Immunohistochemical localization of dipeptidyl aminopeptidase (DAP) IV in the rat submandibular gland during postnatal development

1981 ◽  
Vol 72 (2) ◽  
pp. 229-236 ◽  
Author(s):  
N. Sahara ◽  
K. M. Fukasawa ◽  
K. Fukasawa ◽  
N. Araki ◽  
K. Suzuki
Keyword(s):  
Postnatal Development ◽  
Submandibular Gland ◽  
Immunohistochemical Localization ◽  
Dipeptidyl Aminopeptidase ◽  
Rat Submandibular Gland

Immunohistochemical localization of kallikreins in the rat submandibular gland

Life Sciences ◽  
1975 ◽  
Vol 16 (5) ◽  
pp. 789-790
Author(s):  
Torill Berg Ørstavik ◽  
Per Brandtzaeg ◽  
Kjell Nustad ◽  
Kaare Gautvik
Keyword(s):  
Submandibular Gland ◽  
Immunohistochemical Localization ◽  
Rat Submandibular Gland

scholarly journals Developmental distribution of microperoxisomes in the rat submandibular gland.

1978 ◽  
Vol 26 (11) ◽  
pp. 989-999 ◽  
Author(s):  
B A Mooradian ◽  
L S Cutler
Keyword(s):  
Postnatal Development ◽  
Submandibular Gland ◽  
Acinar Cell ◽  
Secretory Cell ◽  
Fold Increase ◽  
Duct Cells ◽  
Size Number ◽  
Tubule Cells ◽  
Prenatal And Postnatal Development ◽  
Rat Submandibular Gland

The present study investigated the size, number, and distribution of microperoxisomes (MP) during the prenatal and postnatal development of the rat submandibular gland (SMG). A three-fold increase in MP number per cell was observed in the cells of the rudiment from the 15th to the 16th day of gestation. The early secretory and striated duct cells contained about 9.0 MP. The number of MP per secretory cell decreased such that 3.5 MP were found in each mature acinar cell. In the striated duct cells, MP number progressively increased to 40.0. As the convoluted granular tubule cells (CGT) developed from striated duct cells there was an increase in MP number from 16.0 to 26.0/cell. At maturity, the convoluted granular tubule cells contained only 14.0 MP. Throughout development of the SMG, intercalated duct cells showed only rare MP. The data suggests that the number, size, and distribution of MP changes as a function of the particular path of differentiation followed by the various cells in the rat SMG.

scholarly journals Immunohistochemical localization of rat submandibular gland esterase B (homologous to the RSKG-7 kallikrein gene) in relation to other serine proteases of the kallikrein family.

1992 ◽  
Vol 40 (1) ◽  
pp. 83-92 ◽  
Author(s):  
T Berg ◽  
I Wassdal ◽  
K Sletten
Keyword(s):  
Submandibular Gland ◽  
Serine Proteases ◽  
Cross Reactivity ◽  
Immunohistochemical Localization ◽  
Staining Reaction ◽  
Anatomic Distribution ◽  
Family Gene ◽  
Terminal Amino ◽  
Rat Submandibular Gland

The rat submandibular gland contains several members of the kallikrein family. In the present study we purified and raised an antiserum against one of these enzymes, i.e., esterase B, which was first described by Khullar et al. in 1986. N-terminal amino acid analysis revealed complete homology between esterase B and the kallikrein family gene RSKG-7. For characterization of the antiserum, flat-bed isoelectrofocusing with immunoblotting was superior to immunoelectrophoresis and double immunodiffusion in detecting and identifying crossreacting proteins. This was due to the fact that kallikrein-like enzymes were readily separated by isoelectrofocusing, and immunoreactivity was easily detected by the sensitive peroxidase-anti-peroxidase staining after blotting onto nitrocellulose membrane. Immunohistochemical controls were carried out accordingly, including homologous as well as crossreacting antigens. In the submandibular gland, esterase B was detected exclusively in all granular convoluted tubular cells, co-localized with tissue kallikrein and tonin. Some staining was also observed in striated duct cells; however, this staining reaction was induced by cross-reactivity with kallikrein, since staining was abolished by addition of kallikrein as well as esterase B to the primary antiserum. It was therefore concluded that like tonin and antigen gamma, but unlike kallikrein, esterase B was not detected in the striated ducts of the submandibular, parotid, or sublingual glands. This separation in anatomic distribution between esterase B and kallikrein may indicate that prokallikrein activation is not the only biological function of esterase B.

Effects of chemical sympathectomy on postnatal development of the rat submandibular gland

1988 ◽  
Vol 33 (2) ◽  
pp. 127-134
Author(s):  
L.S. Cutler ◽  
Constance P. Christian ◽  
B. Bottaro
Keyword(s):  
Postnatal Development ◽  
Submandibular Gland ◽  
Chemical Sympathectomy ◽  
Rat Submandibular Gland

Acinar structure and membrane regionalization as a prerequisite for exocrine secretion in the rat submandibular gland

1985 ◽  
Vol 78 (1) ◽  
pp. 67-85
Author(s):  
A. Segawa ◽  
N. Sahara ◽  
K. Suzuki ◽  
S. Yamashina
Keyword(s):  
Submandibular Gland ◽  
Exocrine Secretion ◽  
Synthetic Activity ◽  
Inhibitory Effects ◽  
Acinar Structure ◽  
Immuno Histochemistry ◽  
Secretory Products ◽  
Microfilament System ◽  
Dipeptidyl Aminopeptidase ◽  
Rat Submandibular Gland

The significance of glandular organization in exocrine secretion was examined by analysing the functional and morphological features of the dissociated rat submandibular gland with special reference to the acinar structure and luminal specialization. The digestion of the gland with collagenase (C preparation) produced relatively large cellular masses having well-preserved acinar structures. When EGTA and the proteolytic enzyme Dispase were added to the C preparation (CED preparation), the gland was dissociated into small cellular aggregates in which the acinar structure disintegrated. Upon stimulation with either isoproterenol or dibutyryl cyclic AMP, a large amount of peroxidase, one of the secretory products of the rat submandibular gland, was released from C-treated cells, while discharged peroxidase was greatly reduced after the CED preparation was used. Measurements of dye exclusion, oxygen consumption, protein synthetic activity and receptor binding, as well as ultrastructural features and the absence of inhibitory effects of EGTA and Dispase, suggested that the reduced secretory response of CED-treated cells was not attributable to cellular death, denaturation of receptors or the inhibitory effects of EGTA and Dispase. When the localization of dipeptidyl aminopeptidase IV was surveyed by both enzyme histochemistry and immuno-histochemistry, the luminal plasma membrane was the exclusive site for the reaction in C-treated cells as well as intact acini, whereas the entire cell surface was reaction-positive in CED-treated cells. In addition, the luminal microfilament system and tight junctions, as revealed by nitrobenz-oxadiazole-phallacidin staining and freeze-replica studies, respectively, were well-preserved in the C-treated cells, but considerably disorganized in the CED-treated cells. All these results strongly suggest that: (1) luminal specialization plays an important role in exocrine secretion; and (2) normal acinar arrangement provides the luminal specialization.

Developmental Distribution of Microperoxisomes in the Rat Submandibular Gland

1977 ◽  
Vol 35 ◽  
pp. 426-427
Author(s):  
B.A. Mooradian ◽  
L.S. Cutler
Keyword(s):  
Postnatal Development ◽  
Submandibular Gland ◽  
Cell Types ◽  
Functional Differentiation ◽  
Secretory Cells ◽  
Ductal Cells ◽  
Size Number ◽  
Rat Submandibular Gland

In the mature rat submandibular gland (SMG) microperoxisomes have been identified in both acinar secretory cells and ductal cells. The present study was undertaken to investigate the size, number and distribution of microperoxisomes during the pre and postnatal development of the SMG in order to determine if there were changes in cellular microperoxisomes during the functional differentiation of the various cell types.

scholarly journals Immunohistochemical localization of Na+,K+-ATPase in rodent and human salivary and lacrimal glands.

1988 ◽  
Vol 36 (9) ◽  
pp. 1139-1145 ◽  
Author(s):  
D C Winston ◽  
R A Hennigar ◽  
S S Spicer ◽  
J R Garrett ◽  
B A Schulte
Keyword(s):  
Submandibular Gland ◽  
Immunohistochemical Localization ◽  
Secretory Cells ◽  
Mucous Cells ◽  
Duct System ◽  
Lacrimal Glands ◽  
Low Protein ◽  
Rats And Mice ◽  
Rat Submandibular Gland ◽  
Gland Type

The enzyme Na+,K+-ATPase was localized immunohistochemically in major salivary glands of mouse, rat, and human and in exorbital lacrimal glands of the rodents. Immunoreactive Na+,K+-ATPase was abundant in the basolateral membranes of all epithelial cells lining striated and intra- and interlobular ducts of all glands. Reactivity of intercalated ducts varied among gland type and species. Cells lining granular ducts in rodent submandibular gland showed a heterogeneous staining pattern in rat but stained homogeneously in mouse. Secretory cells varied greatly in their content of immunoreactive Na+,K+-ATPase. As with all duct cells, staining was present only at the basolateral surface and was never observed at the luminal surface of reactive secretory cells. Mucous cells failed to show any reactivity in any gland examined. Serous cells showed a gradient of immunostaining intensity ranging from strongly positive in demilunes of human sublingual gland to negative in rat submandibular gland and lacrimal glands of rats and mice. The presence of basolaterally localized Na+,K+-ATPase in most serous cells but not in mucous cells suggests that the enzyme contributes to the ion and water content of copious, low-protein serous secretions. The intense immunostaining of cells in most if not all segments of the duct system supports the idea that the ducts are involved with modification of the primary saliva, and extends this concept to include all segments of the duct system.

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