Disease relevance of MATN2

• Matrilin-2 expression distinguishes clinically relevant subsets of pilocytic astrocytoma [1].
• Matrilin-2 protein expression was similarly elevated in the majority of sporadic PA, but in only one neurofibromatosis 1-associated PA with an unusually aggressive clinical phenotype [1].

High impact information on MATN2

• Interestingly, a distinct heterotrimer consisting of three different chains was formed between matrilin-1, matrilin-2, and matrilin-4 [2].
• A group of 120-150-kDa bands was, after reduction, recognized specifically with an antiserum against the matrilin-2-glutathione S-transferase fusion protein in media of the matrilin-2-expressing cell lines [3].
• Interactions with some non-collagenous protein ligands were even stronger, with matrilin-2 binding to fibrillin-2, fibronectin and laminin-1-nidogen-1 complexes, with K (D) values in the range of 10(-8)-10(-11) M [4].
• Matrilin-2 interacts with itself and with other extracellular matrix proteins [4].
• Transcription of matrilin-2 mRNA in keratinocytes was enhanced by a diffusible factor produced by fibroblasts, suggesting a regulatory mechanism for the production of extracellular matrix at the dermal-epidermal junction [5].

Biological context of MATN2

• Here, we present the genomic organization of the highly conserved mouse and human MATN2 loci, which cover >100 kb and 167.167 kb genomic regions, respectively, and are composed of 19 exons [6].
• We mapped the matrilin-2 gene (MATN2) by fluorescence in situ hybridization at chromosome position 8q22 [7].
• Alternative splicing affected only 19 amino acids in a 75-moiety-long segment, unique to matrilin-2 [7].
• Further, we identified in the human matrilin-2 gene a U12 type AT-AC intron between the last two exons encoding the oligomerization domain [7].
• Matrilin-3 has a similar tissue distribution, while matrilin-2 and -4 occur in a wide variety of extracellular matrices [8].

Anatomical context of MATN2

• We isolated full-length cDNA clones for human matrilin-2, an oligomeric protein, which forms filamentous networks in the extracellular matrices of various tissues [7].
• In vivo, keratinocytes and fibroblasts were both found to express matrilin-2 mRNA and deposit the protein at the basal side of the dermal-epidermal basement membrane [5].
• These findings demonstrate that matrilin-2 is expressed in normal skin by keratinocytes and fibroblasts and may thus contribute to cutaneous homeostasis [5].
• Matrilin-2, formerly described as a component of hard and soft connective tissue matrices, was identified here also as a marker of cells with high differentiation potential: it is expressed predominantly by mesenchyme cells, prechondrocytes and preosteoblasts [9].

Other interactions of MATN2

• Primary structure of human matrilin-2, chromosome location of the MATN2 gene and conservation of an AT-AC intron in matrilin genes [7].
• The recombinant proteins, when used in interaction assays, showed affinity to matrilin-2 itself, but also to other collagenous and non-collagenous extracellular matrix proteins [4].
• In addition, immunoblotting and real-time reverse transcription polymerase chain reaction were used to investigate the expression of matrilin-2 in keratinocyte and fibroblast cultures [5].
• Matrilin-2 is a newly described member of the protein superfamily with von Willebrand factor A-like modules [5].

Analytical, diagnostic and therapeutic context of MATN2

• To examine the expression of matrilin-2 in human skin, the distribution of protein and mRNA was studied by immunohistochemistry and in situ hybridization [5].

References