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Enzymatic Degradation of Bradykinin
Published in Sami I. Said, Proinflammatory and Antiinflammatory Peptides, 2020
Randal A. Skidgel, Ervin G. Erdös
Because of its wide distribution, NEP’s role in vivo can differ in each organ with the different substrates. The skeletal muscle of the dog contains high concentrations of NEP, in contrast to other species where it is lower (Dragovic et al., 1996). Similar to ACE, the importance of the highly active NEP in the male genital tract, especially in prostate glands (Erdös et al., 1985), is not yet known. NEP has also been the subject of many studies, but under the names CALLA (common acute lymphoblastic leukemia antigen) or CD 10 (Letarte et al., 1988; LeBien and McCormack, 1989). CALLA is present in lymphoblasts but is absent from mature lymphocytes. In contrast, it is in neutrophils but absent from progenitor cells (Connelly et al., 1985; Painter et al., 1988). Because of its presence in neutrophils and synovial fibroblasts (Werb and Clark, 1989) and in respiratory tract (Nadel, 1994), it may be an important factor in breaking down inflammatory peptides.
Neuropeptide Inactivation By Peptidases
Published in Gerard O’Cuinn, Metabolism of Brain Peptides, 2020
Gerard O’Cuinn, Brendan O’Connor, Laura Gilmartin, Maria Smyth
Endopeptidase 24.11 (E.C. 3.4.24.11) is a widely distributed membrane-bound neutral endopeptidase which is active against a range of naturally occurring peptide substrates. It was first isolated by Kerr and Kenny from rabbit kidney34. Other workers showed that the endopeptidase activity from brain had similar physiochemical properties to the kidney enzyme where it was termed 'enkephalinase' because of its ability to degrade Met - and Leu - enkephalin35. This name was later shown to be a misnomer as it became clear that the enzyme was capable of cleaving a variety of peptides including the enkephalins, angiotensin I, tachykinins, LH-RH, neurotensin, bradykinin, interleukin-1, substance P, neurokinin A, atrial natriuretic factor and the endothelins36–38. Several other titles were given to the enzyme including 'Neprilysin'39 and neutral endopeptidase 24.1140. In 1983 it was given the title 'endopeptidase 24.11' based on its E.C. number41. More recently in the plasma membranes of many tissues it has been shown to be identical to the common acute lymphoblastic leukemia antigen (CALLA) also known as the CD 10 antigen42.
Clinical Studies In Oncology
Published in Siegfried Matzku, Rolf A. Stahel, Antibodies in Diagnosis and Therapy, 2019
Jan Schmielau, Wolff Schmiegel
Further clinical experience was obtained in patients with acute lymphocytic leukemia (ALL) who were treated with an antibody against the common acute lymphoblastic leukemia antigen (CALLA) CD 10 (Ritz et al., 1981). The murine IgGl J-5 applied in a single dose of 1-170mg per patient successfully decreased CALLA+ blasts but CALLA” lymphoblasts persisted in large amounts. However, lymphoblasts re-expressed CALLA when J-5 was undetectable in the serum, which has been attributed to internalization of the antigen. Even though binding of J-5 to bone marrow cells occurred, regression was not achieved.
Advances in siRNA delivery in cancer therapy
Published in Artificial Cells, Nanomedicine, and Biotechnology, 2018
Aishwarya Singh, Piyush Trivedi, Narendra Kumar Jain
Cyclodextrins are natural polymers, which can form water soluble inclusion complexes with small and large molecules [60]. The cyclodextrin-containing polycation system for the targeted delivery of siRNA was developed [61] . This system consisted of a cyclodextrin – containing polymer, PEG for stability, and human transferrin as the targeting ligand for binding to transferrin receptors, which are often overexpressed on cancer cells. This targeted nanoparticle system, called CALLA-01, was developed for the first siRNA Phase I trial by Calando Pharmaceuticals (Pasadena, CA, USA) [7]. The siRNA in CALLA-01 is designed to inhibit tumour growth via a mechanism to reduce expression of the M2 subunit of ribonucleotide reductase (R2).
miR-155 influences cell-mediated immunity in Balb/c mice treated with aflatoxin M1
Published in Drug and Chemical Toxicology, 2021
Kobra Shirani, Bamdad Riahi Zanjani, Soghra Mehri, Kamal Razavi-Azarkhiavi, Ali Badiee, A. Wallace Hayes, John P. Giesy, Gholamreza Karimi
Spleens were disrupted in Hanks’ Balanced Salt Solution containing 2% fetal bovine serum (FBS). Aggregates and debris were removed by passing the cell suspension through a 70 μm mesh nylon strainer. The cell suspensions were centrifuged at 300 x g for 10 min and resuspended in PBS containing 2% FBS and 1 mM EDTA. T cells were isolated by negative selection using an EasySep™ Mouse T Cell Isolation Kit (StemCell Technologies, Vancouver, BC).Viability of cells was determined by trypan blue exclusion (Quispe Calla et al.2015).
Neprilysin, the kidney brush border neutral proteinase: a possible potential target for ischemic renal injury
Published in Toxicology Mechanisms and Methods, 2020
Runali Sankhe, Manas Kinra, Jayesh Mudgal, Devinder Arora, Madhavan Nampoothiri
NEP is a family of metallopeptidase also identified as neutral endopeptidase 24.11, membrane metallopeptidase (MME), a cluster of differentiation (CD10) and common acute lymphoblastic leukemia antigen (CALLA) (Oefner et al. 2000), endoprotease 24.11, enkephalinase, and membrane metalloendopeptidase EC 3.4.24.11. NEP belongs to the M13 family, a type II integral membrane peptidase (Bayes-Genis et al. 2016). In 1973, NEP was first identified in rat kidney brush border membrane and later purified from rabbit kidney (Kerr and Kenny 1974).