Wed, Oct 14, 2026
Volume 20, Issue 3 (May-Jun 2026)
mljgoums 2026, 20(3): 15-17 |
Back to browse issues page
Download citation:
BibTeX | RIS | EndNote | Medlars | ProCite | Reference Manager | RefWorks
Send citation to:
BibTeX | RIS | EndNote | Medlars | ProCite | Reference Manager | RefWorks
Send citation to:
Samadian E, Golalipour A, Vakili M, Mohammed H, Rashidbaghan A. Effect of urtica dioica agglutinin on breast cancer cell growth. mljgoums 2026; 20 (3) :15-17
URL: http://mlj.goums.ac.ir/article-1-1952-en.html
URL: http://mlj.goums.ac.ir/article-1-1952-en.html
1- Laboratory Sciences Research Center, Golestan University of Medical Sciences, Gorgan, Iran
2- Department of Pathobiology, School of Veterinary Medicine, Shiraz University, Shiraz, Iran
3- Health Management and Social Development Research Center, Golestan University of Medical Sciences, Gorgan, Iran; Department of Biostatistics and Epidemiology, Faculty of Health, Golestan University of Medical Sciences, Gorgan, Iran
4- Laboratory Sciences Research Center, Golestan University of Medical Sciences, Gorgan, Iran; Laboratories of Imam Al-Sadiq Hospital, Ministry of Health, Babylon Governorate, Iraq
5- Neonatal and Children’s Health Research Center, Taleghani Hospital, Janbazan Boulevard, Gorgan, Iran ,rashidbaghan@yahoo.com
2- Department of Pathobiology, School of Veterinary Medicine, Shiraz University, Shiraz, Iran
3- Health Management and Social Development Research Center, Golestan University of Medical Sciences, Gorgan, Iran; Department of Biostatistics and Epidemiology, Faculty of Health, Golestan University of Medical Sciences, Gorgan, Iran
4- Laboratory Sciences Research Center, Golestan University of Medical Sciences, Gorgan, Iran; Laboratories of Imam Al-Sadiq Hospital, Ministry of Health, Babylon Governorate, Iraq
5- Neonatal and Children’s Health Research Center, Taleghani Hospital, Janbazan Boulevard, Gorgan, Iran ,
Full-Text [PDF 450 kb]
(2217 Downloads)
| Abstract (HTML) (11595 Views)
Discussion
Here, we investigated the cytotoxic effect of UDA on the breast cancer cell line MCF-7. UDA significantly inhibited MCF-7 cell growth in a dose- and time-dependent manner (P < 0.01 at 24 hours and P < 0.0001 at 48 hours). The highest proliferation inhibition occurred at 240 µg/mL over 48 hours, with less than 50% inhibition. However, a much weaker effect was observed in nontumorigenic human mammary MCF-10A and normal HEK-293 cells.
As reported in previous studies, several lectins have shown anti-breast cancer activity (20-22). Valentiner et al., 2003, examined six lectins - Helix pomatia agglutinin (HPA), soybean agglutinin (SBA), peanut agglutinin (PNA), Solanum tuberosum agglutinin (STA), wheat germ agglutinin (WGA), and phytohemagglutinin (PHA-L) - on MCF-7 and other breast cancer cell lines. Three lectins inhibited MCF-7 growth during a 24-hour incubation. WGA exhibited the strongest effect, reducing cell growth with an IC50 of 70 µg/mL. At 200 µg/mL, viable cells decreased to 28%. PHA-L showed moderate dose-dependent inhibition, reducing viability to 58% at 200 µg/mL. SBA had the weakest effect, with viable cells decreasing to 77% at the same concentration (14). The inhibitory effect of UDA was most similar to that of SBA, as UDA achieved comparable inhibition at 240 µg/mL over 24 hours.
Deepa et al., 2012, demonstrated that mulberry leaf lectin (MLL) induced strong growth inhibition in MCF-7 cells after 24 hours (IC50: 8.5 µg/mL). Cell cycle analysis revealed 41% of cells in the sub-G1 phase, indicating apoptosis (21). Similarly, Savanur et al. (2014) reported that Sclerotium rolfsii lectin (SRL) significantly inhibited MCF-7 cells. Treatment with 20 µg/mL and 40 µg/mL SRL reduced viability to 50% and 39%, respectively, over 48 hours. Cell cycle analysis showed 33% of treated cells in the sub-G1 phase (indicative of apoptosis) (22). Although both MLL and SRL exhibited stronger inhibitory effects than UDA, further experiments are needed to confirm whether UDA induces apoptosis. If confirmed, the inhibitory effect of UDA could hold significant value in breast cancer treatment.
The proliferation rates of HEK-293 and MCF-10A cells treated with UDA remained approximately 70% and > 90%, respectively, at 240 µg/mL over 48 hours. In contrast, MCF-10A cells treated with SRL retained > 70% viability at a lower concentration (40 µg/mL) over the same period (22). These results suggest that UDA has fewer side effects than SRL, making it a safer candidate for therapeutic applications.
Conclusion
UDA selectively inhibits breast cancer cell proliferation with minimal impact on normal cells, supporting its potential as an anticancer agent. Future research should focus on elucidating its mechanism of action and evaluating its synergistic effects with conventional therapies.
Acknowledgement
We would like to thank all our colleagues at Golestan University of Medical Sciences who helped us with the laboratory work of this research.
Funding Sources
Not applicable.
Ethical Statement
This study was conducted under the ethics approval code issued by Golestan University of Medical Sciences (ID: IR.GOUMS.REC.1400.422).
Conflicts of Interest
There is no conflict of interest to be declared by the authors.
Author Contributions
All the authors made substantial, direct, and intellectual contributions to the work and read and approved the final manuscript.
Data Availability Statement
Data supporting the findings of this study are available from the corresponding author upon reasonable request.
Use of Artificial Intelligence
AI (DeepSeek) was used in part only to prepare the abstract and assist with translation.
Full-Text: (635 Views)
Introduction
Breast cancer is the most prevalent malignancy in women, accounting for 11.7% of all global cancer cases (1). It remains a leading cause of mortality among women, with projections estimating over 1 million annual deaths by 2040 (2). In Iran, breast cancer represents approximately 28.1% of female cancers, with incidence rates expected to rise by 63% by 2025 compared with 2016 (3,4).
Conventional therapies, including surgery, chemotherapy, and immunotherapy, face challenges such as therapy resistance and adverse side effects (5,6). Consequently, natural products, particularly herbal medicines, have gained attention for their potential to target therapy-resistant cancer stem cells (CSCs) and reduce side effects (7).
Urtica dioica (Stinging nettle) is a perennial plant with antiproliferative and antioxidant properties in different cancers (8). Previous studies have reported that its aqueous extract inhibits MCF-7 cell growth and induces apoptosis (9,10). Urtica dioica agglutinin (UDA), a lectin isolated from nettle rhizomes, has been shown to inhibit benign prostatic hyperplasia (BPH) cell proliferation (11). Lectins are carbohydrate-binding proteins with specific characteristics, such as cell agglutination, apoptosis induction, and inhibition of angiogenesis (12). Cytotoxic effects of UDA have been reported in leukemia cell lines, including Jurkat (An acute lymphoblastic leukemia cell line) (13) and HL-60 (A myeloid leukemia cell line), through marked apoptosis induction (14). This study evaluates UDA cytotoxicity against MCF-7 cells while assessing its safety in normal MCF-10A and HEK-293 cells.
Methods
Purification of UDA and agglutination assay
Stinging nettles were harvested from Tonekabon, Iran, during winter and authenticated in the herbarium of Golestan Agricultural and Natural Resources Research and Education Center (Herbarium number: 2541). Rhizomes were washed, cut into small pieces, and used immediately or stored at -20 ºC. UDA was purified by affinity chromatography on a chitin column following established protocols (15). Briefly, after homogenizing rhizomes in 0.1% HCl, extraction was carried out in several stages. Total UDA was purified from Urtica dioica extract by affinity chromatography on a chitin column equilibrated with acetate buffer. After passage of the extract, unbound proteins were washed off with 1 M NaCl. Finally, the lectin was desorbed with 0.5 N acetic acid. The lyophilized UDA was dialyzed against phosphate-buffered saline (PBS). The concentration of UDA was determined using the lectin-specific absorption method (16). Purity was confirmed by SDS-PAGE (8.5 - 9.5 kDa), and agglutination activity was tested using trypsin-treated human erythrocytes (17,18).
Cell culture
The cell lines MCF-7 (human breast cancer cell line), MCF-10A (Human normal breast epithelial cell line), and HEK-293 (Human embryonic kidney cells) were purchased from the Pasteur Institute (Tehran, Iran). The cells were cultured in RPMI-1640 medium (Gibco, USA, Cat. No. 11875093) supplemented with 10% heat-inactivated fetal bovine serum (FBS) (Gibco, USA, Cat. No. A25904DG) and penicillin-streptomycin (Gibco, USA, Cat. No. 15140122).
MTT assay
Cell growth inhibition was measured using the 3-(4, 5-dimethylthiazol-2-yl)-2, 5-diphenyl-tetrazolium bromide (MTT) assay. Cells (1 × 10⁴ cells/well) were treated with UDA (7.5 - 480 µg/mL) for 24 and 48 hours at 37 ºC. Untreated cells served as the negative control. After incubation, 20 μL of MTT solution (5 mg/mL in PBS) (Sigma, USA, A101161) was added to each well, and the cells were incubated at 37 ºC for 4 hours. After DMSO was added to the wells to dissolve the formazan crystals, absorbance was measured at 570 nm. The experiment was performed three times. Cell viability (%) was calculated as (19):
Results
UDA purification
Purified UDA showed agglutination activity at 20 µg/mL and a single band (8.5 - 9.5 kDa) on SDS-PAGE.
Proliferation inhibition by UDA treatment
UDA inhibited MCF-7 proliferation in a dose- and time-dependent manner, with viability dropping below 50% at 240 µg/mL (48 hours) (P < 0.0001). HEK-293 cells exhibited less than 30% toxicity at 480 µg/mL, while MCF-10A viability remained unaffected (Figure 1).
Breast cancer is the most prevalent malignancy in women, accounting for 11.7% of all global cancer cases (1). It remains a leading cause of mortality among women, with projections estimating over 1 million annual deaths by 2040 (2). In Iran, breast cancer represents approximately 28.1% of female cancers, with incidence rates expected to rise by 63% by 2025 compared with 2016 (3,4).
Conventional therapies, including surgery, chemotherapy, and immunotherapy, face challenges such as therapy resistance and adverse side effects (5,6). Consequently, natural products, particularly herbal medicines, have gained attention for their potential to target therapy-resistant cancer stem cells (CSCs) and reduce side effects (7).
Urtica dioica (Stinging nettle) is a perennial plant with antiproliferative and antioxidant properties in different cancers (8). Previous studies have reported that its aqueous extract inhibits MCF-7 cell growth and induces apoptosis (9,10). Urtica dioica agglutinin (UDA), a lectin isolated from nettle rhizomes, has been shown to inhibit benign prostatic hyperplasia (BPH) cell proliferation (11). Lectins are carbohydrate-binding proteins with specific characteristics, such as cell agglutination, apoptosis induction, and inhibition of angiogenesis (12). Cytotoxic effects of UDA have been reported in leukemia cell lines, including Jurkat (An acute lymphoblastic leukemia cell line) (13) and HL-60 (A myeloid leukemia cell line), through marked apoptosis induction (14). This study evaluates UDA cytotoxicity against MCF-7 cells while assessing its safety in normal MCF-10A and HEK-293 cells.
Methods
Purification of UDA and agglutination assay
Stinging nettles were harvested from Tonekabon, Iran, during winter and authenticated in the herbarium of Golestan Agricultural and Natural Resources Research and Education Center (Herbarium number: 2541). Rhizomes were washed, cut into small pieces, and used immediately or stored at -20 ºC. UDA was purified by affinity chromatography on a chitin column following established protocols (15). Briefly, after homogenizing rhizomes in 0.1% HCl, extraction was carried out in several stages. Total UDA was purified from Urtica dioica extract by affinity chromatography on a chitin column equilibrated with acetate buffer. After passage of the extract, unbound proteins were washed off with 1 M NaCl. Finally, the lectin was desorbed with 0.5 N acetic acid. The lyophilized UDA was dialyzed against phosphate-buffered saline (PBS). The concentration of UDA was determined using the lectin-specific absorption method (16). Purity was confirmed by SDS-PAGE (8.5 - 9.5 kDa), and agglutination activity was tested using trypsin-treated human erythrocytes (17,18).
Cell culture
The cell lines MCF-7 (human breast cancer cell line), MCF-10A (Human normal breast epithelial cell line), and HEK-293 (Human embryonic kidney cells) were purchased from the Pasteur Institute (Tehran, Iran). The cells were cultured in RPMI-1640 medium (Gibco, USA, Cat. No. 11875093) supplemented with 10% heat-inactivated fetal bovine serum (FBS) (Gibco, USA, Cat. No. A25904DG) and penicillin-streptomycin (Gibco, USA, Cat. No. 15140122).
MTT assay
Cell growth inhibition was measured using the 3-(4, 5-dimethylthiazol-2-yl)-2, 5-diphenyl-tetrazolium bromide (MTT) assay. Cells (1 × 10⁴ cells/well) were treated with UDA (7.5 - 480 µg/mL) for 24 and 48 hours at 37 ºC. Untreated cells served as the negative control. After incubation, 20 μL of MTT solution (5 mg/mL in PBS) (Sigma, USA, A101161) was added to each well, and the cells were incubated at 37 ºC for 4 hours. After DMSO was added to the wells to dissolve the formazan crystals, absorbance was measured at 570 nm. The experiment was performed three times. Cell viability (%) was calculated as (19):
Results
UDA purification
Purified UDA showed agglutination activity at 20 µg/mL and a single band (8.5 - 9.5 kDa) on SDS-PAGE.
Proliferation inhibition by UDA treatment
UDA inhibited MCF-7 proliferation in a dose- and time-dependent manner, with viability dropping below 50% at 240 µg/mL (48 hours) (P < 0.0001). HEK-293 cells exhibited less than 30% toxicity at 480 µg/mL, while MCF-10A viability remained unaffected (Figure 1).
.PNG) Figure 1. UDA inhibits the proliferation of MCF-7. Cell viability of (A) MCF-7, (B) MCF-10A, and (C) HEK-293 cells measured by MTT assay after 24- and 48-hour UDA treatment with different doses (15 - 240 µg/mL for MCF-7 cells and 7.5 - 480 µg/mL for MCF-10A and HEK-293 cells). Data represent mean ± SEM of three experiments. **P < 0.01, ****P < 0.0001. |
Discussion
Here, we investigated the cytotoxic effect of UDA on the breast cancer cell line MCF-7. UDA significantly inhibited MCF-7 cell growth in a dose- and time-dependent manner (P < 0.01 at 24 hours and P < 0.0001 at 48 hours). The highest proliferation inhibition occurred at 240 µg/mL over 48 hours, with less than 50% inhibition. However, a much weaker effect was observed in nontumorigenic human mammary MCF-10A and normal HEK-293 cells.
As reported in previous studies, several lectins have shown anti-breast cancer activity (20-22). Valentiner et al., 2003, examined six lectins - Helix pomatia agglutinin (HPA), soybean agglutinin (SBA), peanut agglutinin (PNA), Solanum tuberosum agglutinin (STA), wheat germ agglutinin (WGA), and phytohemagglutinin (PHA-L) - on MCF-7 and other breast cancer cell lines. Three lectins inhibited MCF-7 growth during a 24-hour incubation. WGA exhibited the strongest effect, reducing cell growth with an IC50 of 70 µg/mL. At 200 µg/mL, viable cells decreased to 28%. PHA-L showed moderate dose-dependent inhibition, reducing viability to 58% at 200 µg/mL. SBA had the weakest effect, with viable cells decreasing to 77% at the same concentration (14). The inhibitory effect of UDA was most similar to that of SBA, as UDA achieved comparable inhibition at 240 µg/mL over 24 hours.
Deepa et al., 2012, demonstrated that mulberry leaf lectin (MLL) induced strong growth inhibition in MCF-7 cells after 24 hours (IC50: 8.5 µg/mL). Cell cycle analysis revealed 41% of cells in the sub-G1 phase, indicating apoptosis (21). Similarly, Savanur et al. (2014) reported that Sclerotium rolfsii lectin (SRL) significantly inhibited MCF-7 cells. Treatment with 20 µg/mL and 40 µg/mL SRL reduced viability to 50% and 39%, respectively, over 48 hours. Cell cycle analysis showed 33% of treated cells in the sub-G1 phase (indicative of apoptosis) (22). Although both MLL and SRL exhibited stronger inhibitory effects than UDA, further experiments are needed to confirm whether UDA induces apoptosis. If confirmed, the inhibitory effect of UDA could hold significant value in breast cancer treatment.
The proliferation rates of HEK-293 and MCF-10A cells treated with UDA remained approximately 70% and > 90%, respectively, at 240 µg/mL over 48 hours. In contrast, MCF-10A cells treated with SRL retained > 70% viability at a lower concentration (40 µg/mL) over the same period (22). These results suggest that UDA has fewer side effects than SRL, making it a safer candidate for therapeutic applications.
Conclusion
UDA selectively inhibits breast cancer cell proliferation with minimal impact on normal cells, supporting its potential as an anticancer agent. Future research should focus on elucidating its mechanism of action and evaluating its synergistic effects with conventional therapies.
Acknowledgement
We would like to thank all our colleagues at Golestan University of Medical Sciences who helped us with the laboratory work of this research.
Funding Sources
Not applicable.
Ethical Statement
This study was conducted under the ethics approval code issued by Golestan University of Medical Sciences (ID: IR.GOUMS.REC.1400.422).
Conflicts of Interest
There is no conflict of interest to be declared by the authors.
Author Contributions
All the authors made substantial, direct, and intellectual contributions to the work and read and approved the final manuscript.
Data Availability Statement
Data supporting the findings of this study are available from the corresponding author upon reasonable request.
Use of Artificial Intelligence
AI (DeepSeek) was used in part only to prepare the abstract and assist with translation.
Research Article: Research Article |
Subject:
Molecular Medicine
Received: 2025/06/2 | Accepted: 2025/12/10 | Published: 2026/06/19 | ePublished: 2026/06/19
Received: 2025/06/2 | Accepted: 2025/12/10 | Published: 2026/06/19 | ePublished: 2026/06/19
References
1. Zhang J, Wu Y, Li Y, Li S, Liu J, Yang X, et al. Natural products and derivatives for breast cancer treatment: From drug discovery to molecular mechanism. Phytomedicine. 2024;129:155600. [View at Publisher] [DOI] [PMID] [Google Scholar]
2. Arnold M, Morgan E, Rumgay H, Mafra A, Singh D, Laversanne M, et al. Current and future burden of breast cancer: global statistics for 2020 and 2040. Breast. 2022;66:15-23. [View at Publisher] [DOI] [PMID] [Google Scholar]
3. Aryannejad A, Saeedi Moghaddam S, Mashinchi B, Tabary M, Rezaei N, Shahin S, et al. Correction to: National and subnational burden of female and male breast cancer and risk factors in Iran from 1990 to 2019: results from the Global Burden of Disease study 2019. Breast Cancer Res. 2023;25(1):70. [View at Publisher] [DOI] [PMID] [Google Scholar]
4. Soleimani M, Ayyoubzadeh SM, Jalilvand A, Ghazisaeedi M. Exploring the geospatial epidemiology of breast cancer in Iran: identifying significant risk factors and spatial patterns for evidence-based prevention strategies. BMC cancer. 2023;23(1):1219. [View at Publisher] [DOI] [PMID] [Google Scholar]
5. Wang J, Wu SG. Breast cancer: an overview of current therapeutic strategies, challenge, and perspectives. Breast Cancer (Dove Med Press). 2023;15:721-30. [View at Publisher] [DOI] [PMID] [Google Scholar]
6. Shareef M, Ashraf MA, Sarfraz M. Natural cures for breast cancer treatment. Saudi Pharm J. 2016;24(3):233-40. [View at Publisher] [DOI] [PMID] [Google Scholar]
7. Bozorgi A, Khazaei S, Khademi A, Khazaei M. Natural and herbal compounds targeting breast cancer, a review based on cancer stem cells. Iran J Basic Med Sci. 2020;23(8):970. [View at Publisher] [DOI] [PMID] [Google Scholar]
8. Karakol P, Saraydin SU, Bozkurt M, Hepokur C, Inan ZD, Turan M. Anticancer effects of Urtica dioica in breast cancer. Asian Pac J Cancer Prev. 2022;23(2):673-81. [View at Publisher] [DOI] [PMID] [Google Scholar]
9. Fattahi S, Ardekani AM, Zabihi E, Abedian Z, Mostafazadeh A, Pourbagher R, et al. Antioxidant and apoptotic effects of an aqueous extract of Urtica dioica on the MCF-7 human breast cancer cell line. Asian Pac J Cancer Prev. 2013;14(9):5317-23. [View at Publisher] [DOI] [PMID] [Google Scholar]
10. Mohammadi A, Mansoori B, Baradaran PC, Khaze V, Aghapour M, Farhadi M, et al. Urtica dioica extract inhibits proliferation and induces apoptosis and related gene expression of breast cancer cells in vitro and in vivo. Clin Breast Cancer. 2017;17(6):463-70. [View at Publisher] [DOI] [PMID] [Google Scholar]
11. Rashidbaghan A, Mostafaie A, Yazdani Y, Mansouri K. Urtica dioica agglutinin (a plant lectin) has a caspase-dependent apoptosis induction effect on the acute lymphoblastic leukemia cell line. Mol Cell Biol. 2020;66(6):121-6. [View at Publisher] [DOI] [PMID] [Google Scholar]
12. Wagner H, Geiger WN, Boos G, Samtleben R. Studies on the binding of Urtica dioica agglutinin (UDA) and other lectins in an in vitro epidermal growth factor receptor test. Phytomedicine. 1995;1(4):287-90. [View at Publisher] [DOI] [PMID] [Google Scholar]
13. Mejía EGD, Prisecaru VI. Lectins as bioactive plant proteins: a potential in cancer treatment. Crit Rev Food Sci Nutr. 2005;45(6):425-45. [View at Publisher] [DOI] [PMID] [Google Scholar]
14. Valentiner U, Fabian S, Schumacher U, Leathem AJ. The influence of dietary lectins on the cell proliferation of human breast cancer cell lines in vitro. Anticancer Res. 2003;23(2B):1197-206. [View at Publisher] [PMID] [Google Scholar]
15. Rashidbaghan A, Mostafaie A, Yazdani Y, Mansouri K. The agglutinin of common nettle (Urtica dioica L.) plant effects on gene expression related to apoptosis of human acute myeloid leukemia cell line. Biochem Genet. 2021;59(4):1049-64. [View at Publisher] [DOI] [PMID] [Google Scholar]
16. Peumans WJ, Ley MD, Broekaert WF. An unusual lectin from stinging nettle (Urtica dioica) rhizomes. FEBS Lett. 1984;177(1):99-103. [View at Publisher] [DOI] [Google Scholar]
17. Katiyar S, Van Damme EJ, Peumans WJ, Surolia A. Thermodynamic analysis of chitooligosaccharide binding to Urtica dioica agglutinin by isothermal titration calorimetry. Biosci Rep. 1999;19(5):411-9. [View at Publisher] [DOI] [PMID] [Google Scholar]
18. Liener IEt. The photometric determination of the haemagglutination activity of soyin and crude soybean extracts. Arch Biochem Biologys. 1955;54(1):223-31. [View at Publisher] [DOI] [PMID] [Google Scholar]
19. Kaul R, Read J, Mattiasson B. Screening for plant lectins by latex agglutination tests. Phytochemistry. 1991;30(12):4005-4009. [View at Publisher] [DOI] [Google Scholar]
20. Looi CY, Arya A, Cheah FK, Muharram B, Leong KH, Mohamad Kh, et al. Induction of apoptosis in human breast cancer cells via caspase pathway by vernodalin isolated from Centratherum anthelminticum (L.) seeds. PLOS ONE. 2013;8(2):e56643. [View at Publisher] [DOI] [PMID] [Google Scholar]
21. Deepa M, Sureshkumar T, Satheeshkumar PK, Priya S. Purified mulberry leaf lectin (MLL) induces apoptosis and cell cycle arrest in human breast cancer and colon cancer cells. Chem Biol Interact. 2012;200(1):38-44. [View at Publisher] [DOI] [PMID] [Google Scholar]
22. Savanur MA, Eligar SM, Pujari R, Chen C, Mahajan P, Borges A, et al. Sclerotium rolfsii lectin induces stronger inhibition of proliferation in human breast cancer cells than normal human mammary epithelial cells by induction of cell apoptosis. PloS ONE. 2014;9(11):e110107. [View at Publisher] [DOI] [PMID] [Google Scholar]
Send email to the article author
| Rights and permissions | |
 |
This work is licensed under a Creative Commons Attribution-NonCommercial 4.0 International License. |
This work is licensed under a Creative Commons Attribution-NonCommercial 4.0 International License.
Contact us
Tel & Fax: (+98) 17-32450093
E-mail:
goums.ac.ir
yahoo.com