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 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.

Radioimmunoassay for salivary carbonic anhydrase in human parotid saliva

1995 ◽  
Vol 40 (6) ◽  
pp. 567-569 ◽  
Author(s):  
R.T. Fernley ◽  
J. Farthing ◽  
E.J. Cooper
Keyword(s):  
Carbonic Anhydrase ◽  
Parotid Saliva ◽  
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.

scholarly journals Fractionation of human parotid saliva proteins.

1978 ◽  
Vol 253 (20) ◽  
pp. 7556-7565 ◽  
Author(s):  
R.I. Henkin ◽  
R.E. Lippoldt ◽  
J. Bilstad ◽  
R.O. Wolf ◽  
C.K. Lum ◽  
...  
Keyword(s):  
Parotid Saliva ◽  
Human Parotid Saliva

Substrate Specificity of Fucosyltransferase Purified from Human Parotid Saliva

1987 ◽  
Vol 66 (3) ◽  
pp. 756-760 ◽  
Author(s):  
H. Tamagawa ◽  
K. Iwakura ◽  
A. Amano ◽  
S. Shizukuishi ◽  
A. Tsunemitsu
Keyword(s):  
Substrate Specificity ◽  
Parotid Saliva ◽  
Human Parotid Saliva

Studies on histidine-rich polypeptides from human parotid saliva

1976 ◽  
Vol 177 (2) ◽  
pp. 427-436 ◽  
Author(s):  
Bruce J. Baum ◽  
Janice L. Bird ◽  
David B. Millar ◽  
Robert W. Longton
Keyword(s):  
Parotid Saliva ◽  
Human Parotid Saliva
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