scholarly journals Prevalent skipping of an individual exon accounts for shortened protein 4.1 Presles

Blood ◽  
1992 ◽  
Vol 80 (11) ◽  
pp. 2925-2930 ◽  
Author(s):  
S Feddal ◽  
S Hayette ◽  
F Baklouti ◽  
R Rimokh ◽  
R Wilmotte ◽  
...  
Keyword(s):  
Red Blood Cells ◽  
Alternative Splice ◽  
Splice Site ◽  
Blood Cells ◽  
Protein 4.1 ◽  
Alternative Splice Site ◽  
Alternatively Spliced ◽  
Domain Protein

Abstract An asymptomatic shortened variant of protein 4.1 (-8.5 Kd) was first recognized in the red blood cells and designated protein 4.1 Presles. We show here that the missing segment belongs to the 22/24 Kd domain. Protein 4.1 cDNA from reticulocytes was amplified, mapped, and sequenced. The truncation appeared to result from the prevalent skipping of an individual and alternatively spliced exon, also called motif II, whereas this motif is preferentially retained under normal conditions. The same phenomenon was observed in lympho-blastoid cells. Sequencing over 80 bp of intronic sequences 5′ and 3′ of motif II failed to reveal any change. A new alternative splice site was incidently found 81 nucleotide downstream of motif II in both normal and truncated 4.1 mRNA.

scholarly journals Prevalent skipping of an individual exon accounts for shortened protein 4.1 Presles

Blood ◽  
1992 ◽  
Vol 80 (11) ◽  
pp. 2925-2930 ◽  
Author(s):  
S Feddal ◽  
S Hayette ◽  
F Baklouti ◽  
R Rimokh ◽  
R Wilmotte ◽  
...  
Keyword(s):  
Red Blood Cells ◽  
Alternative Splice ◽  
Splice Site ◽  
Blood Cells ◽  
Protein 4.1 ◽  
Alternative Splice Site ◽  
Alternatively Spliced ◽  
Domain Protein

An asymptomatic shortened variant of protein 4.1 (-8.5 Kd) was first recognized in the red blood cells and designated protein 4.1 Presles. We show here that the missing segment belongs to the 22/24 Kd domain. Protein 4.1 cDNA from reticulocytes was amplified, mapped, and sequenced. The truncation appeared to result from the prevalent skipping of an individual and alternatively spliced exon, also called motif II, whereas this motif is preferentially retained under normal conditions. The same phenomenon was observed in lympho-blastoid cells. Sequencing over 80 bp of intronic sequences 5′ and 3′ of motif II failed to reveal any change. A new alternative splice site was incidently found 81 nucleotide downstream of motif II in both normal and truncated 4.1 mRNA.

scholarly journals Are alterations of protein 4.1 involved in the echinocytic transformation of red blood cells? [letter; comment]

Blood ◽  
1994 ◽  
Vol 84 (5) ◽  
pp. 1685-1686 ◽  
Author(s):  
B Agroyannis ◽  
A Dalamangas ◽  
H Tzanatos ◽  
C Fourtounas ◽  
I Kopelias ◽  
...  
Keyword(s):  
Red Blood Cells ◽  
Blood Cells ◽  
Protein 4.1 ◽  
Letter Comment

Factors That Influence Alternative Splice Site Selection in Vitro

1987 ◽  
pp. 97-112 ◽  
Author(s):  
JAMES L. MANLEY ◽  
JONATHAN C.S. NOBLE ◽  
XIN-YUAN FU ◽  
HUI GE
Keyword(s):  
Alternative Splice ◽  
Splice Site ◽  
Site Selection ◽  
Splice Site Selection ◽  
Alternative Splice Site

scholarly journals The concentration of B52, an essential splicing factor and regulator of splice site choice in vitro, is critical for Drosophila development.

1994 ◽  
Vol 14 (8) ◽  
pp. 5360-5370 ◽  
Author(s):  
M E Kraus ◽  
J T Lis
Keyword(s):  
Alternative Splice ◽  
Splice Site ◽  
Developmental Stages ◽  
Immunoblot Analysis ◽  
Splicing Factor ◽  
Dependent Manner ◽  
Concentration Dependent Manner ◽  
Alternative Splice Site

B52 is a Drosophila melanogaster protein that plays a role in general and alternative splicing in vitro. It is homologous to the human splicing factor ASF/SF2 which is essential for an early step(s) in spliceosome assembly in vitro and also regulates 5' and 3' alternative splice site choice in a concentration-dependent manner. In vitro, B52 can function as both a general splicing factor and a regulator of 5' alternative splice site choice. Its activity in vivo, however, is largely uncharacterized. In this study, we have further characterized B52 in vivo. Using Western blot (immunoblot) analysis and whole-mount immunofluorescence, we demonstrate that B52 is widely expressed throughout development, although some developmental stages and tissues appear to have higher B52 levels than others do. In particular, B52 accumulates in ovaries, where it is packaged into the developing egg and is localized to nuclei by the late blastoderm stage of embryonic development. We also overexpressed this protein in transgenic flies in a variety of developmental and tissue-specific patterns to examine the effects of altering the concentration of this splicing factor in vivo. We show that, in many cell types, changing the concentration of B52 adversely affects the development of the organism. We discuss the significance of these observations with regard to previous in vitro results.

Molecular and Cellular Characterization of a New α-Thalassemia Mutation (HBA2:c.94A>C) Generating an Alternative Splice Site and a Premature Stop Codon

Hemoglobin ◽  
2012 ◽  
Vol 36 (3) ◽  
pp. 244-252 ◽  
Author(s):  
Talal Qadah ◽  
Jill Finlayson ◽  
Christopher Newbound ◽  
Nicole Pell ◽  
Michelle Pascoe ◽  
...  
Keyword(s):  
Alternative Splice ◽  
Splice Site ◽  
Stop Codon ◽  
Premature Stop Codon ◽  
Alternative Splice Site ◽  
Thalassemia Mutation

scholarly journals Identification of embryo specific human isoforms using a database of predicted alternative splice forms

2006 ◽  
Vol 3 (1) ◽  
pp. 1-10
Author(s):  
Heike Pospisil
Keyword(s):  
Alternative Splice ◽  
Splice Site ◽  
Splice Variants ◽  
Main Idea ◽  
Protein Isoforms ◽  
Unequal Distribution ◽  
Interesting Candidate ◽  
Alternatively Spliced ◽  
Specific Alternative ◽  
Splice Forms

Abstract Alternative splicing is one of the most important mechanisms to generate a large number of mRNA and protein isoforms from a small number of genes. Its study became one of the hot topics in computational genome analysis. The repository EASED (Extended Alternatively Spliced EST Database, http://eased.bioinf.mdc-berlin.de/) stores a large collection of splice variants predicted from comparing the human genome against EST databases. It enables finding new unpublished splice forms that could be interesting candidate genes for stage specific, diseases specific or tissue specific splicing. The main idea behind selecting specific splice forms is to compare the number and the origin of ESTs confirming one isoform with the number and the origin of ESTs confirming the opposite isoform. A measure asDcs is introduced to take into account the unequal distribution of ESTs per splice site on one hand, and the possible uncertainties due to the relatively low quality of EST data on the other hand. First, the number of ESTs per splice site is scaled with a modified Hill function. The measure asDcs computes in the second step the distance of each pair of ESTs from equipartition. Equipartition exists if for every number of adult ESTs the same number of embryonic ESTs. The effect of several input parameters for the scaling of true EST values is analysed and can be reproduced on http://cardigan.zbh.uni-hamburg.de/asDcs. Some of the obtained best scoring hits for selected parameters (transcription factor P65, drebrin, and fetuin) have been already described in literature as been involved in embryonic development. This result shows the plausibility of this approach and looks promising for the identification of unplublished embryo specific alternative splice sites in human.

Identification of HLA-A*0111N: A Synonymous Substitution, Introducing an Alternative Splice Site in Exon 3, Silenced the Expression of an HLA-A Allele

2005 ◽  
Vol 66 (8) ◽  
pp. 912-920 ◽  
Author(s):  
Judith Reinders ◽  
Erik H. Rozemuller ◽  
Henny G. Otten ◽  
Anna J.S. Houben ◽  
Anne Dormoy ◽  
...  
Keyword(s):  
Alternative Splice ◽  
Splice Site ◽  
Synonymous Substitution ◽  
Alternative Splice Site

scholarly journals Are alterations of protein 4.1 involved in the echinocytic transformation of red blood cells? [letter; comment]

Blood ◽  
1994 ◽  
Vol 84 (5) ◽  
pp. 1685-1686
Author(s):  
B Agroyannis ◽  
A Dalamangas ◽  
H Tzanatos ◽  
C Fourtounas ◽  
I Kopelias ◽  
...  
Keyword(s):  
Red Blood Cells ◽  
Blood Cells ◽  
Protein 4.1 ◽  
Letter Comment

scholarly journals Membrane protein interactions in sickle red blood cells: evidence of abnormal protein 3 function

Blood ◽  
1995 ◽  
Vol 86 (5) ◽  
pp. 1992-1998 ◽  
Author(s):  
OS Platt ◽  
JF Falcone
Keyword(s):  
Membrane Proteins ◽  
Red Blood Cells ◽  
Protein Interactions ◽  
Blood Cells ◽  
Binding Domain ◽  
Protein 4.1 ◽  
Functional Defect ◽  
Sickle Red Blood Cells ◽  
Self Association ◽  
Actin Protein

The pattern of membrane abnormalities in sickle red blood cells suggests that sickle hemoglobin damages membrane proteins. We have previously shown a functional defect in sickle ankyrin, poor spectrin- binding ability. Here we examine the other major binding interactions of sickle membrane proteins including spectrin self-association, binding of ankyrin and protein 4.1 to protein 3, and the formation of the spectrin-actin-protein 4.1 complex. We found that sickle spectrin was normal in self-association and ability to participate in the spectrin-actin-protein 4.1 complex. Sickle protein 4.1 bound normally to protein 3 and formed normal complexes with actin and spectrin, even when sickle spectrin was used. The only major abnormality we found was a reduced ability of sickle protein 3 to bind ankyrin. This functional defect could not be explained experimentally on the basis of cysteine modification or enhanced tyrosine phosphorylation. We conclude that damage of sickle membrane proteins is not a diffuse scattershot process, but is largely confined to regions near membrane-associated hemoglobin, the spectrin-binding domain of ankyrin and the ankyrin- binding domain of protein 3. The mechanism and consequences of this damage continues to be investigated.

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