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Brouwer, Ingeborg. 2010. ‘Effect of Animal and Industrial Trans Fatty Acids on HDL and LDL Cholesterol Levels in Humans – A Quantitative Review.’ Accessed April 05, 2013. http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2830458/

Effects of Animal and Industrial Trans Fatty Acids on HDL and LDL Cholesterol Levels in Humans- A Quantitative Review:

          Trans fatty acids can be obtained from industrial hydrogenation of vegetable oil and fish oils (artificial trans fatty acids) or from the biohydrogenation from ruminant animals such as cows and sheep (natural trans fatty acids). The consumption of these hydrogenated products results in the increase or decrease of HDL and LDL lipoproteins in the body which places a risk on a person’s heart.

            In this report 39 studies were conducted using persons with controlled diets. Twenty-nine used industrial trans fatty acids, six used ruminant trans fatty acids while seventeen used conjugated trans linoleic acid (CLA). Linear regression analysis was uses to determine if these individuals were affected. The slope of the line for LDL to HDL ration was steeper for trans industrial fatty acids than for ruminant fatty acids or CLA. Statistical analysis was used to compare trans fatty acids with saturated fatty acids.

            The results indicated that there was significant weight loss and gain for some individuals with an increased risk of heart and liver disease. There is a quantitative comparison of the effect of ruminant trans fatty acids and CLA with industrial trans fatty acids on blood lipoproteins in humans. The analysis shows that all three classes of trans fatty acids raise the ratio of LDL to HDL. The effect of ruminant trans fatty acids and CLA on the LDL to HDL ratio was less than that of industrial trans fatty acids. The trans fatty acid with double bonds raised the LDL and lowered the HDL levels of cholesterol.         

            Thus, it was concluded that the removal of all the ruminants trans fatty acids (meat and milk) would lower the total trans fatty acid intake. Further studies need to be conducted to determine if the effects are due to chance. It some countries such as Denmark trans fatty acids are banned from the food industry.  

            This article helped me to better understand trans fatty acids to a larger extent. My knowledge of why trans fatty acids has such a negative impact on our bodies was broadened. Although this substance tantalized our taste buds and increases the shelf life of certain products it is a major component of cholesterol molecules. This as it is known leads to atherosclerosis which leads to heart attacks and strokes.

             I hope that after reading this  blog post you try to change your lifestyle to a more healthier way of living. Remember to exercise regularly, drink 6-8 glasses of water, include a large amount of fresh fruits and vegetables, and keep in mind that what you put into your body will affect you sooner or later.

            Byee!

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Pathophysiology of Tay-Sachs disease (TSD) – TSD also referred to as type one GM2-gangliosidosis is a genetic disorder caused by deficiency of the enzyme hexosaminidase A (hex-A) which results in a failure to process a lipid called GM2 ganglioside. Thus results in accumulated lipid in the brain, spleen and tissues. TSD begins in infancy where the child’s head control is lost by six to eight months of age. The infant cannot roll over or sit up. There is tightness of muscles and little flexibility. An excessive drooling and rapid contraction and relaxation of the muscles become evident. Blindness and head enlargement occur by the second year. The disease worsens as the central nervous system progressively deteriorates. Constant nurse care is needed after age two. The disease is a progressive development of retardation, paralysis, blindness and death by the age of three or four years.

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Symptoms of Tay-Sachs Disease include:

– Slowed Development 

– Weakened Muscles 

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– Loss of Motor Skills 
– Seizures 
– Vision and Hearing Loss 
– Mental Retardation 
– Paralysis 
– Cherry-Red Spot (eye abnormality) 

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– Death by Early Childhood

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DID YOU KNOW???

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References:

http://www.drgreene.com/articles/taysachs-disease/

http://www.glogster.com/anecker/tay-sachs-disease/g-6lt56ih88ttmdd3ibba4ra0

http://devonda-r-holmes.blogspot.com/

http://abwarso.tripod.com/id14.html

ȨƞƉ ŏƒ Ąϻȋñö Ąċȉďs & Ƥřȯƫȇȉñs…

Amino Acids-

Proteins are polymers of amino acids joined by peptide bonds. There are 20 different amino acids that make up all proteins on earth. Each of these amino acids has a fundamental design composed of a central carbon (also called the alpha carbon) bonded to:

  • a hydrogen

  • a carboxyl group

  • an amino group

  • a unique side chain or R-group

The characteristic that distinguishes one amino acid from another is its unique side chain and it is the side chain that dictates an amino acids chemical properties. Examples of three amino acids are shown below: 

amino

Glycine is the smallest amino acid. Except for glycine which has a hydrogen as its R-group there is asymmetry about the alpha carbon in all amino acids. All amino acids except glycine can exist in either of two mirror-image forms called stereoisomers which refer to D and L configurations of amino acids. D is more common than the L configuration.

d-lysine

The unique side chains confer unique chemical properties on amino acids, and dictate how each amino acid interacts with the others in a protein. Amino acids can thus be classified as being hydrophobic versus hydrophilic, and uncharged versus positively-charged versus negatively-charged.

 AminoAcids1

Proteins-

Amino acids are covalently bonded together in chains by peptide bonds. If the chain length is short <20 it is called a peptide. Longer chains are called polypeptides or proteins. Peptide bonds are formed between the carboxyl group of one amino acid and the amino group of the next amino acid. Peptide bond formation occurs in a condensation reaction involving loss of a molecule of water. 

l

 

 

 

Levels of Protein Structure:

Structural features of proteins are usually described at four levels of complexity:

  • Primary structure: the linear arrangment of amino acids in a protein and the location of covalent linkages such as disulfide bonds between amino acids.
  • Secondary structure: areas of folding or coiling within a protein; examples include alpha helices and pleated sheets, which are stabilized by hydrogen bonding.
  • Tertiary structure: the final three-dimensional structure of a protein, which results from a large number of non-covalent interactions between amino acids.
  • Quaternary structure: non-covalent interactions that bind multiple polypeptides into a single, larger protein. Hemoglobin has quaternary structure due to association of two alpha globin and two beta globin polyproteins. 

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 The different bonds in a protein structure: 

bonds

Proteins are very important molecules in our cells. They are involved in virtually all cell functions. Each protein within the body has a specific function. Some proteins are involved in structural support, while others are involved in bodily movement, or in defense against germs. Proteins vary in structure as well as function. They are constructed from a set of 20 amino acids and have distinct three-dimensional shapes. Below is a tab;e of several types of proteins and their functions.

The table below are some examples of protein functions:

functions

Why You Need Amino Acids Daily?

Foods with amino acids are the building blocks of protein. That means they are responsible for strength, repair and rebuilding inside your body. Your tissues, your cells, your enzymes and your brain all get their nourishment and protection from amino acids. Amino acids make up 75% of the human body and are vital to every part of human function.

You Can’t Store Amino Acids…The problem with amino acids is that they deteriorate. The body will store extra starch and protein as fat, to use later. Amino acids are not stored, but they can be replaced. There are upwards of twenty different kinds of amino acids that form proteins. Some of these the body makes. The ones it cannot make, called the essential amino acids, it must get from constant consumption of food.

The Best Foods: Meat, eggs, and dairy are sources but it is difficult for strict vegetarians and vegans to get all their essential amino acids. Most vegetarian protein foods, such as beans and seeds, contain only portions of the essentials. An exception to this is soy which contains complete proteins.

 

REFERENCES:

http://ghr.nlm.nih.gov/handbook/howgeneswork/protein

http://alevelnotes.com/Protein-Structure/61

http://www.muscleandstrength.com/articles/the-importance-of-amino-acids.html

http://www.fitday.com/fitness-articles/nutrition/vitamins-minerals/foods-rich-in-amino-acids-for-every-meal.html#b

http://www.vivo.colostate.edu/hbooks/genetics/biotech/basics/prostruct.html

http://biology.about.com/od/molecularbiology/a/aa101904a.htm

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                                         One of the most important aspects of a protein is its shape. The shape of a protein is critical to its function, and this holds true for hemoglobin. The shape of a protein is largely based on the amino acids it contains and whether or not they are charged, attracted to water or repelled by water. According to the sickle cell center at Harvard University, the amino acid substitution that causes sickle cell disease is a mutation of the sixth amino acid from glutamic acid to valine. This is relevant because glutamic acid is a charged amino acid and, as a result, is very attracted to water, whereas valine is repelled by water. This simple substitution occurs at a spot that is critical for the hemoglobin protein’s shape, causing it to have an unusual structure and to be poor at binding to oxygen. Sickle cell anemia is a disease passed down through families in which red blood cells form an abnormal sickle or crescent shape.

images (2)                          sickle-cell-anemia                  images (1)

Picture sowing the various areas                                                                                                                                 affected by sickle cell anemia

The effects of sickle cell anemia cause pain and damage to the organs. Irregularly shaped red blood cells become sluggish, and move more slowly, causing clumping. Red blood cells are normally round, and carry oxygen rich blood. Oxygen is carried by hemoglobin in red blood cells, but in individuals with sickle cell anemia, abnormal hemoglobin levels cause red blood cells to take on a C shape. Red blood cells that are abnormally shaped, as in sickle cell anemia, die before new ones can be produced.

Sickle cell anemia can destroy the organs of the body. Pain and swelling in the toes, feet and ankles might be one of the first signs of sickle cell anemia. Blocked blood vessels can also cause pain in the hands. Sickle cells can block blood flow to other organs, including the spleen, lungs, brain, eyes and the blood vessels that supply the heart and lungs. Infection and pneumonia are possible.
Eye damage, disability from hemorrhagic or ischemic stroke (from lack of oxygen to the brain), enlargement of the spleen, and pulmonary artery hypertension (increased pressure in the lungs) are possible effects of sickle cell anemia. Leg ulcers can occur from poor blood flow to the skin. Kidney failure can occur. Red blood cell destruction that releases too much bilirubin into the bloodstream can lead to gallstones and gallbladder attacks that cause nausea and abdominal pain.

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A child suffering from sickle cell anemia

               lcdmf

            As the daughter of a victim of sickle cell anemia from Madagascar, I spent my whole childhood with sickle cell disease without knowing its name, but aware of the suffering and the pain it causes. After the disease was diagnosed in my daughter a few years ago when she was two, I decided to dedicate myself to ensuring that families, mothers and patients no longer had to live through the hell of ignorance. So in 2008, we set up the first association to fight against sickle cell disease in Madagascar.

sicklecell-anemia-symptom                                                                                                   shortened finger

Treatment: There isn’t a cure for sickle cell anemia, but symptoms can be well-handled with treatment. Antibiotics are used by infections patients and  Hydroxyurea are used to manage pain and reduce simple crises. In severe cases, blood transfusions or bone marrow transplants may be performed.

References:

http://www.ehow.com/how-does_5185869_amino-cause-sickle-cell-anemia_.html

http://www.ncbi.nlm.nih.gov/pubmedhealth/PMH0001554/

http://www.leffortcamerounais.com/2011/08/catuc-hosts-first-international-sickle-cell-conference.html

http://www.fondation-sanofi-espoir.com/en/ngo_lcdmf.php

http://www.youtube.com/watch?feature=player_embedded&v=iKQmQHh4E2w

http://www.youtube.com/watch?v=qe59ar-GZmg

http://www.youtube.com/watch?v=skWYKOcptLQ

There are three videos about patients coping with this disease which are informational.