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1.
Child Care Health Dev ; 40(6): 825-32, 2014 Nov.
Article in English | MEDLINE | ID: mdl-24028505

ABSTRACT

CONTEXT: In 2003, Quebec's Ministry of Health and Social Services (MSSS) and the Ministry of Education, Recreation and Sports (MELS) concluded the Agreement for the complementarity of services between the health and social services network and the education network. The objectives of the current investigation were to evaluate the implementation of this Agreement and its impact upon renewal of practices and services, and to investigate the consequences for children with special needs and their families. The specific focus of this article is to describe parents' perspectives regarding the impact of this Agreement upon them and their children. METHODS: Interviews were conducted with 56 parents of children with disabilities, social maladjustment or learning difficulties across the province of Quebec. Data were analysed using content analysis. RESULTS: Most parents were not directly aware of any contact between school staff and health or social professionals, although discussions might have been held without their knowledge. The intervention plans seemed to be the main vehicle through which some parents perceived collaboration to be occurring. For parents, the impact upon actual practices or collaborative work is either minimal or non-existent. CONCLUSION: School inclusion of children with special needs is a challenge for all societies. The Agreement illustrates the Quebec government's intent to promote an alliance between two complex networks and has the potential to greatly benefit children and their families. However, more concrete action is required in order to realize specific changes regarding work cohesion and service organization for these groups.


Subject(s)
Child Health Services , Disabled Children/psychology , Learning Disabilities/psychology , Parents , Social Isolation/psychology , Social Support , Access to Information , Adolescent , Adult , Attitude of Health Personnel , Child , Child Health Services/organization & administration , Child, Preschool , Cooperative Behavior , Delivery of Health Care , Disabled Children/statistics & numerical data , Education, Special , Female , Health Services Accessibility/organization & administration , Humans , Learning Disabilities/epidemiology , Male , Parents/education , Parents/psychology , Patient Care Team/organization & administration , Patient Satisfaction , Professional-Family Relations , Quebec/epidemiology , Schools/organization & administration , Social Work/organization & administration , Surveys and Questionnaires
3.
Antisense Nucleic Acid Drug Dev ; 10(1): 53-61, 2000 Feb.
Article in English | MEDLINE | ID: mdl-10726661

ABSTRACT

In the past, the use of delta ribozyme as a therapeutic tool was limited because substrate specificity was thought to be determined by only 8 nucleotides. Recently, we have accumulated evidence suggesting that the substrate sequence upstream of the cleavage site, which is not involved in the binding with the delta ribozyme, appears to be essential in the selection of an appropriate cleavage site. To understand the role of this region in efficient cleavage, we synthesized a collection of small substrates that possessed single and multiple mutations in positions -1 to -4 and determined the kinetic parameters of their cleavage using a model antigenomic delta ribozyme. Some substrates were found to be uncleavage, whereas others showed >60-fold difference in relative specificity between the least and most efficiently cleaved substrates. The base at each position from -1 to -4 contributes differently to the ability of a substrate to be cleaved. An optimal sequence for positions -1 to -4 was determined to be -1HRHY(-4) (H = U, C, or A). These results shed light on new features that contribute to the substrate requirement of delta ribozyme cleavage and should increase interest in the use of this unique ribozyme.


Subject(s)
Hepatitis Delta Virus/enzymology , RNA, Catalytic/metabolism , RNA, Messenger/metabolism , Base Sequence , Gene Expression Regulation , Hepatitis Delta Virus/genetics , Kinetics , Molecular Sequence Data , Mutation , Nucleic Acid Conformation , Pyrimidines/metabolism , RNA, Catalytic/genetics , Substrate Specificity
4.
Nucleic Acids Res ; 28(1): 179-80, 2000 Jan 01.
Article in English | MEDLINE | ID: mdl-10592219

ABSTRACT

This is an online database in order to facilitate research on viroid, viroid-like RNAs and human hepatitis delta virus by presenting a large number of sequences and related data in a comprehensive and user-friendly format (e.g., position of their self-catalytic domains, open reading frame, prediction of the most stable secondary structures, etc.). This online database is available on the WWW at http://www.callisto.si. usherb.ca/jpperra


Subject(s)
Databases, Factual , RNA, Viral/genetics , Viroids/genetics , Catalysis
5.
Nucleic Acids Res ; 27(1): 186-7, 1999 Jan 01.
Article in English | MEDLINE | ID: mdl-9847175

ABSTRACT

This is an online database to facilitate research on viroid, viroid-like RNAs and human hepatitis delta virus (vHDV) by presenting a large number of sequences and related data in a comprehensive and user-friendly format (e.g. position of their self-catalytic domains, open reading frame of the vHDV, prediction of the most stable secondary structures, etc.). Most of these RNA species share a common proposed replication pattern known as a DNA-independent rolling circle mechanism. Together, these species form the 'brotherhood' of the smallest known auto-replicable RNAs. This online database is available on the World Wide Web at http://www.callisto.si.usherb.ca/jpperra


Subject(s)
Databases, Factual , Hepatitis Delta Virus/genetics , RNA, Viral/genetics , Viroids/genetics , Humans , Internet , Phylogeny , RNA/genetics , RNA, Catalytic/genetics , RNA, Circular , RNA, Satellite/genetics , Sequence Alignment , Terminology as Topic
6.
J Membr Biol ; 161(2): 183-96, 1998 Jan 15.
Article in English | MEDLINE | ID: mdl-9435274

ABSTRACT

cDNA encoding the full-length hKv1.3 lymphocyte channel and a C-terminal truncated (delta 459-523) form that lacks the putative PKA Ser468 phosphorylation site were stably transfected in human embryonic kidney (HEK) 293 cells. Immunostaining of the transfected cells revealed a distribution at the plasma membrane that was uniform in the case of the full-length channel whereas clustering was observed in the case of the truncated channel. Some straining within the cell cytoplasm was found in both instances, suggesting an active process of biosynthesis. Analyses of the K+ current by the patch-clamp technique in the whole cell configuration showed that depolarizing steps to 40 mV from a holding potential (HP) of -80 mV elicited an outward current of 2 to 10 nA. The current threshold was positive to -40 mV and the current amplitude increased in a voltage-dependent manner. The parameters of activation were -5.7 and -9.9 mV (slope factor) and -35 mV (half activation, V0.5) in the case of the full-length and truncated channels, respectively. The characteristics of the inactivation were 14.2 and 24.6 mV (slope factor) and -17.3 and -39.0 mV (V0.5) for the full-length and truncated channels, respectively. The activation time constant of the full-length channel for potentials ranging from -30 to 40 mV decreased from 18 to 12 msec whereas the inactivation time constant decreased from 6600 msec at -30 mV to 1800 msec at 40 mV. The unit current amplitude measured in cells bathing in 140 mM KCl was 1.3 +/- 0.1 pA at 40 mV, the unit conductance, 34.5 pS and the zero current voltage, 0 mV. Both forms of the channels were inhibited by TEA, 4-AP, Ni2+ and charybdotoxin. In contrast to the native (Jurkat) lymphocyte Kv1.3 channel that is fully inhibited by PKA and PKC, the addition of TPA resulted in 34.6 +/- 7.3% and 38.7 +/- 9.4% inhibition of the full-length and the truncated channels, respectively, 8-BrcAMP induced a 39.4 +/- 5.4% inhibition of the full-length channel but had no effect (8.6 +/- 8.3%) on the truncated channel. Cell dialysis with alkaline phosphatase had no effects, suggesting that the decreased sensitivity of the transfected channels to PKA and PKC was not due to an already phosphorylated channel. Patch extract experiments suggested that the hKv1.3 channel was partially sensitive to PKA and PKC. Cotransfecting the Kv beta 1.2 subunit resulted in a decrease in the value of the time constant of inactivation of the full-length channel but did not modify its sensitivity to PKA and PKC. The cotransfected Kv beta 2 subunit had no effects. Our results indicate that the hKv1.3 lymphocyte channel retains its electrophysiological characteristics when transfected in the Kv beta-negative HEK 293 cell line but its sensitivity to modulation by PKA and PKC is significantly reduced.


Subject(s)
Cyclic AMP-Dependent Protein Kinases/metabolism , Lymphocytes/physiology , Potassium Channels, Voltage-Gated , Potassium Channels/metabolism , Protein Kinase C/metabolism , Cell Line , Electric Conductivity , Fluorescent Antibody Technique, Indirect , Gene Expression , Humans , Kv1.2 Potassium Channel , Kv1.3 Potassium Channel , Lymphocytes/drug effects , Lymphocytes/metabolism , Mutagenesis , Phosphorylation , Potassium Channels/biosynthesis , Potassium Channels/genetics , Potassium Channels/pharmacology , Transfection
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