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Cellular Regulation of Kinin Receptors
Published in Sami I. Said, Proinflammatory and Antiinflammatory Peptides, 2020
Adelbert A. Roscher, Alexander Faussner
In human inflammatory lung diseases, kinins, acting via their B2 and B1 receptors, contribute significantly to both the initial presence of injury and ultimately to the processes that set the stage for repair or chronic airway hyperresponsiveness. In this report we have described and discussed some of the important regulatory modes for kinin receptors that might be involved in the balance between host protection and destruction during inflammation. The further characterization of these mechanisms may in the long term provide a rational basis for designing specific interventions within the kallikrein-kinin system in lung diseases.
Inflammation
Published in George Feuer, Felix A. de la Iglesia, Molecular Biochemistry of Human Disease, 2020
George Feuer, Felix A. de la Iglesia
The sources of most inflammatory proteins and peptides are the several different types of leukocytes. These cells contain many potentially harmful substances within their cytoplasm clustered in granules which are released into the surrounding inflamed tissue and appear in the circulation as various plasma proteins. There are five groups: (1) proteases, antiproteases, and oxidizing enzymes; (2) blood coagulation system; (3) complement systems; (4) kallikreinkinin system; and (5) the fibrinolytic system. In this section only the role of proteases, antiproteases, and oxidants during inflammation in tissue injury will be discussed. The kallikrein-kinin system has protein components, but the active mediators are relatively small peptides derived from proteins of this system.
Cardiac Inhibition of Angiotensin Converting Enzyme: Role of Kinins
Published in Malcolm J. Lewis, Ajay M. Shah, Endothelial Modulation of Cardiac Function, 2020
Wolfgang Linz, Gabriele Wiemer, Bernward A. Schölkens
Different lines of evidence have led to the concept that the renin-angiotensin system (RAS) is functionally divided into circulating and multiple tissue-localized systems (Dzau and Re, 1987; Griendling et al., 1993; Kifor and Dzau, 1987; Lindpaintner et al., 1988; Linz et al., 1989; Schunkert et al., 1990; Yamada et al., 1991). More recently it has become obvious that the same is true for the kallikrein-kinin system (KKS) (Nolly et al., 1992; 1993; 1994a). Thus, the traditional endocrine concept has evolved into a concept of autocrine-paracrine functions of the RAS and KKS (Unger et al., 1991). Since angiotensin-converting enzyme (ACE) is identical with kininase II, ACE-inhibitors may exert part of their pharmacological effects via both of these autocrine-paracrine mechanisms (Unger et al., 1990; Unger et al., 1994).
“The influence of female body mass index, menstrual cycle phase and age on propofol injection pain”
Published in Egyptian Journal of Anaesthesia, 2021
Raham Hasan Mostafa, Mohamed Mohamed Kamal, Marwa Mamdouh Mohamed, Mohamed Abdulmohsen Ismaiel
All phenols irritate skin and mucous membrane. Thus, propofol being an alkylphenol is expected to cause pain [1]. Propofol injection pain (PIP) and its severity may differ among patient populations with an incidence of 28%–90% in adult patients, in the absence of other pretreatments [1]. PIP usually is percepted as tingling, cold, or numbing or, at its worst, a severe burning pain. Despite this discomfort, the incidence of venous sequel, such as phlebitis, is less than 1% [2] PIP may be immediate or delayed after 10–20 seconds. The immediate pain is due to irritation of vein endothelium by free propofol present in the aqueous phase [3], whereas delayed pain is due plasma kallikrein-kinin system activation after propofol contacting with free nerve endings of vessels, thus locally liberating pain mediators [4].
Inhibition of plasma kallikrein–kinin system to alleviate renal injury and arthritis symptoms in rats with adjuvant-induced arthritis
Published in Immunopharmacology and Immunotoxicology, 2018
Jie Zhu, Hui Wang, Jingyu Chen, Wei Wei
The kallikrein–kinin system (KKS) is an important endogenous enzyme system. Physiologically, KKS modulates the function of cardiovascular, kidneys and nervous system4. The KKS consists of two major cascades: ‘plasma KKS’ and ‘tissue KKS’. Plasma kallikrein is different from tissue kallikrein in molecular weight, biological functions and immunological properties5,6. Plasma KKS was involved in thrombosis, fibrinolysis and played a critical role during inflammatory processes in many diseases, such as heart disease, kidney disease and cancer5,7–9. Plasma KKS consists of four plasma proteins: prekallikrein, factor XII, factor XI and high molecular weight kininogen (HK). Upon activation, pre-kallikrein (PK) is converted to the active form kallikrein, which cleaves HK to release bradykinin (BK)10. Plasm KKS was also associated with the adaptive immune responses11. BK is a potent peptide that participates in inflammation, edema and vascular dilation and could change the transformation of antigen-specific T lymphocytes to Th1 and Th2 cell12,13.
Kinin B1 receptors as a therapeutic target for inflammation
Published in Expert Opinion on Therapeutic Targets, 2018
Fatimunnisa Qadri, Michael Bader
One particularly important family of inflammatory mediators playing an integral role during inflammation is the kinins. Kinins are blood- and tissue-derived vasoactive hormones and consist mainly of the nonapeptide, bradykinin (BK, Arg–Pro–Pro–Gly–Phe–Ser–Pro–Phe–Arg), the decapeptide Lys-bradykinin or kallidin (KD), and their carboxy-terminal des-Arg metabolites, des-Arg9-BK (DABK) and des-Arg10-KD (DAKD), respectively. There are two classical pathways for the generation of kinins, the plasma and tissue kallikrein–kinin system (KKS) (Figure 1). Kinins originate from kininogens (high and low molecular weight), which are circulatory glycoproteins primarily synthetized by the liver. The cleavage of kininogens by the proteolytic enzymes, kallikreins, in either plasma or tissue produces the kinins, BK, and KD, respectively. Both BK and KD are highly instable peptides and can be degraded very fast by several kininases including angiotensin-converting enzyme (ACE), neutral endopeptidase (NEP), carboxypeptidase N (CPN), and carboxypeptidase M (CPM). These kininases are divided into two main types on the basis of their enzymology; kininase-I (CPN and CPM), and kininase-II (ACE). Kininase-I enzymes cleave the carboxyterminal arginine from either BK or KD giving rise to the active metabolites, DABK and DAKD, while the kininases-II cleave off the C-terminal dipeptide Phe–Arg [2–6].