A competitive dual-label time-resolved immunofluorometric assay for simultaneous detection of carbonic anhydrase I and II in cerebrospinal fluid

Parkkila, Anna‐Kaisa; Parkkila, Seppo; Serlo, Willy; Reunanen, Mauri; Vierjoki, T; Rajaniemi, Hannu

doi:10.1016/0009-8981(94)90091-4

Cited by 28 publications

(36 citation statements)

References 20 publications

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“…17 Although CAVI was originally predicted to regulate salivary pH or buffer capacity, 20,21 some studies indicate that these variables are not directly associated with CAVI concentration in saliva. 22,23 Therefore, it is possible that besides concentration, CAVI activity in saliva can also be influenced by other variables such as by genetic polymorphisms found in the coding sequences that may modulate the activity of this enzyme. Gene polymorphisms are a mechanism by which individuals may exhibit variations within the range of what is considered biologically normal.…”

Section: Introductionmentioning

confidence: 99%

Association of polymorphisms in the carbonic anhydrase 6 gene with salivary buffer capacity, dental plaque pH, and caries index in children aged 7–9 years

et al. 2009

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Carbonic anhydrase VI is a secreted enzyme that catalyzes the hydration of carbon hydroxide in saliva and other body fluids. This enzyme has been implicated in taste and gastrointestinal dysfunctions, tooth erosion, and caries. The purpose of this study was to analyze the allele and genotype distribution of three polymorphisms in the coding sequences of (CA6) gene and check for possible associations with salivary buffer capacity, number of decayed, missing, and filled teeth in deciduous and permanent teeth (dmft/ DMFT, Decayed/Missing/Filled Teeth), plaque index (PI), and the plaque pH variation (DpH) in children aged 7-9 years. Two hundred and forty-five children from both genders, residents in area with fluoridated water (Piracicaba, São Paulo, Brazil) were divided into two groups: caries free and with caries. The clinical examinations were conducted by a single previously calibrated examiner (k ¼ 0.91) in an outdoor setting using a mirror and a probe, according to WHO criteria index (dmft/DMFT). Approximately 2 h after the first daily meal, the buffer capacity (BC) and the plaque pH were analyzed by means of a pH meter and an ion selective electrode. Plaque pH was measured immediately and 5 min after a mouth rinse with a 10% sucrose solution. The data were submitted to w 2 , Student's, and Mann-Whitney tests (a ¼ 0.05). The PI and DpH of the upper and lower teeth were significantly higher in the carious group than control (Po0.05). There was no difference between the groups in relation to BC. There was no association between the alleles and genotypes distributions for polymorphisms in the CA6 gene exons 2 and 3 and caries experience (P40.05). There was a positive association between buffer capacity and the rs2274327 (C/T) polymorphism. The allele T and genotype TT were significantly less frequent in individuals with the highest buffer capacity (P ¼ 0.023 and 0.045, respectively). This finding encourages future studies relating CA6 gene polymorphisms and their association with malfunctions, such as taste and gastrointestinal alterations, or the differential effect of chemical modulators on the protein products originated from the distinct genotypes of the CA6 gene.

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Section: Introductionmentioning

confidence: 99%

Association of polymorphisms in the carbonic anhydrase 6 gene with salivary buffer capacity, dental plaque pH, and caries index in children aged 7–9 years

et al. 2009

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“…It was originally predicted to regulate salivary pH or buffer capacity (Feldstein & Silverman, 1984;Kadoya et al 1987). Interestingly, results from our laboratory indicate that these variables are not directly associated with CA VI concentration in saliva (Parkkila et al 1993;Kivel a et al 1997a), suggesting that the enzyme may have a different role or that it may participate in these processes together with other CAs. Another novel aspect to the function of CA VI was provided by Thatcher et al (1998), who identified gustin, a salivary protein that has been reported to be associated with the function of taste buds, as human CA VI by protein sequencing, activity profiles and other physical data.…”

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confidence: 73%

“…In 1991, Aldred et al cloned and characterized the cDNA encoding human carbonic anhydrase (HCA) VI. The next major step in research into salivary CA was the development of specific immunofluorometric and radioimmunoassays for HCA VI (Parkkila et al 1993;Fernley et al 1995), which allowed accurate quantification of CA VI in biological matrices such as saliva and serum. CA VI is the only known secreted isoenzyme of the mammalian CA gene family, and has several properties that distinguish it from the well-characterized cytoplasmic isoenzymes.…”

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Salivary carbonic anhydrase isoenzyme VI

Kivelä

Parkkila

et al. 1999

The Journal of Physiology

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112

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“…It is also abundantly expressed in glial cells, and detectable amounts are leaked into the cerebrospinal fluid (CSF) (18). As a high-activity isoenzyme, it plays an important role in various physiological processes regulating the acid-base balance of tissues and biological fluids.…”

Section: Introductionmentioning

confidence: 99%

Carbonic anhydrase isoenzyme II is located in corticotrophs of the human pituitary gland.

Parkkila

Parkkila²,

Rajaniemi³

1996

J Histochem Cytochem.

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We studied the location of carbonic anhydrase (CA) isoenzymes I, II, and VI in human pituitary gland using specific antisera in conjunction with immunoblotting, immunoperoxidase, and double immunofluorescence staining techniques. Stainings with anti-CA II serum showed intense cytoplasmic reaction in the anterior lobe of the pituitary gland. Double immunofluorescence staining was used to identify the cells that expressed CA II. Confocal laser scanning microscopy revealed that, of the anterior pituitary hormones studied, ACTH coincides mainly with CA II in these cells. Stainings with anti-CA I and VI sera were negative in the endocrine cells of the pituitary gland. Western blotting of the pituitary gland with anti-CA II revealed a distinct 29-KD polypeptide band corresponding in molecular weight to CA II, suggesting that the antiserum does not detect any nonspecific protein. Anti-CA I serum similarly showed a major 29-KD band, possibly recognizing the enzyme, which is abundantly present in erythrocytes. The results indicate that CA II is expressed in corticotrophs of human pituitary gland, in which its physiological role may be linked to the regulation of optimal pH in the secretory vesicles for the cleavage of ACTH from its precursor.

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A competitive dual-label time-resolved immunofluorometric assay for simultaneous detection of carbonic anhydrase I and II in cerebrospinal fluid

Cited by 28 publications

References 20 publications

Association of polymorphisms in the carbonic anhydrase 6 gene with salivary buffer capacity, dental plaque pH, and caries index in children aged 7–9 years

Association of polymorphisms in the carbonic anhydrase 6 gene with salivary buffer capacity, dental plaque pH, and caries index in children aged 7–9 years

Salivary carbonic anhydrase isoenzyme VI

Carbonic anhydrase isoenzyme II is located in corticotrophs of the human pituitary gland.

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