|Budget Amount *help
¥6,400,000 (Direct Cost: ¥6,400,000)
Fiscal Year 1991: ¥800,000 (Direct Cost: ¥800,000)
Fiscal Year 1990: ¥5,600,000 (Direct Cost: ¥5,600,000)
In the human or mammalian saliva, more than 50 kinds of high molecular weight substances such as enzyme proteins, immunoglobulins and other specific proteins have been identified. The proteins in whole saliva are derived mainly from salivary glands secretion via the secretory granules of the gland cells. On the other hand, the secretory granules of salivary gland cells often display complex internal substructures, yet little is known of the molecular organization of their contents or the mechanisms involved in packaging of the secretory proteins. In the present study we used post-embedding immunogold labeling with antibodies to several secretory proteins of the human and mongolian gerbil salivary glands, to determine their distribution in the Golgi apparatus and secretory granules of the human and mongolian gerbil parotid and submandibular gland acinar cells. With antibodies to the amylase, proline-rich proteins and histatins, reactivity was found in the Golgi saccules, immature and mature secretory granules, but labeling with a monoclonal antibody to the agglutinin or a polyclonal antibody to the peroxidase, was found in the trans Golgi saccules, trans Golgi network, and immature and mature secretory granules, but not in the medial and cis Golgi saccules. These results suggest that there are two kinds of the protein synthetic pathway in the salivary gland acinar cells.