with a solution of phospholipase C specific to phosphatidylinositol. In contrast, the P26h remained associated to the sperm surface following treatment with trypsin. To document the transfer mechanisms of P26h on the maturing spermatozoa, prostasomes were isolated from the epididymal fluid and subjected to immunodetection. Western blots and immunogold studies showed that P26h was associated to epididymal prostasomes. Phospholipase C treatment performed on epididymal prostasomes, indicated that P26h also is anchored to these vesicles via a phosphatidylinositol. These results suggest that epididymal sperm maturation involves a cell to cell transfer of a phosphaditylinositol-anchored protein and that prostasomes may be implicated in this process.


Assuntos
Oxirredutases do Álcool , Antígenos de Superfície/metabolismo , Moléculas de Adesão Celular/metabolismo , Fosfatidilinositóis/metabolismo , Espermatozoides/imunologia , Animais , Cricetinae , Masculino , Mesocricetus , Cloreto de Sódio , Tripsina/metabolismo , Fosfolipases Tipo C/metabolismo
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