Developmentally Regulated Muscle Type-Specific Alternative Splicing of the COOH-Terminal Variable Region of Fast Skeletal Muscle Troponin T and an Aberrant Splicing Pathway to Encode a Mutant COOH-Terminus

1998 ◽  
Vol 242 (3) ◽  
pp. 540-544 ◽  
Author(s):  
Jian-Ping Jin ◽  
Jennifer Wang ◽  
Ozgur Ogut
Keyword(s):  
Skeletal Muscle ◽  
Alternative Splicing ◽  
Troponin T ◽  
Variable Region ◽  
Muscle Type ◽  
Fast Skeletal Muscle ◽  
Aberrant Splicing ◽  
Developmentally Regulated ◽  
Specific Alternative

Novel developmentally regulated exon identified in the rat fast skeletal muscle troponin T gene

1993 ◽  
Vol 106 (3) ◽  
pp. 903-908 ◽  
Author(s):  
M.J. Morgan ◽  
J.C. Earnshaw ◽  
G.K. Dhoot
Keyword(s):  
Skeletal Muscle ◽  
Troponin T ◽  
Fast Skeletal Muscle ◽  
Mrna Isoforms ◽  
Developmentally Regulated ◽  
Adult Skeletal Muscle ◽  
Alternatively Spliced ◽  
Molecular Masses ◽  
First Time ◽  
Alternatively Spliced Exons

In theory, the rat fast skeletal muscle troponin T gene can generate 64 different isoforms. Here we report the identification of a novel alternative exon (exon y) that increases the potential isoform variation to 128. The inclusion of exon y in fast skeletal muscle troponin T mRNA occurs in perinatal, but not adult, skeletal muscle. Exon y is located between exons 8 and 9. This is the first time that a developmentally regulated exon located amongst a set of alternatively spliced exons has been described. Exon y is included in two mRNA isoforms. The proteins that these mRNAs would encode have molecular masses greater than that of the largest fast skeletal muscle troponin T isoform lacking exon y. These two proteins correlate well in both size and pattern of expression with the two fast skeletal muscle troponin T isoforms expressed in perinatal skeletal muscle. These results indicate that there is coordinated regulation of the splicing of exon y with other alternative exons.

Tissue specificity and alternative splicing of the Na+/Ca2+ exchanger isoforms NCX1, NCX2, and NCX3 in rat

1997 ◽  
Vol 272 (4) ◽  
pp. C1250-C1261 ◽  
Author(s):  
B. D. Quednau ◽  
D. A. Nicoll ◽  
K. D. Philipson
Keyword(s):  
Skeletal Muscle ◽  
Polymerase Chain Reaction ◽  
Alternative Splicing ◽  
Reverse Transcriptase ◽  
Splice Variants ◽  
Variable Region ◽  
Intracellular Loop ◽  
Chain Reaction ◽  
Splicing Isoforms ◽  
Polymerase Chain

The gene coding for the Na+/Ca2+ exchanger NCX1 is characterized by a cluster of six exons (A, B, C, D, E, and F) coding for a variable region in the COOH terminus of the large intracellular loop of the protein. Alternative splicing of these exons generates multiple tissue-specific variants of NCX1. Using reverse transcriptase-polymerase chain reaction, we analyzed eight previously described and four new splicing isoforms of NCX1 in a wide variety of tissues and cells. Exons A and B are mutually exclusive, as shown in earlier studies, and splicing isoforms containing exon A are preferentially expressed in heart, brain, and skeletal muscle, whereas splicing variants with exon B are found in all rat tissues except heart. The second and third isoforms of the Na+/Ca2+ exchanger, NCX2 and NCX3, show a deletion of 37 amino acids in the intracellular loop corresponding to parts of the variable region of NCX1. We identified three splicing isoforms of NCX3 in brain and skeletal muscle by reverse transcriptase-polymerase chain reaction. These splice variants are generated by including either of two alternative exons equivalent to the NCX1 exon A or B and by including or excluding a sequence equivalent to the NCX1 exon C. We did not detect any alternative splicing of NCX2. We examined selected tissues from neonatal and adult rats and found developmental regulation for NCX1 and NCX3 splicing isoforms in skeletal muscle. Specific isoform patterns were also detected for NCX1 and NCX3 in cultured cortical neurons, astrocytes, and oligodendrocytes. We suggest a new terminology to distinguish the different splice variants of individual NCX isoforms.

scholarly journals Conformational modulation of slow skeletal muscle troponin T by an NH2-terminal metal-binding extension

2000 ◽  
Vol 279 (4) ◽  
pp. C1067-C1077 ◽  
Author(s):  
Jian-Ping Jin ◽  
Aihua Chen ◽  
Ozgur Ogut ◽  
Qi-Quan Huang
Keyword(s):  
Skeletal Muscle ◽  
Monoclonal Antibody ◽  
Metal Binding ◽  
Metal Ion ◽  
Troponin I ◽  
Troponin T ◽  
Terminal Region ◽  
Sequence Motif ◽  
Fast Skeletal Muscle ◽  
Slow Skeletal Muscle

Troponin T (TnT) is an essential element in the thin filament Ca2+-regulatory system controlling striated muscle contraction. Alternative RNA splicing generates developmental and muscle type-specific TnT isoforms differing in the hypervariable NH2-terminal region. Using avian fast skeletal muscle TnT containing a metal-binding segment, we have demonstrated a role of the NH2-terminal domain in modulating the conformation of TnT (Wang J and Jin JP. Biochemistry 37: 14519–14528, 1998). To further investigate the structure-function relationship of TnT, the present study constructed and characterized a recombinant protein in which the metal-binding peptide present in avian fast skeletal muscle TnT was fused to the NH2 terminus of mouse slow skeletal muscle TnT. Metal ion or monoclonal antibody binding to the NH2-terminal extension induced conformational changes in other domains of the model TnT molecule. This was shown by the altered affinity to a monoclonal antibody against the COOH-terminal region and a polyclonal antiserum recognizing multiple epitopes. Protein binding assays showed that metal binding to the NH2-terminal extension had effects on the interaction of TnT with troponin I, troponin C, and most significantly, tropomyosin. The data indicate that the NH2-terminal Tx [4–7 repeats of a sequence motif His-(Glu/Ala)-Glu-Ala-His] extension confers a specific conformational modulation in the slow skeletal muscle TnT.

scholarly journals Ankyrin-G in skeletal muscle: Tissue-specific alternative splicing contributes to the complexity of the sarcolemmal cytoskeleton☆

2005 ◽  
Vol 309 (1) ◽  
pp. 86-98 ◽  
Author(s):  
Alexander A. Hopitzan ◽  
Anthony J. Baines ◽  
Marie-Aline Ludosky ◽  
Michel Recouvreur ◽  
Ekaterini Kordeli
Keyword(s):  
Skeletal Muscle ◽  
Alternative Splicing ◽  
Muscle Tissue ◽  
Skeletal Muscle Tissue ◽  
Tissue Specific ◽  
Ankyrin G ◽  
Specific Alternative

The extent of amino-terminal heterogeneity in rabbit fast skeletal muscle troponin T

1987 ◽  
Vol 8 (1) ◽  
pp. 1-12 ◽  
Author(s):  
Margaret M. Briggs ◽  
Jim J. -C. Lin ◽  
Frederick H. Schachat
Keyword(s):  
Skeletal Muscle ◽  
Troponin T ◽  
Fast Skeletal Muscle ◽  
Amino Terminal
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