Barron’s Medical Journal reporting from M.D Anderson In The Texas Medical Center Houston, Texas USA
Houston ( AP ) --- The fight against breast cancer has taken a major step forward. Barron’s Medical Journal has discovered the monoamine oxidase lysyl oxidase LOX gene is responsible for breast cancer spreading to your bones. It is important to note – no one dies from breast cancer on your breast. Breast cancer patients die when breast cancer spreads to your bone and lungs.
This is A Special Report For President Obama And Congress to start expecting a breast cancer cure by the end of this the 2nd term.
A super fantastic finding was found by Dr. Gartland and colleagues a group of Researchers from the UK and Denmark have discovered a protein that encourages breast cancer to spread to the bone the finding that has paved the way for treatments that halt progression of the breast cancer disease
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Dr. Gartland found that when breast cancer cells are deprived of oxygen, they release high levels of LOX. This protein makes holes in the bone of breast cancer patients as a way of preparing it for the arrival of cancer cells.
The main cause of mortality among cancer patients is generally secondary, or metastatic, tumours, but few selective drugs have been identified that specifically target metastasis itself. Now, an exciting report from Erler and colleagues describes the involvement of the monoamine oxidase lysyl oxidase (LOX) in several stages of the migration of malignant cancerous cells from their primary tumour formation site, establishing a new therapeutic target for preventing and treating metastases.
"We show that these lesions subsequently provide a platform for circulating tumor cells to colonize and form bone metastases,". In another part of the study, the team found that introducing LOX to tumor-free mice also led to bone damage. However, they found an existing drug called bisphosphonate - used to treat bone diseases such as osteoporosis - prevented such damage in these mice.
As such, the authors suggest that administering similar treatments to patients with breast cancer could stop the disease spreading to the bone.
Commenting on the findings, study co-leader Dr. Janine Erler, of the University of Copenhagen in Denmark, says:
"Once cancer spreads to the bone it is very difficult to treat. Our research has shed light on the way breast cancer cells prime the bone so it is ready for their arrival. If we were able to block this process and translate our work to the clinic, we could stop breast cancer in its tracks thereby extending patients' lives."
The researchers say their next step is to determine how LOX interacts with bone cells to drive cancer metastasis, which will bring us closer to finding drugs that stop the process. "This could also have implications for how we treat other bone diseases too," adds Dr. Gartland.
Earlier this month, Barron’s Medical Journal reported on a study published in the British Journal of Surgery, which suggests women with hereditary breast cancer are at no higher risk of poor treatment outcomes than breast cancer patients without a family history of the disease.
The lysyl oxidase (LOX) family is an emerging family of amine oxidases that is responsible for lysine-mediated crosslinks found in collagen and elastin. Several novel functions, such as tumor suppression, tumor progression, cellular senescence, chemotaxis and the modification of histones have recently been attributed to the LOX family of proteins. In the search for more human LOX paralogs, in the present study, we identified several expressed sequence tag (EST) clones that showed an alternative exon-intron splice pattern from LOX. These ESTs corresponded to the LOX transcript variant 2 (LOX-v2) that was recently reported in GenBank (accession no. NM_001178102). LOX-v2 mRNA lacks exon 1 of LOX, but contains an additional 222 bp sequence from the 5'-flanking intronic region of exon 2. The deduced LOX-v2 polypeptide contains the characteristic C-terminal domains of the LOX family, but does not contain the N-terminal propeptide region that has been reported to have tumor suppressor activity. In peroxidase-coupled fluorometric assays, LOX-v2 showed β-aminopropionitrile-inhibitable amine oxidase activity toward collagen and elastin. RT-PCR analysis of human tissues revealed a distinct tissue specificity of LOX-v2 expression compared to that of LOX. Promoter assays indicated that an alternative promoter element present in the exon 1 region of LOX was sufficient for the differential expression of LOX-v2. These findings indicate that the human LOX gene encodes 2 variants, LOX and LOX-v2, both of which function as amine oxidases with distinct tissue specificities.
For the science readers:
Entrez Gene summary for LOX: The protein encoded by this gene is an extracellular copper enzyme that initiates the crosslinking of collagens and elastin. The enzyme catalyzes oxidative deamination of the epsilon-amino group in certain lysine and hydroxylysine residues of collagens and lysine residues of elastin. In addition to crosslinking extracellular matrix proteins, the encoded protein may have a role in tumor suppression. Defects in this gene are a cause of autosomal recessive cutis laxa type I (CL type I). Two transcript variants encoding different isoforms have been found for this gene. (provided by RefSeq)
The results of a very important discovery Lox Gene Targeting Results in Perinatal Lethality—A gene- targeting vector was designed to eliminate Lox expression by converting the translation initiation codon (ATG) into a trans- lationally inactive NotI restriction site and inserting the phos- phoglycerate kinase promoter driving the neomycin antibiotic resistance gene (PGK-Neo) (Fig. 1A). This construct was elec- troporated into embryonic stem cells (129/SvJ), and clones un- dergoing homologous 
recombination were injected into blasto- cysts. Resulting chimeric mice were bred to C57BL/6J mice yielding germ line transmission of the targeted allele. Breeding of heterozygous null LOX mice resulted in 0 of 400 animals that were homozygous for the targeted allele at 3 weeks of age. Timed matings were set up to determine the fate of LOX/ mice. LOX/ mice were observed by genotype late in gestation and at parturition with proper Mendelian inheritance (Fig. 1B). Grossly, LOX/ mice were of similar size to wild type and heterozygous littermates at late gestation and parturition.
LOX gene targeting results in decreases in both collagen and elastin cross-links in vivo, confirming the catalytic capacity of LOX demonstrated in vitro. Despite the presence of five lysyl oxidase enzymes, LOX deficiency is lethal, suggesting that other lysyl oxidases are unable to effectively compensate dur- ing development 
for the physiological stresses associated with parturition and life ex utero. LOXL1 mRNA does not increase to compensate for LOX deficiency in the total embryo. The inabil- ity of the other lysyl oxidases to compensate may relate to either distinct substrate specificities of individual enzymes or temporally and spatially unique expression patterns.
This why Barron’s Medical Journal senior science writer says we are going to find a cure by the end of President Obama 2nd term.
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