scholarly journals Comparative developmental analysis of the parotid, submandibular and sublingual glands in the neonatal rat

1982 ◽  
Vol 204 (3) ◽  
pp. 673-679 ◽  
Author(s):  
M G Humphreys-Beher ◽  
D L Hollis ◽  
D M Carlson
Keyword(s):  
Salivary Glands ◽  
Submandibular Gland ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Neonatal Rat ◽  
Leucine Incorporation ◽  
Sublingual Gland ◽  
Neonatal Development ◽  
Glycoprotein Synthesis ◽  
Tissue Specific

Analysis of the soluble protein fractions from the rat parotid, submandibular and sublingual glands by polyacrylamide-gel electrophoresis reveals similarities in overall patterns of protein synthesis at birth. Tissue-specific changes in protein and glycoprotein synthesis occur shortly after birth and again at the time of weaning, 21-28 days later. Incorporation of [3H]thymidine into DNA was at its highest after birth and gradually decreased in both the parotid and submandibular gland, whereas [3H]thymidine incorporation in the sublingual gland was low throughout the time of neonatal development. [14C]Leucine incorporation into total protein increased in all glands with age after birth, showing an accelerated rate 21-28 days later. Trichloroacetic acid/phosphotungstic acid-precipitable [3H]fucose in glycoproteins declined over the time of neonatal development in the parotid and submandibular gland, but its incorporation remained higher in the sublingual gland. alpha-Amylase (EC 3.2.1.1) in the salivary glands increased at the time of weaning, as judged by detectability in sodium dodecyl sulphate/polyacrylamide gels and by immune precipitation. Two membrane-bound enzymes, UDP-galactose:2-acetamido-2-deoxy-D-glucosamine 4 β-galactosyltransferase (EC 2.4.1.22) and UDP-galactose:2-acetamido-2-deoxy-D-galactosaminyl-protein 3 β-galactosyltransferase (no EC number), undergo tissue-specific change rather than changes induced by physiological stimulation of the salivary glands.

Contraction regulates myosin synthesis and myosin content of cultured heart cells

1985 ◽  
Vol 249 (4) ◽  
pp. H763-H769
Author(s):  
P. McDermott ◽  
M. Daood ◽  
I. Klein
Keyword(s):  
Protein Synthesis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Total Cell ◽  
Neonatal Rat ◽  
Cell Protein ◽  
Heart Cells ◽  
Culture Dish ◽  
Total Cell Protein ◽  
Cultured Heart Cells

Cultured neonatal rat heart cells are a useful model for studying the regulation of myocyte growth. The myosin content of heart cells increases between days 1 and 4 in culture. To determine if contraction per se can regulate myocyte growth, myosin content and protein synthesis were compared in spontaneously contracting and noncontracting cultured heart cells. Myosin content, assayed as the total myosin ATPase activity per culture dish, was significantly increased in contracting cells after 3, 4, and 5 days in culture. Protein synthesis was measured by incorporation of [14C]lysine into total cell protein and into sodium dodecyl sulfate-polyacrylamide gel electrophoresis resolved myosin. Contraction stimulated both total cell protein content and protein synthesis by day 3 in culture. Compared with heart cells arrested with 50 mM KCl, myosin synthesis was significantly increased by 96, 112, and 46% at days 2, 3, and 4, respectively. Similar results were observed when myosin content and protein synthesis in contracting myocytes were compared with cells arrested with either 25 mM KCl or 10(-5) M verapamil. The present studies suggest that contraction increases the myosin content in cultured heart cells and that this increase is mediated via a stimulation of myosin synthesis in association with cell growth.

scholarly journals Isolation, characterization and synthesis of α-foetoprotein from neonatal-rat skin

1983 ◽  
Vol 216 (1) ◽  
pp. 227-231
Author(s):  
K Mujoo ◽  
M Ali ◽  
M K Sahib
Keyword(s):  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Gel Filtration ◽  
Explant Culture ◽  
Polyacrylamide Gel ◽  
Neonatal Rat ◽  
Rat Skin ◽  
Packed Volume ◽  
Sepharose 4B

Monospecific anti-[rat alpha-foetoprotein(alpha-FP)] immunoglobulin G was coupled to CNBr-activated Sepharose-4B (4.5 mg/ml packed volume of gel) to yield an adsorbent. The immunoaffinity column was used to isolate alpha-FP from neonatal-rat skin. Purified skin alpha-FP was found to be immunologically and electrophoretically similar to serum alpha-FP. It yielded a single band with mol.wt. 68000 on sodium dodecyl sulphate/polyacrylamide-gel electrophoresis. However, on polyacrylamide-gel electrophoresis under non-denaturing conditions, the alpha-FP displayed slow- and fast-moving variants similar to those observed in serum alpha-FP. A Scatchard plot of oestradiol binding to the alpha-FP yielded an association constant of 2.5 × 10(9)M-1 by dextran-coated-charcoal and 0.75 × 10(8)M-1 by Sephadex-gel-filtration procedures respectively. Skin explants from newborn rats were found to incorporate [14C]leucine into immunoprecipitable intracellular alpha-FP. Cycloheximide inhibited the synthesis of alpha-FP in skin explant culture. Our results indicate that newborn-rat skin contains alpha-FP that is similar to serum alpha-FP and which may arise in neonatal-rat skin as a result of synthesis in situ.

scholarly journals Malignant epithelial tumors in the minor salivary glands, the submandibular gland, and the sublingual gland. Prognostic factors and treatment results

Cancer ◽  
1991 ◽  
Vol 68 (11) ◽  
pp. 2431-2437 ◽  
Author(s):  
Lisbeth Juhler Andersen ◽  
Marianne Hamilton Therkildsen ◽  
Hans Henrik Ockelmann ◽  
Jens Daugård Bentzen ◽  
Torben Schiødt ◽  
...  
Keyword(s):  
Prognostic Factors ◽  
Salivary Glands ◽  
Submandibular Gland ◽  
Sublingual Gland ◽  
Minor Salivary Glands ◽  
Treatment Results ◽  
Epithelial Tumors

scholarly journals Strain-specific differences in the proline-rich proteins and glycoproteins induced in rat salivary glands by chronic isoprenaline treatment

1985 ◽  
Vol 230 (2) ◽  
pp. 369-378 ◽  
Author(s):  
M G Humphreys-Beher
Keyword(s):  
Amino Acid ◽  
Salivary Glands ◽  
Specific Activity ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Apparent Difference ◽  
Marker Enzyme ◽  
Parotid Glands ◽  
Amino Acid Compositions ◽  
Submandibular Glands

Parotid and submandibular glands were isolated from five strains of rat after chronic injection of the β-adrenergic receptor agonist isoprenaline (isoproterenol). The glands were observed to have undergone a marked increase in wet weight, owing to hypertrophy and hyperplasia. The 100 000 g soluble fraction of gland cell lysates were extracted with 10% (w/v) trichloroacetic acid, and the soluble material subsequently analysed by SDS (sodium dodecyl sulphate)/polyacrylamide-gel electrophoresis. By this procedure, evidence was obtained for the induction, in isoprenaline-treated parotid and submandibular glands, of proline-rich proteins with apparent Mr values ranging from 20 000 to 40 000. Heterogeneity was evident in the proteins produced for a specific gland between the rat strains, although the amino acid compositions were the same. Products from induced mRNAs translated in vitro had similar mobilities in SDS/polyacrylamide gels, despite the apparent difference in mobility of trichloracetic acid-extracted proline-rich proteins from the various strains. Strain-specific differences were noted for the proline-rich glycoproteins from control salivary glands as well as those induced as a consequence of isoprenaline treatment. Although the glycoproteins had similar amino acid compositions, there was considerable heterogeneity in the carbohydrate compositions for these proteins, suggesting that the differences were the result of post-translational modifications during glycosylation. Induction of the increased activity of the Golgi membrane marker enzyme UDP-galactose:2-acetamido-2-deoxy-D-glucosamine 4 β-galactosyltransferase (EC 2.4.1.22) occurred to the same extent in the parotid glands of all strains examined. There was no change in the specific activity of a second enzyme, UDP-galactose:N-acetylgalactosaminyl-protein 3 β-galactosyltransferase (no EC designation).

scholarly journals Specific identification of tissue kallikrein in exocrine tissues and in cell-free translation products with monoclonal antibodies

1985 ◽  
Vol 231 (3) ◽  
pp. 721-728 ◽  
Author(s):  
C M Woodley ◽  
J Chao ◽  
H S Margolius ◽  
L Chao
Keyword(s):  
Monoclonal Antibodies ◽  
Submandibular Gland ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Cross Reactivity ◽  
Tissue Kallikrein ◽  
Urinary Kallikrein ◽  
Free Translation ◽  
Antibody Titres ◽  
Kallikrein Activity

A panel of six mouse monoclonal antibodies (IgG1) has been prepared against purified rat urinary kallikrein (EC 3.4.21.35) and characterized. In radioimmunoassay, the antibody titres of ascitic fluid giving 50% binding to 125I-kallikrein range from 1:2 × 10(3) to 1:1 × 10(6). Antibodies from four of the clones show no cross-reactivity with human urinary kallikrein, rat urinary esterase A or tonin. However, antibodies from a fifth clone cross-react with tonin and, from a sixth, with both urinary esterase A and tonin. Three of the kallikrein affinity-purified monoclonal antibodies inhibited, whereas one of the antibodies stimulated, kallikrein activity. Tissue kallikrein from rat submandibular-gland and pancreatic extracts and urine were labelled with [14C]di-isopropyl phosphofluoridate, immunoprecipitated with each of the six monoclonal antibodies and identified to be 38 kDa proteins, similar in size to purified rat urinary kallikrein. Western-blot analysis shows that 125I-labelled kallikrein monoclonal antibodies (V4D11) bind directly to a 38 kDa protein in submandibular-gland and pancreatic extracts and urine. Cell-free translation products of submandibular-gland polyadenylylated[poly(A)+]mRNA were immunoprecipitated with affinity-purified sheep anti-kallikrein antibodies and three monoclonal antibodies (V4D11, V4G6 and V1C3). Sodium dodecyl sulphate/polyacrylamide-gel electrophoresis of these immunoprecipitates revealed that two kallikrein precursors with Mr values of 37 000 and 35 000 are encoded by submandibular-gland mRNA. The third monoclonal antibody, V1C3, which binds to active kallikrein, did not recognize either precursor form. Collectively, the data show that these monoclonal antibodies comprise a set of powerful and specific reagents for studies of tissue kallikreins.

scholarly journals CLINICOPATHOLOGICAL STUDY OF SALIVARY GLAND SWELLING

2020 ◽  
Vol 4 (2) ◽  
Author(s):  
Akshay Akulwar ◽  
Akshay Bavikatte
Keyword(s):  
Salivary Gland ◽  
Salivary Glands ◽  
Submandibular Gland ◽  
Inflammatory Diseases ◽  
Late Presentation ◽  
Final Decision ◽  
X Rays ◽  
Sublingual Gland ◽  
The World ◽  
Neoplastic Lesions

Introduction: Although the salivary, sweat, apocrine, and mammary glands all have similar phylogeny and cellular phenotypes, many lesions are unique to the salivary glands.  Various studies around the world reported incidence for all salivary glands tumors to be between 0.4 and 13.5 cases/100,000. Salivary gland swellings can be broadly classified into inflammatory, non- inflammatory and neoplastic swellings. Acute inflammatory conditions generally can be diagnosed by history and physical examination alone, whereas chronic inflammatory diseases and granulomatous disorders require supplemental diagnostic information including lab tests, imaging studies and biopsy. Accurate pathological diagnosis is necessary for proper management of neoplastic disorders. In this part of the world, the problem of these tumours is more troublesome in management because of their late presentation due to poor economic condition and lack of awareness of health among the general population. It is important to note that diffuse swellings usually signify disease of inflammatory nature. Discrete swelling within the gland usually indicates neoplasia and rarely replace entire gland until very late. Submandibular gland tumours are twice as likely to be malignant, compared to parotid. Sublingual gland tumours are unusual, 80% are malignant.  Material and Methods: Patients included were those admitted to surgical wards with salivary gland swellings due to obstructions of the salivary duct and neoplasia and were willing to participate in the study for investigation and treatment. Patients, hemoglobin level, bleeding time, clotting time, urine, sugar albumin, microscopy, chest screening, ECG, Blood urea, serum Creatinine, RBS was estimated. Specific investigations like FNAC, X-rays of Mandible were done for all patients in the study group. After evaluation of the swellings by clinical examination and by specific investigations, a surgical plan was formulated. The final decision was taken per operatively by the surgeon. The required specimen was sent for histopathologocal examinations. Different modalities of treatment adopted in this study were, surgery or surgery and post-operative radiotherapy. Results: Age of the patients varied from 9 years to 80 years. Average age of the patient was 40.6 years. Out of 40 cases 15(35%) cases was of male and 25(65%) cases of female. 62.5% (25 cases) were found in the parotid gland, 30% cases (12) in submandibular gland and 7.5% cases (3) in the sublingual gland. Out of 40 cases, neoplastic lesions of 65.0 %( 25 cases) and non-inflammatory non neoplastic lesions of 37.5% (15 cases) were seen. Out of 25 salivary gland Keywords: SALIVARY GLAND, TUMOUR, MALIGNANT, BENIGN, FNAC, HISTOPATHOLOGY

Tissue-specific isoform regulation of Na+-K+-ATPase by thyroid hormone in ferrets

1989 ◽  
Vol 257 (2) ◽  
pp. H534-H539 ◽  
Author(s):  
Y. C. Ng ◽  
A. Z. Yao ◽  
T. Akera
Keyword(s):  
Thyroid Hormone ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Developmental Changes ◽  
Ouabain Binding ◽  
Tissue Specific ◽  
Alpha Subunits ◽  
Specific Regulation ◽  
Ferret Heart

We have shown previously that in the ferret heart there are two isoforms of Na+-K+-ATPase, alpha(+) and alpha, and that these isoforms undergo developmental changes. In the present study, we examine regulation of the isoenzymes by thyroid hormone, which is well known to increase activity of Na+-K+-ATPase in different tissue preparations. Ferrets were injected with L-thyroxine (T4) (0.5 mg/kg, sc) for 3 wk. The T4-treated ferrets gained 58 +/- 32 g body wt compared with 366 +/- 24 g for the control ferrets. Plasma 3,5,3'-triiodothyronine concentrations of the T4-treated animals increased about eightfold 16-18 h after the last injection. The number of alpha(+)- and alpha-subunits in heart homogenates estimated by [3H]ouabain binding was 3.5 +/- 0.1 and 2.5 +/- 0.1 pmol/mg protein, respectively [alpha(+)/alpha = 1.40]. In the T4-treated ferrets, there was no significant increase of the alpha(+)-isoform (3.2 +/- 0.2 pmol/mg protein), whereas the number of alpha-isoform increased significantly to 4.1 +/- 0.3 pmol/mg protein [alpha(+)/alpha = 0.78]. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of partially purified cardiac plasma membrane preparations reveals similar pattern of changes of the isoenzymes. In the kidney, however, there was no significant change in the number of alpha-isoform, which is the predominant isoform in the kidney, and T4 does not appear to induce synthesis of alpha(+)-isoform in the kidney. It is concluded that thyroid hormone induces both isoform- and tissue-specific regulation of the Na+-K+-ATPase alpha-subunits in the ferret. These specific regulations of the isoforms seem to suggest important physiological roles of the isoenzymes.

scholarly journals The formation of lipid-linked sugars as intermediates in glycoprotein synthesis in rabbit mammary gland

1978 ◽  
Vol 170 (2) ◽  
pp. 273-283 ◽  
Author(s):  
Brian K. Speake ◽  
David A. White
Keyword(s):  
Ammonium Acetate ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Deae Cellulose ◽  
Total Radioactivity ◽  
Glycoprotein Synthesis ◽  
Molecular Weights ◽  
Oligosaccharide Moiety ◽  
Chloroform Methanol ◽  
Mild Acid

1. The incorporation of d-[1-14C]mannose, d-[2-3H]mannose and N-acetyl-d-[1-14C]-glucosamine into glycoproteins and lipid-linked intermediates of mammary explants obtained from lactating rabbits was studied. The amount of radioactivity incorporated into lipid-linked intermediates was very low compared with the incorporation into protein. Most of the radioactivity incorporated into the chloroform/methanol-soluble fraction was present as neutral lipid. Radioactivity from d-[2-3H]mannose was incorporated mainly into the fatty acid moiety, whereas radioactivity from d-[1-14C]mannose and N-acetyl-d-[1-14C]glucosamine was present in the glycerol moiety of triacylglycerol. 2. The labelled lipid-linked intermediate that was soluble in chloroform/methanol/water (10:10:3, by vol.) was partially characterized and was found to exhibit properties characteristic of an oligosaccharide linked to lipid via a pyrophosphate bridge. It migrated largely as a single zone of radioactivity on t.l.c. and was eluted from a column of DEAE-cellulose acetate as a single peak by 50mm-ammonium acetate. 3. The oligosaccharide moiety was released from the lipid by mild acid hydrolysis. The size of the oligosaccharide was estimated by paper chromatography to be 10 or 11 monosaccharide units. 4. d-[1-14C]Mannose was incorporated largely into glycopeptides with molecular weights in the range 40000–80000, as determined by polyacrylamide-gel electrophoresis in the presence of sodium dodecyl sulphate. Label from N-acetyl-d-[1-14C]glucosamine was incorporated into a glycopeptide with an electrophoretic mobility identical with that of rabbit casein (mol.wt. 32000) as well as into glycopeptides of higher molecular weight. 5. Approx. 50% of the total radioactivity in the protein labelled from N-acetyl-d-[1-14C]glucosamine was present as galactosamine, a component of the carbohydrate portion of rabbit casein. No labelled galactosamine was present in the lipid-linked oligosaccharide labelled from N-acetyl-d-[1-14C]glucosamine. It thus appears that the lipid-linked oligosaccharide is not involved in the glycosylation of casein.

Cytochemical Evidence for Presynatic β-Adrenergic Regulation of Secretion in the Developing Rat Submandibular Gland

1977 ◽  
Vol 35 ◽  
pp. 430-431
Author(s):  
L.S. Cutler
Keyword(s):  
Cyclic Amp ◽  
Adenylate Cyclase ◽  
Submandibular Gland ◽  
Neonatal Rat ◽  
Cyclase Activity ◽  
Adenylate Cyclase Activity ◽  
Parotid Glands ◽  
Adrenergic Agonist ◽  
Rat Submandibular Gland

Many studies previously have shown that the B-adrenergic agonist isoproterenol and the a-adrenergic agonist norepinephrine will stimulate secretion by the adult rat submandibular (SMG) and parotid glands. Recent data from several laboratories indicates that adrenergic agonists bind to specific receptors on the secretory cell surface and stimulate membrane associated adenylate cyclase activity which generates cyclic AMP. The production of cyclic AMP apparently initiates a cascade of events which culminates in exocytosis. During recent studies in our laboratory it was observed that the adenylate cyclase activity in plasma membrane fractions derived from the prenatal and early neonatal rat submandibular gland was retractile to stimulation by isoproterenol but was stimulated by norepinephrine. In addition, in vitro secretion studies indicated that these prenatal and neonatal glands would not secrete peroxidase in response to isoproterenol but would secrete in response to norepinephrine. In contrast to these in vitro observations, it has been shown that the injection of isoproterenol into the living newborn rat results in secretion of peroxidase by the SMG (1).

Biogenesis of Catalase-Positive Rods in Excretory Duct Cells of Salivary Glands

1976 ◽  
Vol 34 ◽  
pp. 62-63
Author(s):  
Dwight K. Romanovicz ◽  
Jacob S. Hanker
Keyword(s):  
Light Microscopy ◽  
Salivary Glands ◽  
Submandibular Gland ◽  
Excretory Duct ◽  
Exocrine Glands ◽  
Duct Cells ◽  
Peroxidatic Activity ◽  
Microscopic Studies ◽  
Different Dimensions

The presence of catalase-positive rods (Fig. 1) of different dimensions, which frequently have a crystalline appearance by light microscopy, has been reported. They seem to be related to peroxisomes which were characterized morphologically and cytochemically in parotid and other exocrine glands of the rat by Hand in 1973. Our light microscopic studies of these spherical microbodies and rods of different sizes, stained by virtue of the peroxidatic activity of their catalase, indicate that they are almost entirely confined to the cells of the striated and execretory ducts of the submandibular gland in the mouse. The rods were usually noted only in the proximity of the ductal microbodies. The latter frequently showed a tendency to appear in linear close array, or even to be contiguous (Fig. 2). This suggested that the rods could be formed by the fusion of microbodies.

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