33515-09-2 Usage
Uses
Different sources of media describe the Uses of 33515-09-2 differently. You can refer to the following data:
1. Gonad-stimulating principle.
2. Gonadorein is a Gonadotropin-releasing hormone. Gonadorelin agonist treatment for men with locoregional prostate cancer may be associated with an increased risk of incident diabetes and ardiovascular disease.
Definition
ChEBI: A ten-membered synthetic oligopeptide comprising pyroglutamyl, histidyl, tryptophyl, seryl, tyrosyl, glycyl, leucyl, arginyl, prolyl and glycinamide residues joined in sequence.
Brand name
Lutrepulse (Ferring Pharmaceuticals).
Biological Activity
luteinizing hormone releasing hormone human acetate salt (lhrh) is a selective acitivator of mmp-2 and mmp-9 [1, 2].luteinizing hormone-releasing hormone (lhrh), also known as gonadotropin-releasing hormone (gnrh) is a trophic peptide hormone which secreted by gnrh neurons and plays an important role in the release of follicle-stimulating hormone (fsh) and luteinizing hormone (lh) from the anterior pituitary [3].mmp-2 (matrix metalloproteinase-2) and mmp-9 (matrix metalloproteinase-9) belong to the mmp family that play an important role in the breakdown of extracellular matrix (ecm) in normal physiological processes, for example, embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis [2].when tested with ishikawa and ecc-1 cell lines, lhrh resulted in the increase of mmp-9 expression which induced cell invasion and it was also showed that gpr101 mediated the lhrh activity and cooperated to function in the metastatic potential of endometrial cancer cells [1]. in human decidual endometrial stromal cells, lhrh with its receptor induced the activation of mmp-2 and mmp-9 [2].
Veterinary Drugs and Treatments
Gonadorelin is indicated (approved) for the treatment of ovarian
follicular cysts in dairy cattle. Additionally, gonadorelin has been
used in cattle to reduce the time interval from calving to first ovulation
and to increase the number of ovulations within the first 3
months after calving. This may be particularly important in increasing
fertility in cows with retained placenta.
In dogs, gonadorelin has been used experimentally to help diagnose
reproductive disorders or to identify intact animals versus castrated
ones by maximally stimulating FSH and LH production. It
has also been used experimentally in dogs to induce estrus through
pulsatile dosing. While apparently effective,
specialized administration
equipment is required for this method.
Gonadorelin has been used in cats as an alternate therapy to FSH
or hCG to induce estrus in cats with prolonged anestrus.
In Europe, a synthetic analogue buserelin has been used in horses
to stimulate cyclic estrus. Its efficacy
rates poorly when compared
to an artificial light program, however.
In human medicine, gonadorelin has been used for the diagnosis
of hypothalamic-pituitary dysfunction,
cryptorchidism, and depression
secondary to prolonged severe stress.
references
[1]. cho-clark, m., et al., gnrh-(1-5) activates matrix metallopeptidase-9 to release epidermal growth factor and promote cellular invasion. mol cell endocrinol, 2015.[2]. wu, h.m., et al., gonadotropin-releasing hormone type ii (gnrh-ii) agonist regulates the motility of human decidual endometrial stromal cells: possible effect on embryo implantation and pregnancy. biol reprod, 2015. 92(4): p. 98.[3]. garnick, m.b. and m. campion, abarelix depot, a gnrh antagonist, v lhrh superagonists in prostate cancer: differential effects on follicle-stimulating hormone. abarelix depot study group. mol urol, 2000. 4(3): p. 275-7.
Check Digit Verification of cas no
The CAS Registry Mumber 33515-09-2 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 3,3,5,1 and 5 respectively; the second part has 2 digits, 0 and 9 respectively.
Calculate Digit Verification of CAS Registry Number 33515-09:
(7*3)+(6*3)+(5*5)+(4*1)+(3*5)+(2*0)+(1*9)=92
92 % 10 = 2
So 33515-09-2 is a valid CAS Registry Number.
33515-09-2Relevant articles and documents
Reaction medium engineering in enzymatic peptide fragment condensation: Synthesis of eledoisin and LH-RH
Bjoerup, Peter,Torres, Josep Lluis,Adlercreutz, Patrick,Clapes, Pere
, p. 891 - 901 (1998)
The influence of different reaction systems on α-chymotrypsin-catalyzed synthesis of eledoisin and LH-RH peptides from (7+4) and (5+5) fragments was investigated. The peptide yield was determined in the following systems: buffered aqueous media, frozen solutions, organic media, and cosolvent mixtures. The experimental set up was tailored to allow the screening of an array of conditions with minimum consumption of peptide fragments (2.1 and 2.5mM). The best yields (22% yield for eledoisin and 68% yield for LH-RH) were obtained in buffered aqueous solutions. It was found that the choice of buffer had a strong influence on the peptide yield; boric-borate and ammonium acetate buffers at pH 9, gave the best results. In buffered aqueous systems, both syntheses were scaled up by using a 10-fold increase in fragment concentration (21 and 25mM). Under these conditions the yields rose to 57% and 80% of eledoisin and LH-RH, respectively. Moreover, during the synthesis of eledoisin and in the presence of boric-borate buffer pH 9, the peptide precipitated from the reaction medium preventing a secondary hydrolysis and facilitating the in situ product purification. Copyright (C) 1998 Elsevier Science Ltd.
IMPROVEMENTS IN SOLID PHASE PEPTIDE SYNTHESIS
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Paragraph 0071-0076, (2017/08/01)
An improved method of deprotection in solid phase peptide synthesis is disclosed. In particular the deprotecting composition is added in high concentration and small volume to the mixture of the coupling solution, the growing peptide chain, and any excess activated acid from the preceding coupling cycle, and without any draining step between the coupling step of the previous cycle and the addition of the deprotection composition for the successive cycle. Thereafter, the ambient pressure in the vessel is reduced with a vacuum pull to remove the deprotecting composition without any draining step and without otherwise adversely affecting the remaining materials in the vessel or causing problems in subsequent steps in the SPPS cycle.
Solid-Phase Synthesis of Peptide Amides on a Polystyrene Support Using Fluorenylmethoxycarbonyl Protecting Groups
Penke, Botond,Rivier, Jean
, p. 1197 - 1200 (2007/10/02)
We have investigated new routes for the synthesis of acid-sensitive amino acids using N-fluorenylmethoxycarbonyl amino acids and mild acid labile side chain protection in order to avoid HF cleavage as final step.The 4-(benzyloxy)benzylamine resin, applied successfully by Pietta and Brenna, proved to be unsuitable for the synthesis of peptide amides since we have found that trifluoroacetic acid treatment of peptide-resins yield the peptide still bearing a p-hydroxybenzyl group on the carboxamide nitrogen.We have successfully used the 2,4-dimethoxybenzhydrylamine support for the synthesis of peptide amides.Cholecystokinin octapeptide and GnRH were synthesized on the 2,4-dimethoxybenzhydrylamine resin and cleaved from the polymer with trifluoroacetic acid-thioanisole (4:1), and 95percent trifluroacetic acid containing phenol (2.5percent) and dimethyl sulfide (2.5percent), respectively.The final cleavage conditions had to be optimized in order to obtain good yields, suggesting that side chain protections of certain amino acids, possibly arginine and tryptophan, may have to be further refined.
