Actividad antineoplásica de la riproximina, una proteína citotóxica inactivadora de ribosomas tipo II – Una revisión

Antônio Rony da Silva Pereira Rodrigues

Resumen


El estudio presenta una síntesis del conocimiento a través de los hallazgos en la literatura sobre la riproximina y su actividad antineoplásica, basada en una revisión en las bases de datos Embase, Scopus, PubMed-Medline y Web of Science. Mediante la aplicación de criterios de selección, se seleccionaron 9 estudios, que después de ser analizados, forman parte de la revi- sión. Los estudios sobre la riproximina son escasos pero en algunos se ha informado sobre la actividad antineoplásica contra las líneas celulares de cáncer de hígado y en la cepa Suit2-007 de adenocarcinoma pancreático, lo que demuestra el potencial antineoplásico, por lo cual se necesita información sobre la aplicación de la proteína en terapias contra el cáncer para proponer una nueva clase de terapias antineoplásicas.

Recibido: 04/05/2023 Aceptado: 31/07/2023

Palabras clave


Bioquímica; Inhibidores de la síntesis de proteínas; Neoplasias

Texto completo:

PDF

Referencias


World Health Organization. Global Cancer Observatory. Cancer

Tomorrow. Lyon, France: WHO, 2020. Disponible en: https://

gco.iarc.fr/tomorrow/en/dataviz/isotype

MMAN Ranjha, B Shafique, L Wang, S Irfan, MN Safdar, MA

Murtaza, HR Nadeem. A comprehensive review on phytochemis-

try, bioactivity and medicinal value of bioactive compounds of

pomegranate (Punica granatum). Adv. Trad. Med., 23(1), 37-57

(2023).

V Mishra, R Mishra, RS Shamra. Ribosome inactivating proteins–

An unfathomed biomolecule for developing multi-stress tolerant

transgenic plants. Int. J. Biol. Macromol, 210, 107-122 (2022).

F Stirpe, MG Battelli. Ribosome-inactivating proteins: progress

and problems. Cell. Mol. Life Sci., 63, 1850-1866 (2006).

R Kumar, A Bhattacharjee, S Tiwari. Plant-derived ribosome-in-

activating proteins involved in defense against plant viruses. Eur.

J. Plant Pathol., 162, 1-23 (2022):

M Puri, I Kaur, MA Perugini, RC Gupta. Ribosome-inactivating

proteins: current status and biomedical applications. Drug Discov.

Today, 17(14), 774-783 (2012).

MR Hartley, JM Lord. Cytotoxic ribosome-inactivating lectins

from plants. Biochim. Biophys. Acta - Proteins and Proteomics,

(1-2), 1-14 (2004).

FWMB Preijers. Rationale for the clinical use of immunotoxins:

monoclonal antibodies conjugated to ribosome-inactivating pro-

teins. Leuk. Lymphoma, 9(4-5), 293-304 (1993).

C Voss, MR Eyol, E Berger. Identification of potent anticancer

activity in Ximenia americana aqueous extracts used by African

traditional medicine. Toxicol. Appl. Pharmacol., 211(3), 177-

(2006).

C Horrix, Z Raviv, E Flescher, C Voss, MR Berger. Plant ribo-

some-inactivating proteins type II induce the unfolded protein re-

sponse in human cancer cells. Cell. Mol. Life Sci., 68, 1269-1281

(2011).

RF Celedonio, ACF Queiroga, WF Celedonio, JF Felício, XBL de

Queiroz, YS de Oliveira, JF do Amaral. Propriedades antidiabéti-

cas das plantas medicinais do gênero Bauhinia: revisão integra-

tiva. Rev. Fitos., 1(1) (2023). https://doi.org/10.32712/2446-

2023.1399

R Whittemore. Combining in nursing research: methods and im-

plications. Nurs. Res., 54(1), 56-62 (2005).

M Ouzzani, H Hammady, Z Fedorowicz, A Elmagarmid. Ray-

yan—a web and mobile app for systematic reviews. Syst. Rev.,

(210) (2016). https://doi.org/10.1186/s13643-016-0384-

A Pervaiz, T Saleem, K Kanwal, SM Raza, S Iqbal, M Zepp, MR

Berger. Expression profiling of anticancer genes in colorectal can-

cer patients and their in vitro induction by riproximin, a ribosomal

inactivating plant protein. J. Cancer Res. Clin. Oncol., 1-13,

(2022). https://doi.org/10.1007/s00432-022-04410-6

MN Sagini, KD Klika, A Orry, M Zepp, J Mutiso, MR Berger.

Riproximin exhibits diversity in sugar binding and modulates

some metastasis-related proteins with lectin like properties in pan-

creatic ductal adenocarcinoma. Front. Pharmacol., 11, e549804

(2020). https://doi.org/10.3389/fphar.2020.549804

A Murtaja, E Eyol, J Xiaoqi, MR Berger, H Adwan. The ribosome

inhibiting protein riproximin shows antineoplastic activity in ex-

perimental pancreatic cancer liver metastasis. Oncol. Lett., 15(2),

-1448 (2018). https://doi.org/10.3892/ol.2017.7526

A Pervaiz, M Zepp, H Adwan, MR Berger. Riproximin modulates

multiple signaling cascades leading to cytostatic and apoptotic ef-

fects in human breast cancer cells. J. Cancer Res. Clin. Oncol.,

, 135-147 (2016). https://doi.org/10.1007/s00432-015-2013-3

Pervaiz A, Adwan H, Berger MR. Riproximin: A type II ribosome

inactivating protein with anti-neoplastic potential induces

IL24/MDA-7 and GADD genes in colorectal cancer cell lines. Int.

J. Oncol, 47(3), 981-990 (2015). https://doi.org/10.3892/ijo.

3073

H Adwan, A Murtaja, K Kadhim Al-Taee, A Pervaiz, T Hielscher,

MR Berger. Riproximin’s activity depends on gene expression

and sensitizes PDAC cells to TRAIL. Cancer Biol. Ther., 5(9),

-1197 (2014). https://doi.org/10.4161/cbt.29503

J Saenger, M Leible, MH Seelig, MR Berger. Chemoembolization

of rat liver metastasis with irinotecan and quantification of tumor

cell reduction. J. Cancer Res. Clin. Oncol., 130, 203-210 (2004).

https://doi.org/10.1007/s00432-003-0523-x

H Bayer, K Essig, S Stanzel, M Frank, JC Gildersleeve, MR Ber-

ger, C Voss. Evaluation of riproximin binding properties reveals a

novel mechanism for cellular targeting. J. Biol. Chem., 287(43),

–35886 (2012). https://doi.org/10.1074/jbc.M112.368548

F Stirpe. Ribosome-inactivating proteins: from toxins to useful

proteins. Toxicon, 67, 12–16 (2013). https://doi.org/10.1016/

j.toxicon.2013.02.005

C Voss, E Eyol, M Frank, CW Lieth, C Voss, MR Berger. Identi-

fication and characterization of riproximin, a new type II ribo-

some‐inactivating protein with antineoplastic activity from Xime-

nia americana. The FASEB Journal, 20(8), 1194-1196 (2006).

http://www.fasebj.org/cgi/doi/10.1096/fj.05–5231fje

H Bayer, N Ey, A Wattenberg, C Voss, MR Berger. Purification

and characterization of riproximin from Ximenia americana fruit

kernels. Protein Expr. Purif., 82(1), 97-105 (2012). https://doi.

org/10.1016/j.pep.2011.11.018

MR Hartley, JM Lo+rd. Cytotoxic ribosome-inactivating lectins

from plants. Biochim. Biophys. Acta, 1701(1-2), 1–14 (2004).

https://doi.org/10.1016/j.bbapap.2004.06.004

LM Roberts, JM Lord. Ribosome-inactivating proteins: entry into

mammalian cells and intracellular routing. Mini Rev. Med.

Chem., 4(5), 505-512 (2004). https://doi.org/10.2174/13895570

LF Reyes. Proteínas inativadoras de ribossomos: identificação de

novas proteínas e estudos de interação da cadeia-A da pulchellina

(PAC) com monocamada de Langmuir. (Tese de doutorado). São

Carlos, Instituto de Física de São Carlos. Universidade de São

Paulo, 34 p. (2011). https://doi.org/10.11606/T.76.2011.tde-

-114447

M Zeng, M Zheng, D Lu, J Wang, W Jiang, O Sha. Anti-tumor

activities and apoptotic mechanism of ribosome-inactivating pro-

teins. Chin. J. Cancer, 34(3), 1-10 (2015). https://doi.org/10.

/s40880-015-0030-x

H Adwan. Riproximin Is A New Plat Lectin With Antineoplastic

Activity Aganist In Rat Pancreatic Cancer. Qatar Found. Annual

Res. Forum, 1, 126 (2013). https://doi.org/10.5339/qfarf.2013.BIOP-0126

H Nie, X Liu, Y Zhang, T Li, C Zhan, W Huo, Y Li. Specific N-

glycans of hepatocellular carcinoma cell surface and the abnormal

increase of core-α-1, 6-fucosylated triantennary glycan via N-

acetylglucosaminyltransferases-IVa regulation. Sci. Rep., 5(1),

(2015). https://doi.org/10.1038/srep16007

S Bharadwaj, SS Rathore, PC Ghosh. Enhancement of the cyto-

toxicity of liposomal ricin by the carboxylic ionophore monensin

and the lysosomotropic amine NH4Cl in Chinese hamster ovary

cells. Int. J. Toxicol., 25(5), 49-59 (2006). https://doi.org/10.

/10915810600846195

IE Herawati, R Lesmana, J Levita, A Subarnas. Cytotoxicity,

apoptosis, migration inhibition, and autophagy-induced by crude

ricin from Ricinus communis seeds in A549 lung cancer cell lines.

Med. Sci. Monit. Basic Res., 28, e936683 (2022). https://doi.org/

12659/MSMBR.936683

L Citores, R Munoz, MA Rojo, P Jimenez, JM Ferreras, T Girbes.

Evidence for distinct cellular internalization pathways of ricin and

nigrin b. Cell. Mol. Biol., 49, OL461–465 (2003).




Depósito Legal: PPI200602ME2232
ISSN: 1856-5301

Creative Commons License
Todos los documentos publicados en esta revista se distribuyen bajo una
Licencia Creative Commons Atribución -No Comercial- Compartir Igual 4.0 Internacional.
Por lo que el envío, procesamiento y publicación de artículos en la revista es totalmente gratuito.