* 104700

AMYLASE, SALIVARY, A; AMY1A


Alternative titles; symbols

AMYLASE, SALIVARY; AMY1


HGNC Approved Gene Symbol: AMY1A

Cytogenetic location: 1p21.1     Genomic coordinates (GRCh38): 1:103,655,519-103,664,554 (from NCBI)


TEXT

Description

Salivary alpha-amylase (EC 3.2.1.1) is a monomeric calcium-binding enzyme that initiates starch digestion in the oral cavity. The alpha-amylase enzymes are produced by the salivary glands (encoded by the AMY1A, AMY1B (104701), and AMY1C (104702) genes), and exocrine pancreas (encoded by the AMY2A (104650) and AMY2B (104650) genes). Additionally, a small amount of alpha-amylase is expressed by the AMY2B gene in the liver. The salivary alpha-amylase protein contains 511 amino acids with a 15-residue signal peptide (summary by Santos et al., 2012).


Cloning and Expression

The alpha-amylases hydrolyze alpha-1,4-glucoside bonds in polymers of glucose units. Kamaryt and Laxova (1965, 1966) found 2 amylase isoenzymes in serum, one produced by the salivary gland and the second by the pancreas (see 104650). In 11 of 120 children, a duplication of pancreatic enzyme band was found on starch gel electrophoresis and in each case 1 parent also showed the duplication. In the mouse the salivary and pancreatic amylases are determined by genes at closely linked loci (Sick and Nielsen, 1964). The separate loci in the human were designated AMY1 (salivary) and AMY2 (pancreatic).


Gene Structure

Nishide et al. (1986) showed that the human salivary alpha-amylase gene is about 10 kb long and has 11 exons.


Mapping

By in situ hybridization combined with high resolution cytogenetics, Zabel et al. (1983) assigned the amylase gene to 1p21, the POMC gene (176830) to 2p23, and the somatostatin gene (182450) to 3q28.

Using amylase DNA probes in somatic cell hybrids, Tricoli and Shows (1984) mapped the amylase genes to the 1p22.1-p21 region.

Gumucio et al. (1988) isolated cosmid clones containing 250 kb of genomic DNA from the human amylase gene cluster. These clones were found to contain 7 distinct amylase genes: 2 pancreatic amylase genes, 3 salivary amylase genes, and 2 truncated pseudogenes. Intergenic distances of 17 to 22 kb separated the amylase gene copies.

Multipoint linkage analysis showed that the amylase gene cluster is located distal to NGFB (162030) (Dracopoli and Meisler, 1990).


Molecular Genetics

Polymorphism of both the salivary and the pancreatic serum amylases has been demonstrated in man. Ward et al. (1971) studied amylase in saliva and identified electrophoretic variants.

Pronk et al. (1982) presented evidence they interpreted as indicating duplication of the salivary amylase locus.

Data on gene frequencies of allelic variants were tabulated by Roychoudhury and Nei (1988).

Dracopoli and Meisler (1990) used a (CA)n repeat sequence immediately upstream from the gamma-actin pseudogene associated with the AMY2B gene (104660) in a study of 40 CEPH families. By PCR amplification of genomic DNA, they identified 6 alleles with (CA)n lengths of 16 to 21 repeats. The average heterozygosity was 0.70.

Large-scale copy number variations (LCVs) involve gains or losses of several kilobases to hundreds of kilobases of genomic DNA among phenotypically normal individuals. To investigate LCVs in the human genome, Iafrate et al. (2004) applied array-based comparative genomic hybridization (array CGH) to the genomes of 55 unrelated individuals. The most common LCV (identified in 49.1% of the individuals studied) encompassed the AMY1A and AMY2A locus (Groot et al., 1991). Iafrate et al. (2004) detected relative gains (in 23.6% of cases) and losses (in 25.5% of cases) at this locus and confirmed the array CGH results using metaphase-interphase FISH, high-resolution fiber FISH, and quantitative PCR. In all they described more than 200 LCVs in the human genome. Twenty-four of these variants were present in more than 10% of the individuals studied, and 6 of these variants were present at a frequency of more than 20%. A chromosome map indicating the location of the LCVs was provided. Carter (2004) commented on this work and the parallel work of Sebat et al. (2004).

Starch consumption is a prominent characteristic of agricultural societies and hunter-gatherers in arid environments. In contrast, rainforest and circum-arctic hunter-gatherers and some pastoralists consume much less starch. This behavioral variation raised the possibility that different selective pressures have acted on amylase, the enzyme responsible for starch hydrolysis. Perry et al. (2007) found that copy number of the AMY1 gene is correlated positively with salivary amylase protein level and that individuals from populations with high starch diets have, on average, more AMY1 copies than those with traditionally low starch diets. Comparisons with other loci in a subset of these populations suggested that the extent of AMY1 copy number differentiation is highly unusual. Higher AMY1 copy numbers and protein levels probably improve the digestion of starchy foods and may buffer against the fitness-reducing effects of intestinal disease.

Using a combination of high-precision measurement methods with segregation analysis, Carpenter et al. (2015) determined that most amylase haplotypes worldwide contain odd numbers of AMY1 repeat units, but that haplotypes carrying even numbers of AMY1 repeats are associated with rearrangements giving rise to CNV of the pancreatic amylase genes AMY2A/2B. As a consequence, the copy numbers of AMY1 and AMY2A/2B are numerically correlated. Data from different paralog ratio tests (PRTs) led to the experimental and read-depth characterization of 4 distinct CNV classes affecting AMY2 genes: a deletion of about 75 kb affecting AMY2A (and AMY1); a duplication of about 116 kb including both AMY2A and AMY2B (and a copy of AMY1); higher-order expansions of AMY2A and AMY2B; and an independent duplication of AMY2A but not AMY2B. Among the regional population groupings used by the 1000 Genomes Project, East Asian populations display few AMY2 variations and nearly all individuals have an even AMY1 diploid copy number; deletions of AMY2 are common among the European and American samples, and duplications of AMY2A/2B are at highest frequency in African samples. Carpenter et al. (2015) stated that the qPCR assay used by Perry et al. (2007) systematically underestimated AMY1 copy number.


Evolution

Groot et al. (1990) presented structural analyses of the human amylase gene cluster that allowed them to construct a model for the evolution of this family of genes by a number of consecutive events involving inter- and intrachromosomal crossovers.

In a study comparing human AMY1 copy number variation with that of chimpanzees and bonobos, Perry et al. (2007) found that the average human has 3 times more AMY1 copies than chimpanzees, and bonobos may not have salivary amylase at all. Outgroup comparisons with other great apes suggested that AMY1 copy number was probably gained in the human lineage, rather than lost in chimpanzees. It is hypothesized that starch-rich plant underground storage organs (USOs) such as bulbs, corms, and tubers were a critical food resource for early hominins. The example of amylase as representative of the importance of diet as a widespread source of selective pressure in human evolution is comparable to that of lactase persistence (223100), which has evolved independently in multiple populations.


REFERENCES

  1. Carpenter, D., Dhar, S., Mitchell, L. M., Fu, B., Tyson, J., Shwan, N. A. A., Ynag, F., Thomas, M. G., Armour, J. A. L. Obesity, starch digestion and amylase: association between copy number variants at human salivary (AMY1) and pancreatic (AMY2) amylase genes. Hum. Molec. Genet. 24: 3472-3480, 2015. [PubMed: 25788522, related citations] [Full Text]

  2. Carter, N. P. As normal as normal can be? (Comment) Nature Genet. 36: 931-932, 2004. [PubMed: 15340426, related citations] [Full Text]

  3. de Soyza, K. Polymorphism of human salivary amylase: a preliminary communication. Hum. Genet. 45: 189-192, 1978. [PubMed: 738721, related citations] [Full Text]

  4. Dracopoli, N. C., Meisler, M. H. Mapping the human amylase gene cluster on the proximal short arm of chromosome 1 using a highly informative (CA)n repeat. Genomics 7: 97-102, 1990. [PubMed: 1692298, related citations] [Full Text]

  5. Groot, P. C., Mager, W. H., Frants, R. R. Interpretation of polymorphic DNA patterns in the human alpha-amylase multigene family. Genomics 10: 779-785, 1991. [PubMed: 1679752, related citations] [Full Text]

  6. Groot, P. C., Mager, W. H., Henriquez, N. V., Pronk, J. C., Arwert, F., Planta, R. J., Eriksson, A. W., Frants, R. R. Evolution of the human alpha-amylase multigene family through unequal, homologous, and inter- and intrachromosomal crossovers. Genomics 8: 97-105, 1990. [PubMed: 2081604, related citations] [Full Text]

  7. Gumucio, D. L., Wiebauer, K., Caldwell, R. M., Samuelson, L. C., Meisler, M. H. Concerted evolution of human amylase genes. Molec. Cell. Biol. 8: 1197-1205, 1988. [PubMed: 2452973, related citations] [Full Text]

  8. Iafrate, A. J., Feuk, L., Rivera, M. N., Listewnik, M. L., Donahoe, P. K., Qi, Y., Scherer, S. W., Lee, C. Detection of large-scale variation in the human genome. Nature Genet. 36: 949-951, 2004. [PubMed: 15286789, related citations] [Full Text]

  9. Ishizaki, K., Noda, A., Ikenaga, M., Ida, K., Omoto, K., Nakamura, Y., Matsubara, K. Restriction fragment length polymorphism detected by human salivary amylase cDNA. Hum. Genet. 71: 261-262, 1985. [PubMed: 2998973, related citations] [Full Text]

  10. Kamaryt, J., Laxova, R. Amylase heterogeneity: some genetic and clinical aspects. Humangenetik 1: 579-586, 1965. [PubMed: 5869482, related citations]

  11. Kamaryt, J., Laxova, R. Amylase heterogeneity variants in man. Humangenetik 3: 41-45, 1966. [PubMed: 6010879, related citations] [Full Text]

  12. McGeachin, R. L. Multiple molecular forms of amylase. Ann. N.Y. Acad. Sci. 151: 208-212, 1968. [PubMed: 4180439, related citations] [Full Text]

  13. Muenke, M., Lindgren, V., de Martinville, B., Francke, U. Comparative analysis of mouse-human hybrids with rearranged chromosomes 1 by in situ hybridization and Southern blotting: high resolution mapping of NRAS, NGFB, and AMY on chromosome 1. Somat. Cell Molec. Genet. 10: 589-599, 1984. [PubMed: 6209808, related citations] [Full Text]

  14. Nishide, T., Nakamura, Y., Emi, M., Yamamoto, T., Ogawa, M., Mori, T., Matsubara, K. Primary structure of human salivary alpha-amylase gene. Gene 41: 299-304, 1986. [PubMed: 2423416, related citations] [Full Text]

  15. Perry, G. H., Dominy, N. J., Claw, K. G., Lee, A. S., Fiegler, H., Redon, R., Werner, J., Villanea, F. A., Mountain, J. L., Misra, R., Carter, N. P., Lee, C., Stone, A. C. Diet and the evolution of human amylase gene copy number variation. Nature Genet. 39: 1256-1260, 2007. [PubMed: 17828263, images, related citations] [Full Text]

  16. Pronk, J. C., Frants, R. R., Jansen, W., Eriksson, A. W., Tonino, G. J. M. Evidence for duplication of the human salivary amylase gene. Hum. Genet. 60: 32-35, 1982. [PubMed: 6176528, related citations] [Full Text]

  17. Pronk, J. C., Jansen, W. J., Pronk, A., Pol, C. F. A. M., Frants, R. R., Eriksson, A. W. Salivary protein polymorphism in Kenya: evidence for a new AMY1 allele. Hum. Hered. 34: 212-216, 1984. [PubMed: 6207099, related citations] [Full Text]

  18. Roychoudhury, A. K., Nei, M. Human Polymorphic Genes: World Distribution. New York: Oxford Univ. Press (pub.) 1988.

  19. Santos, J. L., Saus, E., Smalley, S. V., Cataldo, L. R., Alberti, G., Parada, J., Gratacos, M., Estivill, X. Copy number polymorphism of the salivary amylase gene: implications in human nutritional research. J. Nutrigenet. Nutrigenomics 5: 117-131, 2012. [PubMed: 22965187, related citations] [Full Text]

  20. Sebat, J., Lakshmi, B., Troge, J., Alexander, J., Young, J., Lundin, P., Maner, S., Massa, H., Walker, M., Chi, M., Navin, N., Lucito, R., and 9 others. Large-scale copy number polymorphism in the human genome. Science 305: 525-528, 2004. [PubMed: 15273396, related citations] [Full Text]

  21. Sick, K., Nielsen, J. T. Genetics of amylase isozymes in the mouse. Hereditas 51: 291-296, 1964.

  22. Tricoli, J. V., Shows, T. B. Assignment of alpha-amylase genes to the p22.1-p21 region of chromosome 1. (Abstract) Cytogenet. Cell Genet. 37: 597 only, 1984.

  23. Tricoli, J. V., Shows, T. B. Regional assignment of human amylase (AMY) to p22-p21 of chromosome 1. Somat. Cell Molec. Genet. 10: 205-210, 1984. [PubMed: 6608795, related citations] [Full Text]

  24. Ward, J. C., Merritt, A. D., Bixler, D. Human salivary amylase: genetics of electrophoretic variants. Am. J. Hum. Genet. 23: 403-409, 1971. [PubMed: 5097906, related citations]

  25. Wiebauer, K., Gumucio, D. L., Jones, J. M., Caldwell, R. M., Hartle, H. T., Meisler, M. H. A 78-kilobase region of mouse chromosome 3 contains salivary and pancreatic amylase genes and a pseudogene. Proc. Nat. Acad. Sci. 82: 5446-5449, 1985. [PubMed: 2410924, related citations] [Full Text]

  26. Zabel, B. U., Naylor, S. L., Sakaguchi, A. Y., Bell, G. I., Shows, T. B. High-resolution chromosomal localization of human genes for amylase, proopiomelanocortin, somatostatin, and a DNA fragment (D3S1) by in situ hybridization. Proc. Nat. Acad. Sci. 80: 6932-6936, 1983. [PubMed: 6196780, related citations] [Full Text]


Carol A. Bocchini - updated : 02/04/2019
Victor A. McKusick - updated : 10/18/2007
Victor A. McKusick - updated : 9/27/2004
Creation Date:
Victor A. McKusick : 6/4/1986
carol : 02/05/2019
carol : 02/04/2019
alopez : 10/24/2007
terry : 10/18/2007
terry : 11/2/2004
alopez : 9/30/2004
terry : 9/27/2004
mark : 11/27/1996
mimadm : 2/11/1994
supermim : 3/16/1992
carol : 2/27/1992
carol : 10/21/1991
carol : 12/14/1990
carol : 12/6/1990

* 104700

AMYLASE, SALIVARY, A; AMY1A


Alternative titles; symbols

AMYLASE, SALIVARY; AMY1


HGNC Approved Gene Symbol: AMY1A

Cytogenetic location: 1p21.1     Genomic coordinates (GRCh38): 1:103,655,519-103,664,554 (from NCBI)


TEXT

Description

Salivary alpha-amylase (EC 3.2.1.1) is a monomeric calcium-binding enzyme that initiates starch digestion in the oral cavity. The alpha-amylase enzymes are produced by the salivary glands (encoded by the AMY1A, AMY1B (104701), and AMY1C (104702) genes), and exocrine pancreas (encoded by the AMY2A (104650) and AMY2B (104650) genes). Additionally, a small amount of alpha-amylase is expressed by the AMY2B gene in the liver. The salivary alpha-amylase protein contains 511 amino acids with a 15-residue signal peptide (summary by Santos et al., 2012).


Cloning and Expression

The alpha-amylases hydrolyze alpha-1,4-glucoside bonds in polymers of glucose units. Kamaryt and Laxova (1965, 1966) found 2 amylase isoenzymes in serum, one produced by the salivary gland and the second by the pancreas (see 104650). In 11 of 120 children, a duplication of pancreatic enzyme band was found on starch gel electrophoresis and in each case 1 parent also showed the duplication. In the mouse the salivary and pancreatic amylases are determined by genes at closely linked loci (Sick and Nielsen, 1964). The separate loci in the human were designated AMY1 (salivary) and AMY2 (pancreatic).


Gene Structure

Nishide et al. (1986) showed that the human salivary alpha-amylase gene is about 10 kb long and has 11 exons.


Mapping

By in situ hybridization combined with high resolution cytogenetics, Zabel et al. (1983) assigned the amylase gene to 1p21, the POMC gene (176830) to 2p23, and the somatostatin gene (182450) to 3q28.

Using amylase DNA probes in somatic cell hybrids, Tricoli and Shows (1984) mapped the amylase genes to the 1p22.1-p21 region.

Gumucio et al. (1988) isolated cosmid clones containing 250 kb of genomic DNA from the human amylase gene cluster. These clones were found to contain 7 distinct amylase genes: 2 pancreatic amylase genes, 3 salivary amylase genes, and 2 truncated pseudogenes. Intergenic distances of 17 to 22 kb separated the amylase gene copies.

Multipoint linkage analysis showed that the amylase gene cluster is located distal to NGFB (162030) (Dracopoli and Meisler, 1990).


Molecular Genetics

Polymorphism of both the salivary and the pancreatic serum amylases has been demonstrated in man. Ward et al. (1971) studied amylase in saliva and identified electrophoretic variants.

Pronk et al. (1982) presented evidence they interpreted as indicating duplication of the salivary amylase locus.

Data on gene frequencies of allelic variants were tabulated by Roychoudhury and Nei (1988).

Dracopoli and Meisler (1990) used a (CA)n repeat sequence immediately upstream from the gamma-actin pseudogene associated with the AMY2B gene (104660) in a study of 40 CEPH families. By PCR amplification of genomic DNA, they identified 6 alleles with (CA)n lengths of 16 to 21 repeats. The average heterozygosity was 0.70.

Large-scale copy number variations (LCVs) involve gains or losses of several kilobases to hundreds of kilobases of genomic DNA among phenotypically normal individuals. To investigate LCVs in the human genome, Iafrate et al. (2004) applied array-based comparative genomic hybridization (array CGH) to the genomes of 55 unrelated individuals. The most common LCV (identified in 49.1% of the individuals studied) encompassed the AMY1A and AMY2A locus (Groot et al., 1991). Iafrate et al. (2004) detected relative gains (in 23.6% of cases) and losses (in 25.5% of cases) at this locus and confirmed the array CGH results using metaphase-interphase FISH, high-resolution fiber FISH, and quantitative PCR. In all they described more than 200 LCVs in the human genome. Twenty-four of these variants were present in more than 10% of the individuals studied, and 6 of these variants were present at a frequency of more than 20%. A chromosome map indicating the location of the LCVs was provided. Carter (2004) commented on this work and the parallel work of Sebat et al. (2004).

Starch consumption is a prominent characteristic of agricultural societies and hunter-gatherers in arid environments. In contrast, rainforest and circum-arctic hunter-gatherers and some pastoralists consume much less starch. This behavioral variation raised the possibility that different selective pressures have acted on amylase, the enzyme responsible for starch hydrolysis. Perry et al. (2007) found that copy number of the AMY1 gene is correlated positively with salivary amylase protein level and that individuals from populations with high starch diets have, on average, more AMY1 copies than those with traditionally low starch diets. Comparisons with other loci in a subset of these populations suggested that the extent of AMY1 copy number differentiation is highly unusual. Higher AMY1 copy numbers and protein levels probably improve the digestion of starchy foods and may buffer against the fitness-reducing effects of intestinal disease.

Using a combination of high-precision measurement methods with segregation analysis, Carpenter et al. (2015) determined that most amylase haplotypes worldwide contain odd numbers of AMY1 repeat units, but that haplotypes carrying even numbers of AMY1 repeats are associated with rearrangements giving rise to CNV of the pancreatic amylase genes AMY2A/2B. As a consequence, the copy numbers of AMY1 and AMY2A/2B are numerically correlated. Data from different paralog ratio tests (PRTs) led to the experimental and read-depth characterization of 4 distinct CNV classes affecting AMY2 genes: a deletion of about 75 kb affecting AMY2A (and AMY1); a duplication of about 116 kb including both AMY2A and AMY2B (and a copy of AMY1); higher-order expansions of AMY2A and AMY2B; and an independent duplication of AMY2A but not AMY2B. Among the regional population groupings used by the 1000 Genomes Project, East Asian populations display few AMY2 variations and nearly all individuals have an even AMY1 diploid copy number; deletions of AMY2 are common among the European and American samples, and duplications of AMY2A/2B are at highest frequency in African samples. Carpenter et al. (2015) stated that the qPCR assay used by Perry et al. (2007) systematically underestimated AMY1 copy number.


Evolution

Groot et al. (1990) presented structural analyses of the human amylase gene cluster that allowed them to construct a model for the evolution of this family of genes by a number of consecutive events involving inter- and intrachromosomal crossovers.

In a study comparing human AMY1 copy number variation with that of chimpanzees and bonobos, Perry et al. (2007) found that the average human has 3 times more AMY1 copies than chimpanzees, and bonobos may not have salivary amylase at all. Outgroup comparisons with other great apes suggested that AMY1 copy number was probably gained in the human lineage, rather than lost in chimpanzees. It is hypothesized that starch-rich plant underground storage organs (USOs) such as bulbs, corms, and tubers were a critical food resource for early hominins. The example of amylase as representative of the importance of diet as a widespread source of selective pressure in human evolution is comparable to that of lactase persistence (223100), which has evolved independently in multiple populations.


See Also:

de Soyza (1978); Ishizaki et al. (1985); McGeachin (1968); Muenke et al. (1984); Pronk et al. (1984); Tricoli and Shows (1984); Wiebauer et al. (1985)

REFERENCES

  1. Carpenter, D., Dhar, S., Mitchell, L. M., Fu, B., Tyson, J., Shwan, N. A. A., Ynag, F., Thomas, M. G., Armour, J. A. L. Obesity, starch digestion and amylase: association between copy number variants at human salivary (AMY1) and pancreatic (AMY2) amylase genes. Hum. Molec. Genet. 24: 3472-3480, 2015. [PubMed: 25788522] [Full Text: https://doi.org/10.1093/hmg/ddv098]

  2. Carter, N. P. As normal as normal can be? (Comment) Nature Genet. 36: 931-932, 2004. [PubMed: 15340426] [Full Text: https://doi.org/10.1038/ng0904-931]

  3. de Soyza, K. Polymorphism of human salivary amylase: a preliminary communication. Hum. Genet. 45: 189-192, 1978. [PubMed: 738721] [Full Text: https://doi.org/10.1007/BF00286961]

  4. Dracopoli, N. C., Meisler, M. H. Mapping the human amylase gene cluster on the proximal short arm of chromosome 1 using a highly informative (CA)n repeat. Genomics 7: 97-102, 1990. [PubMed: 1692298] [Full Text: https://doi.org/10.1016/0888-7543(90)90523-w]

  5. Groot, P. C., Mager, W. H., Frants, R. R. Interpretation of polymorphic DNA patterns in the human alpha-amylase multigene family. Genomics 10: 779-785, 1991. [PubMed: 1679752] [Full Text: https://doi.org/10.1016/0888-7543(91)90463-o]

  6. Groot, P. C., Mager, W. H., Henriquez, N. V., Pronk, J. C., Arwert, F., Planta, R. J., Eriksson, A. W., Frants, R. R. Evolution of the human alpha-amylase multigene family through unequal, homologous, and inter- and intrachromosomal crossovers. Genomics 8: 97-105, 1990. [PubMed: 2081604] [Full Text: https://doi.org/10.1016/0888-7543(90)90230-r]

  7. Gumucio, D. L., Wiebauer, K., Caldwell, R. M., Samuelson, L. C., Meisler, M. H. Concerted evolution of human amylase genes. Molec. Cell. Biol. 8: 1197-1205, 1988. [PubMed: 2452973] [Full Text: https://doi.org/10.1128/mcb.8.3.1197-1205.1988]

  8. Iafrate, A. J., Feuk, L., Rivera, M. N., Listewnik, M. L., Donahoe, P. K., Qi, Y., Scherer, S. W., Lee, C. Detection of large-scale variation in the human genome. Nature Genet. 36: 949-951, 2004. [PubMed: 15286789] [Full Text: https://doi.org/10.1038/ng1416]

  9. Ishizaki, K., Noda, A., Ikenaga, M., Ida, K., Omoto, K., Nakamura, Y., Matsubara, K. Restriction fragment length polymorphism detected by human salivary amylase cDNA. Hum. Genet. 71: 261-262, 1985. [PubMed: 2998973] [Full Text: https://doi.org/10.1007/BF00284587]

  10. Kamaryt, J., Laxova, R. Amylase heterogeneity: some genetic and clinical aspects. Humangenetik 1: 579-586, 1965. [PubMed: 5869482]

  11. Kamaryt, J., Laxova, R. Amylase heterogeneity variants in man. Humangenetik 3: 41-45, 1966. [PubMed: 6010879] [Full Text: https://doi.org/10.1007/BF00273017]

  12. McGeachin, R. L. Multiple molecular forms of amylase. Ann. N.Y. Acad. Sci. 151: 208-212, 1968. [PubMed: 4180439] [Full Text: https://doi.org/10.1111/j.1749-6632.1968.tb11890.x]

  13. Muenke, M., Lindgren, V., de Martinville, B., Francke, U. Comparative analysis of mouse-human hybrids with rearranged chromosomes 1 by in situ hybridization and Southern blotting: high resolution mapping of NRAS, NGFB, and AMY on chromosome 1. Somat. Cell Molec. Genet. 10: 589-599, 1984. [PubMed: 6209808] [Full Text: https://doi.org/10.1007/BF01535224]

  14. Nishide, T., Nakamura, Y., Emi, M., Yamamoto, T., Ogawa, M., Mori, T., Matsubara, K. Primary structure of human salivary alpha-amylase gene. Gene 41: 299-304, 1986. [PubMed: 2423416] [Full Text: https://doi.org/10.1016/0378-1119(86)90110-1]

  15. Perry, G. H., Dominy, N. J., Claw, K. G., Lee, A. S., Fiegler, H., Redon, R., Werner, J., Villanea, F. A., Mountain, J. L., Misra, R., Carter, N. P., Lee, C., Stone, A. C. Diet and the evolution of human amylase gene copy number variation. Nature Genet. 39: 1256-1260, 2007. [PubMed: 17828263] [Full Text: https://doi.org/10.1038/ng2123]

  16. Pronk, J. C., Frants, R. R., Jansen, W., Eriksson, A. W., Tonino, G. J. M. Evidence for duplication of the human salivary amylase gene. Hum. Genet. 60: 32-35, 1982. [PubMed: 6176528] [Full Text: https://doi.org/10.1007/BF00281260]

  17. Pronk, J. C., Jansen, W. J., Pronk, A., Pol, C. F. A. M., Frants, R. R., Eriksson, A. W. Salivary protein polymorphism in Kenya: evidence for a new AMY1 allele. Hum. Hered. 34: 212-216, 1984. [PubMed: 6207099] [Full Text: https://doi.org/10.1159/000153465]

  18. Roychoudhury, A. K., Nei, M. Human Polymorphic Genes: World Distribution. New York: Oxford Univ. Press (pub.) 1988.

  19. Santos, J. L., Saus, E., Smalley, S. V., Cataldo, L. R., Alberti, G., Parada, J., Gratacos, M., Estivill, X. Copy number polymorphism of the salivary amylase gene: implications in human nutritional research. J. Nutrigenet. Nutrigenomics 5: 117-131, 2012. [PubMed: 22965187] [Full Text: https://doi.org/10.1159/000339951]

  20. Sebat, J., Lakshmi, B., Troge, J., Alexander, J., Young, J., Lundin, P., Maner, S., Massa, H., Walker, M., Chi, M., Navin, N., Lucito, R., and 9 others. Large-scale copy number polymorphism in the human genome. Science 305: 525-528, 2004. [PubMed: 15273396] [Full Text: https://doi.org/10.1126/science.1098918]

  21. Sick, K., Nielsen, J. T. Genetics of amylase isozymes in the mouse. Hereditas 51: 291-296, 1964.

  22. Tricoli, J. V., Shows, T. B. Assignment of alpha-amylase genes to the p22.1-p21 region of chromosome 1. (Abstract) Cytogenet. Cell Genet. 37: 597 only, 1984.

  23. Tricoli, J. V., Shows, T. B. Regional assignment of human amylase (AMY) to p22-p21 of chromosome 1. Somat. Cell Molec. Genet. 10: 205-210, 1984. [PubMed: 6608795] [Full Text: https://doi.org/10.1007/BF01534909]

  24. Ward, J. C., Merritt, A. D., Bixler, D. Human salivary amylase: genetics of electrophoretic variants. Am. J. Hum. Genet. 23: 403-409, 1971. [PubMed: 5097906]

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Contributors:
Carol A. Bocchini - updated : 02/04/2019
Victor A. McKusick - updated : 10/18/2007
Victor A. McKusick - updated : 9/27/2004

Creation Date:
Victor A. McKusick : 6/4/1986

Edit History:
carol : 02/05/2019
carol : 02/04/2019
alopez : 10/24/2007
terry : 10/18/2007
terry : 11/2/2004
alopez : 9/30/2004
terry : 9/27/2004
mark : 11/27/1996
mimadm : 2/11/1994
supermim : 3/16/1992
carol : 2/27/1992
carol : 10/21/1991
carol : 12/14/1990
carol : 12/6/1990