SIGNALING PATHWAYS COUPLED TO ACTIVATION OF THE KININ B1 RECEPTOR

ADVANCES IN PROTEIN KINASES

dc.creatorBhoola, Kanti Daya
dc.creatorEhrenfeld Slater, Ingrid Pamela
dc.creatorFigueroa Valverde, Carlos Dario
dc.creatorMatus Velasquez, Carola Elizabeth
dc.date2016-12-27T21:49:51Z
dc.date2022-06-17T20:35:56Z
dc.date2016-12-27T21:49:51Z
dc.date2022-06-17T20:35:56Z
dc.date2012
dc.date.accessioned2023-08-21T20:39:08Z
dc.date.available2023-08-21T20:39:08Z
dc.identifier11090292
dc.identifier978953510633-3 
dc.identifierhttps://hdl.handle.net/10533/165365
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/8279498
dc.descriptionKinins are a group of bioactive peptides, which are formed by an endogenous enzymatic cascade consisting of precursor substrates called kininogens and the proteolytic kallikrein enzymes (kininogenases). So far, two kinin-releasing enzymes (kininogenases) have been characterized, plasma (hKB1/LKLB1) and tissue (hK1/KLK1) kallikreins (Fig. 1). Both enzymes are serine proteases that are found in glandular cells, neutrophils, and biological fluids. Kininogens are multifunctional proteins involved in cascade reactions during inflammation (Bhoola et al., 1992), and more recently in carcinogenesis (Bhoola et al., 1992; 2001; Leeb-Lundberg et al., 2005). Kinins namely bradykinin (BK) and kallidin (Lys-BK) are among the most potent pro-inflammatory vasoactive peptides generated during tissue injury and noxious stimulation. BK and Lys-BK undergo metabolic degradation at a variable rate by amino-, carboxy- and endopeptidases found in tissues and biological fluids. The most physiologically relevant enzymes are carboxypeptidase N (from plasma) and carboxypeptidase M (from cell membranes), which remove the carboxy-terminal Arg present at end of the kinin molecule, resulting in the formation of the active metabolites desArg9-BK (DBK) and des-Arg10-kallidin, known also as Lys-des-Arg9-BK (LDBK) (Fig. 1). Furthermore, neutral endopeptidase 24.11 (CD10, enkephalinase) and angiotensin I converting enzyme, act as dipeptidyl carboxypeptidases by removing the dipeptide Phe8- Arg9 from the carboxy terminus end of BK or Lys-BK (Couture et al., 2004). It is important to mention that endopeptidase 24.15 and angiotensin I converting enzyme cleave the dipeptide Ser6-Pro7 from bradykinin 1-7 (BK1-7) to produce bradykinin 1-5 (BK1-5), one of the final metabolites of BK and DBK that possesses the longer half-life of this peptide family. The half-life of kinins depends on the rate and site of destruction, most rapid in the circulation, but less so in the extracellular fluid space and by cells. Actually, in plasma the half-life of BK and LDBK is short (15 to 20 sec) whereas BK1-5, considered in the past an inactive fragment, is considered to have a half-life of 86 to 101 min (Shima et al., 1992; Murphey et al., 2000; 2006; Morinelli et al., 2002). Kinins are a group of bioactive peptides, which are formed by an endogenous enzymatic cascade consisting of precursor substrates called kininogens and the proteolytic kallikrein enzymes (kininogenases). So far, two kinin-releasing enzymes (kininogenases) have been characterized, plasma (hKB1/LKLB1) and tissue (hK1/KLK1) kallikreins (Fig. 1). Both enzymes are serine proteases that are found in glandular cells, neutrophils, and biological fluids. Kininogens are multifunctional proteins involved in cascade reactions during inflammation (Bhoola et al., 1992), and more recently in carcinogenesis (Bhoola et al., 1992; 2001; Leeb-Lundberg et al., 2005). Kinins namely bradykinin (BK) and kallidin (Lys-BK) are among the most potent pro-inflammatory vasoactive peptides generated during tissue injury and noxious stimulation. BK and Lys-BK undergo metabolic degradation at a variable rate by amino-, carboxy- and endopeptidases found in tissues and biological fluids. The most physiologically relevant enzymes are carboxypeptidase N (from plasma) and carboxypeptidase M (from cell membranes), which remove the carboxy-terminal Arg present at end of the kinin molecule, resulting in the formation of the active metabolites desArg9-BK (DBK) and des-Arg10-kallidin, known also as Lys-des-Arg9-BK (LDBK) (Fig. 1). Furthermore, neutral endopeptidase 24.11 (CD10, enkephalinase) and angiotensin I converting enzyme, act as dipeptidyl carboxypeptidases by removing the dipeptide Phe8- Arg9 from the carboxy terminus end of BK or Lys-BK (Couture et al., 2004). It is important to mention that endopeptidase 24.15 and angiotensin I converting enzyme cleave the dipeptide Ser6-Pro7 from bradykinin 1-7 (BK1-7) to produce bradykinin 1-5 (BK1-5), one of the final metabolites of BK and DBK that possesses the longer half-life of this peptide family. The half-life of kinins depends on the rate and site of destruction, most rapid in the circulation, but less so in the extracellular fluid space and by cells. Actually, in plasma the half-life of BK and LDBK is short (15 to 20 sec) whereas BK1-5, considered in the past an inactive fragment, is considered to have a half-life of 86 to 101 min (Shima et al., 1992; Murphey et al., 2000; 2006; Morinelli et al., 2002). Kinins are a group of bioactive peptides, which are formed by an endogenous enzymatic cascade consisting of precursor substrates called kininogens and the proteolytic kallikrein enzymes (kininogenases). So far, two kinin-releasing enzymes (kininogenases) have been characterized, plasma (hKB1/LKLB1) and tissue (hK1/KLK1) kallikreins (Fig. 1). Both enzymes are serine proteases that are found in glandular cells, neutrophils, and biological fluids. Kininogens are multifunctional proteins involved in cascade reactions during inflammation (Bhoola et al., 1992), and more recently in carcinogenesis (Bhoola et al., 1992; 2001; Leeb-Lundberg et al., 2005). Kinins namely bradykinin (BK) and kallidin (Lys-BK) are among the most potent pro-inflammatory vasoactive peptides generated during tissue injury and noxious stimulation. BK and Lys-BK undergo metabolic degradation at a variable rate by amino-, carboxy- and endopeptidases found in tissues and biological fluids. The most physiologically relevant enzymes are carboxypeptidase N (from plasma) and carboxypeptidase M (from cell membranes), which remove the carboxy-terminal Arg present at end of the kinin molecule, resulting in the formation of the active metabolites desArg9-BK (DBK) and des-Arg10-kallidin, known also as Lys-des-Arg9-BK (LDBK) (Fig. 1). Furthermore, neutral endopeptidase 24.11 (CD10, enkephalinase) and angiotensin I converting enzyme, act as dipeptidyl carboxypeptidases by removing the dipeptide Phe8- Arg9 from the carboxy terminus end of BK or Lys-BK (Couture et al., 2004). It is important to mention that endopeptidase 24.15 and angiotensin I converting enzyme cleave the dipeptide Ser6-Pro7 from bradykinin 1-7 (BK1-7) to produce bradykinin 1-5 (BK1-5), one of the final metabolites of BK and DBK that possesses the longer half-life of this peptide family. The half-life of kinins depends on the rate and site of destruction, most rapid in the circulation, but less so in the extracellular fluid space and by cells. Actually, in plasma the half-life of BK and LDBK is short (15 to 20 sec) whereas BK1-5, considered in the past an inactive fragment, is considered to have a half-life of 86 to 101 min (Shima et al., 1992; Murphey et al., 2000; 2006; Morinelli et al., 2002). Kinins are a group of bioactive peptides, which are formed by an endogenous enzymatic cascade consisting of precursor substrates called kininogens and the proteolytic kallikrein enzymes (kininogenases). So far, two kinin-releasing enzymes (kininogenases) have been characterized, plasma (hKB1/LKLB1) and tissue (hK1/KLK1) kallikreins (Fig. 1). Both enzymes are serine proteases that are found in glandular cells, neutrophils, and biological fluids. Kininogens are multifunctional proteins involved in cascade reactions during inflammation (Bhoola et al., 1992), and more recently in carcinogenesis (Bhoola et al., 1992; 2001; Leeb-Lundberg et al., 2005). Kinins namely bradykinin (BK) and kallidin (Lys-BK) are among the most potent pro-inflammatory vasoactive peptides generated during tissue injury and noxious stimulation. BK and Lys-BK undergo metabolic degradation at a variable rate by amino-, carboxy- and endopeptidases found in tissues and biological fluids. The most physiologically relevant enzymes are carboxypeptidase N (from plasma) and carboxypeptidase M (from cell membranes), which remove the carboxy-terminal Arg present at end of the kinin molecule, resulting in the formation of the active metabolites desArg9-BK (DBK) and des-Arg10-kallidin, known also as Lys-des-Arg9-BK (LDBK) (Fig. 1). Furthermore, neutral endopeptidase 24.11 (CD10, enkephalinase) and angiotensin I converting enzyme, act as dipeptidyl carboxypeptidases by removing the dipeptide Phe8- Arg9 from the carboxy terminus end of BK or Lys-BK (Couture et al., 2004). It is important to mention that endopeptidase 24.15 and angiotensin I converting enzyme cleave the dipeptide Ser6-Pro7 from bradykinin 1-7 (BK1-7) to produce bradykinin 1-5 (BK1-5), one of the final metabolites of BK and DBK that possesses the longer half-life of this peptide family. The half-life of kinins depends on the rate and site of destruction, most rapid in the circulation, but less so in the extracellular fluid space and by cells. Actually, in plasma the half-life of BK and LDBK is short (15 to 20 sec) whereas BK1-5, considered in the past an inactive fragment, is considered to have a half-life of 86 to 101 min (Shima et al., 1992; Murphey et al., 2000; 2006; Morinelli et al., 2002).
dc.descriptionFONDECYT
dc.description384
dc.descriptionFONDECYT
dc.languageeng
dc.publisherINTECH
dc.relationinstname: Conicyt
dc.relationreponame: Repositorio Digital RI2.0
dc.relationinstname: Conicyt
dc.relationreponame: Repositorio Digital RI 2.0
dc.relationinfo:eu-repo/grantAgreement/Fondecyt/11090292
dc.relationinfo:eu-repo/semantics/dataset/hdl.handle.net/10533/93479
dc.relationhttp://www.intechopen.com/books/advances-in-protein-kinases / http://cdn.intechopen.com/pdfs/37380.pdf
dc.rightsinfo:eu-repo/semantics/openAccess
dc.titleSIGNALING PATHWAYS COUPLED TO ACTIVATION OF THE KININ B1 RECEPTOR
dc.titleADVANCES IN PROTEIN KINASES
dc.typeCapitulo de libro
dc.typeinfo:eu-repo/semantics/bookPart


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