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Geissoschizine methyl ether


  • Brand : BIOFRON

  • Catalogue Number : BD-P0819

  • Specification : 98.0%(HPLC&TLC)

  • CAS number : 60314-89-8

  • Formula : C22H26N2O3

  • Molecular Weight : 366.45

  • PUBCHEM ID : 6443046

  • Volume : 25mg

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Catalogue Number


Analysis Method






Molecular Weight



White crystalline powder

Botanical Source

Uncaria rhynchophylla(Miq.)Miq. ex Havil.

Structure Type



Standards;Natural Pytochemical;API




Indolo[2,3-a]quinolizine-2-acetic acid, 3-ethylidene-1,2,3,4,6,7,12,12b-octahydro-α-(methoxymethylene)-, methyl ester, (αZ,2S,3E,12bS)-/Methyl (16Z,19E)-16-(methoxymethylene)coryn-19-en-17-oate/methyl (Z)-2-[(2S,3E,12bS)-3-ethylidene-2,4,6,7,12,12b-hexahydro-1H-indolo[2,3-a]quinolizin-2-yl]-3-methoxyprop-2-enoate


methyl (Z)-2-[(2S,3E,12bS)-3-ethylidene-2,4,6,7,12,12b-hexahydro-1H-indolo[2,3-a]quinolizin-2-yl]-3-methoxyprop-2-enoate


Geissoschizine methyl ether, a major indole alkaloid found in Uncaria hook, is a major active component of Yokukansan with psychotropic effects. Geissoschizine methyl ether is potent 5-HT1A receptor agonist[1][2].


1.2±0.1 g/cm3,


Methanol; Acetontrile; DMSO

Flash Point

Boiling Point

Melting Point



InChl Key


WGK Germany


HS Code Reference


Personal Projective Equipment

Correct Usage

For Reference Standard and R&D, Not for Human Use Directly.

Meta Tag

provides coniferyl ferulate(CAS#:60314-89-8) MSDS, density, melting point, boiling point, structure, formula, molecular weight etc. Articles of coniferyl ferulate are included as well.>> amp version: coniferyl ferulate

No Technical Documents Available For This Product.




The process of malignant transformation requires cells to undergo a variety of molecular alterations to acquire growth properties that allow them to divide indefinitely and in an uncontrolled fashion under conditions of low oxygen and poor nutrient supply. Such conditions would normally induce programmed cell death, and malignant cells additionally have to acquire molecular mechanisms to evade apoptotic stimuli in order to survive and to form solid tumours. It is conceivable that antiapoptotic signalling cascades play an equally important role in the development of the pathological cancer phenotype as the dysregulation of proliferative signalling cascades.

Phosphatidyl-inositol 3-kinase (PI3 K), which relays various signalling pathways via the production of phosphatidyl-inositide lipids, has been identified as a central mediator of cell growth, metabolism, migration, and survival (reviewed in Wymann et al, 2003). PI3 K regulates cellular functions by recruiting PI(3, 4, 5)P3 binding proteins to the plasma membrane preferentially via pH domains. The prototype of these molecules is protein kinase B/Akt. Binding to PI(3, 4, 5)P3 results in a conformational change which makes Akt susceptible to phosphorylation at threonine 308 and serine 473 (Alessi and Cohen, 1998). Phosphorylation of Akt results in its activation and dissociation from the membrane. The resolution of the crystal structures of activated Akt and inactive Akt2 has provided further clues about their regulation and activation (Yang et al, 2002; Huang et al, 2003). Substrates of Akt are phosphorylated within the consensus sequence RXRXXS/T (Obata et al, 2000). Several target proteins of Akt involved in antiapoptotic signalling, the regulation of the cell cycle, and insulin homeostasis have been described.

GSK3 was the first protein known to be inactivated by Akt via phosphorylation at serine 9 (Cross et al, 1995). Besides the regulation of glycogen synthesis, GSK3 regulates several intracellular signalling pathways including AP1 (Scalia et al, 2001), CREB (Cross et al, 1995), and the tumour-suppressor gene product APC (Zumbrunn et al, 2001). Akt can promote cellular survival by inhibiting proteins involved in the regulation of apoptosis. One such mechanism is the phosphorylation of the proapoptotic protein Bad at serine 136 by Akt, which creates a binding site for 14-3-3 proteins and thereby prevents Bad from binding and inhibiting the antiapoptotic protein Bcl-xL (Datta et al, 1997). Another direct mechanism is the Akt-mediated phosphorylation of caspase 9 at serine 196 inhibiting its protease- and apoptosis-initiating activity (Cardone et al, 1998). c-FLIP, a dominant-negative homologue of caspase 8, is upregulated in tumour cell lines on a transcriptional level by the Akt pathway through a yet unknown mechanism (Panka et al, 2001). The apoptosis signal-regulating kinase 1 (Ask1) is phosphorylated by Akt at serine 83, leading to its inhibition and a reduced activation of JNK, which under certain circumstances can promote apoptosis (Kim et al, 2001). The forkhead transcription factor FKHRL1 is phosphorylated by Akt at threonine 32 and serine 253, resulting in its retention in the cytoplasm by 14-3-3 proteins. Thus, FKHRL1-mediated transcription of proapoptotic proteins such as the Fas ligand is reduced and cell survival is promoted (Brunet et al, 1999). Other substrates of Akt include phosphofructokinase 2 (Deprez et al, 1997), Iκ-B kinase from the NF-κB pathway (Ozes et al, 1999), and endothelial NO synthase (Dimmeler et al, 1999).

Akt can influence proliferative and cell cycle regulatory pathways and thereby indirectly modulate tumour chemosensitivity by the regulation of Cyclin D stability (Muise-Helmericks et al, 1998) and inhibition of p27Kip1 protein levels (Collado et al, 2000). Furthermore, Akt has been shown to directly phosphorylate the cyclin-dependent kinase inhibitors p21WAF1 at threonine 145 and serine 146 (Zhou et al, 2001) and p27Kip1 at threonine 157 (Liang et al, 2002), leading to their cytosolic retention and neutralisation of their growth-inhibitory effect. In addition, cytoplasmic p21WAF1 binds to ASK1-inhibiting apoptosis (Asada et al, 1999). The p53 pathway is influenced by Akt through phosphorylation of the p53-regulating protein MDM2 at residues serine 166 and 186 (Mayo and Donner, 2001). Akt-mediated phosphorylation of MDM2 results in the translocation of MDM2 from the cytoplasm into the nucleus, leading to reduced cellular p53 protein levels and decreased p53 transcriptional activity.

Since PKB/Akt is involved in such a multitude of apoptosis regulatory pathways, it is not surprising that Akt is overexpressed in a variety of human tumour cell lines and cancers (Bellacosa et al, 1995; Ringel et al, 2001; Roy et al, 2002) and a mediator of oestrogen resistance in breast cancer cells (Campbell et al, 2001). Akt activity in cancers can either be deregulated by constitutive activation or by mutation of PTEN/MMAC1, a phosphatase that directly counteracts Akt through the dephosphorylation of PI-3-, 4-, and 5-P3 (Stambolic et al, 1998). Besides being overexpressed or constitutively activated in certain types of cancer, Akt has been implicated in modulating sensitivity of cancer cells towards standard chemotherapy (Hayakawa et al, 2000; Page et al, 2000; Schmidt et al, 2002; Knuefermann et al, 2003).

Although many apoptotic pathways modulated by Akt have been described, relatively little is known about the actual molecular mechanisms by which Akt suppresses apoptosis after chemotherapeutic treatment of cancer cells. To establish a cellular system that allows in-depth analysis of these pathways, we transfected NCI H460 human NSCLC cells with an expression vector encoding a constitutive form of Akt1 (Schmidt et al, 2002). Here we describe the effects of CA-Akt1 on the modulation of chemosensitivity towards several chemotherapeutic regimen in stable cell clones of NCI H460 NSCLC cells. Furthermore, we describe molecular alterations in various apoptotic pathways that may account for the desensitising effects observed in CA-Akt1-expressing NCI H460 cells.


Molecular alterations in apoptotic pathways after PKB/Akt-mediated chemoresistance in NCI H460 cells


S Hovelmann,1,2 T L Beckers,1,3 and M Schmidt1,1,*

Publish date

2004 Jun 14




Inflammatory effects of ambient particulate matter (PM) air pollution exposures may underlie PM-related increases in cardiovascular disease risk and mortality, although evidence of PM-associated leukocytosis is inconsistent and largely based on small, cross-sectional, and/or unrepresentative study populations.

Our objective was to estimate PM-leukocyte associations among U.S. women and men in the Women’s Health Initiative and Atherosclerosis Risk in Communities study (n=165,675).

We based the PM-leukocyte estimations on up to four study visits per participant, at which peripheral blood leukocytes and geocoded address-specific concentrations of PM≤10, ≤2.5, and 2.5-10μm in diameter (PM10, PM2.5, and PM2.5-10, respectively) were available. We multiply imputed missing data using chained equations and estimated PM-leukocyte count associations over daily to yearly PM exposure averaging periods using center-specific, linear, mixed, longitudinal models weighted for attrition and adjusted for sociodemographic, behavioral, meteorological, and geographic covariates. In a subset of participants with available data (n=8,457), we also estimated PM-leukocyte proportion associations in compositional data analyses.

We found a 12 cells/μL (95% confidence interval: −9, 33) higher leukocyte count, a 1.2% (0.6%, 1.8%) higher granulocyte proportion, and a −1.1% (−1.9%, −0.3%) lower CD8+ T-cell proportion per 10-μg/m3 increase in 1-month mean PM2.5. However, shorter-duration PM10 exposures were inversely and only modestly associated with leukocyte count.

The PM2.5-leukocyte estimates, albeit imprecise, suggest that among racially, ethnically, and environmentally diverse U.S. populations, sustained, ambient exposure to fine PM may induce subclinical, but epidemiologically important, inflammatory effects. https://doi.org/10.1289/EHP5360


Leukocyte Traits and Exposure to Ambient Particulate Matter Air Pollution in the Women’s Health Initiative and Atherosclerosis Risk in Communities Study


Rahul Gondalia,corresponding author1 Katelyn M. Holliday,1,2 Antoine Baldassari,1 Anne E. Justice,1,3 James D. Stewart,1 Duanping Liao,4 Jeff D. Yanosky,4 Stephanie M. Engel,1 Kristina M. Jordahl,5 Parveen Bhatti,5 Steve Horvath,6,7 Themistocles L. Assimes,8 James S. Pankow,9 Ellen W. Demerath,9 Weihua Guan,10 Myriam Fornage,11 Jan Bressler,12 Kari E. North,1,13 Karen N. Conneely,14 Yun Li,15,16,17 Lifang Hou,18,19 Andrea A. Baccarelli,20 and Eric A. Whitsel1,21

Publish date

2020 Jan;




Interstitial lung disease (ILD) is frequently associated with collagen diseases. The prognosis of acute-onset diffuse ILD (AoDILD) occurring in collagen disease patients is very poor. Here, we investigated serum biomarker profiles of AoDILD to find markers predicting outcome in patients with collagen diseases.

A solid-phase antibody array was used for screening 274 biomarkers in pooled sera from collagen disease patients in the AoDILD state and in the stable state. Biomarkers in individual sera were detected without pooling by bead-based immunoassay.

The serum levels of matrix metalloproteinase (MMP)-1, tissue inhibitor of metalloproteinase (TIMP)-1, osteopontin, interleukin (IL)-2 receptor α (IL-2Rα), and IL-1 receptor antagonist were significantly increased in AoDILD, but TIMP-2, MMP-3, and eotaxin 2 levels were decreased. The MMP-3 to MMP-1 ratio was reduced in AoDILD state. This tendency was also observed in RA patients with AoDILD. Moreover, serum IL-6 level was significantly increased in the AoDILD state in patients with acute exacerbation of ILD (AE-ILD). Serum TIMP-1 and IL-2Rα levels were significantly increased in the AoDILD state in patients with drug-induced ILD (DI-ILD), whereas TIMP-2, MMP-3, and eotaxin 2 levels were decreased. The MMP-3 to MMP-1 ratio was reduced in AoDILD state in patients with DI-ILD. The serum TIMP-3, MMP-9, osteopontin, IL-2Rα, MMP-1, and MMP-8 levels were significantly increased in the AoDILD state in patients who subsequently died, whereas TIMP-2 and MMP-3 levels were decreased in those who survived. The MMP-3 to MMP-1 ratio was reduced in AoDILD state in patients who died, but not in those who survived.

Serum biomarker profiles could represent prognosis markers for AoDILD in collagen diseases.


Collagen disease, Biomarker, Cytokine, Interstitial lung disease


Serum biomarker analysis of collagen disease patients with acute-onset diffuse interstitial lung disease


Shomi Oka,1 Hiroshi Furukawa,corresponding author1 Kota Shimada,2,3 Hiromi Hayakawa,1 Naoshi Fukui,1 Naoyuki Tsuchiya,4 and Shigeto Tohma1

Publish date