The Human α-Amylases

Merritt, A. Donald; Karn, Robert C.

doi:10.1007/978-1-4615-8267-0_3

Cited by 24 publications

(32 citation statements)

References 181 publications

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“…Other than AMY1 3, variants were never found in a homozygous state, but were always present with AMY1 1 variant, AMY1 9, has been described in the Bozo tribe (Mali, West Africa) (Pronk and Frants 1979), but not in Caucasians. AMY1 11 is probably identical with one of the PAGE variants mentioned by Merritt and Karn (1977). The variants AMY1 1, AMY1 2, AMY1 3 and AMY1 5 are in accordance with the numbers used by de Soyza (1978;, Ktihnl and Tischberger (1980), Pronk et al (1982;1984) and Boan and Caeiro (1988).…”

Section: Amylase Protein Variantssupporting

confidence: 69%

“…Bank secretion) does not affect the electrophoretic expression of the isozymes (Ogita 1966;Wolf and Taylor 1967;Kauffman et al 1973). The observed complex isozyme pattern can be explained as the result of two posttranslational modifications (glycosylation and deamidation) and one postsecretory modification (deglycosylation) of a single gene product (Merritt and Karn 1977;Bank et al 1991).…”

Section: Introductionmentioning

confidence: 90%

“…Inherited variations in salivary amylase, shown by separation during electrophoresis on agar, agarose or polyacrylamide gels, have been reported by various authors (e.g., Merritt and Karn 1977). However, the frequencies of the individual variants described have been low.…”

Section: Introductionmentioning

confidence: 94%

“…B Relationship between PAGE and IEF patterns of human salivary amylase according to Pronk and Frants (1979). The pattern shown is AMY1 1 chemical and genetic studies (Merritt and Karn 1977;Bank et al 1991). A schematic representation of the salivary amylase pattern of the most common allozyme, AMY1 1, and the explanation for the origination of the different bands is shown in Fig.…”

Section: Interpretation Of the Zymogramsmentioning

confidence: 99%

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Variation in gene copy number and polymorphism of the human salivary amylase isoenzyme system in Caucasians

et al. 1992

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Summary. The polymorphic patterns of human salivary amylase of a large number of individuals of Caucasian origin were determined by using isoelectric focusing and polyacrylamide gel electrophoresis. Nine different salivary amylase protein variants were found; three of them are recorded for the first time and their heredity is shown. Some of the variants are encoded by haplotypes expressing three allozymes. Most variants display low frequencies. Analysis of the relative intensities of variant-specific isozyme bands, combined with segregation analysis, show that extensive quantitative variation is present in the population. The numbers of salivary amylase genes in some families showing quantitative variation at the protein level have been estimated by the polymerase chain reaction. We present evidence that quantitative variations in amylase protein patterns do not always reflect variations in gene copy number but that other mechanisms are also involved.

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Section: Amylase Protein Variantssupporting

confidence: 69%

Section: Introductionmentioning

confidence: 90%

Section: Introductionmentioning

confidence: 94%

Section: Interpretation Of the Zymogramsmentioning

confidence: 99%

See 2 more Smart Citations

Variation in gene copy number and polymorphism of the human salivary amylase isoenzyme system in Caucasians

et al. 1992

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“…Amylase catalyses the hydrolysis of internal α1-4 glucosidic bonds from various glucose polymers [6] and as such is an important enzyme in the early stages of carbohydrate digestion. Catalytically active salivary amylase has been reported to bind to microorganisms and tooth enamel, and as such is perhaps crucial in mediating adherence of pathogens to oral surfaces, and allowing microbial growth through provision of glucose from the breakdown of dietary glucose polymers [7][8][9][10].…”

Section: Introductionmentioning

confidence: 99%

Analysis of the extreme diversity of salivary alpha-amylase isoforms generated by physiological proteolysis using liquid chromatography–tandem mass spectrometry

Bailey

Punyadeera

Cooper-White

et al. 2012

Journal of Chromatography B

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Saliva is a crucial biofluid for oral health and is also of increasing importance as a noninvasive source of disease biomarkers. Salivary alpha-amylase is an abundant protein in saliva, and changes in amylase expression have been previously associated with a variety of diseases and conditions. Salivary alpha-amylase is subject to a high diversity of posttranslational modifications, including physiological proteolysis in the oral cavity. Here we developed methodology for rapid sample preparation and non-targeted LC-ESI-MS/MS analysis of saliva from healthy subjects and observed an extreme diversity of alpha-amylase proteolytic isoforms. Our results emphasize the importance of consideration of posttranslational events such as proteolysis in proteomic studies, biomarker discovery and validation, particularly in saliva.

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Differential distribution of salivary agglutinin and amylase in the Golgi apparatus and secretory granules of human salivary gland acinar cells

et al. 1991

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The secretory granules of salivary glands often display complex internal substructures, yet little is known of the molecular organization of their contents or the mechanisms involved in packaging of the secretory proteins. We used post-embedding immunogold labeling with antibodies to two secretory proteins, agglutinin and alpha-amylase, to determine their distribution in the Golgi apparatus and secretory granules of the human submandibular gland acinar cells. With monoclonal antibodies specific for carbohydrate epitopes of the agglutinin, reactivity was found in the trans Golgi saccules, trans Golgi network, and immature and mature secretory granules. In the granules, labeling was seen in regions of low and medium electron density, but not in the dense cores. Reactivity seen on the apical and basolateral membranes of acinar and duct cells was attributed to a shared epitope on a membrane glycoprotein. Labeling with a polyclonal antibody to amylase was found in the Golgi saccules, immature and mature secretory granules, but not in the trans Golgi network. In the granules, amylase was present in the dense cores and in areas of medium density, but not in the regions of low density. These results indicate that these two proteins are distributed differently within the secretory granules, and suggest that they follow separate pathways between the Golgi apparatus and forming secretory granules. Small vesicles and tubular structures that labeled only with the antibodies to the agglutinin were observed on both faces of the Golgi apparatus and in the vicinity of the cell membrane. These structures may represent constitutive secretion vesicles involved in transport of the putative membrane glycoprotein to the cell membrane.

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The Human α-Amylases

Cited by 24 publications

References 181 publications

Variation in gene copy number and polymorphism of the human salivary amylase isoenzyme system in Caucasians

Variation in gene copy number and polymorphism of the human salivary amylase isoenzyme system in Caucasians

Analysis of the extreme diversity of salivary alpha-amylase isoforms generated by physiological proteolysis using liquid chromatography–tandem mass spectrometry

Differential distribution of salivary agglutinin and amylase in the Golgi apparatus and secretory granules of human salivary gland acinar cells

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