Relevant bibliographies by topics / Maytansinol

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  1. Journal articles
  2. Dissertations / Theses
  3. Book chapters
  4. Conference papers

Academic literature on the topic 'Maytansinol'

Author: Grafiati
Published: 9 March 2023
Last updated: 10 March 2023

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Journal articles on the topic "Maytansinol"

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Bénéchie, Michel, and Françoise Khuong-Huu. "Total Synthesis of (−)-Maytansinol." Journal of Organic Chemistry 61, no. 20 (January 1996): 7133–38. http://dx.doi.org/10.1021/jo960363a.

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BENECHIE, M., and F. KHUONG-HUU. "ChemInform Abstract: Total Synthesis of (-)-Maytansinol." ChemInform 28, no. 5 (August 4, 2010): no. http://dx.doi.org/10.1002/chin.199705299.

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Edwards, A., M. Gladstone, P. Yoon, D. Raben, B. Frederick, and T. T. Su. "Combinatorial effect of maytansinol and radiation in Drosophila and human cancer cells." Disease Models & Mechanisms 4, no. 4 (April 18, 2011): 496–503. http://dx.doi.org/10.1242/dmm.006486.

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Moss, Steven J., Linquan Bai, Sabine Toelzer, Brian J. Carroll, Taifo Mahmud, Tin-Wein Yu, and Heinz G. Floss. "Identification of Asm19 as an Acyltransferase Attaching the Biologically Essential Ester Side Chain of Ansamitocins UsingN-Desmethyl-4,5-desepoxymaytansinol, Not Maytansinol, as Its Substrate." Journal of the American Chemical Society 124, no. 23 (June 2002): 6544–45. http://dx.doi.org/10.1021/ja020214b.

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Lopus, Manu, Emin Oroudjev, Leslie Wilson, Sharon Wilhelm, Wayne Widdison, Ravi Chari, and Mary Ann Jordan. "Maytansine and Cellular Metabolites of Antibody-Maytansinoid Conjugates Strongly Suppress Microtubule Dynamics by Binding to Microtubules." Molecular Cancer Therapeutics 9, no. 10 (October 2010): 2689–99. http://dx.doi.org/10.1158/1535-7163.mct-10-0644.

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Kowalczyk, Lidia, Rupert Bartsch, Christian F. Singer, and Alex Farr. "Adverse Events of Trastuzumab Emtansine (T-DM1) in the Treatment of HER2-Positive Breast Cancer Patients." Breast Care 12, no. 6 (2017): 401–8. http://dx.doi.org/10.1159/000480492.

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The human epidermal growth factor receptor 2 (HER2) is commonly associated with poor prognosis and is overexpressed in approximately 15-20% of all breast cancers. The introduction of HER2-targeted therapies led to significant improvement in the prognosis of patients with HER2-positive breast cancer, for both early and advanced disease. These targeted therapies include the antibodies trastzumab and pertuzumab, the tyrosine kinase inhibitor lapatinib, and the antibody-drug conjugate trastuzumab emtansine (T-DM1). T-DM1 combines the anti-tumor activity of trastuzumab with that of DM1, a highly potent derivative of the anti-microtubule agent maytansine, resulting in increased anti-tumor activity. Notably, this agent has been demonstrated to be safe and is associated with low toxicity rates. However, maytansinoid, the cytotoxic component of T-DM1, does have the potential to induce various adverse events, particularly radiation necrosis, when used in combination with stereotactic radiosurgery. In this review, we aimed to summarize the current literature regarding T-DM1 safety and toxicity, with special emphasis on the existing landmark studies.
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Pitakbut, Thanet, Michael Spiteller, and Oliver Kayser. "Genome Mining and Gene Expression Reveal Maytansine Biosynthetic Genes from Endophytic Communities Living inside Gymnosporia heterophylla (Eckl. and Zeyh.) Loes. and the Relationship with the Plant Biosynthetic Gene, Friedelin Synthase." Plants 11, no. 3 (January 25, 2022): 321. http://dx.doi.org/10.3390/plants11030321.

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Even though maytansine was first discovered from Celastraceae plants, it was later proven to be an endophytic bacterial metabolite. However, a pure bacterial culture cannot synthesize maytansine. Therefore, an exclusive interaction between plant and endophytes is required for maytansine production. Unfortunately, our understanding of plant–endophyte interaction is minimal, and critical questions remain. For example: how do endophytes synthesize maytansine inside their plant host, and what is the impact of maytansine production in plant secondary metabolites? Our study aimed to address these questions. We selected Gymnosporia heterophylla as our model and used amino-hydroxybenzoic acid (AHBA) synthase and halogenase genes as biomarkers, as these two genes respond to biosynthesize maytansine. As a result, we found a consortium of seven endophytes involved in maytansine production in G. heterophylla, based on genome mining and gene expression experiments. Subsequently, we evaluated the friedelin synthase (FRS) gene’s expression level in response to biosynthesized 20-hydroxymaytenin in the plant. We found that the FRS expression level was elevated and linked with the expression of the maytansine biosynthetic genes. Thus, we achieved our goals and provided new evidence on endophyte–endophyte and plant–endophyte interactions, focusing on maytansine production and its impact on plant metabolite biosynthesis in G. heterophylla.
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Cao, Shuo, Yue-Hui Dong, De-Feng Wang, and Zhao-Peng Liu. "Tubulin Maytansine Site Binding Ligands and their Applications as MTAs and ADCs for Cancer Therapy." Current Medicinal Chemistry 27, no. 27 (August 5, 2020): 4567–76. http://dx.doi.org/10.2174/0929867327666200316144610.

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Background: Microtubule Targeting Agents (MTAs) represent the most successful anticancer drugs for cancer chemotherapy. Through interfering with the tubulin polymerization and depolymerization dynamics, MTAs influence intracellular transport and cell signal pathways, inhibit cell mitosis and cell proliferation, and induce cell apoptosis and death. The tubulin maytansine site binding agents are natural or nature-derived products that represent one type of the MTAs that inhibit tubulin polymerization and exhibit potent antitumor activity both in vitro and in vivo. They are used as Antibody-Drug Conjugates (ADCs) in cancer chemotherapy. Methods: Using SciFinder® as a tool, the publications about maytansine, its derivatives, maytansine binding site, maytansine site binding agents and their applications as MTAs for cancer therapy were surveyed with an exclusion on those published as patents. The latest progresses in clinical trials were obtained from the clinical trial web. Results: This article presents an introduction about MTAs, maytansine, maytansine binding site and its ligands, the applications of these ligands as MTAs and ADCs in cancer therapy. Conclusion: The maytansine site binding agents are powerful MTAs for cancer chemotherapy. The maytansine site ligands-based ADCs are used in clinic or under clinical trials as cancer targeted therapy to improve their selectivity and to reduce their side effects. Further improvements in the delivery efficiency of the ADCs will benefit the patients in cancer targeted therapy.
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Tassone, Pierfrancesco, Victor S. Goldmacher, Paola Neri, Antonella Gozzini, Masood A. Shammas, Kathleen R. Whiteman, Linda L. Hylander-Gans, et al. "Cytotoxic activity of the maytansinoid immunoconjugate B-B4–DM1 against CD138+ multiple myeloma cells." Blood 104, no. 12 (December 1, 2004): 3688–96. http://dx.doi.org/10.1182/blood-2004-03-0963.

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We tested the in vitro and in vivo antitumor activity of the maytansinoid DM1 (N2′-deacetyl-N2′-(3-mercapto-1-oxopropyl)-maytansine), a potent antimicrotubule agent, covalently linked to the murine monoclonal antibody (mAb) B-B4 targeting syndecan-1 (CD138). We evaluated the in vitro activity of B-B4–DM1 against a panel of CD138+ and CD138- cell lines, as well as CD138+ patient multiple myeloma (MM) cells. Treatment with B-B4–DM1 selectively decreased growth and survival of MM cell lines, patient MM cells, and MM cells adherent to bone marrow stromal cells. We further examined the activity of B-B4–DM1 in 3 human MM models in mice: (1) severe combined immunodeficient (SCID) mice bearing subcutaneous xenografts; (2) SCID mice bearing green fluorescent protein–positive (GFP+) xenografts; and (3) SCID mice implanted with human fetal bone (SCID-hu) and subsequently injected with patient MM cells. Tumor regression and inhibition of tumor growth, improvement in overall survival, and reduction in levels of circulating human paraprotein were observed in mice treated with B-B4–DM1. Although immunohistochemical analysis demonstrates restricted CD138 expression in human tissues, the lack of B-B4 reactivity with mouse tissues precludes evaluation of its toxicity in these models. In conclusion, B-B4–DM1 is a potent anti-MM agent that kills cells in an antigen-dependent manner in vitro and mediates in vivo antitumor activity at doses that are well tolerated, providing the rationale for clinical trials of this immunoconjugate in MM.
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Tassone, Pierfrancesco, Antonella Gozzini, Victor Goldmacher, Masood A. Shammas, Kathleen R. Whiteman, Daniel R. Carrasco, Cheng Li, et al. "In Vitro and in Vivo Activity of the Maytansinoid Immunoconjugate huN901-N2′-Deacetyl-N2′-(3-Mercapto-1-Oxopropyl)-Maytansine against CD56+ Multiple Myeloma Cells." Cancer Research 64, no. 13 (July 1, 2004): 4629–36. http://dx.doi.org/10.1158/0008-5472.can-04-0142.

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Dissertations / Theses on the topic "Maytansinol"

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MARZULLO, PAOLA. "CHALLENGES AND OPPORTUNITIES OF MAYTANSINOL, CANNABIDIOL AND CALLYSPONGIOLIDE IN NATURAL PRODUCT CHEMISTRY." Doctoral thesis, Università degli Studi di Milano, 2022. http://hdl.handle.net/2434/920111.

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The development of new drugs has long been inspired by Nature as the main source of the biologically active compounds. This practice has motivated total synthesis and diversity-oriented synthesis in the drug discovery and drug design process because natural products offer great opportunities to find new low molecular weight structures active against a wide range of assay targets. Obtaining a synthetic source and creation of derivative analogs would allow a greater understanding of the biologocal effects because natural products has tipically been extracted in complex mixture with other compounds making isolation impossible with useful quantities. With this in mind, the enantioselective syntheses carried out to obtain maytansinol-based conjugates as microtubule modulators, cannabidiol-C4, and two fragments of callyspongiolide are described in this thesis.
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Brünjes, Marco. "Studien zur chemoenzymatischen Synthese und Biosynthese von Maytansinoid-Analoga." [S.l.] : [s.n.], 2006. http://deposit.ddb.de/cgi-bin/dokserv?idn=98052542X.

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Frenzel, Thomas. "Studien zur chemoenzymatischen Synthese von Maytansinoid-Analoga Synthese von seco-Proansamitocin /." [S.l.] : [s.n.], 2005. http://deposit.ddb.de/cgi-bin/dokserv?idn=977228118.

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Wibowo, Mario. "Natural Products from Australian Celastraceae Plants and Their Leucine Transport Inhibition in Prostate Cancer Cells." Thesis, Griffith University, 2018. http://hdl.handle.net/10072/381383.

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Natural products are the main source of approved medicines with more than half of the drugs on the market today being either natural products or natural product derivatives. Moreover, a significant number of these drugs are of plant origins. However, it has been estimated that of the >422,000 plant species currently described, only 15% of this plant diversity have been phytochemically explored. Therefore, there still exists a huge potential in the plant kingdom for the discovery of new chemistry, some of which may result in the identification of lead compounds or drugs for the pharmaceutical industry. Several notable examples of plant-derived natural product drugs are the anticancer compounds vinblastine, vincristine, and paclitaxel, the antimalarial agents artemisinin and quinine, and the Alzheimer drugs galantamine and huperzine A. In regards to plant-derived lead compounds, two pertinent examples include camptothecin, which lead to the development of the anticancer agents, topotecan and irinotecan, and papaverine, which was the lead model for the antihypertension verapamil. The Celastraceae plant family is found worldwide, especially in tropical and subtropical regions; currently there are 88 genera and 1300 species belonging to this flowering plants family. Various molecules possessing numerous biological activities have been reported from Celastraceae. One noteworthy example of an interesting natural product and cancer lead compound from Celastraceae is the alkaloid maytansine, which was further developed into the antibody drug conjugate treatment, transtuzumab emtansine, and is currently used for breast cancer treatment. However, the characteristic secondary metabolites of Celastraceae are the dihydro-β-agarofuran sesquiterpenoids, which have been reported in the literature as both chemotaxonomic markers and privileged structures. The L-type amino acid transporters (LATs) are responsible for the uptake of various amino acids (including leucine) into cells. Leucine is a regulator amino acid of the mTORC1 signalling pathway and one of the essential amino acids that is transported by LATs. Though LATs are expressed in both normal and cancer cells, the overexpression of LATs has been reported in various cancer cells, including those associated with prostate cancer. Thus, the inhibition of leucine uptake may be a novel drug target for cancer treatment. To date, very few natural product LATs inhibitors have been identified. Venulosides, which are all monoterpenoid glycosides, were the first and only natural products (reported by Quinn et al.) that had been reported to inhibit LATs prior to these PhD studies. Their recent discovery highlights the potential of natural products in the discovery of new LAT inhibitors. This knowledge coupled with an interest in the chemistry of the hitherto under-investigated Australian plant family, Celastraceae, motivated us to identify new small molecules from this particular biota and evaluate all compounds isolated or semi-synthesised for their ability to inhibit leucine uptake on the human prostate cancer cell line, LNCaP. The plants that were investigated during these PhD studies included Maytenus bilocularis, Denhamia pittosporoides, and Celastrus subspicata and Denhamia celastroides. In Chapter 2, phytochemical studies of the leaves of the Australian rainforest plant Maytenus bilocularis led to the identification of three new dihydro-β-agarofurans, bilocularins A–C, and six known compounds, namely celastrine A, 1α,6β,8α- triacetoxy-9α-benzoyloxydihydro-β-agarofuran, 1α,6β-diacetoxy-9α-benzoyloxy-8α- hydroxydihydro-β-agarofuran, Ejap-10, 1α,6β-diacetoxy-9β-benzoyloxydihydro-β- agarofuran, and Ejap-2. Bilocularin A was used to generate four semisynthetic ester analogues. The absolute configuration of bilocularins A and B was established by X-ray crystallography study; for bilocularin C, the absolute was determined by comparison of ECD spectra. All compounds were found to be inactive in a cytotoxicity assay against the human prostate cancer cell line LNCaP. However, several compounds were found to exhibit similar potency to verapamil in reversing multidrug resistance in the human leukemia cells (CEM/VCR R). Moreover, 1α,6β,8α-triacetoxy-9α-benzoyloxydihydro- β-agarofuran was shown to inhibit leucine uptake in LNCaP cells with IC50 value of 15.5 μM, which was more potent than the leucine analogue 2-aminobicyclo[2.2.1]- heptane-2-carboxylic acid (BCH). Motivated by these findings with dihydro-β-agarofurans from the leaves of M. bilocularis, we extended our studies (see Chapter 3) to the roots of this plant, which had never been phytochemically explored. Six new dihydro-β-agarofuran sesquiterpenoids (bilocularins D–I), together with three known compounds, namely 1α,2α,6β,15- tetraacetoxy-9β-benzoyloxydihydro-β-agarofuran, pristimerin, and celastrol were successfully isolated. Moreover, the absolute configuration of bilocularin D was established by single-crystal X-ray diffraction analysis. Bilocularins D and G, 1α,2α,6β,15-tetraacetoxy-9β-benzoyloxydihydro-β-agarofuran, and celastrol inhibited leucine uptake in the LNCaP cells with IC50 values ranging from 2.5–27.9 μM. This study identified bilocularins D–F as the first dihydro-β-agarofurans possessing a hydroxyacetate group. Chapter 4 details the identification of two previously undescribed dihydro-β- agarofurans, denhaminols I and J together with four related and known metabolites, 1α,2α,6β,15-tetraacetoxy-9α-benzoyloxy-8-oxodihydro-β-agarofuran, wilforsinine F, 1α,2α,6β,8α,15-pentaacetoxy-9α-benzoyloxydihydro-β-agarofuran, and 1α,2α,6β,15- tetraacetoxy-9β-benzoyloxydihydro-β-agarofuran. These metabolites were purified from the CH2Cl2 extract of the leaves of D. pittosporoides. The structure of denhaminol I was further confirmed by X-ray crystallography analysis, which also established its absolute configuration. Denhaminol I and wilforsinine F were shown to exhibit leucine transport inhibitory activity in LNCaP cells with IC50 of 51.5 μM and 95.5 μM, respectively. Chapter 5, reports on the chemical investigation of CH2Cl2 extract of the leaves of the Australian endemic vine, Celastrus subspicata, which afforded seven previously unknown dihydro-β-agarofurans, celastrofurans A–G and two known compounds, (1S,4R,5S,7R,9S,10S)-9-benzoyloxy-1-furoyloxydihydro-β-agarofuran and (1R,2R,4R,5S,7R,9S,10R)-2-acetoxy-9-benzoyloxy-1-furoyloxydihydro-β-agarofuran. X-ray diffraction and ECD studies were undertaken to define the absolute configurations of celastrofurans A–D. All the isolated compounds from this vine were found to inhibit leucine transport in the human prostate cancer cell line LNCaP with IC50 values ranging from 7.0 to 98.9 μM, which were more potent than the L-type amino acid transporter (LAT) family inhibitor, BCH. Finally, Chapter 6 describes the development of an analytical method using UHPLC-MS that was applied to 16 crude CH2Cl2 extracts from Australian Celastraceae plants. A subset of the available Celastraceae plants from Grifitth University’s NatureBank resource was accessed during these studies that included three barks, one fruit, one leaf, seven roots, two twigs and two mixed samples all of which were collected from the State of Queensland. The data generated were analysed and dereplication performed using scientific databases such as the Dictionary of Natural Products and SciFinder in order to identify new natural products from Celastraceae plants. These investigations led to the large-scale extraction and isolation work on the prioritised Denhamia celastroides fruits sample, which resulted in the purification of the new natural products, denhaminol O–R. and a known analogue denhaminol G. In summary, this thesis describes the isolation and characterisation of 18 new natural products and 12 known metabolites from three Australian Celastraceae plants. The chemical structures of all compounds were determined by detailed interpretation of 1D/2D NMR and MS data and X-ray crystallography studies. Full spectroscopic and spectrometric characterisation of all new compounds was performed using NMR, UV, IR, ECD and specific rotation. The compounds were screened for their leucine uptake inhibition in LNCaP cells and several compounds were identified as leucine uptake inhibitors, which were more potent than the LAT family inhibitor and currently used positive control, BCH. This thesis describes for the first time the inhibition of leucine uptake in prostate cancer cells by dihydro-β-agarofurans; the most potent inhibitor of LAT (bilocularin G, IC50 = 2.5 μM) to date was also reported during these studies. Finally, the new UHPLC-MS methodology developed during these studies was used to rapidly analyse 16 Celastraceae plants, and subsequently prioritise three samples for future metabolomics investigations. The fruits of D. celastroides were chosen for chemical investigation due to most encouraging data. An additional four new compounds (denhaminols O–R) were successfully isolated from the CH2Cl2 of the fruits of D. celastroides. This study exemplified the advantage of UHPLC-MS in combination with scientific databases data analysis in natural products dereplication.
Thesis (PhD Doctorate)
Doctor of Philosophy (PhD)
School of Environment and Sc
Science, Environment, Engineering and Technology
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Brünjes, Marco [Verfasser]. "Studien zur chemoenzymatischen Synthese und Biosynthese von Maytansinoid-Analoga / von Marco Brünjes." 2006. http://d-nb.info/98052542X/34.

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Frenzel, Thomas [Verfasser]. "Studien zur chemoenzymatischen Synthese von Maytansinoid-Analoga : Synthese von seco-Proansamitocin / von Thomas Frenzel." 2005. http://d-nb.info/977228118/34.

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Savoie, Rondeau Isabelle. "Sensibilité des cellules leucémiques aux immunoconjugués anti-CD33." Thèse, 2012. http://hdl.handle.net/1866/9790.

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La leucémie myéloïde aigue (LMA), cancer du sang causé par une prolifération excessive des précurseurs myéloïdes à un stade précoce de maturation, est associée à une survie variant entre 20 et 30% à cinq ans en dépit des traitements de chimiothérapie les plus intensifs. L’antigène CD33 est exprimé chez les cellules malignes dans 90% des LMA ce qui en fait une cible de choix pour le développement d’immunoconjugué (IC). Trois IC composés d’un anticorps monoclonal anti-CD33 couplé à la maytansine, une toxine s’attaquant aux fuseaux mitotiques, ont été créés. Nous avons étudié l’effet de ces IC sur des cellules primaires et des lignées cellulaires LMA et étudier les mécanismes pouvant expliquer différents niveaux de sensibilité. Les études effectuées ont permis de déterminer que le niveau d’expression du CD33 n’explique pas la variation de sensibilité face aux IC. Il a été démontré que les IC anti-CD33 sont internalisés rapidement par la cellule et que le conjugué est retrouvé au niveau de l’endosome en premier lieu. Il a été confirmé que le lysosome est essentiel à l’effet anti-mitotique induit par le conjugué. Aussi, il est proposé que la protéine SOCS3 pourrait jouer un rôle dans la résistance aux IC anti-CD33 en dirigeant le complexe IC-CD33-SOCS3 vers le protéasome et ainsi empêcher la libération du composé toxique par le lysosome. Nous avons aussi conclu que les variations d’agent de liaison et l’augmentation du nombre de molécules toxiques entre les 3 IC n’ont pas été suffisantes pour augmenter leur efficacité à éliminer les cellules LMA. L’évaluation de ces IC ainsi que l’identification des mécanismes de résistance permettra de cibler les patients les plus susceptibles de bénéficier de ce type de traitement et potentiellement d’identifier de nouvelles voies pour améliorer l’efficacité des traitements.
Acute myeloid leukemia (AML), a cancer where hematopoietic precursors are arrested in an early stage of development, is associated with a poor survival rate of 20 to 30% over five years, despite intensive chemotherapy treatments. In approximately 90% of AML cases the malignant cells express CD33 antigen, which makes it a target of choice for development of immunotoxin based therapy. Three immunoconjugates (IC) composed of anti-CD33 monoclonal antibody coupled with maytansine derivative, which prevent tubulin polymerization and thus formation of mitotic spindle, were designed. These three IC were tested for their activity against several AML cell lines and primary AML patient cells and we investigate mechanisms responsible for variation in sensitivity to IC treatment. In this report, we show that differences in number of CD33 molecules on AML cell surface does not explain the observed differences in IC sensitivity. We demonstrate that binding of huMy9-6 antibody to CD33 induces rapid internalization and that it is first process through endosome. We confirm that lysosomal processing is essential for the antimitotic effect induced by IC treatment. Also, we provide evidence that SOCS3 protein may play a role in resistance of AML cells to anti-CD33 therapy by directing IC-CD33-SOCS3 complex to the proteasome and therefore affecting lysosomal decoupling of IC-CD33 and intracellular release of maytansine derivatives. Finally, the linkers and maytansine derivative modifications were not sufficient to increase sufficiently the efficacy of conjugates to eliminate higher numbers of AML cells. The identification of mechanisms responsible for increased resistance of AML cell lines and primary AMLs may allow us to identify IC responsive AML cells and also identify strategies to improve the efficacy of IC treatment.
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Book chapters on the topic "Maytansinol"

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Leistner, Eckhard. "Das Vorkommen von Maytansin in Celastraceen: Ist die Biosynthese des Maytansins eine Stoffwechselleistung der Pflanze oder eines wurzelbürtigen Mikroorganismus?" In Prozessregulation in der Rhizosphäre, 51–54. Wiesbaden: Vieweg+Teubner Verlag, 2003. http://dx.doi.org/10.1007/978-3-663-07809-8_6.

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Erickson, Hans. "Antibody-Maytansinoid Conjugates: From the Bench to the Clinic." In Drug Delivery in Oncology, 375–94. Weinheim, Germany: Wiley-VCH Verlag GmbH & Co. KGaA, 2011. http://dx.doi.org/10.1002/9783527634057.ch13.

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Widdison, Wayne C. "CHAPTER 5. Maytansinoid Payloads for Antibody–Drug Conjugates (ADCs)." In Cytotoxic Payloads for Antibody–Drug Conjugates, 100–116. Cambridge: Royal Society of Chemistry, 2019. http://dx.doi.org/10.1039/9781788012898-00100.

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Lambert, John M., Veronique Blanc, Nathalie Le Bail, and Anne Bousseau. "Targeting CD19 with SAR3419, an anti-CD19-Maytansinoid Conjugate for the Treatment of B Cell Malignancies." In Antibody-Drug Conjugates and Immunotoxins, 149–60. New York, NY: Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4614-5456-4_9.

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Conference papers on the topic "Maytansinol"

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Fishkin, Nathan, Erin Maloney, Ravi Chari, and Rajeeva Singh. "Abstract 4398: Maytansinoid release from thioether linked antibody maytansine conjugates (AMCs) under oxidative conditions: Implication for formulation and forex vivosample analysis in pharmacokinetic studies." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-4398.

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Kusari, S., and M. Spiteller. "Plant-endophyte communication: maytansine as an example." In 67th International Congress and Annual Meeting of the Society for Medicinal Plant and Natural Product Research (GA) in cooperation with the French Society of Pharmacognosy AFERP. © Georg Thieme Verlag KG, 2019. http://dx.doi.org/10.1055/s-0039-3399694.

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Whiteman, Kathleen R., Holly A. Johnson, Xiuxia Sun, Robert Mastico, Susan Emrich, Lauren Clancy, Hans Erickson, and Jan Pinkas. "Abstract 4628: Anti-tumor activity and pharmacokinetics of the anti-FOLR1-maytansinoid conjugate IMGN853 is maintained over a wide range of maytansinoid-to-antibody ratios." In Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-4628.

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Widdison, Wayne C., Sharon Wilhelm, Karen Veale, Yelena Kovtun, Hans Erickson, Charlene Audette, Barbara Leeca, Gregory Jones, and Ravi Chari. "Abstract 2668: Detoxification of metabolites from antibody-maytansinoid conjugates by human liver microsomes." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-2668.

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Sun, Xiuxia, Jose F. Ponte, Nicholas C. Yoder, Jennifer Coccia, Leanne Lanieri, Rassol Laleau, Qifeng Qiu, et al. "Abstract 4531: Effects of drug load on therapeutic index for antibody-maytansinoid conjugates." In Proceedings: AACR 106th Annual Meeting 2015; April 18-22, 2015; Philadelphia, PA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-7445.am2015-4531.

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Kellogg, Brenda, Charlene Audette, Hans Erickson, Michelle Mayo, Michael Okamoto, Jan Pinkas, Xiuxia Sun, et al. "Abstract 4404: Comparativein vivopharmacokinetic properties of antibody-maytansinoid conjugates with alternative non-cleavable linkers." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-4404.

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Singh, Rajeeva, Nathan Fishkin, Yelena Kovtun, Gregory Jones, Jose Ponte, Hans Erickson, Erica Hong, et al. "Abstract C164: New tri-glycyl peptide linker offers advantages for maytansinoid antibody-drug conjugates (ADCs)." In Abstracts: AACR-NCI-EORTC International Conference: Molecular Targets and Cancer Therapeutics--Oct 19-23, 2013; Boston, MA. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1535-7163.targ-13-c164.

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Ab, Olga, Laura M. Bartle, Lingyun Rui, Jennifer Coccia, Holly A. Johnson, Kathleen R. Whiteman, Brenda Kellogg, Lauren Clancy, Xiuxia Sun, and Victor S. Goldmacher. "Abstract 4576: IMGN853, an anti-Folate Receptor I antibody-maytansinoid conjugate for targeted cancer therapy." In Proceedings: AACR 102nd Annual Meeting 2011‐‐ Apr 2‐6, 2011; Orlando, FL. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1538-7445.am2011-4576.

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Widdison, Wayne C., Joe Ponte, Jennifer Coccia, Yulius Setiady, Ling Dong, Anja Skaletskaya, Nathan Fishkin, et al. "Abstract 1618: New peptide-linked anilino-maytansinoid antibody-drug conjugates (ADCs) for the treatment of cancer." In Proceedings: AACR Annual Meeting 2014; April 5-9, 2014; San Diego, CA. American Association for Cancer Research, 2014. http://dx.doi.org/10.1158/1538-7445.am2014-1618.

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Sinkevicius, Kerstin W., Leanne Lanieri, Jenny Lee, Steven Boule, Nicholas C. Yoder, Stuart W. Hicks, Jan Pinkas, Jose F. Ponte, and Richard J. Gregory. "Abstract 219: The potential benefit of lower drug-antibody ratio (DAR) on antibody-maytansinoid conjugatein vivoefficacy." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.sabcs18-219.

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