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1.
J Intellect Disabil Res ; 55(4): 434-40, 2011 Apr.
Article in English | MEDLINE | ID: mdl-21366755

ABSTRACT

BACKGROUND: Worldwide, contraception is frequently used by women for the prevention of conception, to regulate or postpone menstrual bleeding. The study aims to determine the use (number and method) of contraception by women with intellectual disabilities (ID), the indications, sources of referrals and relations with level of ID and age of the women concerned. METHODS: The study group consisted of 234 women aged between 15 and 59 years and residing at a Dutch service provider for persons with ID. Data were obtained via the pharmacy database, attending physicians and individual medical files. RESULTS: Nearly one half (48%, n = 112) of the 234 residential women used some method of contraception: 87 (78%) took pharmacological contraceptive methods, 23 (20%) underwent surgical contraception and 2 (2%) both. Main reasons for contraception were problems with menstruation, behaviour and/or prevention of pregnancy. Requests for contraception were initiated mainly by physicians and parents. Differences between users of different contraceptives with regard to age and level of ID were not statistically significant. CONCLUSIONS: Further studies should focus on the development and implementation of adequate health promotion materials on this subject.


Subject(s)
Contraception Behavior/statistics & numerical data , Disabled Persons/statistics & numerical data , Intellectual Disability , Sexual Behavior/statistics & numerical data , Adolescent , Adult , Contraceptive Agents, Female , Female , Humans , Middle Aged , Young Adult
2.
Plant J ; 26(4): 421-33, 2001 May.
Article in English | MEDLINE | ID: mdl-11439129

ABSTRACT

Plants both produce and utilize carbohydrates and have developed mechanisms to regulate their sugar status and co-ordinate carbohydrate partitioning. High sugar levels result in a feedback inhibition of photosynthesis and an induction of storage processes. We used a genetic approach to isolate components of the signalling pathway regulating the induction of starch biosynthesis. The regulatory sequences of the sugar inducible ADP-glucose pyrophosphorylase subunit ApL3 were fused to a negative selection marker. Of the four impaired sucrose induction (isi) mutants described here, two (isi1 and isi2) were specific to this screen. The other two mutants (isi3 and isi4) showed additional phenotypes associated with sugar-sensing screens that select for seedling establishment on high-sugar media. The isi3 and isi4 mutants were found to be involved in the abscisic acid signalling pathway. isi3 is allelic to abscisic acid insensitive4 (abi4), a gene encoding an Apetala2-type transcription factor; isi4 was found to be allelic to glucose insensitive1 (gin1) previously reported to reveal cross-talk between ethylene and glucose signalling. Here we present an alternative interpretation of gin1 as an allele of the ABA-deficient mutant aba2. Expression analysis showed that ABA is unable to induce ApL3 gene expression by itself, but greatly enhances ApL3 induction by sugar. Our data suggest a major role for ABA in relation to sugar-signalling pathways, in that it enhances the ability of tissues to respond to subsequent sugar signals.


Subject(s)
Abscisic Acid/metabolism , Arabidopsis/genetics , Starch/biosynthesis , Sucrose/pharmacology , Alleles , Arabidopsis/drug effects , Arabidopsis Proteins , Gene Expression Regulation, Plant , Genes, Plant , Genetic Complementation Test , Glucose-1-Phosphate Adenylyltransferase , Models, Biological , Mutation , Nucleotidyltransferases/genetics , Plant Leaves/drug effects , Signal Transduction/genetics , Tissue Distribution
3.
Plant J ; 15(2): 253-63, 1998 Jul.
Article in English | MEDLINE | ID: mdl-9721683

ABSTRACT

The Arabidopsis bZIP transcription factor gene ATB2 has been shown previously to be expressed in a light-regulated and tissue-specific way. Here we describe the precise localization of ATB2 expression, using transgenic lines containing an ATB2 promoter-GUS reporter gene construct. The observed expression pattern suggests a role for ATB2 in the control of processes associated with the transport or utilization of metabolites. Remarkably, expression of the ATB2-GUS reporter gene construct was specifically repressed by sucrose. Other sugars, such as glucose and fructose, alone or in combination, were ineffective. Repression was observed at external sucrose concentrations exceeding 25 mM. Transcript levels of both the endogenous ATB2 gene and the ATB2-GUS reporter gene were not repressed by sucrose, suggesting that sucrose affects mRNA translation. This translational regulation involves the ATB2 leader sequence because deletion of the leader resulted in loss of sucrose repression. Our results provide evidence for a sucrose-specific sugar sensing and signalling system in plants.


Subject(s)
Arabidopsis Proteins , Arabidopsis/genetics , Arabidopsis/metabolism , DNA-Binding Proteins/genetics , Gene Expression Regulation, Plant/physiology , Protein Biosynthesis/drug effects , Sucrose/pharmacology , Transcription Factors/genetics , Basic-Leucine Zipper Transcription Factors , DNA-Binding Proteins/biosynthesis , Gene Expression Regulation, Plant/drug effects , Gene Expression Regulation, Plant/radiation effects , Glucuronidase/biosynthesis , Kinetics , Leucine Zippers , Light , Luciferases/biosynthesis , Polymerase Chain Reaction , Promoter Regions, Genetic , RNA, Messenger/metabolism , Recombinant Fusion Proteins/biosynthesis , Transcription Factors/biosynthesis
4.
Plant Mol Biol ; 37(1): 171-8, 1998 May.
Article in English | MEDLINE | ID: mdl-9620274

ABSTRACT

A light-regulated basic domain/leucine zipper gene, ATB2, was identified in an Arabidopsis thaliana transcription factor gene collection. Both genomic and cDNA clones of ATB2 were isolated. The gene encodes a small protein (18 kDa) which mainly consists of the basic domain and an unusually long leucine zipper. The expression of the ATB2 gene is induced when etiolated or dark-adapted seedlings are transferred to the light. Moreover, its expression is derepressed in dark-grown seedlings of the photomorphogenic mutants cop1 and det1. In mature plants, transcript levels are particularly high in flowers and also light-responsive in these tissues.


Subject(s)
Arabidopsis Proteins , Arabidopsis/genetics , DNA-Binding Proteins/genetics , Gene Expression Regulation, Plant/radiation effects , Genes, Plant , Leucine Zippers , Transcription Factors/genetics , Adaptation, Biological , Amino Acid Sequence , Base Sequence , Basic-Leucine Zipper Transcription Factors , Chloroplasts/metabolism , Darkness , Light , Molecular Sequence Data , Morphogenesis/genetics , Mutation , Plant Proteins/genetics , Transcription, Genetic
5.
Plant Physiol ; 115(1): 7-13, 1997 Sep.
Article in English | MEDLINE | ID: mdl-12223788
6.
Plant Cell ; 7(1): 117-29, 1995 Jan.
Article in English | MEDLINE | ID: mdl-7696878

ABSTRACT

A light-regulated Arabidopsis thaliana homeobox 1 gene (ATH1) was identified in a transcription factor gene collection. Primer extension analysis of this gene showed the presence of two major transcripts with unusually long 5' untranslated leader sequences. The leader sequence of the isolated cDNA clone contains several small open reading frames upstream of the initiation codon of the largest open reading frame coding for the homeodomain protein. This leader sequence was found to affect the translation efficiency negatively in an in vitro translation system. The expression of the ATH1 gene is dependent on the presence of light. After illuminating etiolated or dark-adapted Arabidopsis seedlings, the ATH1 mRNA level increased rapidly. Expression of ATH1 does not require the presence of active chloroplasts because photooxidative destruction of the chloroplast by norflurazon treatment did not influence the ATH1 mRNA level. In dark-grown seedlings of the photomorphogenic constitutive photomorphogenic 1 (cop1) and deetiolated 1 (det1) mutants, the ATH1 mRNA level was elevated. This shows that the gene products of these loci directly or indirectly repress ATH1 expression in etiolated wild-type seedlings. A correlation between the strength of the cop1 allele and the ATH1 mRNA level was found. This relationship suggests a role for the ATH1 protein in the signal transduction pathway downstream of COP1.


Subject(s)
Arabidopsis Proteins , Arabidopsis/genetics , Genes, Homeobox , Homeodomain Proteins/genetics , Plant Proteins/genetics , Transcription Factors/genetics , Amino Acid Sequence , Arabidopsis/growth & development , Arabidopsis/radiation effects , Base Sequence , Chloroplasts/metabolism , DNA, Complementary , Gene Expression Regulation, Plant/radiation effects , Light , Molecular Sequence Data , Mutation , Open Reading Frames , RNA, Messenger/genetics , RNA, Messenger/metabolism , Sequence Homology, Amino Acid , Signal Transduction
7.
Plant Physiol ; 104(2): 515-520, 1994 Feb.
Article in English | MEDLINE | ID: mdl-12232100

ABSTRACT

The effect of a cold treatment on the carbohydrate status of the scales and flower stalk of Tulipa gesneriana L. cv Apeldoorn bulbs during growth after planting was studied and compared with bulbs not given cold treatment. Bulbs were stored dry for 12 weeks at 5[deg]C (precooled) or 17[deg]C (noncooled). Only the 5[deg]C treatment led to rapid flower stalk elongation and flowering following planting at higher temperatures. Precooling enhanced mobilization of starch, fructans, and sucrose in the scales. The cold-stimulated starch breakdown was initially accompanied by increased [alpha]-amylase activity per scale. In noncooled bulbs, [alpha]-amylase activity slightly decreased or remained more or less constant. Cold-induced flower stalk elongation was partially accompanied by a decrease in the sucrose content and an increase in the glucose content and invertase activity per g dry weight. The starch content in internodes initially decreased and subsequently increased; [alpha]-amylase activity per g dry weight of the lowermost internode showed a peak pattern during starch breakdown and increased thereafter. The internodes of noncooled bulbs, on the contrary, accumulated sucrose. Their glucose content and invertase activity per g dry weight remained low. Starch breakdown was not found and [alpha]-amylase activity per g dry weight of the lowermost internode remained at a low level. Precooling of tulip bulbs thus favors reserve mobilization in the scales and flower stalk and glucose accumulation in the elongating internodes.

8.
Plant Mol Biol ; 24(2): 283-94, 1994 Jan.
Article in English | MEDLINE | ID: mdl-8111032

ABSTRACT

Protein import into chloroplasts requires the movement of a precursor protein across the envelope membranes. The conformation of a precursor as it passes from the aqueous medium across the hydrophobic membranes is not known in detail. To address this problem we examined precursor conformation during translocation using the chimeric precursor PCDHFR, which contains the plastocyanin (PC) transit peptide in front of mouse cytosolic dihydrofolate reductase (DHFR). The chimeric protein is targeted to chloroplasts and is competent for import. The conformation of PCDHFR can be stabilized by complexing with methotrexate, an analogue of the substrate of DHFR. Methotrexate strongly inhibits DHFR import into yeast mitochondria (M. Eilers and G. Schatz, Nature 322 (1986) 228-232), presumably because the precursor must unfold to cross the membrane and it cannot do so when complexed with methotrexate. We show here that methotrexate does not block PCDHFR import into chloroplasts. Methotrexate does slow the rate of import, and protects DHFR from degradation once inside chloroplasts. The processed protein is localized in the stroma, indicating that import into thylakoids is impeded. Protease sensitivity assays indicate that the complex of precursor protein with methotrexate changes in conformation during the translocation across the envelope.


Subject(s)
Methotrexate/pharmacology , Tetrahydrofolate Dehydrogenase/metabolism , Amino Acid Sequence , Base Sequence , Biological Transport/drug effects , Chloroplasts/metabolism , DNA , Molecular Sequence Data , Plastocyanin/metabolism , Protein Processing, Post-Translational , Recombinant Fusion Proteins/metabolism
10.
Nurs Times ; 89(11): 19, 1993.
Article in English | MEDLINE | ID: mdl-8247828
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