Cytochemical localization of peroxidase activity in the submandibular salivary gland of the hamster

Bloom, Gunnar D.; Carlsöö, Bengt; Kumlien, A.

doi:10.1007/bf00277457

Cited by 27 publications

(5 citation statements)

References 22 publications

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“…A large number of other soluble peroxidases have also been purified and characterized [5][6][7][8][9][10][11][12]. In histochemical studies, peroxidases of rat salivary, lacrimal and lactating mammary glands, called LPOs [13][14][15][16], are immunologically identical with the peroxidases from bovine salivary, lacrimal and Harderian glands [3,5,17]. Peroxidases isolated from sheep and goat milk and human saliva are also immunologically similar to LPO [7][8][9][18][19][20][21][22].…”

Section: Introductionmentioning

confidence: 99%

Characterization of sheep lacrimal-gland peroxidase and its major physiological electron donor

Mazumdar

Chatterjee

Adak

et al. 1996

Biochemical Journal

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A soluble sheep lacrimal-gland peroxidase was purified to apparent homogeneity. It had a native molecular mass of 75 kDa with a subunit molecular mass of 82 kDa and an isoelectric point of 6.5. Western blotting showed that it shares some of the enzyme antigenic determinants in common with other soluble peroxidases. The enzyme exhibits a Soret peak at 410 nm which is shifted to 431 nm by 5 equiv. of H2O2 due to the formation of compound II. The latter is, however, unstable and gradually returns to the native state. The enzyme forms complexes with CN- and N3- and is reduced by dithionite showing a characteristic reduced peroxidase spectrum. Although the enzyme oxidizes I-, SCN- and Br- optimally at pH 5.5., 5.25 and 5.0 respectively, at physiological pH, it oxidizes I- and SCN- only. Since extracellular SCN- concentration is much higher than I-, SCN- may act as the major electron donor to the enzyme. The second-order rate constants for the reaction of the enzyme with H2O2 (k+1) and of compound I with SCN- (k+2) were 4 X 10(7) M-1 X s-1 and 8.1 X 10(5) M-1 X s-1 respectively. A plot of log Vmax against pH yields a sigmoidal curve consistent with a single ionizable group on the enzyme with a pK(a) value of 5.75, controlling thiocyanate oxidation. In a coupled system with the peroxidase, H2O2, SCN-, GSH, NADPH and glutathione reductase, peroxidase-catalysed SCN- oxidation by H2O2 could be coupled to NADPH consumption. The system is proposed to operate in vivo for the efficient elimination of endogenous H2O2.

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Section: Introductionmentioning

confidence: 99%

Characterization of sheep lacrimal-gland peroxidase and its major physiological electron donor

Mazumdar

Chatterjee

Adak

et al. 1996

Biochemical Journal

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“…By enzyme histochemistry, peroxidase activity has been localized to the acini of mature parotid and submandibular glands of human beings (Riva et al, 1978) and rodents (Strum and Karnovsky, 1969;Bloom et al, 1970;Herzog and Miller, 1970). The onset and subsequent changes in the accumulation of peroxidase activity in the developing submandibular glands of rat (Strum, 1971;Yamashina and Barka, 1972,1974Cutler et al, 1977) and mouse (Osugi, 1977) have been delineated both morphologically and biochemically.…”

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confidence: 99%

Chronology of peroxidase activity in the developing rat parotid gland

Redman

Field

1993

Anat. Rec.

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The course of development of salivary peroxidase, an enzyme that has an important role in oral defense mechanisms, has been well documented in rat submandibular glands. However, the only report on salivary peroxidase activity in the other major salivary glands of the rat has been a cytochemical study of the adult parotid gland. In the present investigation, the accumulation of salivary peroxidase activity in developing parotid glands of rats was followed both biochemically and cytochemically. Specific activity (units per mg protein) attributable to salivary peroxidase began at 1 day after birth, then rose rapidly but unevenly, with peaks at 21 and 70 days, and no difference between the sexes at any age. Activity per gland increased progressively to 42 days in both sexes and was significantly higher in males at 70 days. The cytochemical observations on peroxidase activity localized to the rough endoplasmic reticulum and secretory granules of the developing acini were well correlated with the biochemical findings. Peroxidase-negative cells occurred in immature acini at 1 and 7 days, but only in the intercalated ducts thereafter. This observation suggests that the acini are a source of some of the ductal cells, at least during early postnatal development. The developmental pattern of specific activity differed from those of other rat parotid secretory enzymes, indicating that control of their synthesis during development is noncoordinate. The patterns of specific activity of the parotid and submandibular glands were complementary, suggesting that their combined secretions may supply biologically significant peroxidase activity to the oral cavities of rats throughout postnatal development.

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“…It is generally accepted that the secretory endpiece of the hamster submandibular gland comprises only seromucous secretory cells. Bloom et al, () and Mukunoki () reported PO activity of the secretory granules in the granular duct cells of the hamster submandibular gland (Pinkstaff, ), but no activity was observed in the acinar cells. After fixation of the tissue with a low concentration of glutaraldehyde and incubation in the DAB reaction medium with 0.01% H 2 O 2 , we succeeded in detecting PO activity in the acinar cells as well as in the granular duct cells.…”

Section: Discussionmentioning

confidence: 99%

“…Histochemically, endogenous PO activity has been localized to acini of human mature parotid and submandibular glands (Riva et al, ), rodents (Carlsöö et al, ; Herzog and Miller, ; Moriguchi et al, ; Strum and Karnovsky, ) and Suncus murinus , Insectivora (Moriguchi et al, ). In hamster submandibular gland, Bloom et al () and Mukunoki () reported PO activity of secretory granules in the granular duct cells of the hamster submandibular gland, but no activity was observed in the acinar cells. However, we succeeded in detecting the PO reaction in the acinar cells as well as in the granular duct cells.…”

Section: Introductionmentioning

confidence: 99%

Confocal laser scanning microscopic analysis of ectopic sublingual gland-like tissue inside the hamster submandibular gland

Moriguchi

Utsumi

Ohno

2013

Microsc. Res. Tech.

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Based on its histochemical properties, the secretory portion of the hamster submandibular gland has been classified as seromucous cells. The presence of endogenous peroxidase (PO) reaction was shown in the nuclear envelope, cisternae of endoplasmic reticulum and Golgi apparatus. The 3,3'-diaminobenzidene, tetrahydrochloride (DAB) method revealed bipartite secretory granules containing a PO-positive dense core surrounded by a less dense halo in these cells. In the present investigation, serous and mucous-like cells were found in resin-embedded semi-thin sections of the DAB-reacted hamster submandibular gland. These sections were already on glass slides for routine light microscopic observations, therefore electron microscopic analysis could be unrealizable. We then used reflectance-mode confocal laser scanning microscopy to visualize additional sites of PO activity as detected in these sections. Using this approach, we found mucous cells with PO activity-negative secretory granules and seromucous cells with PO activity-positive spot-like secretory granules of the regular sublingual gland most frequently adjacent to the serous cells with typical electron-dense secretory granules. These cells clearly differ from the seromucous cells with bipartite secretory granules and the granular duct cells with typical electron-dense secretory granules of the hamster submandibular gland. Additionally, secretory endpieces of the ectopic sublingual gland-like tissue empty into the duct of the hamster submandibular gland lobule. Thus, our findings suggest that a mass of sublingual gland tissue extends into the hamster submandibular gland during its development, and PO may be synthesized and secreted into the same duct.

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Cytochemical localization of peroxidase activity in the submandibular salivary gland of the hamster

Cited by 27 publications

References 22 publications

Characterization of sheep lacrimal-gland peroxidase and its major physiological electron donor

Characterization of sheep lacrimal-gland peroxidase and its major physiological electron donor

Chronology of peroxidase activity in the developing rat parotid gland

Confocal laser scanning microscopic analysis of ectopic sublingual gland-like tissue inside the hamster submandibular gland

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