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Expression of TPM1κ, a Novel Sarcomeric Isoform of the TPM1 Gene, in Mouse Heart and Skeletal Muscle.

Dube S, Panebianco L, Matoq AA, Chionuma HN, Denz CR, Poiesz BJ, Dube DK - Mol Biol Int (2014)

Bottom Line: We have cloned the PCR amplified DNA and determined the nucleotide sequences.Conventional RT-PCR data as well as qRT-PCR data, calculating both absolute copy number and relative expression, revealed that the expression of TPM1 κ is significantly lower compared to TPM1 α in both mouse heart and skeletal muscle.To the best of our knowledge, this is the first report of the expression of TPM1 κ in mammalian skeletal muscle.

View Article: PubMed Central - PubMed

Affiliation: Department of Medicine, SUNY Upstate Medical University, 750 East Adams Street, Syracuse, NY 13210, USA.

ABSTRACT
We have investigated the expression of TPM1 α and TPM1 κ in mouse striated muscles. TPM1 α and TMP1 κ were amplified from the cDNA of mouse heart by using conventional RT-PCR. We have cloned the PCR amplified DNA and determined the nucleotide sequences. Deduced amino acid sequences show that there are three amino acid changes in mouse exon 2a when compared with the human TPM1 κ . However, the deduced amino acid sequences of human TPM1 α and mouse TPM1 α are identical. Conventional RT-PCR data as well as qRT-PCR data, calculating both absolute copy number and relative expression, revealed that the expression of TPM1 κ is significantly lower compared to TPM1 α in both mouse heart and skeletal muscle. It was also found that the expression level of TPM1 κ transcripts in mouse heart is higher than it is in skeletal muscle. To the best of our knowledge, this is the first report of the expression of TPM1 κ in mammalian skeletal muscle.

No MeSH data available.


Alignment of the amino acid sequences of TPM1 exon 2a or 2b from various species. The top 4 sequences are 2a and the bottom four sequences are 2b. human (Hu), mouse (Mus), axolotl (ax), and chicken (Chi) sequences are shown. The underlined sequence in human TPM1κ was used to develop the antibody utilized to detect TPM1κ protein. The amino acid residue numbers are as shown. Conserved sequences are indicated by the (·).
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fig6: Alignment of the amino acid sequences of TPM1 exon 2a or 2b from various species. The top 4 sequences are 2a and the bottom four sequences are 2b. human (Hu), mouse (Mus), axolotl (ax), and chicken (Chi) sequences are shown. The underlined sequence in human TPM1κ was used to develop the antibody utilized to detect TPM1κ protein. The amino acid residue numbers are as shown. Conserved sequences are indicated by the (·).

Mentions: cDNA sequencing confirmed the expression of both TPM1α and TPM1κ expression in mouse heart and skeletal muscle. Nucleotide and the deduced amino acid sequences of mouse TPM1α were identical with the published sequence (accession number NM_001164248.1) (data not shown). Also, the nucleotide sequences of mouse TPM1α and TPM1κ as depicted in Figure 5 are identical except for exon 2. As predicted, TPM1α contains exon 2b, but TPM1κ has exon 2a. The deduced amino acid sequences of mouse and human exon 2b of the TPM1 gene are identical. The deduced amino acid sequences of exon 2a of mouse TPM1κ and the published exon 2a sequences in mouse TPM1β (smooth muscle TPM1 isoform) (NM_001164249.1) are also identical. However, some differences were noted when comparing the deduced amino acid sequences of mouse exon 2a with human TPM1 2a (Figure 6). Amino acid residues 72E and 74A in humans are replaced by 72D and 74T in mouse TPM1κ, respectively.


Expression of TPM1κ, a Novel Sarcomeric Isoform of the TPM1 Gene, in Mouse Heart and Skeletal Muscle.

Dube S, Panebianco L, Matoq AA, Chionuma HN, Denz CR, Poiesz BJ, Dube DK - Mol Biol Int (2014)

Alignment of the amino acid sequences of TPM1 exon 2a or 2b from various species. The top 4 sequences are 2a and the bottom four sequences are 2b. human (Hu), mouse (Mus), axolotl (ax), and chicken (Chi) sequences are shown. The underlined sequence in human TPM1κ was used to develop the antibody utilized to detect TPM1κ protein. The amino acid residue numbers are as shown. Conserved sequences are indicated by the (·).
© Copyright Policy - open-access
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC4020292&req=5

fig6: Alignment of the amino acid sequences of TPM1 exon 2a or 2b from various species. The top 4 sequences are 2a and the bottom four sequences are 2b. human (Hu), mouse (Mus), axolotl (ax), and chicken (Chi) sequences are shown. The underlined sequence in human TPM1κ was used to develop the antibody utilized to detect TPM1κ protein. The amino acid residue numbers are as shown. Conserved sequences are indicated by the (·).
Mentions: cDNA sequencing confirmed the expression of both TPM1α and TPM1κ expression in mouse heart and skeletal muscle. Nucleotide and the deduced amino acid sequences of mouse TPM1α were identical with the published sequence (accession number NM_001164248.1) (data not shown). Also, the nucleotide sequences of mouse TPM1α and TPM1κ as depicted in Figure 5 are identical except for exon 2. As predicted, TPM1α contains exon 2b, but TPM1κ has exon 2a. The deduced amino acid sequences of mouse and human exon 2b of the TPM1 gene are identical. The deduced amino acid sequences of exon 2a of mouse TPM1κ and the published exon 2a sequences in mouse TPM1β (smooth muscle TPM1 isoform) (NM_001164249.1) are also identical. However, some differences were noted when comparing the deduced amino acid sequences of mouse exon 2a with human TPM1 2a (Figure 6). Amino acid residues 72E and 74A in humans are replaced by 72D and 74T in mouse TPM1κ, respectively.

Bottom Line: We have cloned the PCR amplified DNA and determined the nucleotide sequences.Conventional RT-PCR data as well as qRT-PCR data, calculating both absolute copy number and relative expression, revealed that the expression of TPM1 κ is significantly lower compared to TPM1 α in both mouse heart and skeletal muscle.To the best of our knowledge, this is the first report of the expression of TPM1 κ in mammalian skeletal muscle.

View Article: PubMed Central - PubMed

Affiliation: Department of Medicine, SUNY Upstate Medical University, 750 East Adams Street, Syracuse, NY 13210, USA.

ABSTRACT
We have investigated the expression of TPM1 α and TPM1 κ in mouse striated muscles. TPM1 α and TMP1 κ were amplified from the cDNA of mouse heart by using conventional RT-PCR. We have cloned the PCR amplified DNA and determined the nucleotide sequences. Deduced amino acid sequences show that there are three amino acid changes in mouse exon 2a when compared with the human TPM1 κ . However, the deduced amino acid sequences of human TPM1 α and mouse TPM1 α are identical. Conventional RT-PCR data as well as qRT-PCR data, calculating both absolute copy number and relative expression, revealed that the expression of TPM1 κ is significantly lower compared to TPM1 α in both mouse heart and skeletal muscle. It was also found that the expression level of TPM1 κ transcripts in mouse heart is higher than it is in skeletal muscle. To the best of our knowledge, this is the first report of the expression of TPM1 κ in mammalian skeletal muscle.

No MeSH data available.