Comparison of Cyclic AMP-dependent Protein Kinases from Salivary Glands of Four Species

Dowd, Frank J.; Cheung, Peter H.; Warren, J; Faerber, T.; Traub, Darren

doi:10.1177/00220345850640100401

Cited by 6 publications

(2 citation statements)

References 13 publications

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“…The intensity of acinar cell labeling ( Table 2) was greatest with antibodies to RII, which is consistent with biochemical studies demonstrating that the type I1 isoenzyme of cAPK is more abundant than the type I isoenzyme in the rat parotid gland (Baum et al, 1981;Dowd et al, 1985;Schwoch et al, 1985). Moreover, the labeling of secretory granules was also greater with anti-RII than anti-RI, which parallels our observations on photoaffinity labeling of R subunits in parotid saliva (Mednieks and Hand, 1984;Mednieks et al, 1987).…”

Section: Lmmunogold Labeling With Polyclonal Antibodiessupporting

confidence: 83%

Localization of cellular regulatory proteins using postembedding immunogold labeling

Hand

Jungmann

1989

Am. J. Anat.

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Cyclic AMP-dependent protein kinase (cAPK) mediates the effects of catecholamines and hormones that cause elevation of intracellular cyclic AMP levels. The holoenzyme is a tetramer consisting of catalytic (C) and cyclic AMP-binding regulatory (R) subunits. The type I and type II cAPK isoenzymes are defined by R subunits (RI and RII) of differing molecular weight, primary structure, and cyclic AMP-binding properties. Postembedding immunogold labeling procedures and specific polyclonal and monoclonal antibodies to RI, RII, and C were used to study the subcellular distribution of cAPK subunits in several tissues. In the rat parotid gland, both RI and RII were present in the cytoplasm, nuclei, and secretory granules of the acinar cells, whereas secretory granules of intercalated and striated duct cells were poorly labeled. These results confirmed that the acinar secretory granules are the source of R subunits previously identified in saliva by specific photoaffinity labeling techniques. Zymogen granules of pancreatic acinar cells and secretory granules of seminal vesicle cells were labeled with antibody to RII. Pancreatic and seminal fluids were shown to contain cyclic AMP-binding proteins. The granules of several endocrine cells (pituitary, pancreatic islet, intestinal) also labeled with RII antibody. Double labeling of ovarian granulosa cells showed that both RI and C were present in the nuclei and cytoplasm. The localization of cAPK subunits revealed by postembedding immunogold labeling is consistent with the postulated regulatory functions of these proteins in gene expression, cell proliferation, exocytosis, and various metabolic events The widespread occurrence of cAPK subunits in secretory granules and their release to the extracellular environment suggests that they play an important role in secretory cell function.

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Section: Lmmunogold Labeling With Polyclonal Antibodiessupporting

confidence: 83%

Localization of cellular regulatory proteins using postembedding immunogold labeling

Hand

Jungmann

1989

Am. J. Anat.

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“…rats (Cong et al 2013(Cong et al , 2015Ding et al 2013;Shi et al 2014;Li et al 2015;Mei et al 2015;Mellas et al 2015;Wang et al 2016). However, the morphological and biochemical characteristics of salivary glands differ among species (Dreizen et al 1968;Dowd et al 1985;Dardick et al 1990). Thus, it is important to identify an experimental animal whose salivary glands are similar to those of humans.…”

Section: Discussionmentioning

confidence: 99%

Expression patterns of tight junction proteins in porcine major salivary glands: a comparison study with human and murine glands

et al. 2018

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Tight junction (TJ) proteins play a dynamic role in paracellular fluid transport in salivary gland epithelia. Most TJ studies are carried out in mice and rats. However, the morphology of rodent salivary glands differs from that of human glands. This study aimed to compare the histological features and the expression pattern of TJ proteins in porcine salivary glands with those of human and mouse. The results showed that porcine parotid glands were pure serous glands. Submandibular glands (SMGs) were serous acinar cell-predominated mixed glands, whereas sublingual glands were mucous acinar cell-predominated. Human SMGs were mixed glands containing fewer mucous cells than porcine SMGs, whereas the acinar cells of murine SMGs are seromucous. The histological features of the duct system in the porcine and human SMGs were similar and included intercalated, striated and excretory ducts, but the murine SMG contained a specific structure, the granular convoluted tubule. TJ proteins, including claudin-1 to claudin-12, occludin and zonula occludin-1 (ZO-1), were detected in the porcine major salivary glands and human SMGs by RT-PCR; however, claudin-6, claudin-9 and claudin-11 were not detected in the murine SMG. As shown by immunofluorescence, claudin-1, claudin-3, claudin-4, occludin and ZO-1 were distributed in both acinar and ductal cells in the porcine and human SMGs, whereas claudin-1 and claudin-3 were mainly present in acinar cells, and claudin-4 was mainly distributed in ductal cells in the murine SMG. In addition, 3D images showed that the TJ proteins arranged in a honeycomb-like structure on the luminal surface of the ducts, whereas their arrangements in acini were irregular in porcine SMGs. In summary, the expression pattern of TJ proteins in salivary glands is similar between human and miniature pig, which may be a candidate animal for studies on salivary gland TJ function.

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Salivary Mucin Secretion

Quissell

Tabak

1989

Comprehensive Physiology

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Comparison of Cyclic AMP-dependent Protein Kinases from Salivary Glands of Four Species

Cited by 6 publications

References 13 publications

Localization of cellular regulatory proteins using postembedding immunogold labeling

Localization of cellular regulatory proteins using postembedding immunogold labeling

Expression patterns of tight junction proteins in porcine major salivary glands: a comparison study with human and murine glands

Salivary Mucin Secretion

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