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Matrilin-2 (matn2) contains a unique domain, between the second von Willebrandfactor A (vWFA) domain and the C-terminal coiled-coil domain, with no sequencehomology with other family members. Complementary DNA (cDNA) sequence analysisof matn2 expression in both mice and humans revealed an alternative splice sitein the region of the unique domain, which forms a short and a long splicing variant(containing an additional 19 amino acids). However, the expression heterogeneityof the alternative spliced variants, and the roles of the unique domain in oligomerizationand proteolysis of matn2 are unknown. In this study, we examined the expressionof the two alternative splice variants of matn2 in several skeletal and non-skeletaltissues by reverse transcription-polymerase chain reaction. Both splice variantsof matn2 were detected at the mRNA level in all tissues studied. To explore thebiochemical significance, several minigene constructs containing the second vWFAdomain, the unique domain (with either a long or short form) and the coiled-coildomain of mouse mini matn2 were generated. Ectopic expression of these constructsdemonstrated that the long form of matn2 is capable of self-assembling into severaloligomeric forms, including a tetramer, trimer, pentamer or multimer; but theshort form is only capable of forming a tetramer, trimer or dimer. Moreover, weobserved that the splice variants of matn2 are important in modulating matn2 cleavagewhen co-expressed with matrilin-1 or matrilin-3. These results indicate that thetwo alternative splice variants have distinct roles in the processes of post-translationalmodification of matn2, which may have an impact on the homeostasis of the matrilinfilamentous network of the extracellular matrix.

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