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58-82-2

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58-82-2 Usage

Receptors

BKs signal via two GPCRs known as the B1 (BDKRB1) and B2 (BDKRB2) receptors. These BK receptor genes were the result of tandem duplication that predated the teleost tetraploidization while no extra copy was found in teleosts. B2 is constitutively expressed and predominant in different tissues while B1 expression is induced by inflammation. B1 expression in inflammatory tissues such as a wound area and vascular injury contributes to the inflammatory edema by its vasodilatory effect on local blood vessels. B2 is ubiquitously expressed in different tissues. In the aorta and large muscular arteries, including the carotid and mesenteric arteries, B2 is localized predominantly in the endothelium. However, in small arterioles toward the urinary bladder, myometrium, breast, etc., B2 is located predominantly in the smooth muscle rather than the endothelium. bdkrb2- overexpressed zebrafish induce IP3 accumulation by BK with an EC50 of 6.6 nM.

Signal transduction pathway

Both B1 and B2 trigger a typical Ca signaling of GPCRs. Receptor activation leads to phospholipase C (PLC) activation, intracellular Ca mobilization, release of endothelium-dependent relaxation factor (EDRF), and activation of PKC and cytosolic PLA2 that results in the release of prostaglandins (PGs). The endothelial nitric oxide synthase (eNOS) is also stimulated by B2 activation, leading to an increase in NO, stimulation of guanylyl cyclase, and an increase in cGMP. Most of these factors are EDRFs and are contributing to the hypotensive effect of BK. However, in smooth muscle cells, B2 activation activates PLC directly, leading to a transient increase in Ca2+ flux to induce muscle contraction. Although BK mostly induces vasorelaxation via endothelium-dependent signalings, in small arterioles where B2 is predominately localized in the smooth muscle cells, BK induces vasoconstriction. In the light of this dual function, [Arg0 ]-BK injection in teleosts was a vasopressor and could be related to a direct stimulation of B2 on smooth muscles, as the endothelium-dependent relaxing system is not prominent in teleosts.

Agonists and Antagonists

[Lys0 , des-Arg9 ]-BK is used as a B1 receptor agonist. Cereport (RMP-7) is a selective B2 agonist, and has been shown to transiently increase the permeability of the blood-brain barrier.?The B1 antagonist BI-113823 possesses an antiinflammatory function. Icatibant (HOE 140 or JE 049) is a potent, specific, and selective peptidomimetic B2 antagonist.

Chemical Properties

Amorphous solid.

Uses

Different sources of media describe the Uses of 58-82-2 differently. You can refer to the following data:
1. Bradykinin is used to lower blood pressure, increase bradykinin (by inhibiting its degradation) further lowering blood pressure. Bradykinin dilates blood vessels via the release of prostacyclin, nitric oxide, and endothelium-derived hyperpolarizing factor.
2. Leucine Enkephalin acetate salt hydrate has been used in the calibration of the Q-Tof Micro hybrid, triple quadrupole-orthogonal acceleration time of flight (TOF) instrument in single-stage TOF mode. It has also been used to perform the calibration of mass spectrometry. It has also been used in liquid chromatography-mass spectrometry (LCMS)/MS for calibration of the system and for relative correction of the spectra.

Definition

ChEBI: A linear nonapeptide messenger belonging to the kinin group of proteins, with amino acid sequence RPPGFSPFR. Enzymatically produced from kallidin in the blood, it is a powerful vasodilator that causes smooth muscle contraction, and may mediate inflammation

Biological Functions

The kallikrein–kinin system is an enzymatic pathway giving rise to two predominant vasoactive peptides, kallidin and bradykinin. Kallikrein, the enzyme responsible for the formation of these peptides, exists in plasma and tissues. However, circulating levels of the end products, kallidin and bradykinin, are quite low because the kallikrein enzymes are present largely in inactive forms. In addition, the short half-life of these peptides (15 seconds) also contributes to low plasma levels. In general, the kinins produce relaxation of vascular smooth muscle and vasodilation. Bradykinin causes vascular smooth muscle relaxation by stimulating the endothelium to release prostacyclin and nitric oxide. Blood flow to the brain, heart, viscera, skeletal muscle, and glands is increased. In nonvascular smooth muscle, bradykinin will produce a contractile response. Other actions of kinins include activation of clotting factors simultaneously with the production of bradykinin. In the kidney, bradykinin production results in an increase in renal papillary blood flow, with a secondary inhibition of sodium reabsorption in the distal tubule. In the peripheral nervous system, bradykinin is important for the initiation of pain signals. It is also associated with the edema, erythema, and fever of inflammation. Bradykinin exerts its physiological effects via two receptors, the B1 and B2 receptors, with most of its physiological effects being mediated by the B2 receptor. The precise function of the B1 receptor is unclear; however, some of the chronic inflammatory responses to bradykinin may be mediated through actions at this receptor. Bradykinin antagonists of the B2 receptor are currently in development and may find utility in the treatment of pain associated with burns and such chronic inflammatory disorders as arthritis, asthma, and chronic pain.

General Description

Induces the release of nitric oxide. Other physiological functions include stimulation of pain receptors, inhibition of cAMP accumulation, induction of smooth muscle contraction, and vasodilation. Also involved in edema resulting from trauma or injury. Improves post-ischemic recovery of heart via a nitric oxide-dependent mechanism.

Hazard

Powerful vasodilator; increased capillary permeability; stimulates pain receptors; contraction of smooth muscle; teratogen; mutagenic.

Biochem/physiol Actions

Product does not compete with ATP.

Clinical Use

9-peptide, produced in response to tissue damage, inflammation, viral infections, etc. Produces pain, increased vascular permeability, and synthesis of prostaglandins.

Check Digit Verification of cas no

The CAS Registry Mumber 58-82-2 includes 5 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 2 digits, 5 and 8 respectively; the second part has 2 digits, 8 and 2 respectively.
Calculate Digit Verification of CAS Registry Number 58-82:
(4*5)+(3*8)+(2*8)+(1*2)=62
62 % 10 = 2
So 58-82-2 is a valid CAS Registry Number.
InChI:InChI=1/C50H73N15O11/c51-32(16-7-21-56-49(52)53)45(72)65-25-11-20-39(65)47(74)64-24-9-18-37(64)43(70)58-28-40(67)59-34(26-30-12-3-1-4-13-30)41(68)62-36(29-66)46(73)63-23-10-19-38(63)44(71)61-35(27-31-14-5-2-6-15-31)42(69)60-33(48(75)76)17-8-22-57-50(54)55/h1-6,12-15,32-39,66H,7-11,16-29,51H2,(H,58,70)(H,59,67)(H,60,69)(H,61,71)(H,62,68)(H,75,76)(H4,52,53,56)(H4,54,55,57)/t32-,33-,34-,35-,36-,37-,38-,39-/m0/s1

58-82-2SDS

SAFETY DATA SHEETS

According to Globally Harmonized System of Classification and Labelling of Chemicals (GHS) - Sixth revised edition

Version: 1.0

Creation Date: Aug 18, 2017

Revision Date: Aug 18, 2017

1.Identification

1.1 GHS Product identifier

Product name bradykinin

1.2 Other means of identification

Product number -
Other names BRADYZIDE

1.3 Recommended use of the chemical and restrictions on use

Identified uses For industry use only.
Uses advised against no data available

1.4 Supplier's details

1.5 Emergency phone number

Emergency phone number -
Service hours Monday to Friday, 9am-5pm (Standard time zone: UTC/GMT +8 hours).

More Details:58-82-2 SDS

58-82-2Relevant articles and documents

Merrifield

, p. 304 (1964)

Discovery of amphipathic dynorphin A analogues to inhibit the neuroexcitatory effects of dynorphin A through bradykinin receptors in the spinal cord

Lee, Yeon Sun,Muthu, Dhanasekaran,Hall, Sara M.,Ramos-Colon, Cyf,Rankin, David,Hu, Jackie,Sandweiss, Alexander J.,De Felice, Milena,Xie, Jennifer Yanhua,Vanderah, Todd W.,Porreca, Frank,Lai, Josephine,Hruby, Victor J.

, p. 6608 - 6616 (2014/05/20)

We hypothesized that under chronic pain conditions, up-regulated dynorphin A (Dyn A) interacts with bradykinin receptors (BRs) in the spinal cord to promote hyperalgesia through an excitatory effect, which is opposite to the well-known inhibitory effect of opioid receptors. Considering the structural dissimilarity between Dyn A and endogenous BR ligands, bradykinin (BK) and kallidin (KD), this interaction could not be predicted, but it allowed us to discover a potential neuroexcitatory target. Well-known BR ligands, BK, [des-Arg10, Leu9]-kallidin (DALKD), and HOE140 showed different binding profiles at rat brain BRs than that previously reported. These results suggest that neuronal BRs in the rat central nervous system (CNS) may be pharmacologically distinct from those previously defined in non-neuronal tissues. Systematic structure-activity relationship (SAR) study at the rat brain BRs was performed, and as a result, a new key structural feature of Dyn A for BR recognition was identified: amphipathicity. NMR studies of two lead ligands, Dyn A-(4-11) 7 and [des-Arg7]-Dyn A-(4-11) 14, which showed the same high binding affinity, confirmed that the Arg residue in position 7, which is known to be crucial for Dyn As biological activity, is not necessary, and that a type I B-turn structure at the C-terminal part of both ligands plays an important role in retaining good binding affinities at the BRs. Our lead ligand 14 blocked Dyn A-(2-13) 10-induced hyperalgesic effects and motor impairment in in vivo assays using na?ve rats. In a model of peripheral neuropathy, intrathecal (i.th.) administration of ligand 14 reversed thermal hyperalgesia and mechanical hypersensitivity in a dose-dependent manner in nerve-injured rats. Thus, ligand 14 may inhibit abnormal pain states by blocking the neuroexcitatory effects of enhanced levels of Dyn A, which are likely to be mediated by BRs in the spinal cord.

Controlled formation of peptide bonds in the gas phase

Lee, Sunyoung,Valentine, Stephen J.,Reilly, James P.,Clemmer, David E.

, p. 15834 - 15837 (2011/11/13)

Photoexcitation (using 157 nm vacuum ultraviolet radiation) of proton-bound peptide complexes leads to water elimination and the formation of longer amino acid chains. Thus, it appears that proton-bound dimers are long-lived intermediates along the pathway to peptide formation. Product specificity can be controlled by selection of specific complexes and the incorporation of blocking groups at the N- or C-termini. The product peptide sequences are confirmed using collision-induced dissociation.

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