Targinta develops first-in-class tumor-targeting antibodies and ADCs for aggressive cancers

The cancer target integrin α10β1

Cancer target with unique properties

Integrin α10β1 is a collagen-binding receptor normally expressed on cartilage cells and some stem cells. The receptor is needed for cells to adhere to surrounding supporting tissue, and is considered important for cells' ability to divide and move in tissues. These are functions that are of importance even for cancer cells. Among other things, the receptor has been shown to play a role in the division of cancer cells and their ability to spread throughout the body. The receptor is highly expressed in solid aggressive cancers including glioblastoma and triple-negative breast cancer, while expression in most normal tissue is absent. Integrin α10β1 can therefore serve as a target molecule for targeted cancer therapies.

Targinta develops two types of targeted antibodies: monoclonal antibodies that act by preventing the growth and spread of cancer cells, and toxin-armed antibodies, so-called ADC (Antibody-Drug Conjugate) that kill cancer cells.

Test tubes in laboratory

ADC technology

ADCs, or antibody-drug conjugates, are antibodies armed with a powerful toxin. The toxins are selectively delivered to cancer cells that express the target molecule.

Three key properties make integrin α10β1 a promising target for ADC development:

  • The target is selectively highly expressed in solid aggressive cancers while expression on normal cells in absent or very low
  • The target transmits important signals for cancer cell survival and migration
  • The target internalizes effectively, allowing rapid cellular uptake of toxins

The absence of the target molecule in most normal tissue reduces the risk of off-target side effects. Given that integrin α10β1 is primarily being expressed in aggressive, invasive cancers with very poor prognosis, integrin α10-antibodies can be assumed to have a good risk/benefit profile.


Targinta runs two parallel drug projects where the antibody candidates are directed against the unique target protein integrin α10β1. One project aims to produce directly tumor-killing antibodies, which is done through the production of chemotherapy-conjugated integrin α10-antibodies, so-called α10-ADC (Antibody-drug conjugate). The other project involves the development of function-blocking integrin α10-antibodies, that among other things prevent spreading and metastasis of cancer cells.
ADC* targeting integrin α10β1
Integrin α10β1-mAb

TARG10: Integrin α10β1-mAb
TARG9: ADC* targeting integrin α10β1

* Antibody-drug conjugate


TARG9 is an ADC, a tumor-targeting antibody armed with a powerful toxin. The ADC selectively homes to and is taken up by cancer cells expressing integrin α10, where the toxin is released and kills the cells.

TARG9 has shown promising preclinical effects in glioblastoma and in triple-negative breast cancer. This includes integrin α10-dependent cell death in both glioblastoma and TNBC and also a so called bystander effect, i.e. that TARG9 kills the cell it binds to, as well as neighboring cells.

Further, it has been confirmed that TARG9 is efficiently internalized upon binding to integrin α10, wich is essential for the selective release of the toxin inside the cancer cell. It has also been shown that TARG9 prevents tumor growth in preclinical models for glioblastoma and TNBC.

TARG10 illustration


TARG10 is a tumor-targeting and function-blocking antibody that acts by preventing cancer cells from dividing and growing, and, importantly, from spreading to other parts of the body. TARG10 can also be used as an ADC.

The function-blocking integrin α10 antibody TARG10 inhibits the growth of glioblastoma and triple-negative breast cancer and reduces the spread of cancer cells and prevent the formation of metastases.

  • Reduced adhesion of cancer cells to the extracellular environment
  • Reduced migration, proliferation and survival of cancer cells
  • Reduced tumor growth in preclinical models for glioblastoma and TNBC
  • Reduced metastasis in TNBC
TARG10 illustration

Cancer Indications

Aggressive and life-threatening cancers where effective treatment is lacking are a major medical problem. New treatment concepts are needed to successfully treat these cancers. Targinta's unique target molecule integrin α10β1 has the potential to meet those needs. The Company's targeted integrin α10-antibodies have shown promising efficacy in preclinical studies on two highly malignant cancers, glioblastoma and triple-negative breast cancer. This provides ample opportunity to develop completely new drugs against aggressive cancer.

Triple-negative breast cancer

Triple-negative breast cancer is an aggressive form of cancer with a high risk of recurrence and metastasis. Around 300,000 people are being diagnosed globally each year. The five-year survival rate for patients with disseminated triple-negative breast cancer is about 12 percent.

The market value for the treatment of triple-negative breast cancer in the eight major markets is estimated to be USD 2.1 billion in 2025.

Early stage triple-negative breast cancer is treated with surgery in combination with radiotherapy and/or chemotherapy.  More advanced or recurring disease is treated with chemotherapy as well as with targeted therapies (PARP inhibitors) and immunotherapy (PD-1 inhibitors). In addition, an ADC (anti-trop2) has recently been approved and is being used for a subgroup of patients.


Glioblastoma (grade 4 glioma) is the most common and most aggressive form of brain cancer in adults. It grows rapidly and tends to relapse after treatment. About 30,000 patients are diagnosed with glioblastoma in the United States and Europe every year. The five-year survival rate for patients with glioblastoma is about 3 percent.

The market value of glioblastoma treatment in the seven major markets is estimated at USD 1.4 billion in 2027.

Glioblastoma drug therapy is essentially restricted to systemic or local chemotherapy.

The blood brain barrier is a significant obstacle for antibody-based treatments. There is essentially no exposure of the brain as long as the blood brain barrier is intact. The integrity of the barrier is however compromised in glioblastoma, resulting in increased exposure after systemic administration. Targinta is evaluating additional ways to administer the drug in order to increase exposure, such as local instillation onto the affected brain surface at the time of surgery.

Other cancer indications

Targinta is evaluating the possibility of developing TARG9 and TARG10 for additional cancers beyond triple-negative breast cancer and glioblastoma. The target molecule integrin α10β1is also expressed in, for example, lung cancer, prostate cancer, pancreatic cancer and in certain forms of sarcoma, providing opportunities for broaden the use of the Company's drug candidates.

Brain tumor illustration

Scientific publications

Chmielarska Masoumi K., Huang X., Sime W. ,Mirkov A., Munksgaard Thorén M., Massoumi R. and Lundgren-Åkerlund E. ”Integrin 10-Antibodies Reduce Glioblastoma Tumor Growth and Cell Migration.” Cancers (Basel) 13, 1184 (2021).

Munksgaard Thorén M., Chmielarska Masoumi K., Krona C., Huang X., Kundu S.,Schmidt L., Forsberg-Nilsson K., Floyd Keep M., Englund E., Nelander S.,Holmqvist B. and Lundgren-Åkerlund E. "Integrin α10, a Novel Therapeutic Target in Glioblastoma, Regulates Cell Migration, Proliferation, and Survival." Cancers (Basel). 11, 587 (2019).

Wenke A-K., Kjellman C., Lundgren-Åkerlund E., Uhlmann C., Haass N K., Herlyn M and Bosserhoff A K. "Expression of integrin alpha10 is induced in malignant melanoma." Cell Oncology. 29(5):373-86 (2007).

Camper, L., Holmvall, K., Wängnerud, C., Aszódi, A. and Lundgren-Åkerlund, E. "Distribution of the collagen-binding integrin α10β1 during mouse development." Cell Tissue Res. 306, 107-116 (2001).

Bengtsson, T., Camper, L., Schneller, M. and Lundgren-Åkerlund, E.  "Characterization of the mouse integrin subunit α10 gene and comparison with its human homologue. Genomic structure, chromosomal localization and identification of splice variants." Matrix Biology 20, 565–76 (2001).

Camper L., Hellman U. and Lundgren-Åkerlund E. "Isolation, cloning, and sequence analysis of the integrin subunit alpha10, a beta1-associated collagen binding integrin expressed on chondrocytes." J Biol Chem. 7;273 (32):20383-9 (1998).

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