Explore chapters and articles related to this topic
Inflammatory bowel disease
Published in Phillip D. Smith, Richard S. Blumberg, Thomas T. MacDonald, Principles of Mucosal Immunology, 2020
Giovanni Monteleone, Markus F. Neurath, Britta Siegmund
Autophagy is a cellular process that is classically responsible for the degradation of damaged organelles or long-lived proteins. It is activated by a variety of conditions associated with starvation and cellular stress such as that associated with the unfolded protein response as a consequence of stress caused by the accumulation of misfolded protein within the endoplasmic reticulum (ER) as well as the presence of cell-associated bacteria. Genes associated with bacterial sensing such as those encoding NOD2 (as discussed) and intelectin-1 have been associated with Crohn's disease, genes associated with autophagy such as autophagy-related gene 16 like-1 (ATG16L1) and that encoding immunity-related guanosine triphosphatase (IRGM) have been associated with Crohn's disease, and genes associated with ER stress such as those encoding X-box binding protein-1 (XBP1) and orsomucoid 1-like 3 (ORMDL3) have also been associated with both Crohn's disease and ulcerative colitis. Although the functional mechanisms for these susceptibilities are incompletely understood, as discussed later, they highlight the primary importance of innate immunity and the intestinal epithelium in the immunopathogenesis of IBD.
The Development of Improved Therapeutics through a Glycan- “Designer” Approach
Published in Peter Grunwald, Pharmaceutical Biocatalysis, 2019
Other newly discovered lectins that could be used to enhance the innate immune system are intelectins—soluble lectins with capacity of binding to galactofuranose saccharides. The galactofuranose is naturally occurring in various bacteria, but not in humans, therefore making the saccharide a potent immunomodulator (Tsuji et al., 2001). Intelectins were showed to be expressed in the heart, small intestine, colon and thymus with much lesser amount expressed in human spleen and uterus (Tsuji et al., 2001). It was suggested that the intelectin serves as a defense receptor against pathogens causing endocarditis (e.g., Streptococci group).
Effects of TNF inhibitors and an IL12/23 inhibitor on changes in body weight and adipokine levels in psoriasis patients: a 48-week comparative study
Published in Journal of Dermatological Treatment, 2022
Nahide Onsun, Tahsin Çağdaş Akaslan, Kadriye Sallahoglu, Aliye Sevdem Gülcan, Huri Bulut, Ayşegül Yabacı
Serum samples were thawed and Human LEP (Leptin) (Catalog No: E-EL-H0113, Elabscience Biotechnology Inc., Houston, TX, USA), Human ITLN1 (Intelectin 1/Omentin) (Catalog No: E-EL-H2028 Elabscience Biotechnology Inc.) and Human ADP/Acrp30 (Adiponectin) (Catalog No: E-EL-H5811, Elabscience Biotechnology Inc.) ELISA kits were used for quantitative measurement of leptin, adiponectin, and omentin levels. Samples and standards were added to appropriate wells pre-coated with Anti-Human monoclonal antibody before incubation. Biotin was added to all wells and combined with streptavidin-HRP to form an immune complex; then incubation was performed again, with washing to remove the uncombined enzyme. Chromogen solutions A and B were added for the color of the liquid to change to blue. With the effect of acid, the color finally becomes yellow. Optical density was read on a standard automated plate reader at 450 nm (Thermo Scientific Microplate Reader, Thermo Fisher, USA). Detection ranges of the kits were between 78.13–5000 pg/mL for leptin, 0.63–40 ng/mL for omentin, and 78.13–5000 pg/mL for adiponectin.
Relationship of circulating chemerin and omentin levels with Th17 and Th9 cell immune responses in patients with asthma
Published in Journal of Asthma, 2018
Qing Zhou, Yu Fu, Liangan Hu, Qian Li, Meng Jin, E. Jiang
Adipokines (adiponectin and leptin) are known to influence asthma prevalence and severity [6], but there is limited information on the role of certain novel adipokines like chemerin and omentin in asthma and immune responses. Chemerin is an 18-kDa protein secreted by the adipose tissue that modulates the immune system function through binding to the chemerin receptor (Chemerin R, chemokine-like receptor 1 (CMKLR1), and G protein-coupled receptor) [7]. Omentin (also known as intelectin), a 34-kDa adipocytokine, is produced in the visceral adipose tissue, and may direct the therapeutic development under inflammation-related conditions [8]. Recent studies in murine models implicate chemerin [9] and omentin [10] in allergic asthma.
Effects of omentin on flap viability: an experimental research on rats
Published in Journal of Plastic Surgery and Hand Surgery, 2019
Fatih Burak Efeoğlu, Ali Gökkaya, Furkan Erol Karabekmez, Tülin Fırat, Metin Gorgu
Omentin was first isolated from intestinal Paneth cells. Omentin, also known as intelectin, is an adipose tissue-specific adipokine, which is secreted from visceral omental adipose tissue [2]. Adipokines have endocrine properties and play important roles in the inflammatory response. They are also involved in appetite and sleep regulation and serve as biomarkers of various diseases. Omentin regulates nitric oxide (NO) synthase. Previous research showed that omentin appeared to have a positive effect on endothelium dysfunction and that it antagonized noradrenalin-induced vasoconstriction via its effects on NO [3–5]. Therefore, at least in theory, omentin may be a potential agent for increasing flap viability [3, 4].