Dipeptidyl peptidase IV activity in the blood of the American alligator (Alligator mississippiensis)

Merchant, Mark; Monroe, Caleb; Falconi, Rodolfo

doi:10.1016/j.cbpb.2009.07.010

Cited by 7 publications

(7 citation statements)

References 37 publications

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“…For instance, serum complement activities have been described for the American alligator [19], the freshwater and saltwater crocodiles [20], the broad-snouted caiman [21], and the American crocodile [22]. In addition, dipeptidyl peptidase IV activity has been characterized in the American alligator [23] and the American crocodile [24]. Furthermore, several Merchant et al [10] showed that the antibacterial activities of all 23 species of crocodilian correlated with molecular and morphological hypotheses of crocodilian diversification.…”

Section: Discussionmentioning

confidence: 99%

Comparison of Serum Phospholipase A2 Activities of All Known Extant Crocodylian Species

Merchant¹,

McAdon²,

Mead³

et al. 2017

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Serum samples from all 23 extant crocodilian species were tested for phospholipase A 2 (PLA 2 ) activity against nine different bacterial species. The data were used to generate a PLA 2 activity profile for each crocodilian species, and the data were used to compare the activities of the three main lineages (Alligatoridae, Crocodylidae, and Gavialidae), the seven different genera, and to compare all of the 23 individual species. The data revealed that the three lineages of crocodilians (Alligatoridae, Crocodylidae, and Gavialidae) exhibited PLA 2 activities toward nine species of bacteria that were statistically distinguishable. In addition, the PLA 2 activities of crocodilians in a specific genus tended to be more similar to other members in their genus than to members of other crocodilian genera.

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Section: Discussionmentioning

confidence: 99%

Comparison of Serum Phospholipase A2 Activities of All Known Extant Crocodylian Species

Merchant¹,

McAdon²,

Mead³

et al. 2017

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“…The amount of product formed, using different volumes of Komodo dragon serum, is higher that observed for crocodilian species when comparable volumes were used. By way of comparison, the maximum activity observed in this study was 160.5 ± 3.6 nmol of product formed (100 µL serum), while 200 µL of serum from the American alligator (Alligator mississippiensis) produced a maximum of 90 nmol [17]. Likewise, serum from the American crocodile (Crocodylus acutus) produced only 8 nmol [18], and sera from the broad-snouted caiman (Caiman latirostris) and the yacare caiman (Caiman yacare) produced approximately 120 and 100 nmol of product, respectively [19].…”

Section: Resultsmentioning

confidence: 63%

“…Kinetic analysis of the rate of product AFC formation by Komodo dragon peripheral blood DPPIV showed a near-linear increase in the rate of accumulation of approximately 1.12 nmol/min from 5-180 min. The rate of product formation observed using a constant volume of Komodo dragon serum, was higher than that observed for similar volumes of serum from a variety of crocodilian species [16][17][18]20]. The increase in DPPIV activity shows that the Komodo dragon has a high capacity for N-terminal proteolysis of specific sequences, and a potentially high capability for facilitation of immunocompetence [2,7].…”

Section: Figure 2 Inhibition Of Dppiv Activity In Komodo Dragon Serumentioning

confidence: 70%

“…To date, the majority of work with DPPIV in reptiles has been focused on snake venoms [21]. However, a few studies exist in which the soluble serum DPPIV have been characterized in crocodilians [16][17][18]20]. Although these studies did not link DPPIV activity to immune competency, it was assumed that these activities were immunologically important, due to the presence in the peripheral circulation.…”

Section: Resultsmentioning

confidence: 99%

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Characterization of Dipeptidyl Peptidase IV Enzyme Activity in Serum of the Komodo Dragon (Varanus komodoensis)

Merchant

Henry²,

Falconi³

et al. 2015

IJBCRR

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Aims: Soluble serum dipeptidyl peptidase IV (DPPIV) is a protease that cleaves dipeptides from proteins that have alanine or proline next to the N-terminal amino acid. This enzyme demonstrates substantial immune function by regulating T-lymphocyte activity, T-cell chemotaxis, growth, and proliferation during an inflammatory response. The goal of this study was to characterize DPPIV activity in the serum of the Komodo dragon (Varanus komodoensis). Study design: Place and Duration of Study: Serum was collected from eight Komodo dragons at the San Antonio Zoo (n = 5) and Houston Zoo (n = 3) in June of 2012. The samples were analyzed for DPPIV enzyme activity in the Department of Chemistry at McNeese State University in Lake Charles, Louisiana, USA Methodology: We used Ala-Pro-AFC, a dipeptide conjugated to a fluorescent probe via an amide linkage, to measure the activity of DPPIV in the serum of Komodo dragons (Varanus komodoensis). The fluorescent intensity of the product formed was measured at excitation and emission wavelengths of 395 and 530 nm, respectively, in a fluorimeter. Results: Incubation of different volumes of serum from the Komodo dragon with Ala-Pro-AFC resulted in a volume-dependent increase in fluorescent intensity, which was decreased in a concentration-dependent manner by diprotin A, a specific inhibitor of DPPIV activity. Kinetic analysis showed that the DPPIV enzyme activity was detectable after five minutes, and that was nearly linear for three hours. A thermal profile showed that Komodo dragon DPPIV exhibited dramatically reduced activities at low temperatures (5-10 o C), but activity increased linearly with temperature and was maximal at the highest temperature tested (40 o C). Conclusion: These results from this study indicate that Komodo dragons exhibit considerably high serum DPPIV activities, which are likely to contribute to T-cell activation and function, and act as a bridge between innate and adaptive immunity in these ancient vertebrates.

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“…Alligators thermoregulate to an internal body temperature of 31˚C -32˚C [30], where many physiological parameters such as cardiac function [31] and general metabolism [32], are optimized. In addition, many immunological parameters, such as serum complement [33], phospholipase A 2 [34], and dipeptidyl peptidase IV [35] activities have been shown to exhibit comparable thermal characteristics. At temperatures higher than the preferred body temperature the activity ChT remains high (Figure 3).…”

Section: Discussionmentioning

confidence: 99%

Characterization of Chitotriosidase Enzyme Activity in the Serum of the American Alligator (<i>Alligator mississippiensis</i>)

Kidder¹,

Falconi²,

Merchant³

2018

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Chitotriosidase (ChT) is an endoglucosaminidase enzyme that cleaves chitinous substrates and has been strongly associated with innate immune activity and the ability to identify non-selftissues. This enzyme activity was detected and characterized the serum from the American alligator (Alligator mississippiensis) using a fluorometric probe. Alligator serum exhibited volume-dependent activity, with activity (2.1 ± 0.3 μmol/min) observed at dilutions as low as a 1:150, and maximum activity (5.2 ± 0.6 μmol/min) measured at a dilution of 1:30. Alligator serum ChT showed linear activity for approximately 20 min, at which time activity decreased exponentially, presumably due to the depletion of substrate. In addition, the ChT activity in alligator serum was temperature-dependent with low activity at 5˚C, a sharp increase from 10˚C-30˚C, and maximal activity from 30˚C-40˚C. The activity was inhibited in the presence of water-soluble chitin, but not mannan, indicating the specificity of the enzyme. The presence of ChT in alligator serum is likely to be partially responsible for the potent innate immune system of these crocodylians, and particularly antifungal activities.

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Dipeptidyl peptidase IV activity in the blood of the American alligator (Alligator mississippiensis)

Cited by 7 publications

References 37 publications

Comparison of Serum Phospholipase A2 Activities of All Known Extant Crocodylian Species

Comparison of Serum Phospholipase A2 Activities of All Known Extant Crocodylian Species

Characterization of Dipeptidyl Peptidase IV Enzyme Activity in Serum of the Komodo Dragon (Varanus komodoensis)

Characterization of Chitotriosidase Enzyme Activity in the Serum of the American Alligator (<i>Alligator mississippiensis</i>)

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Dipeptidyl peptidase IV activity in the blood of the American alligator (Alligator mississippiensis)

Cited by 7 publications

References 37 publications

Comparison of Serum Phospholipase A2 Activities of All Known Extant Crocodylian Species

Comparison of Serum Phospholipase A2 Activities of All Known Extant Crocodylian Species

Characterization of Dipeptidyl Peptidase IV Enzyme Activity in Serum of the Komodo Dragon (Varanus komodoensis)

Characterization of Chitotriosidase Enzyme Activity in the Serum of the American Alligator (&lt;i&gt;Alligator mississippiensis&lt;/i&gt;)

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Characterization of Chitotriosidase Enzyme Activity in the Serum of the American Alligator (<i>Alligator mississippiensis</i>)