scholarly journals Radioimmunoassay of carbonic anhydrase VI in saliva and sheep tissues

1991 ◽  
Vol 274 (2) ◽  
pp. 313-316 ◽  
Author(s):  
R T Fernley ◽  
R D Wright ◽  
J P Coghlan
Keyword(s):  
Carbonic Anhydrase ◽  
Parotid Gland ◽  
Saliva Sample ◽  
Secretion Rate ◽  
Parotid Saliva ◽  
Carbonic Anhydrase Vi ◽  
Conscious Sheep ◽  
Submandibular Saliva ◽  
Inter Assay Variation ◽  
Stimulation Of

A specific and sensitive radioimmunoassay has been developed for the measurement of the secreted carbonic anhydrase isoenzyme (CA VI) in sheep saliva and tissues. The assay can detect as little as 75 pg of CA VI, and the antibody used does not cross-react with CA II or CA III. The intra-assay variation, measured using a saliva sample, was 3.0%, whereas the inter-assay variation was 10.5%. The concentration of CA VI in parotid saliva from normal, resting sheep was 5.6 +/- 3.0 micrograms.ml-1 (n = 42) or 79.4 +/- 35.7 micrograms.mg of total protein-1. With feeding, the CA VI concentrations increased an average of 6-fold. The secretion rate of CA VI from the vascularly isolated neurotomized parotid gland of the anaesthetized sheep was 0.62 +/- 0.40 micrograms.min-1, compared with a rate of 11.7 +/- 7.8 micrograms.min-1 from the parotid gland of normal conscious sheep. Stimulation of the parotid-gland preparation by the muscarinic agent bethanechol increased the secretion rate to 438 +/- 172 microgram.min-1 (n = 8), and electrical stimulation of the secretomotor Moussu nerve increased CA VI secretion rate to 634 +/- 330 micrograms.min-1 (n = 4). Submandibular saliva from anaesthetized sheep contained 6.9 +/- 2.1 micrograms of CA VI.ml-1 (n = 3). The only tissues found to contain measurable amounts of CA VI were the parotid (6.4 micrograms.mg of protein-1) and submandibular (1.8 micrograms.mg of protein-1) salivary glands. The sublingual salivary gland, kidney, lung, adrenal, brain, skeletal muscle, liver, heart, pancreas, small intestine and cerebrospinal fluid did not have a measurable CA VI content.

Secretion of calcium and phosphate by the dog parotid gland

1961 ◽  
Vol 201 (4) ◽  
pp. 599-602 ◽  
Author(s):  
L. L. Langley ◽  
O. R. Grimes ◽  
D. F. Cockrell
Keyword(s):  
Steady State ◽  
Parotid Gland ◽  
Plasma Calcium ◽  
Secretion Rate ◽  
Phosphate Level ◽  
Organic Fraction ◽  
Parotid Saliva ◽  
Plasma Phosphate ◽  
Stop Flow

In dog parotid saliva, calcium is two to three times more concentrated than it is in the plasma. Phosphate in the saliva is less than one-fifth that of the plasma. Increasing the plasma phosphate level by a factor of 7 increases the saliva phosphate only twice. Salivary calcium varies almost proportionately with plasma calcium. After parotid secretion begins, the concentrations of both calcium and phosphate progressively decrease until a steady state is reached. Calcium and phosphate concentrations increase slightly in the saliva as the secretion rate decreases. At very slow rates there is a more marked increase. During the stop-flow procedure both calcium and phosphate concentrations increase, but to a strikingly different degree and at different sites in the gland. The increase in phosphate is almost exclusively the organic fraction. It is concluded that water and electrolytes are transferred from plasma to saliva by processes that are not coupled, and that proceed at varying and independent rates. The site of these transfers is distal, probably at the level of the ducts.

The development of parotid salivation in the lamb

1961 ◽  
Vol 12 (6) ◽  
pp. 1126 ◽  
Author(s):  
AD Wilson ◽  
DE Tribe
Keyword(s):  
Body Weight ◽  
Electrical Stimulation ◽  
Parotid Gland ◽  
Histological Examination ◽  
The Body ◽  
Parotid Glands ◽  
Fresh Weight ◽  
Parotid Saliva ◽  
Submaxillary Glands ◽  
Stimulation Of

The development of the parotid gland was studied in lambs reared under the following three dietary conditions: (a) lambs freely grazed with their ewes; (b) lambs hand-reared on milk and hay; (c) lambs hand-reared on milk alone. Weekly measurements were made of the saliva flowing from the cannulated parotids of two anaesthetized lambs from each group, during reflex and electrical stimulation of their glands. The fresh weights of the parotid and submaxillary glands and of the four stomachs were also recorded. Before 4 weeks of age, all the parotid glands were physiologically immature, secreting only 0.1–0.2 g saliva/g parotid tissue/min. The parotids of the grazing lambs developed rapidly from 4 to 6 weeks of age and reached adult capacity of 0.50–0.65 g/g/min between 7 and 10 weeks of age. The parotids of the lambs receiving millr and hay developed more slowly than the grazing lambs, while the parotids of the lambs receiving milk only scarcely developed at all. The histological examination of these glands showed that the parotids of the 2-week-old lambs were immature. Differentiation in the grazing group occurred at 4–6 weeks of age, while no differentiation occurred in the lambs fed milk only. The rate of flow of parotid saliva from all lambs was significantly correlated with the fresh weight of rumen tissue. The parotid gland increased in weight in relation to the rumen weight and not to the body weight.

scholarly journals Characterization of Lacrimal Gland Carbonic Anhydrase VI

2002 ◽  
Vol 50 (6) ◽  
pp. 821-827 ◽  
Author(s):  
Yuzo Ogawa ◽  
Keiji Matsumoto ◽  
Takashi Maeda ◽  
Riyoko Tamai ◽  
Takashi Suzuki ◽  
...  
Keyword(s):  
Carbonic Anhydrase ◽  
Parotid Gland ◽  
Lacrimal Gland ◽  
Tissue Concentration ◽  
Acinar Cells ◽  
Pcr Analysis ◽  
Acid Base Balance ◽  
Subunit Molecular Weight ◽  
Base Balance ◽  
Carbonic Anhydrase Vi

We have previously demonstrated by immunohistochemistry the presence of secreted carbonic anhydrase (CA VI) in the acinar cells of the rat lacrimal glands. In this study we purified the sheep lacrimal gland CA VI to homogeneity and demonstrated by Western analysis that it has the same apparent subunit molecular weight (45 kD) as the enzyme isolated from saliva. RT-PCR analysis showed that CA VI mRNA from the lacrimal gland was identical to that of the parotid gland CA VI mRNA. An RIA specific for sheep CA VI showed the lacrimal gland tissue concentration of the enzyme to be 4.20 ± 2.60 ng/mg protein, or about 1/7000 of the level found in the parotid gland. Immunohistochemistry (IHC) and in situ hybridization (ISH) showed that lacrimal acinar cells expressed both immunoreactivity and mRNA for CA VI. Moreover, CA VI immunoreactivity was occasionally observed in the lumen of the ducts. Unlike the parotid gland, in which all acinar cells expressed CA VI immunoreactivity and mRNA, only some of the acinar cells of the lacrimal gland showed expression. These results indicate that the lacrimal gland synthesizes and secretes a very small amount of salivary CA VI. In tear fluid, CA VI is presumed to have a role in the maintenance of acid/base balance on the surface of the eye, akin to its role in the oral cavity.

Gustin from Human Parotid Saliva Is Carbonic Anhydrase VI

1998 ◽  
Vol 250 (3) ◽  
pp. 635-641 ◽  
Author(s):  
B.J. Thatcher ◽  
A.E. Doherty ◽  
E. Orvisky ◽  
B.M. Martin ◽  
R.I. Henkin
Keyword(s):  
Carbonic Anhydrase ◽  
Parotid Saliva ◽  
Carbonic Anhydrase Vi ◽  
Human Parotid Saliva

scholarly journals CHOP-Dependent Stress-Inducible Expression of a Novel Form of Carbonic Anhydrase VI

1999 ◽  
Vol 19 (1) ◽  
pp. 495-504 ◽  
Author(s):  
John Sok ◽  
Xiao-Zhong Wang ◽  
Nikoleta Batchvarova ◽  
Masahiko Kuroda ◽  
Heather Harding ◽  
...  
Keyword(s):  
Carbonic Anhydrase ◽  
Target Gene ◽  
Target Genes ◽  
Direct Evidence ◽  
Nuclear Protein ◽  
Intracellular Form ◽  
Carbonic Anhydrase Vi ◽  
Responsive Element

ABSTRACT CHOP (also called GADD153) is a stress-inducible nuclear protein that dimerizes with members of the C/EBP family of transcription factors and was initially identified as an inhibitor of C/EBP binding to classic C/EBP target genes. Subsequent experiments suggested a role for CHOP-C/EBP heterodimers in positively regulating gene expression; however, direct evidence that this is the case has so far not been uncovered. Here we describe the identification of a positively regulated direct CHOP-C/EBP target gene, that encoding murine carbonic anhydrase VI (CA-VI). The stress-inducible form of the gene is expressed from an internal promoter and encodes a novel intracellular form of what is normally a secreted protein. Stress-induced expression of CA-VI is both CHOP and C/EBPβ dependent in that it does not occur in cells deficient in either gene. A CHOP-responsive element was mapped to the inducibleCA-VI promoter, and in vitro footprinting revealed binding of CHOP-C/EBP heterodimers to that site. Rescue of CA-VIexpression in c/ebpβ−/− cells by exogenous C/EBPβ and a shorter, normally inhibitory isoform of the protein known as LIP suggests that the role of the C/EBP partner is limited to targeting the CHOP-containing heterodimer to the response element and points to a preeminent role for CHOP in CA-VI induction during stress.

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