Archives

  • 2018-07
  • 2019-04
  • 2019-05
  • 2019-06
  • 2019-07
  • 2019-08
  • 2019-09
  • 2019-10
  • 2019-11
  • 2019-12
  • 2020-01
  • 2020-02
  • 2020-03
  • 2020-04
  • 2020-05
  • 2020-06
  • 2020-07
  • 2020-08
  • 2020-09
  • 2020-10
  • 2020-11
  • 2020-12
  • 2021-01
  • 2021-02
  • 2021-03
  • 2021-04
  • 2021-05
  • 2021-06
  • 2021-07
  • 2021-08
  • 2021-09
  • 2021-10
  • 2021-11
  • 2021-12
  • 2022-01
  • 2022-02
  • 2022-03
  • 2022-04
  • 2022-05
  • 2022-06
  • 2022-07
  • 2022-08
  • 2022-09
  • 2022-10
  • 2022-11
  • 2022-12
  • 2023-01
  • 2023-02
  • 2023-03
  • 2023-04
  • 2023-05
  • 2023-06
  • 2023-08
  • 2023-09
  • 2023-10
  • 2023-11
  • 2023-12
  • 2024-01
  • 2024-02
  • 2024-03
  • 2024-04
  • 2024-05

    • Although ACE genetic variance does not influence the level

    2024-01-30

    Although ACE genetic variance does not influence the level of bradykinin significantly, the bradykinin level tends to be affected by ACE inhibitor therapy used by patients. ACE inhibitor reduces the ACE activity that may lead to the accumulation of serum bradykinin. The level of bradykinin tends to increase in patients treated with captopril and, conversely, to decrease in patients treated using lisinopril, even though statistically there was no significant difference. This condition might be caused by the large standard deviation as a result of the low sample number. Therefore, adequate samples are needed to analyse the statistical significance of ACE gene I/D variant with the level of bradykinin serum. The phenomenon indicated that ACE inhibitor influenced serum bradykinin levels. This can be seen from the binding affinity between captopril and lisinopril in each ACE domain. Lisinopril has a higher binding affinity for the C-domain of ACE, which indicates that lisinopril inhibits the C-domain of ACE more efficiently than the N-domain. These data correspond with in vitro data that show that the inhibitory constant (Ki) of lisinopril is lower in the C-domain than in the N-domain [20]. This phenomenon is supported by our serum bradykinin level data. The serum bradykinin level in hypertensive patients with ID/DD PLX7904 receiving lisinopril tended to be higher than in those with II genotype, although the difference is not statistically significant. Captopril was bound to N- and C-domains with similar affinity. The data are analogous to a previous study that found that captopril has a similar binding affinity in the two domains [21]. This result means that captopril could bind into the two ACE domains, but its inhibitory potency is higher in the N-domain than in the C-domain. Interestingly, the level of bradykinin serum in patients receiving captopril was greater in the II genotype than in the DD genotype. Because I allele might have only the N-domain, captopril could bind effectively, so the I variant showed a slightly higher serum bradykinin serum level than the D allele.
    Conclusion
    Ethics
    Conflict of interest
    Introduction Angiotensin-converting enzyme (ACE) is familiar as a dipeptidyl caboxy peptidase, identified from tissues and body fluids of human body, which play a critical role in the human cardiovascular systems (Coates, 2003). ACE is a metallopeptidase membrane protein and it also degrades bradykinin, which regulates different physiological processes and exerts antihypertensive effects through the Kinin-nitric oxide system (KNOS). Therefore, ACE and renin are two key enzymes were reported as a regulating enzymes in the Renin Angiotensin System. To overcome the negative effect of ACE and renin, various inhibitory agents were used, known as an antihypertensive agents/medicines (Guang, Phillips, Jiang, & Milani, 2012). Many researchers reported the studies regarding isolation, purification and characterization of ACE-inhibitors using the different lactic cultures. Proteinase activity of lactic acid bacteria, hydrolyzes the milk proteins especially, caseins in to peptides, which can be further used as nitrogen source by lactic acid bacteria for their growth. Many scientists have been researched the isolation, production and purification of ACE-inhibitory agents, which are reported to be released after the proteolytic of milk proteins by some lactic cultures and probiotic strains of Lactobacillus delbrueckii ssp. bulgaricus, Lactobacillus helveticus, Lactococcus lactis ssp. cremoris, Streptococcus salivarius ssp. thermophilus, and Lc. lactis ssp. diacetylactis (Fitzgerald and Murray, 2006, Korhonen and Pihlanto, 2006). Camel milk is known for its medicinal properties since many centuries and also studies reported the beneficial effects on human health. Compositional data analysis showed that, camel milk is enriched with ascorbic acid and niacin, and also analysis reported the higher content of Copper and iron in camel milk as compared to the bovine milk (El-Agamy, 2006). Scientific data are available on isolation, purification, characterization, and production of bioactive peptides with bio functionalities from bovine milk using lactic acid bacteria (LAB) (Fitzgerald and Murray, 2006, Hayes et al., 2007), however, only limited reports are available on the novelty of bioactive peptides derived from Indian breed camel milk. Worldwide, only some researchers worked on the isolation, purification and characterization of ACE-inhibitory bioactive peptides from fermented camel milk. Some primitive work regarding the bio-functionality of fermented camel milk using proteolytic or probiotic strain is available. So, this study would serve as a guide to the researchers for identifying novel peptides from fermented camel milk.