Purification of hyaluronidase as an anticancer agent inhibiting CD44

被引:10
作者
Shakouri, Amir [1 ]
Parvan, Reza [2 ]
Adljouy, Nasim [2 ]
Abdolalizadeh, Jalal [3 ,4 ]
机构
[1] Tabriz Univ Med Sci, Drug Appl Res Ctr, Tabriz, Iran
[2] Tabriz Univ Med Sci, Biotechnol Res Ctr, Tabriz, Iran
[3] Tabriz Univ Med Sci, Immunol Res Ctr, Tabriz, Iran
[4] Tabriz Univ Med Sci, Paramed Fac, Tabriz, Iran
关键词
hyaluronic acid; hyaluronidase; anticancer; CD44; RECOMBINANT HUMAN HYALURONIDASE; VENOM HYALURONIDASE; ACID; OLIGOSACCHARIDES; CHEMOTHERAPY; EXPRESSION; CARCINOMA; COMPLEX; BINDING; GROWTH;
D O I
10.1002/bmc.4709
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Hyaluronidase (Hyal) can be employed to accomplish a diversity of complications related to hyaluronic acid (HA). Hyal contains some classes of catalysts that cleave HA. This enzyme is detected in several human tissues as well as in animal venoms, pathogenic organisms and cancers. Destructive cancer cells regularly increase the CD44 receptor existing in a cell membrane. This receptor acts as an exact receptor for HA, and HA is recognized to motivate the migration, spread, attack and metastasis of cancer cells. Nearly all of the methods used to purify Hyal are highly costly and not proper for industrial applications. This survey aims to review different methods of Hyal purification, which acts as an anticancer agent by degrading HA in tissues and thus inhibiting the CD44-HA interaction. Hyal can be successfully employed in the management of cancer, which is associated with HA-CD44. This review has described different methods for Hyal purification to prepare an origin to develop a novel purification technique for this highly appreciated protein. Using multiple columns is not applicable for the purification of Hyal and thus cannot be used at the industrial level. It is better to use affinity chromatography of anti-Hyal for Hyal with one-step purification.
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页数:9
相关论文
共 69 条
[1]   Affinity Purification of Tumor Necrosis Factor-alpha Expressed in Raji Cells by Produced scFv Antibody Coupled CNBr-Activated Sepharose [J].
Abdolalizadeh, Jalal ;
Zolbanin, Jafar Majidi ;
Nouri, Mohammad ;
Baradaran, Behzad ;
Movassaghpour, AliAkbar ;
Farajnia, Safar ;
Omidi, Yadollah .
ADVANCED PHARMACEUTICAL BULLETIN, 2013, 3 (01) :19-23
[2]  
[Anonymous], 2014, PLOS ONE
[3]  
Bansal Jyoti, 2010, Indian J Dent Res, V21, P575, DOI 10.4103/0970-9290.74232
[4]   Isolation and purification of bovine testicular hyaluronidase [J].
Barsukov, AK ;
Kozhevnikova, OV ;
Khokhryakova, AV .
APPLIED BIOCHEMISTRY AND MICROBIOLOGY, 2003, 39 (06) :549-552
[5]  
Baumgartner G, 1998, CANCER LETT, V131, P1
[6]   Hyaluronan Synthase 2 (HAS2) Promotes Breast Cancer Cell Invasion by Suppression of Tissue Metalloproteinase Inhibitor 1 (TIMP-1) [J].
Bernert, Berit ;
Porsch, Helena ;
Heldin, Paraskevi .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2011, 286 (49) :42349-42359
[7]   Tumour tissue transport after intraperitoneal anticancer drug delivery [J].
Carlier, Charlotte ;
Mathys, Ada ;
De Jaeghere, Emiel ;
Steuperaert, Margo ;
De Wever, Olivier ;
Ceelen, Wim .
INTERNATIONAL JOURNAL OF HYPERTHERMIA, 2017, 33 (05) :534-542
[8]  
Cohen BE., 2015, J Clin Investigat Dermatol, V3, P7
[9]   Hyaluronidase-triggered anticancer drug and siRNA delivery from cascaded targeting nanoparticles for drug-resistant breast cancer therapy [J].
Ding, Jie ;
Liang, Tingxizi ;
Zhou, Ying ;
He, Zhiwei ;
Min, Qianhao ;
Jiang, Liping ;
Zhu, Junjie .
NANO RESEARCH, 2017, 10 (02) :690-703
[10]   Urinary retinoic acid receptor-β2 gene promoter methylation and hyaluronidase activity as noninvasive tests for diagnosis of bladder cancer [J].
Eissa, Sanaa ;
Zohny, Samir F. ;
Shehata, Hanan Hussien ;
Hegazy, Marwa G. A. ;
Salem, Ahmed M. ;
Esmat, Mohamed .
CLINICAL BIOCHEMISTRY, 2012, 45 (06) :402-407