Jump to content

CSRP3

This article was updated by an external expert under a dual publication model. The corresponding peer-reviewed article was published in the journal Gene. Click to view.
From Wikipedia, the free encyclopedia
(Redirected from CSRP3 (gene))

CSRP3
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesCSRP3, CLP, CMD1M, CMH12, CRP3, LMO4, MLP, cysteine and glycine rich protein 3
External IDsOMIM: 600824; MGI: 1330824; HomoloGene: 20742; GeneCards: CSRP3; OMA:CSRP3 - orthologs
Orthologs
SpeciesHumanMouse
Entrez

8048

13009

Ensembl

ENSG00000129170

ENSMUSG00000030470

UniProt

P50461

P50462

RefSeq (mRNA)

NM_003476
NM_001369404

NM_001198841
NM_013808

RefSeq (protein)

NP_003467

NP_001185770
NP_038836

Location (UCSC)Chr 11: 19.18 – 19.21 MbChr 7: 48.48 – 48.5 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Cysteine and glycine-rich protein 3 also known as cardiac LIM protein (CLP) or muscle LIM protein (MLP) is a protein that in humans is encoded by the CSRP3 gene.[5]

CSRP3 IS a small 194 amino acid protein, which is specifically expressed in skeletal and cardiac muscle.[6][7] In rodents, CSRP3 has also been found to be expressed in neurons.[8]

Gene

[edit]

The CSRP3 gene was discovered in rat in 1994.[5] In humans it was mapped to chromosome 11p15.1,[9][10] where it spans a 20kb genomic region, organized in 6 exons. The full length transcript is 0.8kb,[9][11] while a splice variant, originating from the alternative splicing of exons 3 and 4, was recently identified and designated MLP-b.[12]

Structure

[edit]

MLP contains two LIM domains (LIM1 and LIM2), each being surrounded by glycine-rich regions, and the two separated by more than 50 residues.[13] LIM domains offer a remarkable ability for protein-protein interactions.[14] Furthermore, MLP carries a nuclear localization signal at amino acid positions 64-69 [15] MLP can be acetylated/deacetylated at the position 69 lysine residue (K69), by acetyltransferase (PCAF) and histone deacetylase 4 (HDAC4), respectively.[16] In myocytes, MLP has the ability to oligomerize, forming dimers, trimers and tetramers, an attribute that impacts its interactions, localization and function.[17]

Protein interactions and localization

[edit]

MLP has been identified to bind to an increasing list of proteins, exhibiting variable subcellular localization and diverse functional properties. In particular, MLP interacts with proteins at the:

  1. Z-line, including telethonin (T-cap), alpha-actinin (ACTN), cofilin-2 (CFL2), calcineurin, HDAC4, MLP-b as well as to MLP itself;[11][12][16][18][19][20][21]
  2. costameres, where it binds to zyxin, integrin linked kinase (ILK) and beta1-spectrin;[18][22][23]
  3. intercalated discs, where it associates with the nebulin-related anchoring protein (NRAP);[24]
  4. nucleus, where it binds to the transcription factors MyoD, myogenin and MRF4.[25]

M-line as well as plasma membrane localization of MLP has also been observed, however, the protein associations mediating this subcellular distribution are currently unknown.[17][26] These diverse localization patterns and binding partners of MLP suggest a multitude of roles relating both to the striated myocyte cytoskeleton and the nucleus.[27] The role of MLP in each of these two cellular compartments appears to be dynamic, with studies demonstrating nucleocytoplasmic shuttling, driven by its nuclear localization signal, over time and under different conditions.[27]

Function

[edit]

In the nucleus, MLP acts as a positive regulator of myogenesis and promotes myogenic differentiation.[5] Overexpression of MLP enhances myotube differentiation, an effect attributed to the direct association of MLP with muscle specific transcription factors such as MyoD, myogenin and MRF4 and consequently the transcriptional control of fundamental muscle-specific genes.[5][12][25] In the cytoplasm, MLP is an important scaffold protein, implicated in various cytoskeletal macromolecular complexes, at the sarcomeric Z-line, the costameres, and the microfilaments.[11][12][16][18][19][20][21] At the Z-line, MLP interacts with different Z-line components [11][12][16][18][19][20][21][28][29] and acts as a scaffold protein promoting the assembly of macromolecular complexes along sarcomeres and actin-based cytoskeleton [11][22][24][30][31] Moreover, since the Z-line acts as a stretch sensor,[32][33][34][35] MLP is believed to be involved in mechano-signaling processes. Indeed, cardiomyocytes from MLP transgenic or knock-out mouse exhibit defective intrinsic stretch responses, due to selective loss of passive stretch sensing.[11][26] At the costameres, another region implicated in force transmission, MLP is thought to be contributing in mechanosensing through its interactions with β1 spectrin and zyxin. However, the precise role of MLP at the costameres has not been extensively investigated yet.

At the microfilaments, MLP is implicated in actin remodeling (or actin dynamics) through its interaction with cofilin-2 (CFL2). Binding of MLP to CFL2 enhances the CFL2-dependent F-actin depolymerization,[19] with a recent study demonstrating that MLP can act directly on actin cytoskeleton dynamics through direct binding that stabilizes and crosslinks actin filaments into bundles.[36]

Additionally, MLP is indirectly related to calcium homeostasis and energy metabolism. Specifically, acetylation of MLP increases the calcium sensitivity of myofilaments and regulates contractility,[16] while the absence of MLP causes alterations in calcium signaling (intracellular calcium handling) with defects in excitation-contraction coupling.[37][38][39] Furthermore, lack of MLP leads to local loss of mitochondria and energy deficiency.[40]

Animal studies

[edit]

In rodents, MLP is transiently expressed in amacrine cells of the retina during postnatal development.[41] In the adult nervous system it is expressed upon axonal injury,[42] where it plays an important role during regenerative processes, functioning as an actin cross-linker, thereby facilitating filopodia formation and increasing growth cone motility.[8]

Clinical significance

[edit]

MLP is directly associated with striated muscle diseases.[43] Mutations in the CSRP3 gene have been detected in patients with dilated cardiomyopathy (DCM) [e.g. G72R and K69R], and hypertrophic cardiomyopathy (HCM) [e.g. L44P, S46R, S54R/E55G, C58G, R64C, Y66C, Q91L, K42/fs165], while the most frequent MLP mutation, W4R, has been found in both of these patient populations.[11][15][26][44][45][46][47] Biochemical and functional studies have been performed for some of these mutant proteins, and reveal aberrant localization and interaction patterns, leading to impaired molecular and cellular functions. For example, the W4R mutation abolishes the MLP/T-cap interaction, leading to mislocalization of T-cap, Z-line instability and severe sarcomeric structural defects.[11] The C58G mutation causes reduced protein stability due to enhanced ubiquitin-dependent proteasome degradation[44] while the K69L mutation, which is within the predicted nuclear localization signal of MLP, abolishes the MLP/α-actinin interaction and causes altered subcellular distribution of the mutant protein, showing predominant perinuclear localization.[47] Alterations in the protein expression levels of MLP, its oligomerization or splicing have also been described in human cardiac and skeletal muscle diseases: both MLP protein levels and oligomerization are down-regulated in human heart failure,[17][20] while MLP levels are significantly changed in different skeletal myopathies, including facioscapulohumeral muscular dystrophy, nemaline myopathy and limb girdle muscular dystrophy type 2B.[48][49][50] Moreover, significant changes in MLP-b protein expression levels, as well as deregulation of the MLP:MLP-b ratio have been detected in limb girdle muscular dystrophy type 2A, Duchenne muscular dystrophy and dermatomyositis patients.[12]

Animal models

[edit]

Animal models are providing insight into MLP's function in striated muscle. Ablation of Mlp (MLP-/-) in mice affects all striated muscles, although the cardiac phenotype is more severe, leading to alterations in cardiac pressure and volume, aberrant contractility, development of dilated cardiomyopathy with hypertrophy and progressive heart failure.[31][37][51] At the histological level there is dramatic disruption of the cardiomyocyte cytoarchitecture at multiple levels, and pronounced fibrosis.[24][31][39][52] Other cellular changes included alterations in intracellular calcium handling, local loss of mitochondria and energy deficiency.[37][38][39] Crossing MLP-/- mice with phospholamban (PLN) -/-, or β2-adrenergic receptor (β2-AR) -/-, or angiotensin II type 1a receptor (AT1a) -/-, or β-adrenergic receptor kinase 1 inhibitor (bARK1) -/- mice, as well as overexpressing calcineurin rescued their cardiac function, through a series of only partly understood molecular mechanisms.[53][54][55][56][57] Conversely crossing MLP-/- mice with β1-adrenergic receptor (β1-AR) -/- mice was lethal, while crossing MLP-/- mice with calcineurin -/- mice, enhanced fibrosis and cardiomyopathy.[53][54] A gene knockin mouse model harboring the human MLP-W4R mutation developed HCM and heart failure, while ultrastructural analysis of its cardiac tissue revealed myocardial disarray and significant fibrosis, increased nuclear localization of MLP concomitantly with reduced sarcomeric Z-line distribution.[26] Alterations in MLP nucleocytoplasmic shuttling, which are possibly modulated by changes in its oligomerization status, have also been implicated in hypertrophy and heart failure, independently of mutations.[17][27] Studies in Drosophila revealed that genetic ablation of Mlp84B, the Drosophila homolog of MLP, was associated with pupal lethality and impaired muscle function.[28] Mechanical studies of Mlp84B-null flight muscles indicate that loss of Mlp84B results in decreased muscle stiffness and power generation.[58] Cardiac-specific ablation of Mlp84B caused decreased lifespan, impaired diastolic function and disturbances in cardiac rhythm.[59] Overall, these animal models have provided critical evidence on the functional significance of MLP in striated muscle physiology and pathophysiology.

Notes

[edit]

References

[edit]
  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000129170 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000030470 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ a b c d Arber S, Halder G, Caroni P (October 1994). "Muscle LIM protein, a novel essential regulator of myogenesis, promotes myogenic differentiation". Cell. 79 (2): 221–31. doi:10.1016/0092-8674(94)90192-9. PMID 7954791. S2CID 26650433.
  6. ^ Gehmlich K, Geier C, Milting H, Fürst D, Ehler E (2008). "Back to square one: what do we know about the functions of muscle LIM protein in the heart?". Journal of Muscle Research and Cell Motility. 29 (6–8): 155–8. doi:10.1007/s10974-008-9159-4. PMID 19115046. S2CID 9251900.
  7. ^ Knöll R, Hoshijima M, Chien KR (2001). "Muscle LIM protein in heart failure". Experimental and Clinical Cardiology. 7 (2–3): 104–5. PMC 2719181. PMID 19649232.
  8. ^ a b Levin E, Leibinger M, Gobrecht P, Hilla A, Andreadaki A, Fischer D (January 2019). "Muscle LIM Protein Is Expressed in the Injured Adult CNS and Promotes Axon Regeneration". Cell Reports. 26 (4): 1021–1032.e6. doi:10.1016/j.celrep.2018.12.026. PMID 30673598.
  9. ^ a b Fung YW, Wang R, Liew CC (June 1996). "Characterization of a human cardiac gene which encodes for a LIM domain protein and is developmentally expressed in myocardial development". Journal of Molecular and Cellular Cardiology. 28 (6): 1203–10. doi:10.1006/jmcc.1996.0111. PMID 8782062.
  10. ^ Fung YW, Wang RX, Heng HH, Liew CC (August 1995). "Mapping of a human LIM protein (CLP) to human chromosome 11p15.1 by fluorescence in situ hybridization". Genomics. 28 (3): 602–3. doi:10.1006/geno.1995.1200. PMID 7490106.
  11. ^ a b c d e f g h Knöll R, Hoshijima M, Hoffman HM, Person V, Lorenzen-Schmidt I, Bang ML, Hayashi T, Shiga N, Yasukawa H, Schaper W, McKenna W, Yokoyama M, Schork NJ, Omens JH, McCulloch AD, Kimura A, Gregorio CC, Poller W, Schaper J, Schultheiss HP, Chien KR (December 2002). "The cardiac mechanical stretch sensor machinery involves a Z disc complex that is defective in a subset of human dilated cardiomyopathy". Cell. 111 (7): 943–55. doi:10.1016/s0092-8674(02)01226-6. PMID 12507422. S2CID 15082967.
  12. ^ a b c d e f Vafiadaki E, Arvanitis DA, Papalouka V, Terzis G, Roumeliotis TI, Spengos K, Garbis SD, Manta P, Kranias EG, Sanoudou D (July 2014). "Muscle lim protein isoform negatively regulates striated muscle actin dynamics and differentiation". The FEBS Journal. 281 (14): 3261–79. doi:10.1111/febs.12859. PMC 4416226. PMID 24860983.
  13. ^ Weiskirchen R, Pino JD, Macalma T, Bister K, Beckerle MC (December 1995). "The cysteine-rich protein family of highly related LIM domain proteins". The Journal of Biological Chemistry. 270 (48): 28946–54. doi:10.1074/jbc.270.48.28946. PMID 7499425.
  14. ^ Buyandelger B, Ng KE, Miocic S, Piotrowska I, Gunkel S, Ku CH, Knöll R (July 2011). "MLP (muscle LIM protein) as a stress sensor in the heart". Pflügers Archiv. 462 (1): 135–42. doi:10.1007/s00424-011-0961-2. PMC 3114083. PMID 21484537.
  15. ^ a b Bos JM, Poley RN, Ny M, Tester DJ, Xu X, Vatta M, Towbin JA, Gersh BJ, Ommen SR, Ackerman MJ (May 2006). "Genotype-phenotype relationships involving hypertrophic cardiomyopathy-associated mutations in titin, muscle LIM protein, and telethonin". Molecular Genetics and Metabolism. 88 (1): 78–85. doi:10.1016/j.ymgme.2005.10.008. PMC 2756511. PMID 16352453.
  16. ^ a b c d e Gupta MP, Samant SA, Smith SH, Shroff SG (April 2008). "HDAC4 and PCAF bind to cardiac sarcomeres and play a role in regulating myofilament contractile activity". The Journal of Biological Chemistry. 283 (15): 10135–46. doi:10.1074/jbc.M710277200. PMC 2442284. PMID 18250163.
  17. ^ a b c d Boateng SY, Belin RJ, Geenen DL, Margulies KB, Martin JL, Hoshijima M, de Tombe PP, Russell B (January 2007). "Cardiac dysfunction and heart failure are associated with abnormalities in the subcellular distribution and amounts of oligomeric muscle LIM protein". American Journal of Physiology. Heart and Circulatory Physiology. 292 (1): H259–69. doi:10.1152/ajpheart.00766.2006. PMID 16963613. S2CID 9591608.
  18. ^ a b c d Louis HA, Pino JD, Schmeichel KL, Pomiès P, Beckerle MC (October 1997). "Comparison of three members of the cysteine-rich protein family reveals functional conservation and divergent patterns of gene expression". The Journal of Biological Chemistry. 272 (43): 27484–91. doi:10.1074/jbc.272.43.27484. PMID 9341203.
  19. ^ a b c d Papalouka V, Arvanitis DA, Vafiadaki E, Mavroidis M, Papadodima SA, Spiliopoulou CA, Kremastinos DT, Kranias EG, Sanoudou D (November 2009). "Muscle LIM protein interacts with cofilin 2 and regulates F-actin dynamics in cardiac and skeletal muscle". Molecular and Cellular Biology. 29 (22): 6046–58. doi:10.1128/MCB.00654-09. PMC 2772566. PMID 19752190.
  20. ^ a b c d Zolk O, Caroni P, Böhm M (June 2000). "Decreased expression of the cardiac LIM domain protein MLP in chronic human heart failure". Circulation. 101 (23): 2674–7. doi:10.1161/01.cir.101.23.2674. PMID 10851202.
  21. ^ a b c Heineke J, Ruetten H, Willenbockel C, Gross SC, Naguib M, Schaefer A, Kempf T, Hilfiker-Kleiner D, Caroni P, Kraft T, Kaiser RA, Molkentin JD, Drexler H, Wollert KC (February 2005). "Attenuation of cardiac remodeling after myocardial infarction by muscle LIM protein-calcineurin signaling at the sarcomeric Z-disc". Proceedings of the National Academy of Sciences of the United States of America. 102 (5): 1655–60. Bibcode:2005PNAS..102.1655H. doi:10.1073/pnas.0405488102. PMC 547821. PMID 15665106.
  22. ^ a b Flick MJ, Konieczny SF (May 2000). "The muscle regulatory and structural protein MLP is a cytoskeletal binding partner of betaI-spectrin". Journal of Cell Science. 113 (9): 1553–64. doi:10.1242/jcs.113.9.1553. PMID 10751147.
  23. ^ Postel R, Vakeel P, Topczewski J, Knöll R, Bakkers J (June 2008). "Zebrafish integrin-linked kinase is required in skeletal muscles for strengthening the integrin-ECM adhesion complex". Developmental Biology. 318 (1): 92–101. doi:10.1016/j.ydbio.2008.03.024. PMID 18436206.
  24. ^ a b c Ehler E, Horowits R, Zuppinger C, Price RL, Perriard E, Leu M, Caroni P, Sussman M, Eppenberger HM, Perriard JC (May 2001). "Alterations at the intercalated disk associated with the absence of muscle LIM protein". The Journal of Cell Biology. 153 (4): 763–72. doi:10.1083/jcb.153.4.763. PMC 2192386. PMID 11352937.
  25. ^ a b Kong Y, Flick MJ, Kudla AJ, Konieczny SF (August 1997). "Muscle LIM protein promotes myogenesis by enhancing the activity of MyoD". Molecular and Cellular Biology. 17 (8): 4750–60. doi:10.1128/mcb.17.8.4750. PMC 232327. PMID 9234731.
  26. ^ a b c d Knöll R, Kostin S, Klede S, Savvatis K, Klinge L, Stehle I, Gunkel S, Kötter S, Babicz K, Sohns M, Miocic S, Didié M, Knöll G, Zimmermann WH, Thelen P, Bickeböller H, Maier LS, Schaper W, Schaper J, Kraft T, Tschöpe C, Linke WA, Chien KR (March 2010). "A common MLP (muscle LIM protein) variant is associated with cardiomyopathy". Circulation Research. 106 (4): 695–704. doi:10.1161/CIRCRESAHA.109.206243. PMID 20044516.
  27. ^ a b c Boateng SY, Senyo SE, Qi L, Goldspink PH, Russell B (October 2009). "Myocyte remodeling in response to hypertrophic stimuli requires nucleocytoplasmic shuttling of muscle LIM protein". Journal of Molecular and Cellular Cardiology. 47 (4): 426–35. doi:10.1016/j.yjmcc.2009.04.006. PMC 2739242. PMID 19376126.
  28. ^ a b Clark KA, Bland JM, Beckerle MC (June 2007). "The Drosophila muscle LIM protein, Mlp84B, cooperates with D-titin to maintain muscle structural integrity". Journal of Cell Science. 120 (Pt 12): 2066–77. doi:10.1242/jcs.000695. PMID 17535853. S2CID 23791613.
  29. ^ Clark KA, Kadrmas JL (June 2013). "Drosophila melanogaster muscle LIM protein and alpha-actinin function together to stabilize muscle cytoarchitecture: a potential role for Mlp84B in actin-crosslinking". Cytoskeleton. 70 (6): 304–16. doi:10.1002/cm.21106. PMC 3716849. PMID 23606669.
  30. ^ Arber S, Caroni P (February 1996). "Specificity of single LIM motifs in targeting and LIM/LIM interactions in situ". Genes & Development. 10 (3): 289–300. doi:10.1101/gad.10.3.289. PMID 8595880.
  31. ^ a b c Arber S, Hunter JJ, Ross J, Hongo M, Sansig G, Borg J, Perriard JC, Chien KR, Caroni P (February 1997). "MLP-deficient mice exhibit a disruption of cardiac cytoarchitectural organization, dilated cardiomyopathy, and heart failure". Cell. 88 (3): 393–403. doi:10.1016/s0092-8674(00)81878-4. PMID 9039266. S2CID 16597001.
  32. ^ Frank D, Frey N (March 2011). "Cardiac Z-disc signaling network". The Journal of Biological Chemistry. 286 (12): 9897–904. doi:10.1074/jbc.R110.174268. PMC 3060542. PMID 21257757.
  33. ^ Gautel M (February 2011). "The sarcomeric cytoskeleton: who picks up the strain?". Current Opinion in Cell Biology. 23 (1): 39–46. doi:10.1016/j.ceb.2010.12.001. PMID 21190822.
  34. ^ Luther PK (2009). "The vertebrate muscle Z-disc: sarcomere anchor for structure and signalling". Journal of Muscle Research and Cell Motility. 30 (5–6): 171–85. doi:10.1007/s10974-009-9189-6. PMC 2799012. PMID 19830582.
  35. ^ Buyandelger B, Ng KE, Miocic S, Gunkel S, Piotrowska I, Ku CH, Knöll R (June 2011). "Genetics of mechanosensation in the heart". Journal of Cardiovascular Translational Research. 4 (3): 238–44. doi:10.1007/s12265-011-9262-6. PMC 3098994. PMID 21360311.
  36. ^ Hoffmann C, Moreau F, Moes M, Luthold C, Dieterle M, Goretti E, Neumann K, Steinmetz A, Thomas C (August 2014). "Human muscle LIM protein dimerizes along the actin cytoskeleton and cross-links actin filaments". Molecular and Cellular Biology. 34 (16): 3053–65. doi:10.1128/MCB.00651-14. PMC 4135597. PMID 24934443.
  37. ^ a b c Esposito G, Santana LF, Dilly K, Cruz JD, Mao L, Lederer WJ, Rockman HA (December 2000). "Cellular and functional defects in a mouse model of heart failure". American Journal of Physiology. Heart and Circulatory Physiology. 279 (6): H3101–12. doi:10.1152/ajpheart.2000.279.6.H3101. PMID 11087268. S2CID 2090600.
  38. ^ a b Kemecsei P, Miklós Z, Bíró T, Marincsák R, Tóth BI, Komlódi-Pásztor E, Barnucz E, Mirk E, Van der Vusse GJ, Ligeti L, Ivanics T (September 2010). "Hearts of surviving MLP-KO mice show transient changes of intracellular calcium handling". Molecular and Cellular Biochemistry. 342 (1–2): 251–60. doi:10.1007/s11010-010-0492-8. PMID 20490897. S2CID 33877175.
  39. ^ a b c Su Z, Yao A, Zubair I, Sugishita K, Ritter M, Li F, Hunter JJ, Chien KR, Barry WH (June 2001). "Effects of deletion of muscle LIM protein on myocyte function". American Journal of Physiology. Heart and Circulatory Physiology. 280 (6): H2665–73. doi:10.1152/ajpheart.2001.280.6.H2665. PMID 11356623. S2CID 12682659.
  40. ^ van den Bosch BJ, van den Burg CM, Schoonderwoerd K, Lindsey PJ, Scholte HR, de Coo RF, van Rooij E, Rockman HA, Doevendans PA, Smeets HJ (February 2005). "Regional absence of mitochondria causing energy depletion in the myocardium of muscle LIM protein knockout mice". Cardiovascular Research. 65 (2): 411–8. doi:10.1016/j.cardiores.2004.10.025. PMID 15639480.
  41. ^ Levin E, Leibinger M, Andreadaki A, Fischer D (2014-06-19). "Neuronal expression of muscle LIM protein in postnatal retinae of rodents". PLOS ONE. 9 (6): e100756. Bibcode:2014PLoSO...9j0756L. doi:10.1371/journal.pone.0100756. PMC 4063954. PMID 24945278.
  42. ^ Levin E, Andreadaki A, Gobrecht P, Bosse F, Fischer D (April 2017). "Nociceptive DRG neurons express muscle lim protein upon axonal injury". Scientific Reports. 7 (1): 643. Bibcode:2017NatSR...7..643L. doi:10.1038/s41598-017-00590-1. PMC 5428558. PMID 28377582.
  43. ^ Vafiadaki E, Arvanitis DA, Sanoudou D (July 2015). "Muscle LIM Protein: Master regulator of cardiac and skeletal muscle functions". Review. Gene. 566 (1): 1–7. doi:10.1016/j.gene.2015.04.077. PMC 6660132. PMID 25936993.
  44. ^ a b Geier C, Gehmlich K, Ehler E, Hassfeld S, Perrot A, Hayess K, Cardim N, Wenzel K, Erdmann B, Krackhardt F, Posch MG, Osterziel KJ, Bublak A, Nägele H, Scheffold T, Dietz R, Chien KR, Spuler S, Fürst DO, Nürnberg P, Ozcelik C (September 2008). "Beyond the sarcomere: CSRP3 mutations cause hypertrophic cardiomyopathy". Human Molecular Genetics. 17 (18): 2753–65. doi:10.1093/hmg/ddn160. PMID 18505755.
  45. ^ Geier C, Perrot A, Ozcelik C, Binner P, Counsell D, Hoffmann K, Pilz B, Martiniak Y, Gehmlich K, van der Ven PF, Fürst DO, Vornwald A, von Hodenberg E, Nürnberg P, Scheffold T, Dietz R, Osterziel KJ (March 2003). "Mutations in the human muscle LIM protein gene in families with hypertrophic cardiomyopathy". Circulation. 107 (10): 1390–5. doi:10.1161/01.cir.0000056522.82563.5f. PMID 12642359.
  46. ^ Hershberger RE, Parks SB, Kushner JD, Li D, Ludwigsen S, Jakobs P, Nauman D, Burgess D, Partain J, Litt M (May 2008). "Coding sequence mutations identified in MYH7, TNNT2, SCN5A, CSRP3, LBD3, and TCAP from 313 patients with familial or idiopathic dilated cardiomyopathy". Clinical and Translational Science. 1 (1): 21–6. doi:10.1111/j.1752-8062.2008.00017.x. PMC 2633921. PMID 19412328.
  47. ^ a b Mohapatra B, Jimenez S, Lin JH, Bowles KR, Coveler KJ, Marx JG, Chrisco MA, Murphy RT, Lurie PR, Schwartz RJ, Elliott PM, Vatta M, McKenna W, Towbin JA, Bowles NE (2002). "Mutations in the muscle LIM protein and alpha-actinin-2 genes in dilated cardiomyopathy and endocardial fibroelastosis". Molecular Genetics and Metabolism. 80 (1–2): 207–15. doi:10.1016/s1096-7192(03)00142-2. PMID 14567970.
  48. ^ Sanoudou D, Corbett MA, Han M, Ghoddusi M, Nguyen MA, Vlahovich N, Hardeman EC, Beggs AH (September 2006). "Skeletal muscle repair in a mouse model of nemaline myopathy". Human Molecular Genetics. 15 (17): 2603–12. doi:10.1093/hmg/ddl186. PMC 3372923. PMID 16877500.
  49. ^ von der Hagen M, Laval SH, Cree LM, Haldane F, Pocock M, Wappler I, Peters H, Reitsamer HA, Hoger H, Wiedner M, Oberndorfer F, Anderson LV, Straub V, Bittner RE, Bushby KM (December 2005). "The differential gene expression profiles of proximal and distal muscle groups are altered in pre-pathological dysferlin-deficient mice". Neuromuscular Disorders. 15 (12): 863–77. doi:10.1016/j.nmd.2005.09.002. PMID 16288871. S2CID 8690648.
  50. ^ Winokur ST, Chen YW, Masny PS, Martin JH, Ehmsen JT, Tapscott SJ, van der Maarel SM, Hayashi Y, Flanigan KM (November 2003). "Expression profiling of FSHD muscle supports a defect in specific stages of myogenic differentiation". Human Molecular Genetics. 12 (22): 2895–907. doi:10.1093/hmg/ddg327. PMID 14519683.
  51. ^ Omens JH, Usyk TP, Li Z, McCulloch AD (February 2002). "Muscle LIM protein deficiency leads to alterations in passive ventricular mechanics". American Journal of Physiology. Heart and Circulatory Physiology. 282 (2): H680–7. doi:10.1152/ajpheart.00773.2001. PMID 11788418. S2CID 9501573.
  52. ^ Wilson AJ, Schoenauer R, Ehler E, Agarkova I, Bennett PM (January 2014). "Cardiomyocyte growth and sarcomerogenesis at the intercalated disc". Cellular and Molecular Life Sciences. 71 (1): 165–81. doi:10.1007/s00018-013-1374-5. PMC 3889684. PMID 23708682.
  53. ^ a b Fajardo G, Zhao M, Urashima T, Farahani S, Hu DQ, Reddy S, Bernstein D (October 2013). "Deletion of the β2-adrenergic receptor prevents the development of cardiomyopathy in mice". Journal of Molecular and Cellular Cardiology. 63: 155–64. doi:10.1016/j.yjmcc.2013.07.016. PMC 3791213. PMID 23920331.
  54. ^ a b Heineke J, Wollert KC, Osinska H, Sargent MA, York AJ, Robbins J, Molkentin JD (June 2010). "Calcineurin protects the heart in a murine model of dilated cardiomyopathy". Journal of Molecular and Cellular Cardiology. 48 (6): 1080–7. doi:10.1016/j.yjmcc.2009.10.012. PMC 2891089. PMID 19854199.
  55. ^ Minamisawa S, Hoshijima M, Chu G, Ward CA, Frank K, Gu Y, Martone ME, Wang Y, Ross J, Kranias EG, Giles WR, Chien KR (October 1999). "Chronic phospholamban-sarcoplasmic reticulum calcium ATPase interaction is the critical calcium cycling defect in dilated cardiomyopathy". Cell. 99 (3): 313–22. doi:10.1016/s0092-8674(00)81662-1. PMID 10555147. S2CID 1299470.
  56. ^ Rockman HA, Chien KR, Choi DJ, Iaccarino G, Hunter JJ, Ross J, Lefkowitz RJ, Koch WJ (June 1998). "Expression of a beta-adrenergic receptor kinase 1 inhibitor prevents the development of myocardial failure in gene-targeted mice". Proceedings of the National Academy of Sciences of the United States of America. 95 (12): 7000–5. Bibcode:1998PNAS...95.7000R. doi:10.1073/pnas.95.12.7000. PMC 22717. PMID 9618528.
  57. ^ Yamamoto R, Akazawa H, Ito K, Toko H, Sano M, Yasuda N, Qin Y, Kudo Y, Sugaya T, Chien KR, Komuro I (December 2007). "Angiotensin II type 1a receptor signals are involved in the progression of heart failure in MLP-deficient mice". Circulation Journal. 71 (12): 1958–64. doi:10.1253/circj.71.1958. PMID 18037754.
  58. ^ Clark KA, Lesage-Horton H, Zhao C, Beckerle MC, Swank DM (August 2011). "Deletion of Drosophila muscle LIM protein decreases flight muscle stiffness and power generation". American Journal of Physiology. Cell Physiology. 301 (2): C373–82. doi:10.1152/ajpcell.00206.2010. PMC 3154547. PMID 21562304.
  59. ^ Mery A, Taghli-Lamallem O, Clark KA, Beckerle MC, Wu X, Ocorr K, Bodmer R (January 2008). "The Drosophila muscle LIM protein, Mlp84B, is essential for cardiac function". The Journal of Experimental Biology. 211 (Pt 1): 15–23. doi:10.1242/jeb.012435. PMID 18083727.
[edit]
Retrieved from "https://en.wikipedia.org/w/index.php?title=CSRP3&oldid=1250181300"