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Gene Review

Mylpf  -  myosin light chain, phosphorylatable, fast...

Rattus norvegicus

Synonyms: DTNB, Fast skeletal myosin light chain 2, G2, MLC-2, MLC2, ...
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Disease relevance of Mylpf

  • In an attempt to ascertain whether structural variants of MLC2 are expressed in hypertrophic heart muscle, we examined the RNAs from spontaneously hypertensive rat where there is a natural progression of hypertrophy associated with an increase in blood pressure [1].
  • On the basis of the nuclease S1 protection assay with uniformly labeled single-stranded pRLC429 DNA, subcloned into M13mp18 phage vector, we conclude that the rat atrial muscle also contains MLC2 of the ventricular type [1].
  • Because the response of cardiac hypertrophy is characterized by the induction of expression for muscle-specific genes, the effect of IGF-I on steady-state levels of mRNA for myosin light chain-2 (MLC-2) and troponin I and for skeletal and cardiac alpha-actin isoforms was evaluated by Northern blot analysis [2].
  • Apparent Km values for DTNB, Escherichia coli Trx, and rat Trx were 116, 34, and 3.7 microM, respectively [3].
  • To restrict expression to cardiomyocytes, we have constructed two recombinant adenoviruses (Ad-MLC2-250betagal and Ad-MLC2-2100betagal) containing the beta-galactosidase reporter gene under the control of the 250- or 2100-bp rat ventricle-specific cardiac myosin light chain-2v promoter (MLC-2v) [4].

High impact information on Mylpf


Chemical compound and disease context of Mylpf


Biological context of Mylpf

  • The predicted amino acid sequence for rat heart MLC2 showed a high homology with the sequences available for the chicken (83%) and human heart (80%) MLC2s [1].
  • We have isolated and characterized a cDNA recombinant plasmid (pRLC429) specific for the rat heart myosin light chain 2 (MLC2) [1].
  • The rat cardiac MLC-2 gene has seven exons which display complete conservation with the exon structure of the rat fast twitch skeletal MLC-2 gene [12].
  • A cultured myocardial cell model was used to examine the role of protein kinase C-dependent pathways in the transcriptional activation of two cardiac muscle genes [myosin light chain 2 (MLC-2) and atrial natriuretic factor (ANF)] during alpha-adrenergic receptor-mediated hypertrophy [13].
  • The effects of AA and ET together on phosphorylation of TnI or MLC2 were not additive.(ABSTRACT TRUNCATED AT 250 WORDS)[14]

Anatomical context of Mylpf

  • However, the homology between rat heart MLC2 and its counterpart in rat skeletal muscle is relatively low (67%) [1].
  • Thus, the gene encoding the putative smooth muscle RLC appears to have originated by duplication of the same ancestor that gave rise to the sarcomeric MLC-2 genes [6].
  • These studies show that EGF receptor activation is necessary but not sufficient for ANP and MLC2 responses to activation of G(q)-coupled receptors in ventricular myocytes, because inhibitory mechanisms can oppose such stimulation [15].
  • Utilizing this model of cardiac hypertrophy, we have examined the effects of alpha-adrenergic stimulation on the accumulation of sarcomeres and the expression of a rat cardiac myofibrillar gene, myosin light chain-2 (MLC-2) [16].
  • Receptor antibodies stimulated adipocyte glucose transport maximally but their effect, unlike that of insulin, was not inhibited by DTNB [17].

Associations of Mylpf with chemical compounds

  • Incubation with either PMA, AA, or ET resulted in similar increases in 32Pi incorporation into troponin I (TnI) and myosin light chain 2 (MLC2), which was inhibited by preincubation with the protein kinase C antagonist calphostin C [14].
  • Both oxidized and reduced glutathione influence inhibitory neurotransmission in a manner similar to that of the sulfhydryl redox agents dithiothreitol (DTT) and 5,5'-dithio-bis-(2-nitrobenzoic acid) (DTNB) [18].
  • The exception was 5,5'-dithiobis-(2-nitrobenzoic acid) (DTNB), which enhanced the number of insulin-binding sites up to 2-fold with no effect on the equilibrium constant [19].
  • A cell-impermeable reagent 5,5'-dithiobis(nitrobenzoic acid) (DTNB) had no effect on specific insulin binding but caused a dose-dependent decrease in both I-(S-S)-R and insulin-stimulated glucose transport [17].
  • However, active MKK inhibited phenylephrine- and Raf-1-induced expression from the ANF and MLC-2 promoters [7].

Regulatory relationships of Mylpf

  • These results suggest that PPAR alpha ligands have a potential to regulate MLC-2, which is a contractile protein in cardiomyocytes and may play a part of role in the pathogenesis of cardiac hypertrophy [20].

Other interactions of Mylpf

  • Expression of constitutively active MKK induce ERK2 kinase activity and caused expression from the c-Fos promoter, but did not significantly activate expression of reporter genes under the control of either the ANF or MLC-2 promoters [7].
  • IGF-I (10(-7) M) increased mRNA levels for MLC-2 and troponin I as early as 60 minutes with maximum levels by 6 hours, which were maintained for as long as 24 hours [2].
  • The finding that activated PKC increases cardiac gene transcription suggests that activation of this enzyme may be a proximal signal for coregulation of two cardiac genes, MLC-2 and ANF, during the course of myocardial cell hypertrophy [13].
  • A DNA sequence in the MLC-2 promoter that is a target for inhibition by active MKK, but not CL100, was mapped to a previously characterized DNA element (HF1) that is responsible for cardiac specificity [7].
  • Adrenomedullin partially blocked phenylephrine-mediated transcriptional activation of ANP and MLC-2 reporter gene expression in cardiomyocytes and this effect was mimicked by 2 microM forskolin, suggesting that this response was mediated via the activation of adenylate cyclase [21].

Analytical, diagnostic and therapeutic context of Mylpf

  • Following alpha-adrenergic stimulation, cultured myocardial cells displayed a severalfold increase in the number of sarcomeric units, as assessed by electron microscopy, an increase in cellular MLC-2 content, and a 2-3 fold increase in the steady state levels of MLC-2 mRNA [16].
  • Stimulation of myofibrillar gene expression by PGF2 alpha was demonstrated by Northern and Western blot analysis for myosin light chain-2 (MLC-2) and by transient transfection experiments with MLC-2 luciferase expression plasmids [22].
  • DTNB, an exogenous oxidizing agent, induced dose-dependent alleviation of thermal hyperalgesia in rats with CCI of the sciatic nerve and caused analgesia in sham-operated rats [8].
  • The envelope proteins of SR-11 virus were localized within the M segment ORF by amino-terminal sequence analysis of purified G1 and G2 [23].
  • We found that several epitopes defined by monoclonal antibodies to the G2 protein were highly conserved as detected by HAI tests and ELISA [24].


  1. Heart myosin light chain 2 gene. Nucleotide sequence of full length cDNA and expression in normal and hypertensive rat. Kumar, C.C., Cribbs, L., Delaney, P., Chien, K.R., Siddiqui, M.A. J. Biol. Chem. (1986) [Pubmed]
  2. Insulin-like growth factor-I induces hypertrophy with enhanced expression of muscle specific genes in cultured rat cardiomyocytes. Ito, H., Hiroe, M., Hirata, Y., Tsujino, M., Adachi, S., Shichiri, M., Koike, A., Nogami, A., Marumo, F. Circulation (1993) [Pubmed]
  3. A new selenoprotein from human lung adenocarcinoma cells: purification, properties, and thioredoxin reductase activity. Tamura, T., Stadtman, T.C. Proc. Natl. Acad. Sci. U.S.A. (1996) [Pubmed]
  4. Heart-specific targeting of beta-galactosidase by the ventricle-specific cardiac myosin light chain 2 promoter using adenovirus vectors. Griscelli, F., Gilardi-Hebenstreit, P., Hanania, N., Franz, W.M., Opolon, P., Perricaudet, M., Ragot, T. Hum. Gene Ther. (1998) [Pubmed]
  5. Allosteric modulation of the NMDA receptor by dihydrolipoic and lipoic acid in rat cortical neurons in vitro. Tang, L.H., Aizenman, E. Neuron (1993) [Pubmed]
  6. Cloning and characterization of mammalian myosin regulatory light chain (RLC) cDNA: the RLC gene is expressed in smooth, sarcomeric, and nonmuscle tissues. Taubman, M.B., Grant, J.W., Nadal-Ginard, B. J. Cell Biol. (1987) [Pubmed]
  7. Inhibition of a signaling pathway in cardiac muscle cells by active mitogen-activated protein kinase kinase. Thorburn, J., Carlson, M., Mansour, S.J., Chien, K.R., Ahn, N.G., Thorburn, A. Mol. Biol. Cell (1995) [Pubmed]
  8. Redox modulation of peripheral T-type Ca2+ channels in vivo: alteration of nerve injury-induced thermal hyperalgesia. Todorovic, S.M., Meyenburg, A., Jevtovic-Todorovic, V. Pain (2004) [Pubmed]
  9. Differential response of the NADH oxidase of plasma membranes of rat liver and hepatoma and HeLa cells to thiol reagents. Morré, D.J., Morré, D.M. J. Bioenerg. Biomembr. (1995) [Pubmed]
  10. Sulfhydryl oxidation reduces hippocampal susceptibility to hypoxia-induced spreading depression by activating BK channels. Hepp, S., Gerich, F.J., Müller, M. J. Neurophysiol. (2005) [Pubmed]
  11. Increased phosphorylation of myosin light chain associated with slow-to-fast transition in rat soleus. Bozzo, C., Stevens, L., Toniolo, L., Mounier, Y., Reggiani, C. Am. J. Physiol., Cell Physiol. (2003) [Pubmed]
  12. Structure, organization, and expression of the rat cardiac myosin light chain-2 gene. Identification of a 250-base pair fragment which confers cardiac-specific expression. Henderson, S.A., Spencer, M., Sen, A., Kumar, C., Siddiqui, M.A., Chien, K.R. J. Biol. Chem. (1989) [Pubmed]
  13. Transcriptional activation of the cardiac myosin light chain 2 and atrial natriuretic factor genes by protein kinase C in neonatal rat ventricular myocytes. Shubeita, H.E., Martinson, E.A., Van Bilsen, M., Chien, K.R., Brown, J.H. Proc. Natl. Acad. Sci. U.S.A. (1992) [Pubmed]
  14. Arachidonic acid-dependent phosphorylation of troponin I and myosin light chain 2 in cardiac myocytes. Damron, D.S., Darvish, A., Murphy, L., Sweet, W., Moravec, C.S., Bond, M. Circ. Res. (1995) [Pubmed]
  15. UTP transactivates epidermal growth factor receptors and promotes cardiomyocyte hypertrophy despite inhibiting transcription of the hypertrophic marker gene, atrial natriuretic peptide. Morris, J.B., Pham, T.M., Kenney, B., Sheppard, K.E., Woodcock, E.A. J. Biol. Chem. (2004) [Pubmed]
  16. Alpha 1-adrenergic stimulation of cardiac gene transcription in neonatal rat myocardial cells. Effects on myosin light chain-2 gene expression. Lee, H.R., Henderson, S.A., Reynolds, R., Dunnmon, P., Yuan, D., Chien, K.R. J. Biol. Chem. (1988) [Pubmed]
  17. Disulfide exchange between insulin and its receptor. A possible post-binding step in insulin action. Clark, S., Harrison, L.C. J. Biol. Chem. (1983) [Pubmed]
  18. Differential modulation by sulfhydryl redox agents and glutathione of GABA- and glycine-evoked currents in rat retinal ganglion cells. Pan, Z.H., Bähring, R., Grantyn, R., Lipton, S.A. J. Neurosci. (1995) [Pubmed]
  19. Enhancement of insulin binding to rat white adipocytes at 15 degrees C by 5,5'-dithiobis-(2-nitrobenzoic acid). Independence of the reagent's sulfhydryl group reactivity. Phillips, P.E., Lipkin, E.W., de Haën, C. J. Biol. Chem. (1988) [Pubmed]
  20. Peroxisome proliferator-activated receptor alpha (PPAR alpha) agonist, WY-14,643, increased transcription of myosin light chain-2 in cardiomyocytes. Hamano, T., Kobayashi, K., Sakairi, T., Hayashi, M., Mutai, M. The Journal of toxicological sciences. (2001) [Pubmed]
  21. Adrenomedullin is a regulated modulator of neonatal cardiomyocyte hypertrophy in vitro. Autelitano, D.J., Ridings, R., Tang, F. Cardiovasc. Res. (2001) [Pubmed]
  22. Prostaglandin F2 alpha stimulates hypertrophic growth of cultured neonatal rat ventricular myocytes. Adams, J.W., Migita, D.S., Yu, M.K., Young, R., Hellickson, M.S., Castro-Vargas, F.E., Domingo, J.D., Lee, P.H., Bui, J.S., Henderson, S.A. J. Biol. Chem. (1996) [Pubmed]
  23. Coding properties of the S and the M genome segments of Sapporo rat virus: comparison to other causative agents of hemorrhagic fever with renal syndrome. Arikawa, J., Lapenotiere, H.F., Iacono-Connors, L., Wang, M.L., Schmaljohn, C.S. Virology (1990) [Pubmed]
  24. Serological relationships among viruses in the Hantavirus genus, family Bunyaviridae. Chu, Y.K., Rossi, C., Leduc, J.W., Lee, H.W., Schmaljohn, C.S., Dalrymple, J.M. Virology (1994) [Pubmed]
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