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Recombinant Human MIC-1 / NAG-1 / GDF-15:
Scientific Background and Collaboration Opportunity

Scientific Background
Macrophage inhibitory cytokine 1 (MIC-1), also known as non-steroidal anti-inflammatory drugs (NSAIDs) activated gene (NAG-1), growth differentiation factor 15 (GDF-15), prostate differentiation factor (PDF), or placental bone morphogenetic protein (PLAB), is a member of the transforming growth factor beta (TGF-beta) super-family. MIC-1, like most members of the TGF-beta family, is a multifunctional growth factor. The nature of its effects depends on the cellular context and cell type. It has been found to play a role in the regulation and repair of some organs, including the heart and lungs. Also, it has been observed that it responds to differing levels of iron in the blood. Besides that, it has been discovered to participate in appetite control and adipose tissue modulation. Moreover, it has been found to be involved in cellular processes such as inflammation, apoptosis, and tumorigenesis. Differing levels of MIC-1 have been observed in dozens of cancer types. Here is a look at some of MIC-1 potential therapeutic or diagnostics applications.

Therapeutic Potential: Identifying and Treating Cancer

Cancer Type

MIC-1 Effect

Result

Breast

Elevated levels of MIC-1 in breast cancer cells.

There is an over expression of MIC-1 in tumors compared to normal tissues. MIC-1 also increased the ERK1 phosphorylation.1

Cervical

Elevated levels of MIC-1 in cervical cancer.

MIC-1 is a potential biomarker of cervical cancer progression as it is over expressed.2

Glioblastoma

Elevated levels of MIC-1 in CSF.

 

TSA induced MIC-1 expression which induced apoptosis.

There is a heightened level of MIC-1 in both the glioblastoma cells 3 as well as in the cerebro spinal fluid (CSF), but not in the plasma. Moreover, increased CSF MIC-1 levels corresponded to shorter survival.4

Another study examined how the addition of trichostatin A (TSA) would affect MIC-1. TSA up-regulated MIC-1 expression and indirectly increased MIC-1 promoter activity. Furthermore, interfering RNA experiments link MIC-1 expression to apoptosis induced by TSA.5

Colorectal Carcinoma (CRC)

Elevated levels of serum MIC-1 levels in CRC.

 

 

AST caused expression of MIC-1, leading to apoptosis.

 

Anisomycin induced MIC-1 gene expression which took part in apoptosis.

MIC-1 is up-regulated in colorectal cancers as well as premalignant adenomas. There is a progressive increase in serum MIC-1 levels between control group, adenomatous polyps group, and CRC group. Moreover, serum MIC-1 levels correlated positively with the extent of the disease.6

Astragalus saponins (AST) caused over expression of MIC-1, leading to PARP cleavage and apoptosis. Furthermore, PI3K or Akt inhibitors intensified AST induced MIC-1 activation.7

Anisomycin induced MIC-1 gene expression which was involved in the ribotoxin induced apoptotic pathway. MIC-1 was induced apoptosis related gene products like urokine type plasminogen activator and its receptor.8

Pancreatic

Elevated levels of serum MIC-1 in cancer cells.

 

 

CDODA-Me induced MIC-1 and induces apoptosis in pancreatic cancer lines

Serum MIC-1 levels were higher in patients with pancreatic adenocarcinoma, ampullary carcinoma, and cholangiocellular carcinomas compared to benign pancreatic neoplasms and chronic pancreatitis, which in turn were higher than the healthy controls.9

CDODA-Me induces apoptosis in Panc1 and Panc28 cells. It also induced proapoptotic proteins MIC-1, Egr-1, and ATF-3.10

Gastric

Elevated levels of MIC-1 in gastric cancers.

 

MIC-1 inhibits gastrointestinal tumorigenesis.

In SNU620 cells, MIC-1 levels were tenfold higher in cancer patients than in healthy controls. Moreover, MIC-1 expression increased in metastatic gastric cancers.11
    
However, in a different study it was found that MIC-1 expression stronger in intestinal metaplasia and adenoma than normal gastric epithelium. Moreover, MIC-1 expression was weaker in gastric cancer than normal gastric tissue, with MIC-1 expression being inversely correlated with tumor strength, with about 50% of T3 tumors lacking MIC-1 expression.12

In another study MIC-1 was given to transgenic mice to study the effect of MIC-1 on urethane induced pulmonary lesions. The MIC-1 mice had only pulmonary adenomas as compare to both adenomas and adenocarcinomas for the control nice. Moreover, the MIC-1 mice had fewer tumors and the tumors were smaller in size. There was significantly more apoptosis observed in the MIC-1 mice. As importantly, there were fewer inflammatory cells observed in the lung tissue of the MIC-1 mice than the control mice.13

Prostate

MIC-1 is induced by chemotherapy but contributes to tumor cell resistance.

 

MIC-1 prostate cancer cells in bone induce osteoclasts.

Chemotherapy using docetaxel and mitoxantrone with MIC-1 present in prostate cancer cells resulted in resistance to the chemotherapy. MIC-1 was either over expressed due to the chemotherapy or recombinant MIC-1 was added to the cancer cells.14

A second study observed that MIC-1 in prostate cancer cells that grow in bone induce osteoclast formation and cachexia in the mice. Bone formation was significantly higher in the control mice, but the tumors were significantly smaller in the MIC-1 mice.15

Melanoma

Elevated levels of MIC-1 in melanomas, especially metastatic melanomas.

MIC-1 is highly expressed in melanoma cells. Moreover, metastatic melanomas have an even stronger expression of MIC-1. Knockdown of MIC-1 expression showed a decrease in tumorigenicity.16

Therapeutic Potential: Cardiovascular Diseases


Cardiovascular Event

MIC-1 Effect

Iron Regulation

MIC-1 is strongly up regulated by the depletion of iron and that response is reversed with the addition of iron. Moreover, MIC-1 is more sensitive than hypoxia to iron depletion and MIC-1 is independent of hypoxia inducible factor and iron regulatory proteins.17

Thalassemia

Serum MIC-1 levels in Thalassemia patents are significantly higher than in healthy control. The MIC-1 over expression suppresses hepcidin and contributes to the iron overload.18

Congenital Dyserythropoietic Anemia (CDA)

CDA patients express significantly higher levels of MIC-1 compare to control and contribute to the suppression of hepcidin.19

Hypertrophy

MIC-1 enhanced cardiac hypertrophic growth following pressure overload stimulation, demonstrating a loss in ventricular performance whereas control group maintained function.20

Ischemia / Reperfusion Protection

Induction of MIC-1 in the heart protects the heart from ischemia / reperfusion (I/R) injury by preventing apoptosis of cardiomyocytes.21

Dyspnea

A significant difference between the MIC-1 average value for individuals with cardiogenic dyspnea compared to non-cardiogenic dyspnea.23

Idiopathic Pulmonary Arterial Hypertension

MIC-1 is an independent predictor of adverse outcomes of idiopathic pulmonary arterial hypertension.23

ST-Segment Elevation Myocardial Infarction (STEMI)

MIC-1 provides prognostic information and can be an independent biomarker in STEMI.24

Chronic Heart Failure (CHF)

MIC-1 is an independent predictor of mortality and can be used as a biomarker of the risk of death in patients with CHF.25

Cardiovascular (CV)

MIC-1 carries information on CV dysfunction and disease that is not captured by traditional CV risk factors in elderly individuals.26

 

 
Therapeutic Potential: Other


Application

MIC-1 Effect

Identifying Rheumatoid Arthritis (RA)

Serum MIC-1 levels were higher in all RA patients compared to controls and reflected disease severity independently of classic RA markers. Furthermore, allelic variation of MIC-1 were linked with earlier severe treatment resistant chronic RA and with algorithms including the serum MIC-1 levels could predict response to hemopoietic stem cell transplant and the severity of the disease.27

Organ repair and regulation

MIC-1 was induced after surgical, toxic, ischemic, and hyperoxic kidney or lung injuries. Moreover, MIC-1 induction was independent of protein synthesis.28 The same lab further demonstrated that MIC-1 was induced in diseased livers.29

Granule Cells

Cerebellar granule neurons (CGN) survive in a high potassium environment but undergo apoptosis in a when switched to low potassium environment. MIC-1 prevents cell death at low potassium environment.30

Weight control in cancer patients

There is a direct relationship between MIC-1 and cancer associated weight loss. MIC-1 is a regulator of appetite and a major factor in cancer cachexia.31

Obesity

While increased MIC-1 levels induce weight loss in cancer patients, it does not induce weight loss in obese or diabetic patients. Diabetic patients have higher serum MIC-1 levels than the obese group, which in turn had higher serum MIC-1 levels than the control group.32

Dermal response to light

MIC-1 was the most prominently gene induced by blue or near UV light but not green or red light in the human dermis. Both mRNA and protein levels of MIC-1 were up regulated by the short wavelength light.33

Collaboration Opportunity
SBH Sciences human GDF-15/MIC-1 is a soluble disulfide linked homodimeric protein consisting of two 114 amino-acid polypeptide chains (25,000 MW).

SBH Sciences is offering highly pure naturally expressed human MIC-1. We are the producer of this product that is already available for the R&D market.

SBH Sciences is looking for partners to investigate human MIC-1 as therapeutic agent, as well as a diagnostic tool.

We are open for suggestions and would be pleased to hear from you.

 

References:

1. Wollmann W et al, Carcinogenesis, 26(5) 900-7, May 2005

2. Wan F et al, International Journal of Cancer, 123(1) 32-40, Jul 1, 2008

3. Strelau J et al, Cancer Letters, 270(1) 30-9, Oct 19, 2008

4. Shnaper S et al, International Journal of Cancer, Jun 11, 2009

5. Yoshioka H, Eling TE et al, The Journal of Biological Chemistry, 283(48) 33129-37,
     Nov 28, 2008

6. Brown DA et al, Clinical Cancer Research, 9(7) 2642-50, Jul 2003

7. Auyeung KK et al, International Journal of Cancer, 125(5) 1082-91, Feb 27, 2009

8. Yang H et al, Biochemical Pharmacology, Jun 18, 2009

9. Koopmann J et al, Clinical Cancer Research, 10(7) 2386-92, Apr 1,  2004

10. Jutooru I et al, Molecular Carcinogenesis, 48(8) 692-702, Jan 5,  2009

11. Baek KE et al, Clinica Chimica Acta, 401(1-2) 128-33, Mar 2009

12. Park JY et al, Journal of Cancer Research and Clinical Oncology, 134(9) 1029-35,
      Sep 2008

13. Cekanova M, Eling TE et al, Cancer Prevention Research, 2(5) 450-8, May 2009

14. Huang CY et al, Clinical Cancer Research, 13(19) 5825-33, Oct 1,  2007

15. Wakchoure S et al, The Prostate, 69(6) 652-61, May 1,  2009

16. Boyle GM et al, The Journal of Investigative Dermatology, 129(2) 383-91, Feb 2009

17. Lakhal S et al, Blood, 113(7) 1555-63, Feb 12 2009

18. Tanno T, Eling TE et al, Nature Medicine, 13(9) 1096-101 Sep 2007

19. Tamary H et al, Blood, 112(13) 5241-4, Dec 15, 2008

20. Xu J et al, Circulation Research, 98(3) 342-50, Feb 17, 2006

21. Kempf T et al, Circulation Research, 98(3) 251-60, Feb 17, 2006

22. Stejskal D et al, Clinical Biochemistry, Mar 31, 2009

23. Nickel N et al, American Journal of Respiratory and Critical Care Medicine, 178(5) 534-41,
     Sep 1,  2008

24. Kempf T et al, European Heart Journal, 28(23) 2858-65, Dec 2007

25. Kempf T et al, Journal of the American College of Cardiology, 50(11) 1054-60,
      Sep 11, 2007

26. Lind L et al, European Heart Journal, Jun 26, 2009

27. Brown DA et al, Arthritis and Rheumatism, 56(3) 753-64, Mar 2007

28. Zimmers TA et al, Shock, 23(6) 543-8, Jun 2005

29. Zimmers TA et al, The Journal of Surgical Research, 130(1) 45-51, Jan 2006

30. Subramaniam S et al, The Journal of Biological Chemistry, 278(11) 8904-12,
      Mar 14, 2003

31. Johnen H et al, Nature Medicine, 13(11) 1333-40, Nov 2007

32. Dostalova I et al, European Journal of Endocrinology, Jun 10, 2009

33. Akiyama M et al, FEBS Letters, 583(5) 933-7, Mar 4, 2009

Note:  #4, #8, #22, #26, #32 already accepted to be published.



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