Amylase and lysozyme differentiate their localization within the serous secretory granule of the human salivary gland.

Machino, Mitsuo; Morioka, Hiroyuki; Tachibana, Masayoshi

doi:10.1267/ahc.19.329

Cited by 9 publications

(10 citation statements)

References 11 publications

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“…Amylase and salivary agglutinin [recently demonstrated to be identical to the lung scavenger receptor cysteine-rich protein gp-340 (Prakobphol et al 2000)] are present in the rER, Golgi complex, and in forming and mature granules of parotid and submandibular serous cells (Takano et al 1991(Takano et al ,1993. Acidic proline-rich proteins and the proline-rich polypeptide P-C also are present in the secretory granules of these cells (Takano et al 1993;Kimura et al 1998), and lysozyme and cyclic AMP receptor proteins are present in the serous granules of all three major salivary glands (Machino et al 1986;Miyazaki et al 2001;Piludu et al 2002). In many species, including humans, the secretory granules of serous salivary gland cells display a variety of substructures (reviewed in Tandler and Phillips 1993).…”

Section: Discussionmentioning

confidence: 99%

Immunocytochemical Localization of Histatins in Human Salivary Glands

Ahmad

Piludu

Oppenheim

et al. 2004

J Histochem Cytochem.

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Connecticut (ARH)S U M M A R Y Histatins are a family of salivary proteins with bactericidal and fungicidal activities that contribute to the innate defense of the oral cavity. Histatins are present in the serous granules of the parotid and submandibular glands. The important role of histatins in saliva, and the limited information on their cellular and subcellular distribution, prompted us to further define the localization of histatins in the major salivary glands. Immunogold-silver staining of 1-m sections of plastic-embedded tissue with anti-histatin antibody revealed histatin immunoreactivity in the serous acinar cells of the parotid and submandibular glands, the serous demilune cells of the submandibular and sublingual glands, and in occasional intercalated duct cells. No reactivity was seen in mucous cells or in striated or excretory duct cells. Electron microscopic observations of thin sections labeled with anti-histatin and gold-labeled secondary antibodies revealed immunoreactivity associated with the rough endoplasmic reticulum and Golgi complex and in secretory granules of serous acinar and demilune cells. The granules of parotid acinar cells exhibited relatively uniform labeling of their content, whereas the granules of serous cells in the submandibular and sublingual glands showed variable labeling of the dense and light regions of their content. A few intercalated duct cells adjacent to the acinar cells also exhibited labeled granules. These results suggest that the serous cells of the major glands are the main source of histatins in human saliva. They are also consistent with several previous studies demonstrating the variable distribution of different proteins within the granule content.

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Section: Discussionmentioning

confidence: 99%

Immunocytochemical Localization of Histatins in Human Salivary Glands

Ahmad

Piludu

Oppenheim

et al. 2004

J Histochem Cytochem.

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“…Earlier studies using postembedding immunoperoxidase or immunogold techniques on conventionally embedded specimens have demonstrated lysozyme in the secretory granules of serous cells in human parotid and submaxillary (Machino et al 1986), bronchial, nasal, and laryngotracheal glands (Bowes and Corrin 1977;Spicer et al 1977;Tachibana et al 1984), as well as in rat and human Paneth cell granules (Spicer et al 1977;Montero and Erlandsen 1978;Franken et al 1989;Montero and Segura 1989;Stirling 1992). In all of these publications, lysozyme antigenicity was confined solely to the secretory granules of the various serous epithelial cells.…”

Section: Discussionmentioning

confidence: 98%

“…Post-embedding immunolabeling techniques have been applied to routinely processed (mostly GA and osmiumfixed, epoxy-embedded) tissue for demonstrating lysozyme (Erlandsen et al 1974;Bowes and Corrin 1977;Pincus and Said 1977;Tachibana et al 1984;Machino et al 1986;Resnitzky et al 1994).…”

Section: Discussionmentioning

confidence: 99%

“…Muramidase in tears, saliva, milk, and in the secretions of the digestive, respiratory and genital tracts probably represents synthesis by the corresponding epithelial cells (Mason and Taylor 1975;Bowes and Corrin 1977;Pincus and Said 1977;Spicer et al 1977;Montero and Erlandsen 1978;Machino et al 1984Machino et al , 1986Franken et al 1989;Haller et al 1992).…”

Section: Introductionmentioning

confidence: 99%

“…On the other hand, Klockars and Osserman (1974) and Mason and Taylor (1975) did not detect any lysozyme expression in the rat or human parotid gland. Using protein A-gold immunocytochemistry, Machino et al (1986) established lysozyme labeling in the electron opaque central core of serous secretory granules in osmicated Epon sections of human parotid and submandibular glands. Regrettably, these authors did not describe its cellular distribution.…”

Section: Introductionmentioning

confidence: 99%

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Lysozyme expression in the rat parotid gland: light and electron microscopic immunogold studies

Staneva-Dobrovski

1997

Histochemistry and Cell Biology

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Lysozyme (muramidase) is capable of direct bacteriolytic action by hydrolyzing glycosidic bonds in bacterial cell walls. Although it is broadly distributed in vertebrate tissues and secretions, the cellular and subcellular localizations of the enzyme are still not well known. The present study examines the distribution of lysozyme expression in the various cell types of LR gold-embedded rat parotid gland, applying a postembedding immunogold-silver staining technique for light microscopy. Simultaneously, a postembedding immunogold method for electron microscopy was used to determine the cellular compartments engaged in the biosynthesis and exocytosis of lysozyme. Silver-amplified immunogold staining for lysozyme demonstrated identical localization in both paraffin and semithin LR-gold sections: in the supranuclear parts of acinar and intercalated duct cells. Staining intensity varied even between adjacent cells. In the electron microscope, immunogold labeling was detected over the cell compartments associated with protein synthesis and exocytosis in acinar and intercalated duct cells. Lysozyme antigenic sites were visible over endoplasmic reticulum and throughout the Golgi apparatus, being intense over the trans-Golgi network, but even stronger in the condensing vacuoles and most prominent over secretory granules in both cell types. The findings provide the first immunocytochemical evidence of the synthesis and secretion of lysozyme in parotid acinar and intercalated duct cells.

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Differential distribution of salivary agglutinin and amylase in the Golgi apparatus and secretory granules of human salivary gland acinar cells

et al. 1991

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The secretory granules of salivary glands 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. We used post-embedding immunogold labeling with antibodies to two secretory proteins, agglutinin and alpha-amylase, to determine their distribution in the Golgi apparatus and secretory granules of the human submandibular gland acinar cells. With monoclonal antibodies specific for carbohydrate epitopes of the agglutinin, reactivity was found in the trans Golgi saccules, trans Golgi network, and immature and mature secretory granules. In the granules, labeling was seen in regions of low and medium electron density, but not in the dense cores. Reactivity seen on the apical and basolateral membranes of acinar and duct cells was attributed to a shared epitope on a membrane glycoprotein. Labeling with a polyclonal antibody to amylase was found in the Golgi saccules, immature and mature secretory granules, but not in the trans Golgi network. In the granules, amylase was present in the dense cores and in areas of medium density, but not in the regions of low density. These results indicate that these two proteins are distributed differently within the secretory granules, and suggest that they follow separate pathways between the Golgi apparatus and forming secretory granules. Small vesicles and tubular structures that labeled only with the antibodies to the agglutinin were observed on both faces of the Golgi apparatus and in the vicinity of the cell membrane. These structures may represent constitutive secretion vesicles involved in transport of the putative membrane glycoprotein to the cell membrane.

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Amylase and lysozyme differentiate their localization within the serous secretory granule of the human salivary gland.

Cited by 9 publications

References 11 publications

Immunocytochemical Localization of Histatins in Human Salivary Glands

Immunocytochemical Localization of Histatins in Human Salivary Glands

Lysozyme expression in the rat parotid gland: light and electron microscopic immunogold studies

Differential distribution of salivary agglutinin and amylase in the Golgi apparatus and secretory granules of human salivary gland acinar cells

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