Amylase levels in the tissues and body fluids of several primate species

doi:10.1016/0300-9629(82)90045-7

Comparative Biochemistry and Physiology Part A: Physiology

Volume 72, Issue 1, 1982, Pages 267-269

Comparative Biochemi...

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Abstract

1.
1. Serum amylase levels in the gorilla, orang-utan, chimpanzee and squirrel monkey are similar to man. Serum amylase in the Rhesus macaque is almost a whole order of magnitude higher than man.
2.
2. Of the several species tested, all have appreciable amylase in saliva or the parotid gland except the squirrel monkey.
3.
3. High levels of amylase were found in the pancreas of all species tested. Amylase was found in the livers of all species tested.
4.
4. In in vivo experiments with squirrel monkeys, injection of puromycin did not alter serum amylase levels.

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Cited by (26)

Salivary amylase - The enzyme of unspecialized euryphagous animals
2015, Archives of Oral Biology
Citation Excerpt :
Because of a low starch content of this diet, probably amylase is not a component of their saliva. In contrast, high amylase levels (2400 U/g) have been detected in the saliva of collared mangabey (Cercocebus torquatus).117 Primarily the monkey feeds on seeds, nuts, fruits and leaves and infrequently on small animals suggesting that salivary amylase would be advantageous.
Alpha-amylase (EC 3.2.1.1) is the most abundant enzyme in the saliva of man and of several vertebrates. In humans, salivary amylase is mainly formed in the parotid gland; its activity is of high inter-individual and intra-individual variability. The physiological functions of α-amylase have not yet been explored completely. It is well known that the enzyme cleaves the α-(1,4)-glycosidic bonds of polysaccharides. Furthermore it plays an important role in initial bioadhesion in man, facilitating carbohydrate metabolism and bacterial adherence at the tooth surface and therewith caries initiation. Nevertheless, it is still a matter of interest why humans have such high amounts of salivary amylase.
The review presents an evolutionary approach by considering salivary amylase in the animal kingdom with special focus on mammalians divided into the three main nutritional types carnivores, herbivores, and omnivores; it was postulated that for most mammalian animals salivary α-amylase is essential.
The enzyme has been detected in saliva of some herbivores and many omnivorous animals, but not in pure carnivores. Focusing on ruminants, negligible levels or an absence of α-amylase was determined. Presence and activity probably differ depending on the species-specific diet. Animals feeding on unripe fruits, seeds, roots and bulbs exhibit higher activity of salivary α-amylase than species consuming ripe fruits, insects, and vertebrates.
In contrast to carnivores and most herbivores, omnivores have considerable amounts of amylase in their saliva. Though, the starch-digesting enzyme has been investigated well, the physiological function of amylase in saliva has not yet been explored completely. It can be hypothesized that nutritional habits affect expression of enzymes in the saliva of animals. It has to be verified, whether α-amylase is genetically or epigenetically determined. As a consequence of the development of agriculture, and following dietary changes, amylase can be recognized as a nutritional and evolutionary marker. Interdisciplinary evolutionary research might offer new perspectives for preventive dentistry.
Insights into hominin phenotypic and dietary evolution from ancient DNA sequence data
2015, Journal of Human Evolution
Citation Excerpt :
Humans have an average of approximately six total copies of the salivary amylase gene (AMY1), whereas chimpanzees, who consume relatively small amounts of dietary starch compared with most human populations (Hohmann et al., 2006), have only two diploid copies, or one per chromosome (Perry et al., 2007). The variable number of AMY1 gene copies observed among humans is positively correlated with salivary amylase protein levels (Bank et al., 1992; Perry et al., 2007), suggesting that the human-chimpanzee copy number difference likewise explains the substantial between-species difference in salivary amylase protein expression (McGeachin and Akin, 1982). Differences in the average number of AMY1 copies between modern human populations with relatively higher versus lower levels of dietary starch intake and the pattern of variation relative to other copy number variable loci suggests that a greater number of AMY1 copies may have been adaptive under conditions of high starch consumption (Perry et al., 2007).
Nuclear genome sequence data from Neandertals, Denisovans, and archaic anatomically modern humans can be used to complement our understanding of hominin evolutionary biology and ecology through i) direct inference of archaic hominin phenotypes, ii) indirect inference of those phenotypes by identifying the effects of previously-introgressed alleles still present among modern humans, or iii) determining the evolutionary timing of relevant hominin-specific genetic changes. Here we review and reanalyze published Neandertal and Denisovan genome sequence data to illustrate an example of the third approach. Specifically, we infer the timing of five human gene presence/absence changes that may be related to particular hominin-specific dietary changes and discuss these results in the context of our broader reconstructions of hominin evolutionary ecology. We show that pseudogenizing (gene loss) mutations in the TAS2R62 and TAS2R64 bitter taste receptor genes and the MYH16 masticatory myosin gene occurred after the hominin-chimpanzee divergence but before the divergence of the human and Neandertal/Denisovan lineages. The absence of a functional MYH16 protein may explain our relatively reduced jaw muscles; this gene loss may have followed the adoption of cooking behavior. In contrast, salivary amylase gene (AMY1) duplications were not observed in the Neandertal and Denisovan genomes, suggesting a relatively recent origin for the AMY1 copy number gains that are observed in modern humans. Thus, if earlier hominins were consuming large quantities of starch-rich underground storage organs, as previously hypothesized, then they were likely doing so without the digestive benefits of increased salivary amylase production. Our most surprising result was the observation of a heterozygous mutation in the first codon of the TAS2R38 bitter taste receptor gene in the Neandertal individual, which likely would have resulted in a non-functional protein and inter-individual PTC (phenylthiocarbamide) taste sensitivity variation, as also observed in both humans and chimpanzees.
Stress affects salivary alpha-Amylase activity in bonobos
2012, Physiology and Behavior
Citation Excerpt :
Therefore, the variation in the degree of activation of different stress response systems might reflect alternative coping mechanisms or individual traits (reviewed in [31]). While some New World primate species do not produce sAA [32], all Old World primates thus far investigated for the production of sAA do, including macaques, baboons [32–35], and hominoidae such as chimpanzees, orangutans, and gorillas [36–39]. However, in comparison to chimpanzees, bonobos, the fourth African great ape, have increased AMY1 copy numbers, but AMY1 in bonobos has a distributed coding sequence.
Salivary alpha-Amylase (sAA) is a starch digesting enzyme. In addition to its function in the context of nutrition, sAA has also turned out to be useful for monitoring sympathetic nervous system activity. Recent studies on humans have found a relationship between intra-individual changes in sAA activity and physical and psychological stress. In studies on primates and other vertebrates, non-invasive monitoring of short-term stress responses is usually based on measurements of cortisol levels, which are indicative of hypothalamic–pituitary–adrenal activity. The few studies that have used both cortisol levels and sAA activity indicate that these two markers may respond differently and independently to different types of stress such that variation in the degree of the activation of different stress response systems might reflect alternative coping mechanisms or individual traits. Here, we present the first data on intra- and inter-individual variation of sAA activity in captive bonobos and compare the results with information from other ape species and humans. Our results indicate that sAA activity in the bonobo samples was significantly lower than in the human samples but within the range of other great ape species. In addition, sAA activity was significantly higher in samples collected at times when subjects had been exposed to stressors (judged by changes in behavioral patterns and cortisol levels) than in samples collected at other times. Our results indicate that bonobos possess functioning sAA and, as in other species, sAA activity is influenced by autonomic nervous system activity. Monitoring sAA activity could therefore be a useful tool for evaluating stress in bonobos.
Saliva research in zoos - An aid for appropriate feeding of nutritional specialists
2011, Zoologische
Between 2008 and 2010 the Zoological gardens in Rheine, Stuttgart, Karlsruhe, Cologne and Zurich took part in a research project initiated by scientists of the Institute of Animal Science, University of Bonn. Saliva was collected from various zoo animals to determine certain dietary adaptations on enzymatic and physiological levels that might explain or change our current understanding of animal nutrition and the feeding in zoo environments. The interest was primarily focused on species with specialized nutritional needs or fermentation strategies such as geladas, chimpanzees, camels and zebras. The work produced highly valuable data especially on geladas, which, despite from their adaptation to grass diet, revealed to have the enzymatic precondition (salivary amylase) to use starch-rich food items very effectively. Therefore, to prevent obesity in captive geladas, the reduction of starchy food in their daily rations is mandatory. Finally, saliva sampling is an easy, cost-effective and non-invasive procedure, the use of which is both practical and attractive in a zoo environment. In the future, the world-wide emerging field of salivary research might give birth to new applications of saliva as a tool to detect biomarkers of physiology and diseases in zoo animals.
Sleep quantitation in common marmoset, cotton top tamarin and squirrel monkey by non-invasive actigraphy
2006, Comparative Biochemistry and Physiology - A Molecular and Integrative Physiology
Sleep quantitation data on the Neotropical primate species, apart from the squirrel monkey, are still sparse. As such, we have quantitated sleep in the common marmosets (Callithrix jacchus), cotton top tamarins (Saguinus oedipus) and squirrel monkeys (Saimiri sciureus) reared in one primate facility simultaneously, by non-invasive actigraphy. The range in total sleep time/24 h measured for male adult common marmosets, cotton top tamarins and squirrel monkeys were 713–793 min (n = 4), 707–889 min (n = 4) and 459–475 min (n = 2) respectively. The range in sleep episode length /12 h dark phase for marmosets, tamarins and squirrel monkeys were 21–52 min (n = 3), 10–28 min (n = 4) and 9–15 min (n = 2) respectively. Since vigilance is a critical evolutionary adaptive feature of predator avoidance among Callitrichid monkeys and squirrel monkeys, the shorter ranges in sleep episode length recorded, even under captivity, in this study could be interpreted as probable indicators of such vigilance behavior during the rest phase. We hypothesize that the vigilance behavior when it exists during a primate's active phase should also prevail when it is at rest (sleep). This hypothesis deserves additional testing in female Callitrichid monkeys.
Salivary alpha-amylase stress reactivity in advanced-aged marmosets (Callithrix jacchus): Impacts of cognitive function and oral health status
2024, American Journal of Primatology

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Comparative Biochemistry and Physiology Part A: Physiology

Abstract

References (19)

Amylase levels in the tissues and body fluids of the domestic cat (Felis catus)

Comp. Biochem. Physiol.

Amylase distribution in extrapancreatic extrasalivary tissues

Archs Biochem. Biophys.

The in vivo effects of puromycin on amylase levels in the serum, liver, salivary glands and pancreas of the rat

Archs Biochem. Biophys.

Amylase in isolated liver cells

J. biol. Chem.

Factors affecting amylase output by the isolated perfused liver

Archs Biochem. Biophys.

Amylase and other protein components of parotid saliva of the baboon, Papio anubis

Comp. Biochem. Physiol.

Normal serum biochemical values of Macaca arctoides, Macaca fascicularis and Macaca radiata

Lab. Anim. Sci.

An ultrastructural study of the submandibular glands of the squirrel monkey, Saimiri sciureus

J. Morphol.

Normal values for blood constituents of the baboon

Lab. Anim. Sci.

Cited by (26)

Salivary amylase - The enzyme of unspecialized euryphagous animals

Insights into hominin phenotypic and dietary evolution from ancient DNA sequence data

Stress affects salivary alpha-Amylase activity in bonobos

Saliva research in zoos - An aid for appropriate feeding of nutritional specialists

Sleep quantitation in common marmoset, cotton top tamarin and squirrel monkey by non-invasive actigraphy

Salivary alpha-amylase stress reactivity in advanced-aged marmosets (Callithrix jacchus): Impacts of cognitive function and oral health status