Detection of EMMPRIN in the Trigeminal Ganglion in Rats
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The overall neuronal function is based on precise neuronal connections, which are considered to be mediated by common recognition strategies with guidance cues provided by adhesion molecules in combination with diffusible repellents and attractants1). It has been reported that extracellular matrix proteins, members of the immunoglobulin (Ig) superfamily, integrins, and cadherins can modulate the growth, differentiation and survival of various types of nerve cells2-9). Extracellular Matrix Metalloproteinase Inducer (EMMPRIN) is a highly glycosylated membrane protein belonging to the Ig superfamily10,11). EMMPRIN is composed of two immunoglobulin domains in the extracellular region, a single transmembrane domain and a short cytoplasmic domain containing 39 amino acids. The strong expression of EMMPRIN in the mouse and the rat has been detected in the brain as well as other organs, including testis, kidney, heart, liver, and small intestine10,12-15), suggesting that EMMPRIN in mammals has diverse biological functions. The trigeminal nerve conveys information through three main divisions, the ophthalmic, the maxillary, and the mandibular. A majority of the trigeminal sensory neurons have their cell bodies clustered in the trigeminal ganglia (TG)16). In mammals, the proportion of unmyelinated fibers to myelinated is much lower in trigeminal nerve branches than in spinal nerves. This unique characteristics in the trigeminal nerve may influence its response to injury. Therefore, an in-depth understanding of trigeminal molecular mechanisms may be required so that the diverse and complex clinical problems can be solved. Preliminary experiments demonstrated that EMMPRIN is active in expression at postnatal periods. The present study was investigated for the first time the localization of EMMPRIN and its function in the TG. Furthermore, changes in EMMPRIN expression was examined in the TG after surgical cut of branches of the trigeminal nerve as a model of nerve injury.
Abstract
The overall neuronal function is based on precise neuronal connections, which are considered to be mediated by common recognition strategies with guidance cues provided by adhesion molecules in combination with diffusible repellents and attractants1). It has been reported that extracellular matrix proteins, members of the immunoglobulin (Ig) superfamily, integrins, and cadherins can modulate the growth, differentiation and survival of various types of nerve cells2-9). Extracellular Matrix Metalloproteinase Inducer (EMMPRIN) is a highly glycosylated membrane protein belonging to the Ig superfamily10,11). EMMPRIN is composed of two immunoglobulin domains in the extracellular region, a single transmembrane domain and a short cytoplasmic domain containing 39 amino acids. The strong expression of EMMPRIN in the mouse and the rat has been detected in the brain as well as other organs, including testis, kidney, heart, liver, and small intestine10,12-15), suggesting that EMMPRIN in mammals has diverse biological functions. The trigeminal nerve conveys information through three main divisions, the ophthalmic, the maxillary, and the mandibular. A majority of the trigeminal sensory neurons have their cell bodies clustered in the trigeminal ganglia (TG)16). In mammals, the proportion of unmyelinated fibers to myelinated is much lower in trigeminal nerve branches than in spinal nerves. This unique characteristics in the trigeminal nerve may influence its response to injury. Therefore, an in-depth understanding of trigeminal molecular mechanisms may be required so that the diverse and complex clinical problems can be solved. Preliminary experiments demonstrated that EMMPRIN is active in expression at postnatal periods. The present study was investigated for the first time the localization of EMMPRIN and its function in the TG. Furthermore, changes in EMMPRIN expression was examined in the TG after surgical cut of branches of the trigeminal nerve as a model of nerve injury.
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