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Last update 23 Jan 2025

ITGA3

Last update 23 Jan 2025

Basic Info

Synonyms

alpha 3 subunit of VLA-3 receptor, antigen CD49C, antigen identified by monoclonal antibody J143

+ [16]

Introduction

Integrin alpha-3/beta-1 is a receptor for fibronectin, laminin, collagen, epiligrin, thrombospondin and CSPG4. Integrin alpha-3/beta-1 provides a docking site for FAP (seprase) at invadopodia plasma membranes in a collagen-dependent manner and hence may participate in the adhesion, formation of invadopodia and matrix degradation processes, promoting cell invasion. Alpha-3/beta-1 may mediate with LGALS3 the stimulation by CSPG4 of endothelial cells migration. (Microbial infection) Integrin ITGA3:ITGB1 may act as a receptor for R.delemar CotH7 in alveolar epithelial cells, which may be an early step in pulmonary mucormycosis disease progression.

Drugs associated with ITGA3

Probody drug conjugates targeting ITGA3(CytomX)

Target

ITGA3

Mechanism

ITGA3 inhibitors

Active Org.-

Originator Org.

CytomX Therapeutics, Inc.

Active Indication-

Inactive Indication

Neoplasms

Drug Highest PhasePending

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

100 Clinical Results associated with ITGA3

100 Translational Medicine associated with ITGA3

0 Patents (Medical) associated with ITGA3

1,222

Literatures (Medical) associated with ITGA3

01 Mar 2025·Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease

Knockdown of LAMA3 enhances the sensitivity of colon cancer to oxaliplatin by regulating the Hippo-YAP pathway

Article

Author: Bu, Junguo ; Zou, Yujiao ; Li, Jiqiang ; Zeng, Rong ; Yu, Yahui

BACKGROUNDOxaliplatin is the first-line chemotherapy for patients with colon cancer (CC). However, its resistance limits its therapeutic efficacy.METHODSOxaliplatin resistance-associated differentially expressed genes (DEGs) in the GSE42387 and GSE227315 datasets were identified through bioinformatics methods. Functional experiments were conducted both in vitro and in vivo to evaluate the roles of laminin subunit alpha 3 (LAMA3) in drug resistance and tumorigenesis. The downstream molecular mechanisms were explored using Kyoto Encyclopedia of Genes and Genomes (KEGG) pathway enrichment analysis and western blot.RESULTSSix hub genes associated with oxaliplatin resistance were identified, including LAMB3, ITGA3, COL4A6, COL12A1, LAMA3, and LAMC2, all of which were highly expressed in oxaliplatin-resistant CC cell lines. LAMA3 knockdown sensitized CC cells to oxaliplatin treatment, resulting in further inhibition of proliferation, migration, and invasion, as well as an increase in apoptosis in CC cells. Additionally, LAMA3 knockdown promoted the therapeutic efficacy of oxaliplatin in the CC xenograft tumor models. Mechanistically, overexpression of YAP notably counteracted the enhanced sensitivity to oxaliplatin caused by LAMA3 knockdown, indicating that LAMA3 modulates oxaliplatin sensitivity in CC through the Hippo-YAP pathway.CONCLUSIONLAMA3 knockdown promotes CC sensitivity to oxaliplatin via modulating the Hippo-YAP pathway, providing new therapeutic targets for the CC treatment.

15 Jan 2025·Bioconjugate Chemistry

Peptide Nanocarriers for Targeted Delivery of Nucleic Acids for Cancer Therapy

Article

Author: Li, Zigang ; Xing, Yun ; Li, Xi ; Li, Xinyu ; Zhang, Yaping ; Wang, Dongyuan ; Song, Chunli ; Zhang, Lixiang ; Sha, Xinrui ; Jiang, Leying ; Yin, Feng ; Jiao, Zijun ; Yao, Zhiyong

Peptides have been extensively studied in nanomedicine with great bioactivity and biocompatibility; however, their poor cell-membrane-penetrating properties and nonselectivity greatly limit their clinical applications. In this study, tumor-targeting therapy was achieved by modifying our previously developed efficient peptide vector with the cancer-targeting peptide RGD, enabling it to specifically target tumor cells with a high expression of RGD-binding receptors. B-cell lymphoma-2 antisense oligonucleotides were selected as the target model to validate the effectiveness of the delivery carriers. Results demonstrated that this delivery system can be efficiently and selectively taken up by RGD receptor-positive cells (α_vβ₃ integrin receptor), further inducing effective target gene knockdown. Overall, this system provided a promising strategy for the targeted delivery of nucleic acid drugs.

01 Jan 2025·The Journal of Pathology

Podocyte YAP ablation decreases podocyte adhesion and exacerbates FSGS progression through α3β1 integrin

Article

Author: Zheng, Zhihuang ; Hu, Chencheng ; Xu, Jitu ; Wu, Huijuan ; Xu, Yanyong ; Meng, Shenghao ; Zhao, Zhonghua ; Zhong, Jiayan ; Zhang, Luming ; Zhu, Siqi ; Zhang, Zhigang ; Xu, Xitong ; Liu, Jun ; Jia, Wenyao ; Shao, Guangze ; Gu, Yue

AbstractSevere proteinuria in focal segmental glomerulosclerosis (FSGS) is closely associated with decreased adhesion, and subsequent loss, of podocytes. Yes‐associated protein (YAP) is a key transcriptional coactivator that plays a significant role in maintaining cellular homeostasis. However, its role in podocyte adhesion and its specific mechanism in FSGS progression remain unclear. In this study, an adriamycin (ADR)‐induced FSGS model was established using podocyte‐specific Yap knockout (KO) mice and control mice. These mice were further treated with Pyrintegrin, an agonist of α3β1 integrin, or a vehicle. Additionally, an ADR‐induced FSGS model was constructed using podocyte‐specific Itga3 KO mice, which were subsequently treated with 1‐oleoyl lysophosphatidic acid (LPA), a YAP activator, or a vehicle. Our findings demonstrated that YAP was positively correlated with podocyte adhesion. Podocyte‐specific Yap KO mice exhibited reduced levels of α3β1 integrin and podocyte adhesion. Yap KO aggravated the ADR‐induced reduction in α3β1 integrin and podocyte adhesion, resulting in significantly increased segmental or global glomerulosclerosis and proteinuria. Notably, treatment with a β1 integrin agonist partially ameliorated the decrease of podocyte adhesion and the worsening FSGS progression caused by Yap KO. Mechanistically, YAP was found to transcriptionally regulate α3‐ and β1 integrin via transcriptional enhanced associate domain 3 (TEAD3), with TEAD3 binding to the promoter region of Itga3. Furthermore, Itga3 KO or knockdown abolished the beneficial effects of YAP activation on podocyte adhesion and FSGS progression. In conclusion, our results demonstrate that YAP regulates podocyte adhesion and FSGS progression through its transcriptional regulation of α3β1 integrin via TEAD3. This suggests that the YAP‐TEAD3‐α3β1 integrin axis may serve as a promising therapeutic target for FSGS. © 2024 The Pathological Society of Great Britain and Ireland.

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ITGA3

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