Nuclear matrix

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In biology, the nuclear matrix is the network of fibres found throughout the inside of a cell nucleus and is somewhat analogous to the cell cytoskeleton. However, in contrast to the cytoskeleton, the nuclear matrix has been proposed to be a highly dynamic structure, perhaps more like a dynamic sponge with open compartments for free diffusion of molecules in the nucleus.[citation needed] The nuclear matrix, along with the nuclear lamina aid in organizing the genetic information within the cell.

The exact function of this matrix is still disputed, and its very existence has recently been called into question.[1] Evidence for such a structure was recognised as long ago as 1948 (Zbarskii and Debov), and consequently many proteins associated with the matrix have been discovered. The presence of intra-cellular proteins is largely indisputable, and it is well recognized that proteins such as the Scaffold, or Matrix Associated Proteins (SAR or MAR) have some role in the organisation of chromatins. There is evidence that the nuclear matrix is involved in regulation of gene expression in Arabidopsis thaliana.[2]

Justification of the nuclear matrix hypothesis[edit]

For a long time the question whether a polymer meshwork, a “nuclear matrix” or “nuclear-scaffold” or "NuMat"[3] is an essential component of the in vivo nuclear architecture has remained a matter of debate. While there are arguments that the relative position of chromosome territories (CTs), the equivalent of condensed metaphase chromosomes at interphase, may be maintained due to steric hindrance or electrostatic repulsion forces between the apparently highly structured CT surfaces, this concept has to be reconciled with observations according to which cells treated with the classical matrix-extraction procedures maintain defined territories up to the point where a minor subset of acidic nuclear matrix proteins is released – very likely those proteins that governed their association with the nuclear skeleton.[citation needed] The nuclear matrix proteome consists of structural proteins, chaperones, DNA/RNA-binding proteins, chromatin remodeling and transcription factors. The complexity of NuMat is an indicator of its diverse structural and functional significance.[3]

S/MARs (scaffold/matrix attachment elements), the DNA regions that are thought to attach genomic DNA to the nuclear skeleton, show an ever increasing spectrum of established biological activities. All these activities are in agreement with (or most easily explained by) the nuclear matrix hypothesis. This is one justification for maintaining this concept before equally plausible alternative models emerge.[citation needed]

S/MARs find increasing use for the rational design of vectors with widespread use in gene therapy and biotechnology. Nowadays S/MAR functions can be modulated, improved and custom-tailored to the specific needs of novel vector systems.[citation needed]

Nuclear matrix and cancer[edit]

The nuclear matrix composition on human cells has been proven to be cell type and tumor specific. It has been clearly demonstrated that the nuclear matrix composition in a tumor is different from its normal counterparts.[4] This fact could be useful to characterize cancer markers and to predict the disease even earlier. These markers have been found in urine and blood and could potentially be used in early detection and prognosis of human cancers.[citation needed]

See also[edit]


  1. ^ Pederson T (March 2000). "Half a century of "the nuclear matrix"". Molecular Biology of the Cell. 11 (3): 799–805. doi:10.1091/mbc.11.3.799. PMC 14811. PMID 10712500.
  2. ^ Tetko IV, Haberer G, Rudd S, Meyers B, Mewes HW, Mayer KF (March 2006). "Spatiotemporal expression control correlates with intragenic scaffold matrix attachment regions (S/MARs) in Arabidopsis thaliana". PLoS Computational Biology. 2 (3): e21. Bibcode:2006PLSCB...2...21T. doi:10.1371/journal.pcbi.0020021. PMC 1420657. PMID 16604187.
  3. ^ a b Kallappagoudar S, Varma P, Pathak RU, Senthilkumar R, Mishra RK (September 2010). "Nuclear matrix proteome analysis of Drosophila melanogaster". Molecular & Cellular Proteomics. 9 (9): 2005–18. doi:10.1074/mcp.M110.001362. PMC 2938118. PMID 20530634.
  4. ^ Rynearson AL, Sussman CR (June 2011). "Nuclear structure, organization, and oncogenesis". Journal of Gastrointestinal Cancer. 42 (2): 112–7. doi:10.1007/s12029-011-9253-5. PMID 21286858.

Further reading[edit]