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GENTAUR Europe BVBA Voortstraat 49, 1910 Kampenhout BELGIUM Tel 0032 16 58 90 45 Fax 0032 16 50 90 45 This email address is being protected from spambots. You need JavaScript enabled to view it.">This email address is being protected from spambots. You need JavaScript enabled to view it. |
GENTAUR BULGARIA
53 Iskar Str. 1191 Kokalyane, Sofia
Tel 0035924682280
Fax 0035929830072
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GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50
Fax 01 43 25 01 60
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GmbH Marienbongard 20
52062 Aachen Deutschland
Tel (+49) 0241 56 00 99 68
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GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531
Fax 020 8445 9411
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GENTAUR Poland Sp. z o.o.
ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
Tel 058 710 33 44
Fax 058 710 33 48
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GENTAUR Nederland BV
Kuiper 1
5521 DG Eersel Nederland
Tel 0208-080893
Fax 0497-517897
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GENTAUR SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6, 24122 Bergamo
Tel 02 36 00 65 93
Fax 02 36 00 65 94
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GENTAUR Spain
Tel 0911876558
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Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
Phone/Fax:
(408) 780-0908
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GENPRICE Inc. invoicing/ accounting:
6017 Snell Ave, Suite 357
San Jose, CA. 96123
Serbia, Macedonia,
Montenegro, Croatia:
Tel 0035929830070
Fax 0035929830072
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GENTAUR Romania
Tel 0035929830070
Fax 0035929830072
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GENTAUR Greece
Tel 00302111768494
Fax 0032 16 50 90 45
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Other countries
Luxembourg +35220880274
Schweiz Züri +41435006251
Danmark +4569918806
Österreich +43720880899
Ceská republika Praha +420246019719
Ireland Dublin +35316526556
Norge Oslo +4721031366
Finland Helsset +358942419041
Sverige Stockholm +46852503438
Magyarország Budapest +3619980547
Malaria Pf_Pv Ag Rapid Test Kit
Malaria Pf_Pv Ag Rapid Test Kit
Principle: Immunochromatographic assay
Cassette: 4mm
Kit Size: 25 Tests
Specimen: Whole Blood
CE Mark: Yes
Storage & Stability
Store at 2-30°C; Expiry period 24 months.
Features and advantages:
- 1. State-of-arts workmanships and severe lab testing processes; Product CE approved and quality system ISO13485 certified;
- 2. Easy assay procedure and rapid results reading; High sensitivity and specificity;
- 3. Full-aspects OEM service provided. Design according to customers unique requirements. Help improving customer’s brand value.
Intended Use
Malaria Pf/Pv Antigen Rapid Test is a lateral flow immunochromatographic assay for the qualitative simultaneous detection of Malaria P.falciparum specific histidine rich protein-2(Pf HRP-2) (for Pf) and the LDH (for Pv) in human whole blood as an aid in the diagnosis of Malaria infection. The test is recommended for professional use only. All results must be interpreted together with other clinical information available to the physicians.
Materials Provided
25 X Test Devices, each test cassette is packed in a foil pouch with a dropper (5ul) and a package of desiccant.
25 X Disposable blood lancet
25 X Alcohol pad
1 X Assay Buffer
1 X Instructions for Use
Ordering Information:
CAT # |
PRODUCT |
CE |
SPECIMEN |
SENSITIVITY |
ACCURACY |
FORMAT |
KIT SIZE |
RI742C |
Malaria Pf/Pv Ag |
√ |
Whole blood |
98.10%/96.86% |
99.03%/99.03% |
Cassette |
25 |
Result interpretation Time
The testing results should be read at 20 minutes after a specimen is applied to the sample well of the device.
Performance Characteristics
Sensitivity and specificity: Comparative testing with the traditional Microscopic examination method shows that Malaria Pf/Pv Antigen Test is capable to detect out malaria infection when in blood specimen plasmodium protozoa of Plasmodium falciparum or plasmodium protozoa of P. vivax reaches 50pcs/ul.
Clinical study between Malaria Pf/v Antigen Test and Microscopic examination method demonstrates that Malaria Pf/Pv Antigen Test has a sensitivity of 98.10% and specificity of 99.39% for P.falciparum.
Clinical study between Malaria Pf/Pv Antigen Test and Microscopic examination method demonstrates that Malaria Pf/Pv Antigen Test has a nn2xssensitivity of 96.86%, and specificity of 99.76% for P. vivax.
Precision: within-run and between-run precisions have been determined by testing 10 replicates of three specimens: a negative, a low positive and a strong positive. The agreement between the test results and the expected results were 100%.
Contact our international sales team to know more about Gentaur products, prices; purchase & distribution; and oem.
Protein in the body - effective against hepatitis C
Protein in the body can improve its ability to detect and treat viral infections such as influenza and hepatitis C. This conclusion leads a laboratory study by researchers from the University Institute of cancer in Pittsburgh, USA.
To start playback in the body, the virus actually "invaded" cells and "takes" control over them.
Experts explain that, despite progress in the field of vaccines and treatment diseases caused by viral infections remain among the leading causes of death in the world. According to them, there is a need for a new type of security and the new discovery appears to be promising for further studies.
Scientists isolated protein of similar oligoadenylate synthetase-occurring in humans, suffering from liver cancer, prichinen of hepatitis C. When the Expert increase the levels of this protein in human cells, observed inhibition of virus replication.
In later study found that murine organisms in which there is no presence of the protein are susceptible to a large extent of a viral infection, in comparison to those who have it.
Viruses affect the ribonucleic acid (RNA), including hepatitis C, influenza and respiratory syncytial virus, using RNA as the genetic material, when played back.
The types of treatment, based on the protein like oligoadenylate synthetase, can enhance the ability of cells to detect RNA, used by the virus, and thus to activate the immune system to stop its reproduction.
Discovered a gene that increases intelligence
U.S. scientists have identified a gene in the gray matter of the brain, which they say is responsible for intelligence.
These are proteins called " Clotho " which raises brain skills and increases IQ by six points , regardless of the age of the person.
Researchers examined the cerebral cortex.
According to previous studies cortical thickness is closely related to mental abilities , memory, attention , perceptual awareness , thought and language , but so far there is no evidence exactly which genes are associated with these laws .
It turns out that " Clotho " is a powerful stimulant of learning , thinking and memory. This is because the protein increases the strength of connections between nerve cells in the brain.
Scientists hope that this discovery will help in the treatment and prevention of various types of dementia.
They found that " Clotho " plays a key role in many processes related to starenieto . It is directly related to life expectancy and susceptibility to stroke.
Where in this gene has been observed a defect , people start aging prematurely, but when it is stimulated , life could be extended by a few years , while slow bone loss , prevents blood clots occur on and improves overall health of the elderly .
Scientists warn that no matter how miraculous it seems this gene probably causes some side effects in the body.
During the experiment, they noticed that individuals whose lives went on , proved to much smaller capacities for multiplication.
It is also likely " Clotho " cause predisposition to disease of diabetes .
Bovine Cystocercosis ELISA
The GENTAUR Bovine living cysticercosis ELISA is based on 2 mouse monoclonal antibodies that detect only protein of living Cystocerkosis infections. The ELISA can detect Cystocercosis from as low as 10 infections in one adult cattle on 500 ul of crude serum.
The results on Urine are not 100% accurate due to false positives.
Name: Bovine living cysticercosis ELISA
Product reference: 04-bov-cysto-ELISA
Price: 455 Euro / 96 wells
Use: Low detection of living infections, not quantitative but qualitative
Deze ELISA geeft een juiste diagnose in 100% van alle positieve gevallen, wanneer er meer dan 10 cysticercen aanwezig zijn in het karkas( keuringsverslag) Indien er tussen de 1 en 10 cysticercen aanwezig zijn daalt dit naar 65%. In theorie is 1 cysticerc voldoende om een mens te infecteren.
Name: Rabbit polyclonal anti living bovine cystocercosis
Product reference: 04-bov-cysto-rab500
Price: 195 Euro / 500ul
Use: crude rabbit serum used for WB 1/500, ELISA capture antibody
Bovine cystocercosis is a parasitic disease that afflicts the muscles of cattle and is caused by larvae of the human tapewormTaenia Saginata. If people consume beef containing these parasites they can acquire intestinal tapeworm infections.
Bovine cystercosis, also known as bladder worm or beef tape worm, is a parasitc zoonosis due to the cestode Taenia saginata. It causes few symptoms in the animal but it is an important zoonosis. |
Classification |
OIE, List B disease |
Susceptible species |
The beef is a intermediate host and man is the final host. |
Distribution |
Bovine cysticervosis is worldwilde distributed. In the Pacific it is only reported in Australia and New Zealand. |
Clinical signs |
In animals there is usually no clinical sign associated. However heavy infections may cause myocarditis andheart failure associated with developing cysts in the heart. |
Post-mortem findings |
Lesions consist of cysticerci in cysts, they are 5-8 mm by 3-5 mm, translucid and filled with a brownish to pinkish liquid, sometimes the 'head' of the metacestodes can be see as a white spot. Cysts are essentially found in the following muscles:
More rarely cysts are found in the liver, the lungs and the brain. |
Differential diagnosis |
Lesions must be differentiated from sarcosporidiosis and toxoplasmosis. |
Specimens required for diagnosis |
The diagnosis is usually made during meat inspection. However serologic test has been developed. |
Transmission |
Beef usually get infected by grazing on pasture contaminated by human feces (which can come from sewage water or direct pollution). Occasionally in-utero contamination occurs. Human get infected by eating unproperly cooked meat (<60°C) |
Risk of introduction |
Introduction could occur through importation of infected cattle, meat or material contaminated by human feces. Humans can also introduce it into the country. |
Control / vaccines |
Control is done through public hygien and proper meat inspection at slaughterhouse. Cysts can be destroyed by freezing at -18°C for 5 days or at -10°C for 10 days or by cooking at 56°C for 5 minutes. |
References |
|
Detectietest ter confirmatie van de visuele postmortem diagnose van rundercysticercose
IWT project 080132
Better Protein Creation May Be Secret of Longevity for the World's Longest-Living Rodent
Naked mole rats have what any animal would want. They live long lives—about 30 years—and stay healthy until the very end. Now biologists at the University of Rochester have new insights into the animal's longevity—better-constructed proteins.
Proteins are involved in nearly all functions of an animal cell, and consequently, are essential to all organisms. But before proteins can do their job, they must fold into the appropriate shapes that allow them to connect to and interact with other structures in the cell. In a paper published this week in the Proceedings of the National Academy of Sciences, Vera Gorbunova and Andrei Seluanov describe their discovery of the process in naked mole rats that leads to virtually perfect proteins.
"While this is basic research," said Gorbunova, "we hope our findings encourage further studies on better protein synthesis."
Their work focused on naked mole rat ribosomes—the site of protein creation in the animal's cells—and began by happenstance. Gorbunova and Seluanov were working with ribosome RNA (rRNA) when they made a discovery. After applying a dye to a sample, they studied it under ultraviolet light only to find three dark bands—representing concentrations of different rRNA molecules—not the two bands that are characteristic of all other animals, suggesting that there is a "hidden break" in the naked mole rat rRNA. Since rRNA is an essential part of the protein-creation mechanism, the two biologists decided to see if the broken rRNA affects the quality of naked mole rat proteins.
Ribosome RNA strands act as scaffolds on the ribosome, a protein synthesis machine. Changing the shape of the scaffold can have a profound effect on the organization of the ribosome parts.
Gorbunova and Seluanov discovered that the naked mole rat's rRNA scaffold is indeed unique. The rRNA strands split at two specific locations and discard the intervening segment. Instead of floating off on their own, the two remaining pieces from each strand stay close to each other and act as a scaffold on which ribosomal proteins are assembled to create a functional ribosome—a molecular machine that puts amino acids together to create proteins. And the results are impressive.
When the ribosome connects amino acids together to create a protein a mistake is occasionally introduced when an incorrect amino acid is inserted. Gorbunova and Seluanov found that the proteins made by naked mole rat cells are up to 40 times less likely to contain such mistakes than the proteins made by mouse cells.
"This is important because proteins with no aberrations help the body to function more efficiently," said Seluanov.
The next step for the biologists is to split mouse rRNA in the same way to see if it would lead to improved protein creation.
The two biologists hope their work will eventually result in pharmaceutical treatments that modulate protein synthesis in humans, though any medical solution is a long way off.
New role for protein family could provide path to how crop traits are modified
Pioneering new research from a team of Indiana University Bloomington biologists has shown for the first time that a protein which has been long known to be critical for the initiation of protein synthesis in all organisms can also play a role in the regulation of gene expression in some bacteria, and probably land plants as well.
The protein, called translation initiation factor 3, or IF3, is one of three proteins that make up the core structure of the machinery needed to guide the joining of messenger RNAs and ribosomes as protein translation commences. These three proteins have been widely considered to simply operate in a constitutive manner and play little, if any, role in regulating the expression of genes.
The new findings, from the laboratory of David M. Kehoe, professor of biology in the Indiana University Bloomington College of Arts and Sciences, reveals that IF3, in addition to its well-accepted function during translation initiation, also regulates the expression of genes that encode components of the photosynthetic machinery in response to changes in the color of light in the surrounding environment, a process known as "chromatic acclimation."
These photosynthesis genes produce red-pigmented proteins called phycoerythrin in cyanobacteria when the cells are grown in green light and allow these organisms to efficiently absorb the predominant ambient light color for photosynthesis. The team uncovered the novel function of IF3 while searching for mutants that incorrectly regulated phycoerythrin. The discovery of this mutant was at first surprising, because in all other bacteria that have been examined, mutations in infC (the gene that encodes IF3) are lethal.
The team solved this puzzle by uncovering a second infC gene in Fremyella diplosiphon, the model organism for the study of light color responsiveness in cyanobacteria. While both IF3s, which have been named IF3a and IF3b, can act in the traditional role of translation initiation, only IF3a was found to also regulate photosynthetic gene expression.
By exploring the genomes of hundreds of prokaryotes and eukaryotes in collaboration with members of the laboratory of Indiana University Distinguished Professor and Class of 1955 Professor Jeffrey Palmer, the group identified a wide range of species whose genomes appear to have the potential to encode multiple IF3s, with one organism apparently encoding five distinct IF3 family members. And since almost none of these species are capable of chromatic acclimation, Kehoe believes that multiple IF3s must be used to regulate a wide range of environmental and perhaps developmental responses in both prokaryotes and eukaryotes.
"Particularly interesting was our finding that IF3 families exist in a number of plant species, including commercially important crops," Kehoe said. "This means that new approaches to the modification of traits in agriculturally significant plant species may be possible by manipulating the expression patterns of different IF3 family members."
The discovery has generated excitement for an additional reason. Historically, scientists have had a difficult time studying IF3 because it is so essential for translation initiation that it can not be altered without causing death. In fact, it remains one of the few proteins involved in translation for which no effective antibiotic has been developed. But the ability of the Kehoe team to delete either of the two infC genes in F. diplosiphon without causing lethality will allow the group to modify both IF3a and IF3b at will.
"Now that we know that F. diplosiphon contains two functionally different IF3s, and that each is nonessential, we have a unique opportunity to enhance our understanding of how the structural features of IF3 are related to its function," Kehoe said. "Advancing our understanding of the role of IF3 in translation is likely to provide opportunities to develop new antibiotics that are targeted to this class of proteins."
"A unique role for translation initiation factor 3 in the light color regulation of photosynthetic gene expression" is now available in early online editions of the Proceedings of the National Academy of Sciences. Co-authors with Kehoe and Palmer were Andrian Gutu, a former Ph.D. student in the Kehoe lab who is now a Howard Hughes Medical Institute Postdoctoral Fellow at Harvard University; April Nesbit, a former postdoctoral researcher in the Kehoe lab who is now a lecturer at Purdue Northwest; and Andrew Alverson, a former postdoctoral fellow in the Palmer lab who is now a faculty member at the University of Arkansas. Primary funding for the work was provided by the National Science Foundation, with support provided to Nesbit by the National Institutes of Health.
New function for a molecule interleukin-7 (IL-7)
The molecule interleukin-7 (IL-7) is an important immune system messengers that a sufficient number of T cells guaranteed at present in the body's defenses. ETH Zurich researchers have now shown that IL-7 has another important function: it improves the function of the lymphatic drainage collect moisture that has leaked from the blood vessels into the body tissues and back into the bloodstream. In the future, these insights for lymphedema patients, the lymphatic system is not working properly useful, what tissue to become fluid retention and swelling.
The predisposition to the development of lymphedema can on the one hand, are hereditary. On the other hand, lymphedema often. During the period after a tumor operation Primary tumors are surgically excised tumor and lymph nodes are often removed because they can contain metastases. Tumor in the course of such a surgical procedure is the lymphatic tissue is damaged. This tissue fluid is often not properly arranged, so that the occurrence of lymphedema in 20 to 30 percent of patients.
No drug treatment yet
Currently wearing the only treatment options for patients with lymphedema compression stockings and undergoing a medical manual lymphatic drainage massage therapist. "In IL-7, we have a molecule and a mechanism for improving lymphatic drainage for lymphedema therapy, useful to be discovered," says study leader Cornelia Halin, Assistant Professor of Drug Discovery Technologies.
In their study, the researchers found that IL-7, which shape is formed by the so-called endothelial cells. The lymphatic vessel wall These cells also bear receptors, IL-7 in a certain way based on the lock-and-key principle. "Although we have not formally proven that so far, we assume that the lymphatic endothelial cells produce the neurotransmitter, may directly affect their own function," says Halin. To date, IL-7 is one of only a few molecules have been identified that support lymphatic drainage. A few years ago, researchers discovered that the other endogenous growth factor VEGF-C, a molecule of interest in this context is perhaps also.
Findings from an animal model
Halin and her colleagues showed the drainage support function of IL-7 by drainage experiments in mice, where blue, albumin-binding dye in the skin of the mouse injected ear. It is noteworthy that albumin, a naturally occurring protein that is transported from the tissues via the lymphatics. By quantifying the dye in the tissue remained one day after the injection, the researchers were able to determine how well worked the lymphatic these animals.
In carrying out this experiment, mice, in which a functional IL-7 receptor, it is noted that these mice to only remove half the dye out of the ear skin in order to compare with a functional mouse IL-7 receptor. However, they observed a significant increase in lymphatic drainage in mice with increased IL-7 production. Finally she IL-7 protein is in a third experiment, unchanged administered healthy mice and found that a therapeutic treatment done to improve lymphatic drainage function.
Been tested in patients
The researchers are now planning similar experiments in mice in which lymph vessels are surgically destroyed, similar to the situation in patients after cancer surgery. Here, the researchers want to test whether treatment with IL-7 or IL-7 could lymphedema would be prevented. Reduce the existing lymphedema administered
The long-term goal is to explore the potential of IL-7-based drugs for lymphedema. In particular, IL-7 has been tested in clinical trials, although for different indications: due to its immune-stimulatory activity on T cells, IL-7 is currently undergoing in patients with immunodeficiency diseases such as HIV or hepatitis infection or bone marrow tested transplants.
Automatic Biochemistry Analyzer 6020
Price: 6860 Euro
Recombinant Protein
Product Name: |
Recombinant Aedes aegypti 37 kDa salivary gland allergen Aed a 2(D7) for Aedes aegypti (Yellowfever mosquito) (Culex aegypti) |
|
Product Type: | Recombinant Protein | |
Application: | Immunogen,ELISA | |
Code: | CSB-YP321587AXQ >> Yeast CSB-EP321587AXQ >> E.coli CSB-BP321587AXQ >> Baculovirus CSB-MP321587AXQ >> Mammalian cell |
|
Size: | 1mg | |
Protein Names: | Recommended name: 37 kDa salivary gland allergen Aed a 2 Alternative name(s): Protein D7 Allergen= Aed a 2 |
|
Gene Names: | Name:D7 ORF Names:AAEL006424 |
|
Species: |
Aedes aegypti (Yellowfever mosquito) (Culex aegypti) |
|
Product Info: | His tagged | |
Purity: | >90% | |
Storage Buffer: | PBS pH 7.4, 50% glycerol | |
Storage: | Store at -20℃, for extended storage, conserve at -20℃ or -80℃. | |
Notes: | Repeated freezing and thawing is not recommended. Store working aliquots at 4℃ for up to one week. | |
AA sequence: |
STGPFDPEEMLFTFTRCMEDNLEDGPNRLPMLAKWKEWINEPVDSPATQCFGKCVLVRTG LYDPVAQKF
DASVIQEQFKAYPSLGEKSKVEAYANAVQQLPSTNNDCAAVFKAYDPVHKA HKDTSKNLFHGNKELTKG LYEKLGKDIRQKKQSYFEFCENKYYPAGSDKRQQLCKIRQYT VLDDALFKEHTDCVMKGIRYITKNNEL DAEEVKRDFMQVNKDTKALEKVLNDCKSKEPSN AGEKSWHYYKCLVESSVKDDFKEAFDYREVRSQIYA FNLPKKQVYSKPAVQSQVMEIDGK QCPQ |
|
Expression Region: | 18-321 | |
Recombinant Aedes aegypti 37 kDa salivary gland allergen Aed a 2(D7) for Aedes aegypti (Yellowfever mosquito) (Culex aegypti)
CSB-YP321587AXQ >> Yeast € 2090/ mg
CSB-EP321587AXQ >> E.coli € 1680/ mg
CSB-BP321587AXQ >> Baculovirus € 2540/200ug
CSB-MP321587AXQ >> Mammalian cell € 2980/200ug
Expression Region :18-321aa;full length.
Protein in Blood Exerts Natural Anti-Cancer Protection
Researchers from Thomas Jefferson University's Kimmel Cancer Center have discovered that decorin, a naturally occurring protein that circulates in the blood, acts as a potent inhibitor of tumor growth modulating the tumor microenvironment.
The study, published June 24 online in the Proceedings of the National Academy of Sciences, suggests it may be possible to harness the power of this naturally occurring anticancer agent as a way to treat cancer, including metastases.
In several different publications it has been described the ability of decorin to affect a number of biological processes including inflammatory responses, wound healing, and angiogenesis.
In this new article, the study's senior investigator, Renato Iozzo, M.D., Ph.D., has labeled decorin a "soluble tumor repressor" -- the first to be found that specifically targets new blood vessels, which are pushed to grow by the cancer, and forces the vessel cells to "eat" their internal components. This reduces their potential to feed the cancer overall causing an inhibition of tumor progression.
"The tumor suppressors we all know are genes inside tumors that a cancer deletes or silences in order to continue growing. I call decorin a tumor repressor because its anti-tumor activity comes from the body, outside the cancer," says Dr. Iozzo, Professor of Pathology & Cell Biology, Biochemistry & Molecular Biology at Kimmel Cancer Center.
"Decorin is a soluble compound that we found has a powerful, natural protective effect against cancer -- an exciting finding that we believe will open up a new avenue for both basic research and clinical application," Dr. Iozzo says. "Acting from the outside of the cells, decorin is able to modify the behavior of the cancer cells and of the normal cells in order to slow down the progression of the tumor. For this reason, decorin acts as a guardian of the matrix, the complicated structure built around the cells in our body."
Absence of decorin promotes tumor growth
Decorin has long been known to be involved in human development. It is so named because deposits of decorin "decorate" collagen fibrils after the human body forms.
A second pool of decorin has been found circulating in blood after production by connective tissue throughout the body. This connective tissue is part of the extracellular matrix, which provides both structural support and biological regulation of tissue cells.
But no one has understood the biological function of this second pool of decorin, according to Dr. Iozzo.
The research team, including the two co-first authors, Simone Buraschi, Ph.D., and Thomas Neill, a graduate student, who work in the laboratory of Dr. Iozzo, decoded the function of soluble decorin. They found that addition of exogenous decorin to the tumor microenvironment induces autophagy, a mechanism by which cells discard unnecessary or damaged intracellular structures. "This process regulates a lot of cellular activities," says Dr. Iozzo.
The researchers specifically found that decorin evoked autophagy in both microvascular and macrovascular endothelial cells -- cells that line the interior surface of blood vessels.
"This matters because autophagy can exert a potential oncosupressive function by acting to discard critical cell components that would otherwise be involved in promotion of tumor growth through angiogenesis, the production of new blood vessels that can provide nutrition to the tumor," Dr. Iozzo says. "In contrast, absence of decorin permits tumor growth."
Therefore, the presence of decorin in the surroundings of the tumor is essential to control tumorigenesis and formation of new blood vessels, he says. Moreover, Dr. Iozzo's laboratory has characterized for the first time Peg3, a known tumor-suppressor gene, as a master player in the autophagy process induced by decorin. "This discovery is important as it opens up to the study of new unexplored genes and signaling pathways in the field of autophagy," he says.
"Circulating decorin represents a fundamental cellular process that acts to combat tumor angiogenesis," Dr. Iozzo says. "Treatment based on systemic delivery of decorin may represent a genuine advance in our ongoing war against cancer."
The study was funded by the National Institutes of Health grants R01 CA39481, R01 CA47282, and R01 CA120975.
Collaborating researchers from LifeCell Corporation, in Branchburg, New Jersey, and Goethe University in Frankfurt, Germany, also contributed to the study.