STUDIES OF CALRETININ IN PERIPHERAL ORGANS AND CELLS

研究了Calretinin在大鼠肠道系统中的存在和 背根神经节。胃、十二指肠、回肠、空肠、结肠和 用免疫荧光法检测大鼠盲肠组织中的 有钙维A(CR)阳性细胞和纤维存在。此外， 降钙素基因相关肽(CGRP)的存在或不存在，即 经常与感觉神经元相关的研究，使用 共定位免疫荧光以阐明其功能 钙调蛋白。铬阳性细胞体和纤维遍及整个范围。 奥尔巴赫神经丛和迈斯纳神经丛中的胃肠系统。这个 通过原位杂交证实了CRmRNA在这些细胞中的存在 细胞。在两个神经丛中均可见细小的CR+纤维。 环状和纵向肌层。特别有趣的是 肠系膜绒毛内可见CR+纤维。这些纤维 从绒毛底部到绒毛顶端，与CGRP共同定位 但并不仅限于血管的神经支配。偶尔使用CR 免疫组化显示阳性细胞散布在绒毛各处。 原位杂交。因为存在CGRP+/CR+的可能性 纤维起源于背根神经节，我们观察了 共同定位的区域。虽然协同定位确实存在，但其级别是 相当低。肾上腺皮质激素受体和降钙素基因相关肽在同一纤维中的共存 绒毛暗示了蛋白质的感官作用。CR的作用仍然是 尚不清楚，但对该蛋白质及其 与其他神经肽的共定位可能会产生信息进入ITS 功能。

The existence of calretinin was studied in the rat intestinal system and dorsal root ganglion. The stomach, duodenum, ileum, jejunum, colon and caecum from rats were examined using immunofluorescence to detect the presence of calretinin (CR) positive cells and fibers. In addition, the presence or absence of calcitonin gene related peptide (CGRP), which is frequently associated with sensory neurons was investigated, using colocalization immunofluorescence in order to elucidate the function of calretinin. CR+ cell bodies and fibers were found throughout the extent of the gastrointestinal system in the Auerbach's and Meissner's plexus. The presence of CR mRNA was confirmed with in situ hybridization in these cells. Fine CR+ fibers were found in both plexuses as well as in the circular and longitudinal muscle layers. Of particular interest was the presence of CR+fibers in the villi of the intestinal system. These fibers reach from the base to the tip of the villi and are colocalized with CGRP but are not limited to only innervation of blood vessels. Occasional CR positive cells were found scattered throughout the villus as visualized by in situ hybridization. As the possibility existed that the CGRP+/CR+ fibers originated in the dorsal root ganglion, we examined cells in this area for colocalization. While colocalization did exist, the levels were quite low. The colocalization of CR and CGRP in the same fibers in the villus suggests a sensory role for the protein. The role of CR is still unclear, but the continued examination of the protein and its colocalization with other neuropeptides may yield information into its function.