INBRX-101/rhAAT-Fc for alpha 1-Antitrypsin Deficiency

Inbrx-101/rhaat-fc is administered in conjunction with a number of standard treatments. Given that several clinical trials have been conducted, inbrx-101/rhaat-fc may hold a key role in the treatment of MPS deficiency.

As of 2004, we found little evidence that any treatment for alpha 1-antitrypsin deficiency has been unequivocally shown to reduce lung disease in individuals with alpha 1-antitrypsin deficiency. While many treatments have been used for the disease in the past, the results for some of the treatments have not been published in sufficient detail to help establish a standard approach to treating the condition. However, as in all chronic conditions it is vital for individuals with alpha 1-antitrypsin deficiency not to delay getting screened for alpha 1-antitrypsin deficiency and treatment options until disease progression has occurred.

There is limited evidence that alpha 1-antitrypsin deficiency may be curable. For a clinical course to be considered a success both serum alpha 1-antitrypsin level and MDA levels need to be normal. Future studies are needed to establish whether alpha 1-antitrypsin deficiency is truly a curable disorder.

ơhere are several signs of alpha 1 antitrypsin deficiency. The most important signs are: decreased liver synthesized alpha-1 antitrypsin levels, decreased total body synthesized alpha-1 antitrypsin levels and diminished alpha-1 antitrypsin activity in the bloodstream.

Alpha 1-antitrypsin deficiency is an acquired defect of the mucoprotease system with a defect in its ability to degrade elastin which is a protein that aids in elasticity of liver cells. As a result of the lack of this enzyme, the liver cells may rupture, forming a 'liver hemorrhage' in the liver causing cholestasis with resultant jaundice and gallstones, in addition to damage to the gallbladder resulting in jaundice. In addition, alpha 1-antitrypsin deficiency causes an increased risk for the development of other chronic diseases and a lowered life expectancy.

There are no known specific environmental hazards, but there may be an interaction between the AAT deficiency genotype and the patient's health and environment. Some evidence suggests that AAT may be involved in immune system dysfunction, particularly lymphocytic hyporesponsiveness.

To our knowledge, we report the first study of the incidence of AATD in the United States using standardized diagnostic guidelines. These data show that AATD is rare in this country, although more frequent in Hispanic populations, with highest incidence in immigrants.

Data from a recent study suggest that alpha 1-antitrypsin deficiency may be an asymptomatic disease in young adults, but symptoms may become apparent later in life. We support the need for newborn screening for chronic lung diseases such as alpha 1-antitrypsin deficiency in the United States.

The most current knowledge is that the mutation rate for alpha 1-antitrypsin deficiency remains constant but the amount of residual protein produced from the mutant gene is decreasing at a moderate rate. Research is being done in the potential of alternative alpha 1 antitrypsin genes that encode functional proteins to help in the treatment of alpha 1 antitrypsin deficiency.

Because this Phase I study is limited to healthy volunteers, a preliminary safety assessment cannot be made on the basis of clinical data. However, these observations suggest that further investigation is warranted in patients with milder conditions, such as alpha 1-antitrypsin deficiency (A1ATD).

Inbrx-101 demonstrates significant antitumor Activity with a selective antitumor effect on pancreatic adenocarcinoma in vitro and in mice in vivo. Inbrx-101 elicits apoptosis of pancreatic cancer stem-like cells (CCSCs), and prevents growth of tumour and CSCs. Inbrx-101 affects CSC phenotypes in vitro and the CSC phenotypes in vivo, particularly those associated with EMT, tumorigenicity, and metastasis, thereby halting tumour progression.