Exploring the Plant Kingdom for Sources of Skincare Cosmeceuticals
Mahendra Rai, Shandesh Bhattarai, Chistiane M. Feitosa in Wild Plants, 2020
Eighty percent of the dry weight of skin is considered to be collagen and is responsible for the tensile strength of the skin. Collagenases are a type of metalloproteinase that can cleave molecules in the extracellular matrix. Elastase is a proteolytic enzyme involved in the degradation of the extracellular matrix that contains elastin. Elastin provides much of the elastic recoil properties of skin, arteries, lungs, and ligaments. Loss of elastin is a major part of what causes visible signs of aging in the skin. Hyaluronic acid has a role in retaining the moisture, structure, and elasticity of the skin while facilitating rapid tissue proliferation, regeneration, and repair. The levels of collagen, elastin, and hyaluronic acid would decrease with aging, and this could lead to a loss of strength and flexibility in the skin, causing the emergence of wrinkles (Ndlovu et al. 2013). Moreover, the high levels of ROS induce the action of collagenase, elastase, and hyaluronidase, which can further contribute to skin aging (Labat-Robert et al. 2000, Ndlovu et al. 2013). However, natural materials with anti-collagenase, anti-elastase, and anti-hyaluronidase properties can help to prevent the undesirable age-associated destruction of collagen, elastin, and hyaluronic acid (Thring et al. 2009, Ndlovu et al. 2013).
Do I Have IBS?
Melissa G. Hunt, Aaron T. Beck in Reclaim Your Life From IBS, 2022
Exocrine pancreatic insufficiency (EPI) is a condition in which the pancreas doesn’t produce enough of the enzymes that help with certain aspects of digestion. Most people know that the pancreas makes insulin, which is crucial to managing glucose or blood sugar. But few people know that the pancreas also makes a number of digestive enzymes, including amylase (which breaks down carbohydrates), lipase (which breaks down fats), and protease and elastase (which break down proteins). If you can’t break down food, it passes through the intestines partially undigested, which can result in abdominal pain, gas, bloating, diarrhea (typically), or constipation, and, if it’s severe, weird poop that looks pale and oily, and can smell bad and sometimes floats (because there’s too much fat in it). One of the main causes of EPI is chronic pancreatitis, so if you’ve ever experienced even one incident of pancreatitis, it’s worth being tested for EPI. The easiest test for EPI is a stool test called the fecal elastase test (FE-1). Elastase is one of the digestive enzymes. If there is little or no elastase in your stool, that can indicate EPI.
Granulocyte Protease Action: a Possible Cause of Bleeding in Leukemia
László Muszbek in Hemostasis and Cancer, 2019
The enzyme is localized in the azurophil granules of the cells.16 A serine protease with an Mr of 30,000, elastase exhibits maximum activity at pH 8.5. The natural substrates of elastase are important structural proteins, e.g., elastin, cartilage proteoglycan, various types of collagen, and fibronectin. The enzyme is inhibited by α1-protease inhibitor and α2-macroglobulin. The NH2-terminal sequence of elastase is highly homologous with that of the pancreatic elastase, but there are also several differences between the two enzymes. Granulocyte elastase is a glycoprotein, whereas pancreatic elastase does not contain carbohydrate. In contrast to pancreatic enzyme, the zymogen form of elastase was not yet found, therefore, it is assumed that it occurs in the granules in the active state.17,19,20
Biofilm inhibition and anti-quorum sensing activity of phytosynthesized silver nanoparticles against the nosocomial pathogen Pseudomonas aeruginosa
Published in Biofouling, 2019
Saloni Shah, Swapnil Gaikwad, Shuchi Nagar, Shatavari Kulshrestha, Viniti Vaidya, Neelu Nawani, Sarika Pawar
Another important QS-mediated virulence factor is elastase. The influence of Pb-AgNPs on the activity of elastase was determined. Elastase is a zinc metalloprotease that degrades several host tissue components including elastin, collagen and fibrin, and also interferes with the host defense system by preventing the secretion of immune components such as immunoglobulins and cytokines (Pearson et al. 1997; Bjarnsholt et al. 2010). Figure 4b shows the reduction in elastase activity of PAO1 with increased sub-lethal concentrations of Pb-AgNPs with reductions of 18.45 ± 7.12, 36.64 ± 5.53, 56.43 ± 2.48 and 77.40 ± 1.02% at 2, 4, 6 and 8 μg ml−1, respectively. A significant reduction in elastase activity due to Pb-AgNPs provides good evidence of their potential to make P. aeruginosa susceptible to host immune responses (Prateeksha et al. 2017).
Effect of reserpine on Pseudomonas aeruginosa quorum sensing mediated virulence factors and biofilm formation
Published in Biofouling, 2018
Debaprasad Parai, Malabika Banerjee, Pia Dey, Arindam Chakraborty, Ekramul Islam, Samir Kumar Mukherjee
P. aeruginosa secretes pyocyanin, a greenish blue pigment responsible for its pathogenicity during the acute infection (Essar et al. 1990). Although 100 μg ml−1 of reserpine did not inhibit pyocyanin production significantly, increasing concentrations inhibited pyocyanin production in a concentration-dependent manner (Figure 7A). The production rate showed a fall of ~41% and ~67% with IC50 and IC80 treatments, respectively. These results can be correlated with the images obtained from the pellicle assay (Figure 4B), where the characteristic colour of pyocyanin was visibly decreased with IC50 and IC80. Rhamnolipids are bio-surfactants produced by P. aeruginosa that have a role in swarming motility and biofilm architecture (Gutierrez et al. 2013). The IC25, IC50 and IC80 of reserpine significantly decreased rhamnolipid production by 86.9, 59.6 and 39% respectively (Figure 7B). Proteases ensure bacterial invasion into the tissues during infection and are considered as virulence factors in P. aeruginosa (El-Mowafy et al. 2014). Protease production decreased to ~50% with IC50, ~35% with IC80 and ~4% with IC25 (Figure 7C). Elastase has tissue damaging properties and thus it plays a significant role in infection severity (Ohman et al. 1980). Reserpine at IC25, IC50, and IC80 reduced elastase production by nearly 5, 33 and 40%, respectively.
Stenotrophomonas maltophilia – a low-grade pathogen with numerous virulence factors
Published in Infectious Diseases, 2019
Angelina Trifonova, Tanya Strateva
The gelatinase production of S. maltophilia is an important biochemical characteristic of the species (over 85% of the strains are producers). Although in other bacteria the enzyme participates in biofilm formation, host tissue degradation, and avoidance of immune response by inactivating the complement system [29], data on its role as a virulence factor in S. maltophilia are scarce [1,6]. A case of ecthyma gangrenosum due to bacteraemia with S. maltophilia was reported in a patient with leukaemia [17]. The exoenzyme profile of the isolate included both gelatinase and elastase. One of the functions of elastase is degradation of the elastic lamina of blood vessels facilitating release of bacterial cells into subcutaneous tissue [17]. A study of clinical S. maltophilia isolates established that elastase activity is dependent on incubation time and temperature (all tested strains demonstrate elastin hydrolysis at 30 °C after 72 h). According to the authors, previous results showing a low prevalence of the enzyme, are due to absence of standard methodology in laboratory practice [30].
Related Knowledge Centers
- Bacteria
- Collagen
- Elastin
- Enzyme
- Molecular Biology
- Protease
- Protein
- Serine Protease
- Gene
- Pseudomonas Aeruginosa