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Integrins are heterodimeric cell surface membrane proteins linking the extracellularmatrix to actin. α7B integrin is detected in proliferating and adult myofibers,whereas α7A plays a role in regenerating muscle fibers with a minor function inmature muscle fibers. The expression levels of β1A appear to be very low, whereasβ1D appears to be the predominant integrin form in mature muscle. Consideringthe important features of masseter muscle we have studied integrin expressionin masseter muscle specimens of surgical patients with posterior right crossbiteand comparing them to left side masseter muscle specimens. Our results showedthat the expression of integrins was significantly lower in the crossbite sidemuscle. Furthermore, the most important finding is that β1A is clearly detectablein adult masseter muscle. This behavior could be due to the particular compositionof masseter, since it contains hybrid fibers showing the capacity to modify thecontractile properties to optimize the energy efficiency or the action of themuscle during contraction. Moreover, masseter is characterized by a high turnoverof muscle fibers producing a regeneration process. This may indicate a longertime to heal, justifying the loss of β1D and the consequential increase of β1A.Thus, our data provide the first suggestion that integrins in masseter muscleplay a key role regulating the functional activity of muscle and allowing theoptimization of contractile forces.

Expression of muscle-specific integrins in masseter muscle fibers during malocclusion disease