The invention provides a method for treating acute myeloid leukemia (AML) in a subject in need thereof, said method comprising administering a therapeutically effective amount of an arginine-depleting agent to the subject, wherein the AML is of the French-American-British (FAB) subtype M0 (undifferentiated acute myeloblastic leukemia), M2 (acute myeloblastic leukemia with maturation), M4 (acute myeloblastic leukemia with maturation), M4 eos (acute myelomonocytic leukemia with eosinophilia), M5 (acute monocytic leukemia), M6 (acute erythroid leukemia) or M7 (acute megakaryoblastic leukemia).

The present invention relates to medical devices in the form of mucoadhesive films for the release of live lactic bacteria and bifidobacteria (probiotics) and/or for the release and maintenance of their pharmacologically useful enzyme activities.

Methods and compositions therefor of treating GAMT deficiency or guanidino acetate (GAA) toxicity in a subject comprising administration of an arginine depleting enzyme. An therapeutic formulation can include an arginase, an arginine deiminase or a combination thereof and optionally other compounds, and can be adapted for intravenous or subcutaneous administration to a subject.

Autophagy is the principal catabolic response to nutrient starvation. However, excessive autophagy can be cytotoxic or cytostatic, and contribute to cell death, but its mechanism of induction remains elusive. Here, it was demonstrated that prolonged arginine starvation by ADI-PEG20 induced an autophagy-dependent death of argininosuccinate synthetase 1 (ASS1)-deficient breast cancer cells. Consequently, arginine depleting agents such as ADI-PEG20 may be used in methods for killing one or more argininosuccinate synthetase 1 (ASS1)-deficient breast cancer cells. Further, abundance of ASS1 was either low or absent in more than 60% of 149 random breast cancer biosamples, which could be exploited as candidates for arginine starvation therapy.

The present invention provides a pharmaceutical composition containing albumin-binding arginine deiminase (AAD) fusion protein for treating cancer or other arginine-dependent diseases. The AAD fusion protein can be purified from both soluble and insoluble fractions of crude proteins, binds to human serum albumin (HSA) or animal serum albumin and has its high activity with longer half life for efficient depletion of arginine in cancer cells. The specific activities of wild-type ADI and AAD fusion protein in the present invention are about 20 and about 19 U/mg (at physiological pH 7.4), respectively. The composition can be used alone or in combination with at least one chemotherapeutic agent to give a synergistic effect on cancer treatment and/or inhibiting metastasis. The AAD fusion protein can also be used as a component for detection and quantitative analysis of arginine in a testing kit for various samples including blood, food and analytical samples.

A recombinant arginine deiminase including a fluorescent group attached via an optional linker to the side chain of a cysteine residue useful for qualitative and quantitative detection of L-arginine in a sample, and methods of use and preparation thereof.

Autophagy is the principal catabolic response to nutrient starvation. However, excessive autophagy can be cytotoxic or cytostatic, and contribute to cell death, but its mechanism of induction remains elusive. Here, it was demonstrated that prolonged arginine starvation by ADI-PEG20 induced an autophagy-dependent death of argininosuccinate synthetase 1 (ASS1)-deficient breast cancer cells. Consequently, arginine depleting agents such as ADI-PEG20 may be used in methods for killing one or more argininosuccinate synthetase 1 (ASS1)-deficient breast cancer cells. Further, abundance of ASS1 was either low or absent in more than 60% of 149 random breast cancer biosam pies, which could be exploited as candidates for arginine starvation therapy.

The present invention relates generally to isolated to arginine deiminase (ADI) proteins that have reduced cross-reactivity with anti-ADI-PEG 20 antibodies as compared to ADI-PEG 20, but which can have functional characteristics comparable to or better than ADI-PEG 20, compositions comprising the ADI proteins, and related methods of treating arginine-dependent diseases or related diseases such as cancer.

The invention provides methods for improving efficiency of fermentation by arginine supplementation, and genetically modified bacterium for use therefor. More particularly the invention provides methods for (i) increasing the production ATP intensive products with arginine supplementation, (ii) increasing utilization of arginine by a C1-fixing bacterium; and (iii) providing C1-fixing bacterium with optimized arginine de-aminase pathways.

To obtain an anti-PAD2 antibody having excellent PAD2 inhibitory activity. Provided is an anti-PAD2 antibody that specifically binds to positions 341 to 357 of PAD2. Also provided is an anti-PAD2 antibody that specifically binds to a peptide consisting of an amino acid sequence set forth in SEQ ID NO: 1.