06 December, 2011

Interesting article!

High normal HbA1C is a strong predictor of type 2 Diabetes in general population


30 August, 2011


Linagliptin is an inhibitor of DPP-4, an enzyme that degrades the incretin hormones glucagon-like peptide-1 (GLP-1) and glucose-dependent insulinotropic polypeptide (GIP). Both GLP-1 and GIP increase insulin biosynthesis and secretion from pancreatic beta cells in the presence of normal and elevated blood glucose levels. GLP-1 also reduces glucagon secretion from pancreatic alpha cells, resulting in a reduction in hepatic glucose output. Thus, linagliptin stimulates the release of insulin in a glucose-dependent manner and decreases the levels of glucagon in the circulation

28 May, 2011


International association for medical assiatance to travellers


To convert Insulin readings:-
Divide pmol/L by 6.945 to get µIU/mL
Multiply µIU/mL by 6.945 to get pmol/L

To convert Iron (total ) readings:-
Divide µmol/L by 0.179 to get µg/dL
Multiply µg/dL by 0.179 to get µmol/L

To convert LDL and HDL readings:-
Divide the mg/dL by 38.67 to get mmol/L.
Multiply the mmol/L by 38.67 to get mg/dL.
Divide the mmol/L by 0.0259 to get mg/dL
Multiply the mg/dL by 0.0259 to get mmol/

To convert Magnesium readings:-
Divide the µg/dl by 5.494 to get µmol/L
Multiply the µmol/L by 5.494 to get µg/dl

To convert Potassium readings:-
Divide the mEq/l by 1 to get mmol/L.
Multiply the mmol/L by 1 to get mEq/l. This is therefore a 1-1 conversion. (The two are the same!)

To convert Protein (serum total) readings:-
Divide g/dl by 0.1000 to get g/L
Multiply g/L by 0.1000 to get g/dl
Divide g/L by 10.0 to get g/dL
Multiply g/dL by 10.0 to get g/L
To convert Protein (urine/fluid total) readings:-
Divide mg/dl by 0.1000 to get mg/L
Multiply mg/L by 0.1000 to get mg/dl

To convert the Reticulocyte count readings:-
Conventional units use ‘% of RBCs’
SI units use ‘Proportion of 1.0’
Divide ‘Proportion of 1.0’ by 0.01 to get ‘% of RBCs’
Multiply ‘% of RBCs’ by 0.01 to get ‘Proportion of 1.0’

To convert Selenium readings:-
Divide the µg/dl by 7.896 to get µmol/L
Multiply the µmol/L by 7.896 to get µg/dl

To convert Serum Magnesium readings:-
Divide mmol/L by 0.411 to get mg/dl
Multiply mg/dL by 0.411 to get mmol/L
Divide the mg/dl by 2,430 to get mmol/L
Multiply the mmol/L by 2.430 to get mg/dl
Or if your results are given in mEq/L then:-
Divide mmol/L by o.5o to get mEq/L
Multiply mEq/L by 0.50 to get mmol/L
Divide mEq/L by 2.0 to get mmol/L
Multiply mmol/L by 2.0 to get mEq/L

To convert Serum Zinc readings:-
Divide the µg/dl by 6.541 to get µmol/L
Multiply the µmol/L by 6.541 to get µg/dl.
Divide µmol/L by 0.153 to get µg/dL
Multiply the µg/dL by 0.153 to get µmol/L

To convert Sodium readings:-
Divide the mEq/l by 1 to get mmol/L.
Multiply the mmol/L by 1 to get mEq/l. This is therefore a 1-1 conversion. (The two are the same!)

To convert Thyroxine, free (T4) readings:-
Divide pmol/L by 12.87 to get ng/dL (nanograms per decilitre)
Multiply ng/dL by 12.87 to get pmol/L (picomoles per litre)
To convert Thyroxine, total (T4) readings:-
Divide nmol/L by 12.87 to get µg/dL
Multiply µg/dL by 12.87 to get nmol/L
To convert Total Cholesterol readings:-
Divide the mmol/L by 0.0259 to get mg/dL
Multiply the mg/dL by 0.0259 to get mmol/L
To convert Triiodothyronine free (T3) readings:-
Divide pmol/L by 0.0154 to get pg/dL
Multiply pg/dL by 0.0154 to get pmol/L

To convert Triiodothyronine total (T3) readings:-
Divide nmol/L by 0.0154 to get ng/dL
Multiply ng/dL by 0.0154 to get nmol/L

To convert Triglyceride readings:-
Divide the mg/dL by 88.57 to get mmol/L.
Multiply the mmol/L by 88.57 to get mg/dL.
Divide mmol/L by 0.0113 to get mg/dL
Multiply mg/dL by 0.0113 to get mmol/L

To convert Urea Nitrogen (BUN) readings:-
Divide mmol/L by 0.357 to get mg/dL
Multiply mg/dL by 0.357 to get mmol/L

To convert Uric Acid readings:-
Divide µmol/L by 59.48 to get mg/dL
Multiply mg/dL by 59.48 to get µmol/L

To convert Vitamin A (retinol) readings:-
Divide µmol/L by 0.0349 to get µg/dL
Multiply µg/dL by 0.0349 to get µmol/L

To convert Vitamin B6 (pyridoxine) readings:-
Divide nmol/L by 4.046 to get ng/mL
Multiply ng/mL by 4.046 to get nmol/L

To convert Vitamin B12 (cyanocobalamin) readings:-
Divide pmol/L by 0.738 to get pg/mL
Multiply pg/mL by 0.738 to get pmol/L

To convert Vitamin C (ascorbic acid) readings:-
Divide µmol/L by 56.78 to get mg/dL
Multiply mg/dL by 56.78 to get µmol/L

To convert Vitamin D readings:-
a)1,25-Dihydroxyvitamin D
Divide pmol/L by 2.6 to get pg/mL
Multiply pg/mL by 2.6 to get pmol/L
b)25-Hydroxyvitamin D readings:-
Divide nmol/L by 2.496 to get ng/mL
Multiply ng/mL by 2.496 to get nmol/L

To convert Vitamin E readings:-
Divide µmol/L by 23.22 to get mg/dL
Multiply mg/dL by 23.22 to get µmol/L

To convert Vitamin K readings:-
Divide nmol/L by 2.22 to get ng/mL
Multiply ng/mL by 2.22 to get nmol/L


U/L stands for units per litre
mIU/1 stand for milli International Units/litre
Sometimes the conventional units are given in g/L instead of g/dl. If that is the case do the following conversion first.
Divide g/L by 10.0 to get g/dL
Multiply g/dL by 10.0 to get g/L.

To convert Acetoacetic acid readings:-
Divide mmol/L by 0.098 to get mg/dL
Multiply mg/dL by 0.098 to get mmol/L

To convert Acetone readings:-
Divide mmol/L by 0.172 to get mg/dL
Multiply mg/dL by 0.172 to get mmol/L

To convert Albumin readings:-
Divide the g/L by 10 to get g/dL.
Multiply the g/dL by 10 to get g/L.

To convert Bilirubin readings: -
Divide the mol/L by 17.1 to get mg/dl.
Multiply the mg/dl by 17.1 to get mol/L.

In the red blood cell, white blood cell and platelet count, because of the different units being used, the two readings are identical and don’t actually need conversion. If you want to do the maths yourself (Multiply or divide by 1) the factors are as set out below.

To convert Red blood cell count readings:- (see note above)
Conventional units use ‘cells x 10*6/µL’
SI units use ‘cells x 10*12/L’
Divide ‘cells x 10*12/L’ by 1.0 to get ‘cells x 10*6/µL’
Multiply ‘cells x 10*6/µL’ by 1.0 to get ‘cells x 10*12/L’
To convert White blood cell count readings:- (see note above)
Conventional units use ‘cells x 10*3/µL’
SI units use ‘cells x 10*9/L’
Divide ‘cells x 10*9/L’ by 1.0 to get ‘cells x 10*3/µL’
Multiply ‘cells x 10*3/µL’ by 1.0 to get ‘cells x 10*9/L’
To convert Platelets (thrombocytes) readings: - (see note above)
Conventional units use ‘number of platelets x 10*3/µL’
SI units use ‘number of platelets x 10*9/L’
Divide ‘number of platelets x 10*9/L’ by 1.0 to get ‘number of platelets x 10*3/µL’
Multiply ‘number of platelets x 10*3/µL’ by 1.0 to get ‘number of platelets x 10*9/L’

To convert Blood Glucose readings:-
Divide the mg/dL by 18 to get mmol/L.
Multiply the mmol/L by 18 to get mg/dL.
Divide the mmol/L by 0.0555 to get mg/dL
Multiply the mg/dL by 0.0555 to get mmol/L

To convert BUN readings:-
Divide the mmol/L by 0.357 to get mg/dL.
Multiply the mg/dL by 0.357 to mmol/L.

To convert Bromide readings:-
Divide mmol/L by 0.125 to get mg/dL
Multiply mg/dL by 0.125 to get mmol/L

To convert Calcium readings:-
Divide mmol/L by 0.25 to get mg/dL
Multiply mg/dL by 0.25 to get mmol/L
Divide mmol/L by 0.05 to get mEq/L
Multiply mEq/L by 0.05 to get mmol/L

To convert Total Cholesterol readings:-
Divide the mmol/L by 0.0259 to get mg/dL
Multiply the mg/dL by 0.0259 to get mmol/L
To convert HDL and LDL readings:-
Divide the mg/dL by 38.67 to get mmol/L.
Multiply the mmol/L by 38.67 to get mg/dL.
Divide the mmol/L by 0.0259 to get mg/dL
Multiply the mg/dL by 0.0259 to get mmol/

To convert Copper readings:-
Divide µmol/L by 0.157 to get µg/dL
Multiply µg/dL by 0.157 to get µmol/L

To convert Cortisol readings:-
Divide nmol/L by 27.95 to get µg/dL
Multiply µg/dL by 27.95 to get nmol/L (nanomoles per litre)

To convert C-peptide readings:-
Divide the nmol/L by 0.333 to get ng/mL.
Multiply the ng/mL by 0.333 to get nmol/L

To convert Creatine readings:-
Divide mol/L by 76.26 to get mg/dL
Multiply mg/dL by 76.26 to get mol/L.

To convert Creatinine readings:-
Divide the mol/L by 88.4 to get mg/dL.
Multiply the mg/dL by 88.4 to get mol/L.

To convert Creatinine clearance readings:-
Divide the ml/s by 0.0167 to get ml/min.
Multiply the ml/min L by 0.0167 to get ml/s.

To convert degrees C to degrees F
Take the degrees C, multiply by 9. Divide the answer by 5. Add 32. That will give you your degrees F.
Eg. 37 x 9 = 333.
333 / 5 = 66.6.
66.6 + 32 = 98.6 degrees F
(Therefore 37 deg C equals 98.6 deg F)
To convert degrees F to degrees C
Take the degrees F, minus 32, divide the answer by 9, multiply that answer by 5.That will give you your degrees C.
Eg. 98.6 - 32 = 66.6
66.6 / 9 = 7.4
7.4 x 5 = 37 degrees C

To convert Fluoride readings:-
Divide µmol/L by 52.6 to get µg/mL
Multiply µg/mL by 52.6 to get µmol/L

To convert Glycated haemoglobin (glycosylated hemoglobin A1, A1C)
Conventional units use term - % of total hemoglobin
SI units use term - proportion of total haemoglobin
Divide ‘proportion of total haemoglobin’ by 0.01 to get ‘% of total hemoglobin’.
Multiply ‘% of total hemoglobin’ by 0.01 to get ‘proportion of total haemoglobin’

To convert Haemoglobin readings:- (See Note below)
Divide mmol/L by 0.6206 to get g/dl
Multiply g/dl by 0.6206 to get mmol/L
Note -
Sometimes the conventional units are given in g/L instead of g/dl. If that is the case do the following conversion first.
Divide g/L by 10.0 to get g/dL
Multiply g/dL by 10.0 to get g/L.
To convert Hematocrit readings:-
Conventional units use %
SI units use ‘proportion of 1.0’
Divide ‘proportion of 1.0’ by 0.01 to get %
Multiply % by 0.01 to get ‘proportion of 1.0’


1. Chronic pancreatitis.
This occurs when digestive enzymes attack and destroy the pancreas.
The main causes of chronic pancreatitis are alcoholism, blocked or narrowed pancreatic duct due to some form of trauma or cyst, and heredity. Occasionally no reason can be found.

2. Hemochromatosis.
A genetic disorder that causes the body to absorb excess iron from food.
The excess iron builds up in the cells of the liver, heart, pancreas, and other organs and eventually destroys them.

3. Polycystic ovary syndrome. (PCOS)
Polycystic ovary syndrome is a complex condition that affects the ovaries. The ovarian cysts inhibit the natural female hormones, which eventually leads to insulin resistance.

4. Cushing's disease.
This is a hormonal disorder caused by prolonged exposure of the body's tissues to high levels of the hormone cortisol spontaneously produced by the adrenals or by excessive use of cortisol or other similar steroid hormones. The latter may be used to treat life threatening disease such as asthma, rheumatoid arthritis, systemic lupus, inflammatory bowel disease, some allergies etc.

5. Acromegaly.
Rare hormone disorder resulting from over production of growth hormone by the pituitary gland, usually due to a tumour on that gland. It most commonly affects middle-aged adults.

6. Somatostatinoma and Aldosteronoma-induced hypokalaemia.
Rare conditions caused by pancreatic tumours that can cause diabetes, at least in part by inhibiting insulin secretion. Successful removal of the tumour can cause the diabetes to disappear.

7. Cystic Fibrosis.
Cystic Fibrosis is a genetic disease. CF causes the incapacitation of the pancreas by fibrosis and can lead to Type 2 diabetes.

8. Adenocarcinomas.
Cancer that begins in cells that line the inside of organs. Almost all pancreatic cancers are of this type.

9. The stiff-man syndrome.
An autoimmune disorder of the central nervous system characterised by stiffness of the axial muscles (the skeletal muscles of the head and trunk) with painful spasms. Patients usually have Glutamic Acid Decarboxylase (GAD) antibodies and many develop Type 1 diabetes.

10. Wolfram's syndrome.
A rare autosomal recessive disorder (due to a mutated gene) characterised by diabetes mellitus, diabetes insipidus, optic atrophy (eye problems), and deafness.

11. Rabson-Mendenhall syndrome.
An extremely rare pediatric genetic disorder caused by a mutation in the insulin receptor gene. It results in severe insulin resistance.
Initial symptoms include abnormalities of the head, face, teeth and nails. Also Acanthosis nigricans, a skin disorder where the skin becomes dark in colour and velvety in texture, especially in the folds of the neck, groin and underarms.

12. Leprechaunism.
A rare pediatric genetic disorder that is associated with extreme insulin resistance. It leads to mental and physical retardation, coarse features, Acanthosis nigricans and early death.

13. Phaeochromocytoma.
A rare tumour found in the adrenal glands. It causes an excess of adrenaline to be produced. The diabetes associated with this will go away once the tumour has been removed.

14. Glucagonoma.
A rare pancreatic tumour. Malignant glucagonomas are islet cell pancreatic tumours. Insulin can be over produced, leading to diabetes.

15. Toxins.
Certain toxins, like Vacor (a rat poison), can permanently destroy pancreatic beta cells, leaving one with a Type 1 diabetes.

16. Infections.
Certain viral infections have resulted in the destruction of beta cells. Examples are congenital rubella, cytomegalovirus, and adenovirus and mumps.

17. Drugs. (chemically induced diabetes)
Pentamidine (treats some forms of pneumonia and parasitic infections)
Nicotinic acid
Glucocorticoids (used as anti-inflammatories)
Thyroid hormone
Alpha-blockers (used to treat blood-pressure)
Beta-blockers (used to treat blood-pressure)
Thiazides (used in blood-pressure control)
Furosemide (a diuretic, used in blood pressure control)
Dilantin (a drug used to treat epilipsy)
Estrogen-containing products (such as oral contraceptives and hormone replacement therapy)
Interferon-alpha therapy (Patients can develop diabetes associated with islet cell auto-antibodies and, in certain instances, severe insulin deficiency)

18. Insulin-receptor disorders.
Anti-insulin receptor antibodies are occasionally found in patients with systemic lupus erythematosus and other autoimmune diseases. They bind to the insulin receptor and so reducing the binding of insulin.

19. Insulin autoimmune syndrome.
The person has antibodies against insulin. This rare disease was first reported in 1970 and of the 200 cases so far 90% come from Japan.

20. Diseases of the pancreas such as:-
Fibrocalculous pancreatopathy.
Trauma / pancreatectomy.

21 May, 2011

Useful Websites


Air Travel & Diabetes

Make sure all medication has the proper labels with the name that matches the passenger’s ticket
Give yourself enough time to check in and board the plane. Anticipate that you will be stopped, searched, and possibly questioned about your diabetes supplies. As stress can affect your diabetes, give yourself enough time to comfortably navigate security checkpoints.
Be prepared with a prescription from your doctor for every diabetes supply you may be carrying. Again, make sure that the prescription name matches the one on your ticket.
Make sure you bring syringes and vials of insulin in their original packaging and with a prescription. Even if you use an insulin pump, be sure to bring back-up insulin and syringes.
Don’t panic if your insulin cannot be refrigerated for the flight. It will last in room temperature for up to several weeks.
If you need to bring extra diabetes supplies that are in excess of the amount allowed in your carry on, be sure to pack them in your checked luggage. Since checked baggage may be subjected to cold temperatures, be sure to carefully insulate any insulin bottles. Inspect the insulin after you arrive for crystallization or cloudiness. If you suspect that the insulin may be spoiled, discard the bottle and do not use it.

20 May, 2011

Detemir structure!!

08 May, 2011

conditions associated with obesity

Abdominal obesity
Acanthosis nigricans
Bardet–Biedl syndrome
Blood sugar regulation
Burnt-out diabetes mellitus
Combined hyperlipidemia
Diabetes mellitus
Diabetes mellitus type 2
Diseases of affluence (coronary heart disease, cerebrovascular disease, peripheral vascular disease, certain forms of cancer, asthma, alcoholism, gout, allergies and depression,
Essential hypertension
Fatty liver
Gastroesophageal reflux disease
Genu valgum
Infertility in polycystic ovary syndrome
Metabolic syndrome
Muscle atrophy
Non-ketonic hyperglycemic coma
Obesity hypoventilation syndrome
Obstructive sleep apnea
Pelvic lipomatosis
Polycystic ovary syndrome
Portal-visceral hypothesis
Prader–Willi syndrome
Stretch marks
Varicose veins


Fatty liver, also known as fatty liver disease (FLD), is a reversible condition where large vacuoles of triglyceride fat accumulate in liver cells via the process of steatosis (i.e. abnormal retention of lipids within a cell). Despite having multiple causes, fatty liver can be considered a single disease that occurs worldwide in those with excessive alcohol intake and those who are obese (with or without effects of insulin resistance). The condition is also associated with other diseases that influence fat metabolism. Morphologically it is difficult to distinguish alcoholic FLD from non alcoholic FLD and both show micro-vesicular and macrovesicular fatty changes at different stages.
Accumulation of fat may also be accompanied by a progressive inflammation of the liver (hepatitis), called steatohepatitis. By considering the contribution by alcohol, fatty liver may be termed alcoholic steatosis or non-alcoholic fatty liver disease (NAFLD), and the more severe forms as alcoholic steatohepatitis (part of alcoholic liver disease) and non-alcoholic steatohepatitis (NASH).

Fatty liver is commonly associated with alcohol or metabolic syndrome (diabetes, hypertension, obesity and dyslipidemia) but can also be due to any one of many causes
Metabolic causes
Abetalipoproteinemia, glycogen storage diseases, Weber-Christian disease, acute fatty liver of pregnancy, lipodystrophy
Nutritional causes
Malnutrition, total parenteral nutrition, severe weight loss, refeeding syndrome, jejuno-ileal bypass, gastric bypass, jejunal diverticulosis with bacterial overgrowth
Drugs and toxins
Amiodarone, methotrexate, diltiazem, highly active antiretroviral therapy, glucocorticoids, tamoxifen, environmental hepatotoxins (e.g., phosphorus, mushroom poisoning)
Inflammatory bowel disease, HIV, Hepatitis C especially genotype 3, and Alpha 1-antitrypsin deficiency

know ur glucose level by looking into ur eyes!!

The body can be a confusing place, and when you’re ill sometimes you just wish you could see what the problem is. For diabetics, that wish may be coming true. Professor Jin Zhang at the University of Western Ontario has developed contact lenses that would change color as the user’s glucose levels varied. The new device is made by embedding nanoparticles into standard hydrogel. These particles react with glucose in the tears and change color. The colour change is slight, but it could alert diabetics to dangerous sugar levels without the need for regular blood tests. According to the University’s News site.
While it could be very useful for diaetes in theory, the nanoparticle embedding process is probably going to find better applications outside of medicine. Passive monitoring through a contact lens, while ingenious, doesn’t seem like the most economic approach. And we’ve already seen how stem cell treatments, or implants, are likely to help fight or even cure diabetes in the future.

World diabetes day

World Diabetes Day is the primary global awareness campaign of the diabetes mellitus world and is held on November 14 of each year. It was introduced in 1991 by the International Diabetes Federation and the World Health Organization in response to the alarming rise of diabetes around the world. World Diabetes Day is a campaign that features a new theme chosen by the International Diabetes Federation each year to address issues facing the global diabetes community. While the campaigns last the whole year, the day itself marks the birthday of Frederick Banting who, along with Charles Best, first conceived the idea which led to the discovery of insulin in 1922.
Each year, World Diabetes Day is centred on a theme related to diabetes. Topics covered have included diabetes and human rights, diabetes and lifestyle, diabetes and obesity, diabetes in the disadvantaged and the vulnerable, and diabetes in children and adolescents.
For 2009–2013, the theme is Diabetes Education and Prevention.


Glycated hemoglobin (glycosylated hemoglobin, hemoglobin A1c, HbA1c, A1C, or Hb1c; sometimes also HbA1c) is a form of hemoglobin which is measured primarily to identify the average plasma glucose concentration over prolonged periods of time. It is formed in a non-enzymatic glycation pathway by hemoglobin's exposure to plasma glucose. Normal levels of glucose produce a normal amount of glycated hemoglobin. As the average amount of plasma glucose increases, the fraction of glycated hemoglobin increases in a predictable way. This serves as a marker for average blood glucose levels over the previous months prior to the measurement.
In diabetes mellitus, higher amounts of glycated hemoglobin, indicating poorer control of blood glucose levels, have been associated with cardiovascular disease, nephropathy, and retinopathy.

In the normal 120-day lifespan of the red blood cell, glucose molecules react with hemoglobin, forming glycated hemoglobin. In individuals with poorly controlled diabetes, the quantities of these glycated hemoglobins are much higher than in healthy people.
Once a hemoglobin molecule is glycated, it remains that way. A buildup of glycated hemoglobin within the red cell, therefore, reflects the average level of glucose to which the cell has been exposed during its life-cycle. Measuring glycated hemoglobin assesses the effectiveness of therapy by monitoring long-term serum glucose regulation. The HbA1c level is proportional to average blood glucose concentration over the previous four weeks to three months. Some researchers state that the major proportion of its value is related to a rather shorter period of two to four weeks.


Hemoglobin A1c was first separated from other forms of hemoglobin by Huisman and Meyering in 1958 using a chromatographic column. It was first characterized as a glycoprotein by Bookchin and Gallop in 1968. Its increase in diabetes was first described in 1969 by Samuel Rahbar et. Al. The reactions leading to its formation were characterized by Bunn and his co-workers in 1975.The use of hemoglobin A1c for monitoring the degree of control of glucose metabolism in diabetic patients was proposed in 1976 by Anthony Cerami, Ronald Koenig and coworkers.

03 May, 2011

Liposuction - Do we lose or gain??

A new study has revealed that the fat removed by liposuction returns and gets “redistributed upstairs” – around the shoulders, arms and upper abdomen after a year.
Rudolph Leibel, an obesity researcher at the University of Columbia, told the New York Times that the body controls the number of fat cells as carefully as it controls the amount of fat. When a fat cell dies, it grows a new one to replace it.
Liposuction, however, surgically destroys the fishnet structure under the skin, which may be why the fat cells don’t regrow in the place from which they were removed. The body compensates for their loss by growing fat cells in other areas.
“It’s another chapter in the ‘You can’t fool Mother Nature’ story,” Leibel said.
The study involved 32 women aged in their midthirties and of average weight. Under half (14) had a small amount of fat removed by liposuction from hips and thighs, while the remainder (18) acted as controls.
Identical measurements of all the women were carried out at six weeks, six months and a year, which revealed how the body “defends” its fat.
After six weeks the treated patients had lost 2.1% of their fat, compared to 0.28% in the control group, but this difference had disappeared at one year.
Though the women’s thighs remained thinner after a year, the missing fat had found its way back to their stomachs. The study was recently published in the journal Obesity.
courtesy - TOI

29 April, 2011

What do you ppl wanna see next??

hi everybody!! i have posted topics which i can think of.. suggest me some topics which you would like to see on this blog..

10 March, 2011


Kidney function

GFR is best measured by injecting compounds such as inulin, radioisotopes such as 51chromium-EDTA, 125I-iothalamate, 99mTc-DTPA or radiocontrast agents such as iohexol, but these techniques are complicated, costly, time-consuming and have potential side-effects. Creatinine is the most widely used biomarker of kidney function. It is inaccurate at detecting mild renal impairment, and levels can vary with muscle mass and protein intake. Formulas such as the Cockcroft and Gault formula and the MDRD formula try to adjust for these variables.
Cystatin C has a low molecular weight (approximately 13.3 kilodaltons), and it is removed from the bloodstream by glomerular filtration in the kidneys. If kidney function and glomerular filtration rate decline, the blood levels of cystatin C rise. Serum levels of cystatin C are a more precise test of kidney function (as represented by the glomerular filtration rate, GFR) than serum creatinine levels. This finding is based mainly on cross-sectional studies (on a single point in time). Longitudinal studies (that follow cystatin C over time) are scarcer; some studies show promising results. Cystatin C levels are less dependent on age, sex, race and muscle mass compared to creatinine. Cystatin C measurements alone have not been shown to be superior to formula-adjusted estimations of kidney function. As opposed to previous claims, cystatin C has been found to be influenced by body composition. It has been suggested that cystatin C might predict the risk of developing chronic kidney disease, thereby signaling a state of 'preclinical' kidney dysfunction.
Studies have also investigated cystatin C as a marker of kidney function in the adjustment of medication dosages.
Cystatin C levels have been reported to be altered in patients with cancer, (even subtle) thyroid dysfunction and glucocorticoid therapy in some but not all[ situations. Other reports have found that levels are influenced by cigarette smoking and levels of C-reactive protein. Levels seem to be increased in HIV infection, which might or might not reflect actual renal dysfunction. The role of cystatin C to monitor GFR during pregnancy remains controversial. Like creatinine, the elimination of cystatin C via routes other than the kidney increase with worsening GFR.

cardiovascular disease

Kidney dysfunction increases the risk of death and cardiovascular disease. Several studies have found that increased levels of cystatin C are associated with the risk of death, several types of cardiovascular disease (including myocardial infarction, stroke, heart failure, peripheral arterial disease and metabolic syndrome) and healthy aging. Some studies have found cystatin C to be better in this regard than serum creatinine or creatinine-based GFR equations. Because the association of cystatin C with long term outcomes has appeared stronger than what could be expected for GFR, it has been hypothesized that cystatin C might also be linked to mortality in a way independent of kidney function. In keeping with its housekeeping gene properties, it has been suggested that cystatin C might be influenced by the basal metabolic rate.

Neurological disorders

Mutations in the cystatin 3 gene are responsible for the Icelandic type of hereditary cerebral amyloid angiopathy, a condition predisposing to intracerebral haemorrhage, stroke and dementia. The condition is inherited in a dominant fashion.
Since cystatin 3 also binds amyloid β and reduces its aggregation and deposition, it is a potential target in Alzheimer's disease. Although not all studies have confirmed this, the overall evidence is in favor of are role for CST3 as a susceptibility gene for Alzheimer's disease. Cystatin C levels have been reported to be higher in subjects with Alzheimer's disease.
The role of cystatin C in multiple sclerosis and other demyelinating diseases (characterized by a loss of the myelin nerve sheath) remains controversial.


Cystatin C levels are decreased in atherosclerotic (so-called 'hardening' of the arteries) and aneurysmal (saccular bulging) lesions of the aorta. Genetic and prognostic studies also suggest a role for cystatin C. Breakdown of parts of the vessel wall in these conditions is thought to result from an imbalance between proteinases (cysteine proteases and matrix metalloproteinases, increased) and their inhibitors (such as cystatin C, decreased).
A few studies have looked at the role of cystatin C or the CST3 gene in age-related macular degeneration. Cystatin C has also been investigated as a prognostic marker in several forms of cancer. Its role in pre-eclampsia remains to be confirmed.

06 March, 2011


This post is specially for my esteemed colleague Dr.Deepa from M.V Hospital for Diabetes.

Cystatin C or cystatin 3 (formerly gamma trace, post-gamma-globulin or neuroendocrine basic polypeptide), a protein encoded by the CST3 gene, is mainly used as a biomarker of kidney function. Recently, it has been studied for its role in predicting new-onset or deteriorating cardiovascular disease. It also seems to play a role in brain disorders involving amyloid (a specific type of protein deposition), such as Alzheimer's disease.
In humans, all cells with a nucleus (cell core containing the DNA) produce cystatin C as a chain of 120 amino acids. It is found in virtually all tissues and bodily fluids. It is a potent inhibitor of lysosomal proteinases (enzymes from a special subunit of the cell that break down proteins) and probably one of the most important extracellular inhibitors of cysteine proteases (it prevents the breakdown of proteins outside the cell by a specific type of protein degrading enzymes). Cystatin C belongs to the type 2 cystatin gene family.

Cystatin C was first described as 'gamma-trace' in 1961 as a trace protein together with other ones (such as beta-trace) in the cerebrospinal fluid and in the urine of patients with renal failure. Grubb and Löfberg first reported its amino acid sequence. They noticed it was increased in patients with advanced renal failure. It was first proposed as a measure of glomerular filtration rate by Grubb and coworkers in 1985.

i will be posting more details on Cystatin c assay in my next post...

02 March, 2011


Designer Tobias Förtsch has created a virtual prototype for a noninvasive (and nonexistent) glucose monitor that seems to be inspired by iPod MP3 players. The only problem, of course, is that the search goes on for technology that can properly do glucose measurements without having people prick themselves for a drop of blood.
The small device measures sugar levels using a display with an LED scale between a low result and a high result in different colors. Low sugar levels are shown in red. A normal level appears in white white and a high level goes orange. It stores the result and transfers it via bluetooth to a mobile phone and computer so your doctor has instant access.
The flexibility comes in how you measure your levels. A detachable sensor clips to your earlobe and gives you auditory feedback when your levels get to high. The same info gets transfered to your phone and computer. If your blood chemistry gets out of hand, a call can be made via your mobile to alert your doctor.


Incretins are a group of gastrointestinal hormones that cause an increase in the amount of insulin released from the beta cells of the islets of Langerhans after eating, even before blood glucose levels become elevated. They also slow the rate of absorption of nutrients into the blood stream by reducing gastric emptying and may directly reduce food intake. As expected, they also inhibit glucagon release from the alpha cells of the Islets of Langerhans. The two main candidate molecules that fulfill criteria for an incretin are glucagon-like peptide-1 (GLP-1) and Gastric inhibitory peptide (also known as: glucose-dependent insulinotropic polypeptide or GIP). Both GLP-1 and GIP are rapidly inactivated by the enzyme dipeptidyl peptidase-4 (DPP-4).
GLP-1 (7-36) amide is not very useful for treatment since it must be administered by continuous subcutaneous infusion. Several long-lasting analogs that have insulinotropic activity have been developed and two, exenatide (Byetta) and liraglutide (Victoza), have been approved for use in the U.S. The main disadvantage of these GLP-1 analogs is that they must be administered by subcutaneous injection.
Another approach is to inhibit the enzyme that inactivates GLP-1 and GIP, DPP-4.
Several DPP-4 inhibitors that can be taken orally as a tablet have been developed.
Few available in India are


Taspoglutide is a pharmaceutical drug. It is a glucagon-like peptide-1 analog, under investigation for treatment of type 2 diabetes being co-developed by Ipsen and Roche.
Two phase II trials reported it was effective and well tolerated.
Of the eight planned phase III clinical trials of weekly taspoglutide (4 against exenatide, sitagliptin, insulin glargine, and pioglitazone) at least five were active in 2009. Preliminary results in early 2010 were favourable. (At least one of the 8 planned phase III trials had not started recruiting by end 2009.)
As of September 2010, Roche had halted Phase III clinical trials due to a incidences of serious hypersensitivity reactions and gastrointestinal side effects.


Albiglutide is a GLP-1 analog drug under investigation by GlaxoSmithKline for treatment of type 2 diabetes. It is a dipeptidyl peptidase-4-resistant glucagon-like peptide-1 dimer fused to human albumin.

Albiglutide has a half life of 4 to 7 days, which is considerably longer than the other two GLP-1 analogs approved for market use, exenatide (Byetta) and liraglutide (Victoza). GLP-1 drugs are currently only available for subcutaneous administration on a daily basis, so a GLP-1 drug with a longer half-life is desirable. Such a drug would only need to be injected biweekly or weekly instead of daily, reducing the discomfort and inconvenience of GLP-1 administration considerably.
It has not yet been determined whether albiglutide is as effective an antidiabetic agent as GLP-1 drugs currently on the market, and final data remains to be published regarding the incidence of adverse effects related to the drug. To evaluate the efficacy and safety of the drug, albiglutide is undergoing eight Phase III clinical trials.

21 January, 2011


Microalbuminuria is a condition where very small amounts of the protein albumin pass through your kidneys and into your urine. This can be a sign of underlying conditions such as kidney disease or cardiovascular disease.

blood contains cells and proteins that you need, as well as waste products that your body needs to get rid of. Your blood is filtered by your kidneys and waste products are removed from your body in your urine. Usually, cells and proteins stay in your blood, but sometimes a small amount of protein is lost into your urine along with other waste products.

Microalbuminuria is when the level of the protein albumin in your urine is always slightly raised. Microalbuminuria is defined as 30 to 300mg of albumin being lost in your urine per day. This is different to proteinuria, which is when the levels of protein in your urine are higher than 300mg a day.

Microalbuminuria means that the blood vessels involved in filtering waste products in your kidneys are damaged. Microalbuminuria may be the first sign of kidney damage or kidney disease. People with type 1 and type 2 diabetes may have kidney damage as a complication of their diabetes. If you have diabetes and microalbuminuria is detected early, there are treatments that can reduce the damage to your kidneys.

Microalbuminuria can also be a sign of more widespread damage to your blood vessels, including those of your heart. Microalbuminuria can be a sign that you're at an increased risk of heart disease, particularly if you have type 2 diabetes.

Causes of microalbuminuria -
High blood pressure
Diabetic kidney disease
Urinary tract infection
Heart failure
Uncontrolled blood sugar levels
Blood in urine