Kallidin

Last updated
Kallidin
Kallidin.svg
Kallidin 3D.png
Names
IUPAC name
L-Lysyl-L-arginyl-L-prolyl-L-prolyl-glycyl-L-phenylalanyl-L-seryl-L-prolyl-L-phenylalanyl-L-arginine
Identifiers
3D model (JSmol)
ChemSpider
ECHA InfoCard 100.005.853 OOjs UI icon edit-ltr-progressive.svg
MeSH Kallidin
PubChem CID
UNII
  • InChI=1S/C56H85N17O12/c57-24-8-7-18-36(58)46(76)67-37(19-9-25-63-55(59)60)51(81)73-29-13-23-44(73)53(83)72-28-11-21-42(72)49(79)65-32-45(75)66-39(30-34-14-3-1-4-15-34)47(77)70-41(33-74)52(82)71-27-12-22-43(71)50(80)69-40(31-35-16-5-2-6-17-35)48(78)68-38(54(84)85)20-10-26-64-56(61)62/h1-6,14-17,36-44,74H,7-13,18-33,57-58H2,(H,65,79)(H,66,75)(H,67,76)(H,68,78)(H,69,80)(H,70,77)(H,84,85)(H4,59,60,63)(H4,61,62,64)/t36-,37-,38-,39-,40-,41-,42-,43-,44-/m0/s1 Yes check.svgY
    Key: FYSKZKQBTVLYEQ-FSLKYBNLSA-N Yes check.svgY
  • InChI=1/C56H85N17O12/c57-24-8-7-18-36(58)46(76)67-37(19-9-25-63-55(59)60)51(81)73-29-13-23-44(73)53(83)72-28-11-21-42(72)49(79)65-32-45(75)66-39(30-34-14-3-1-4-15-34)47(77)70-41(33-74)52(82)71-27-12-22-43(71)50(80)69-40(31-35-16-5-2-6-17-35)48(78)68-38(54(84)85)20-10-26-64-56(61)62/h1-6,14-17,36-44,74H,7-13,18-33,57-58H2,(H,65,79)(H,66,75)(H,67,76)(H,68,78)(H,69,80)(H,70,77)(H,84,85)(H4,59,60,63)(H4,61,62,64)/t36-,37-,38-,39-,40-,41-,42-,43-,44-/m0/s1
    Key: FYSKZKQBTVLYEQ-FSLKYBNLBR
  • O=C(N[C@H](C(=O)N[C@H](C(=O)O)CCC/N=C(\N)N)Cc1ccccc1)[C@H]5N(C(=O)[C@@H](NC(=O)[C@@H](NC(=O)CNC(=O)[C@H]3N(C(=O)[C@H]2N(C(=O)[C@@H](NC(=O)[C@@H](N)CCCCN)CCC/N=C(\N)N)CCC2)CCC3)Cc4ccccc4)CO)CCC5
Properties
C56H85N17O12
Molar mass 1188.403 g·mol−1
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).
Yes check.svgY  verify  (what is  Yes check.svgYX mark.svgN ?)

Kallidin belongs to the family kinins, which are the peptide hormones. [1] Kallidin is a decapeptide whose sequence is H-Lys-Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg-OH. Removal of the N-terminal lysine by Factor XII, [2] or to a leser extent aminopeptidase [3] yields the potently bioactive bradykinin molecule.

Contents

Effects of Kinins

Kallidin is a bioactive kinin peptide formed in response to injury from kininogen precursors through the action of kallikreins. [4] Like all kinins, kallidin, the deca-peptide, plays an important role in several body pathologies. Kinins can regulate the blood pressure by increasing the level of vasopressor substances. [1] [5] They can also bind to the B1 and B2 cell surface receptors, which are G-protein coupled receptors. [6] The mediation of the B1 receptors by des-Arg kinins as agonists can be expressed in several medical issues, such as cancer and trauma. [5] By binding to the B2 receptors, kinins, endogenous agonists, can regulate the vasodilatation and bronchioconstriction. [1]

Chemical Mechanisms

Since kinins are peptides, they can be cleaved by the peptidases. Peptidases such as the serine peptidases, carboxypeptidase N and carboxypeptidase M cleave kinins into des-Arg-bradykinin and Lys-des-Arg-bradykinin. [7] [8]

Clarification

Kallidin is identical to bradykinin with an additional lysine residue added at the N-terminal end and signals through the bradykinin receptor.[ citation needed ]

Despite exhibiting similar functions and reactivities, kinins can be differentiated by combining an amino-terminal-directed radioimmunoassay with a carboxy-terminal-directed radioimmunoassay in combination with HPLC. [1]

See also

References

  1. 1 2 3 4 Hilgenfeldt, U.; Linke, R.; Riester, U.; Konig, W.; Breipohl, G. (June 1995). "Strategy of Measuring Bradykinin and Kallidin and Their Concentration in Plasma and Urine" . Analytical Biochemistry. 228 (1): 35–41. doi:10.1006/abio.1995.1311.
  2. ↑ Golias, C.; Charalabopoulos, A.; Stagikas, D.; Charalabopoulos, K.; Batistatou, A. (2007). "The kinin system - bradykinin: Biological effects and clinical implications. Multiple role of the kinin system - bradykinin". Hippokratia. 11 (3): 124–128. PMC   2658795 . PMID   19582206.
  3. ↑ , https://www.nature.com/articles/2121271a0
  4. ↑ Campbell, Duncan John (2013). "Bradykinin Peptides". Handbook of Biologically Active Peptides. pp. 1386–1393. doi:10.1016/B978-0-12-385095-9.00188-3. ISBN   978-0-12-385095-9.
  5. 1 2 Guevara-Lora, Ibeth; Labedz, Anna; Skrzeczynska-Moncznik, Joanna; and Kozik, Andrzej (2011-08-01). "Bradykinin and des-Arg10-kallidin enhance the adhesion of polymorphonuclear leukocytes to extracellular matrix proteins and endothelial cells". Cell Communication & Adhesion. 18 (4): 67–71. doi:10.3109/15419061.2011.617854. ISSN   1541-9061. PMID   21942713.
  6. ↑ Hall, Judith M.; Morton, Ian K. M. (1997-01-01), Farmer, Stephen G. (ed.), "2 - The Pharmacology and Immunopharmacology of Kinin Receptors" , The Kinin System, Handbook of Immunopharmacology, London: Academic Press, pp. 9–43, doi:10.1016/b978-012249340-9/50004-8, ISBN   978-0-12-249340-9 , retrieved 2025-05-03
  7. ↑ Pelorosso, Facundo Germán; Brodsky, Paula Tamara; Zold, Camila Lidia; Rothlin, Rodolfo Pedro (June 2005). "Potentiation of des-Arg9-Kallidin-Induced Vasoconstrictor Responses by Metallopeptidase Inhibition in Isolated Human Umbilical Artery" . The Journal of Pharmacology and Experimental Therapeutics. 313 (3): 1355–1360. doi:10.1124/jpet.105.083063. PMID   15764737.
  8. ↑ Herwald, Heiko; Müller-Esterl, Werner; Renné, Thomas (2008). "Kinins". Encyclopedia of Molecular Pharmacology. pp. 673–676. doi:10.1007/978-3-540-38918-7_86. ISBN   978-3-540-38916-3.
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