Expression of matrilin-2 in liver cirrhosis and hepatocellular carcinoma

Szabó, E; Páska, Cs; Lódi, Csaba; Batmunkh, Enkhjargal; Holczbauer, Ágnes; Korpos, Éva; Deák, F.; Kiss, Imrich; Kiss, András; Schaff, Z.

doi:10.1055/s-2005-869772

Cited by 3 publications

(4 citation statements)

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“…This complexity is three-fold. First, in the physiological condition, there are a mixture of different homo-oligomers and hetero-oligomers (8,11,13,16,17). These oligomers are participants of the extracellular matrix network (1-3).…”

Section: Discussionmentioning

confidence: 99%

“…Matn2 is one of the major components of basement membranes and a putative adaptor molecule of the extracellular matrix, which can form both collagen-dependent and collagen-independent filamentous networks (1)(2)(3)14,15), and has been involved in the reorganization of tissue architecture in liver cirrhosis and hepatocellular carcinoma (16), the balance of keratinocyte and fibroblasts in response to wounding (17), and participated in peripheral nerve regeneration (18), and is downregulated in the early phase of muscle injury and then increased in its late phase (19). Matn2 expression was elevated in the majority of cases of human sporadic pilocytic astrocyoma (20), liver cirrhosis and hepatocellular carcinoma (16). Seven putative Smad-binding sites exist within the human matn2 promoter as well as exon I (17).…”

Section: Discussionmentioning

confidence: 99%

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Distinct roles of two alternative splice variants of matrilin-2 in protein oligomerization and proteolysis

Zhang

Shao

Wang

et al. 2012

Molecular Medicine Reports

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Abstract. Matrilin-2 (matn2) contains a unique domain, between the second von Willebrand factor A (vWFA) domain and the C-terminal coiled-coil domain, with no sequence homology with other family members. Complementary DNA (cDNA) sequence analysis of matn2 expression in both mice and humans revealed an alternative splice site in the region of the unique domain, which forms a short and a long splicing variant (containing an additional 19 amino acids). However, the expression heterogeneity of the alternative spliced variants, and the roles of the unique domain in oligomerization and proteolysis of matn2 are unknown. In this study, we examined the expression of the two alternative splice variants of matn2 in several skeletal and non-skeletal tissues by reverse transcription-polymerase chain reaction. Both splice variants of matn2 were detected at the mRNA level in all tissues studied. To explore the biochemical significance, several minigene constructs containing the second vWFA domain, the unique domain (with either a long or short form) and the coiled-coil domain of mouse mini matn2 were generated. Ectopic expression of these constructs demonstrated that the long form of matn2 is capable of self-assembling into several oligomeric forms, including a tetramer, trimer, pentamer or multimer; but the short form is only capable of forming a tetramer, trimer or dimer. Moreover, we observed that the splice variants of matn2 are important in modulating matn2 cleavage when co-expressed with matrilin-1 or matrilin-3. These results indicate that the two alternative splice variants have distinct roles in the processes of post-translational modification of matn2, which may have an impact on the homeostasis of the matrilin filamentous network of the extracellular matrix. IntroductionMatrilin-2 (matn2) is the largest member of the matrilin family, with multiple domains of extracellular matrix protein, and plays a role in the formation of filamentous network structures and connects different molecules, such as collagens, other matrilins, aggrecan, small leucine-rich proteoglycans or cartilage oligomeric matrix protein (COMP), to form the extracellular macromolecular network with adaptor functions (1-3). Based on the analysis of the mouse matn2 sequence, the precursor containing 956 amino acids consists of an N-terminal putative signal peptide, two von Willebrand factor type A-like domains (vWFA) connected by 10 epidermal growth factor-like (EGF) repeats, one unique domain and a series of heptad repeats at its C-terminal coiledcoil domain; the predicted molecular mass is approximately 106.8 kDa (2-3). The vWFA domain is one of the ubiquitously distributed structural modules. There are seven vWFA domains in all four members of the matrilin family. The vWFA domain-containing molecules have been identified ubiquitously in the extracellular matrix, cell membrane and nucleus, and they participate in cell adhesion, protein-protein interaction and the formation of multiprotein complexes (4-5). The EGF domain is another ubiquitously distri...

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Distinct roles of two alternative splice variants of matrilin-2 in protein oligomerization and proteolysis

Zhang

Shao

Wang

et al. 2012

Molecular Medicine Reports

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“…Outside the CNS, MATN2 is a structural component of the ECM in many tissues, including the skin (18)(19)(20). Changes in MATN2 gene expression have further been linked to various inflammation-associated diseases, such as cancer and fibrosis; however, its specific functions remain unclear (21). In the context of peripheral nerve crush injury it has, however, been shown that Matn2 KO mice have delayed and incomplete recovery of neurological function and impaired axonal outgrowth, suggesting a potential role for MATN2 in peripheral nervous system repair (22).…”

Section: Introductionmentioning

confidence: 99%

Axonally derived matrilin-2 induces proinflammatory responses that exacerbate autoimmune neuroinflammation

Jonas¹,

Thiem²,

Wagener³

et al. 2014

J. Clin. Invest.

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“…Emellett májcirrózis és hepatocelluláris karcinóma esetén is expressziójának jelentős növekedését figyelték meg [56]. Fiziológiás körülmények között a portális erek falában található meg nagy mennyiségben, ami HCC esetén a tumor ereire jellemző inkább [56].…”

Section: áTtétek Képződése a Hepatocelluláris Karcinóma Soránunclassified

Talidomid analógok hatásának vizsgálata jelölésmentes szűrőrendszeren és a hepatocelluláris karcinóma egér modelljén

Nagy¹

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Expression of matrilin-2 in liver cirrhosis and hepatocellular carcinoma

Cited by 3 publications

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Distinct roles of two alternative splice variants of matrilin-2 in protein oligomerization and proteolysis

Distinct roles of two alternative splice variants of matrilin-2 in protein oligomerization and proteolysis

Axonally derived matrilin-2 induces proinflammatory responses that exacerbate autoimmune neuroinflammation

Talidomid analógok hatásának vizsgálata jelölésmentes szűrőrendszeren és a hepatocelluláris karcinóma egér modelljén

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