Lipoproteins are biochemical compounds consisting of proteins and lipids that transport lipids like cholesterol through the bloodstream. They are classified based on density and include chylomicrons, very low density lipoproteins, low density lipoproteins, and high density lipoproteins. Lipoproteins metabolize through exogenous and endogenous pathways to transport lipids from the intestines and liver to tissues.

1. LIPOPROTEINS

2. It is a biochemical compound that consists both proteins and lipids. It is bonded by water. Many toxins, enzymes, transporters and adhesins are lipoproteins. Other examples are High-density Lipoproteins and Low Density Lipoproteins. What are Lipoproteins?

3. Its main function is to transfer Lipids such as cholesterol via the Blood stream. It helps the body to sustain its Nerve Cells and other vital cells in our body. It also helps the lipids to transport energy to the muscles. What are the functions of Lipoproteins?

4. Lipoproteins are classified into two, very dense and less dense. Very dense lipoproteins contain more lipids than proteins. They are categorized by Electrophoresis and ultracentrifugation. How to classify Lipoproteins by Density?

5. Chylomicrons- Carry Triacyl Glycerol to the liver, skeletal muscles and adipose tissue. Very Low Density Lipoproteins(VDL)- Carry newly synthesized Triacyl Glycerol to the liver and from the liver to the adipose tissue. What are the classifications of Lipoprotein by density?

6. Intermediate Density Lipoproteins (IDL)- The buffer between VLDL and HDL and are not detectable in the blood. They exist in very small amounts. Low Density Lipoproteins (LDL)- It carries Cholesterol from the liver to the body. High Density Lipoproteins (HDL)- It collects cholesterol from the body tissues then transported to the Liver.

7. In the exogenous pathway, small intestines were prepared to absorb lipids from food. Then, they were assembled together with Apoliprotein B-48 then merged to Chylomicrons. From the epithelial cells, they were circulated to the lymph vessels. The Chylomicrons were later drained to the bloodstream. How does the Lipoproteins metabolize through the Exogenous Pathway?

8. In the bloodstream, HDL would donate Apoliprotein C-II and Apoliprotein E to the Chylomicrons that were circulating. The sole purpose of Apoliprotein C-II was to activate Lipoprotein Lipase, an enzyme on the endothelial cells. LPL triggers the Hydrolysis of triglycerides which then ultimately releases them from the Chylomicrons. The lipids could then be absorbed by the muscles and other tissues in the body.

9. VLDL particles, formed when Apolipoprotein B-100 merged with Triacyl Glycerol and Cholesterol, would be first released to the blood stream. Then it would be loaded with Apolipoprotein C-II and Apolipoprotein E from HDL particles to become mature. How about the Endogenous pathway?

10. Mature VLDL would then be hydrolized by LPL that was activated by the Apolipoprotein C-II. Then, the lipids would be released and as the result, the VLDL would be converted to Intermediate Density Lipoproteins. They would be circulated back to the liver for reabsorption.

13. include ovalbumin from egg white,lactalbumin from milk, and serum albumin from blood serum.

14. make up about half of the protein in human serum, where their main functions are to maintain normal water balance between blood and tissues by osmotic mechanisms and to serve as transport proteins for less soluble substances that can bind to them, such as amino acids.

16. It binds water, cations (such as Ca2+, Na+ and K+), fatty acids, hormones, bilirubin and drugs

17. Regulate the colloidal osmotic pressure of blood

18. Transportation of nutrients and wastes

19. Binding of toxins and heavy metals

21. High albumin (Hyperalbuminemia) – always caused by dehydration

22. Normal range of human serum albumin in adults (>3 y. o.) is 3.5 to 5 g/dL.

24. can also be measured quantitively and qualitatively with electrophoresis.

25. Protein electrophoresis is used to categorize globulins into the following four categories:

26. Alpha 1 globulins

27. Alpha 2 globulins

28. Beta globulins

30. Alpha 1-antichymotrypsin

31. Orosomucoid (acid glycoprotein)

32. Serum amyloid A

34. Alpha-2u globulin

35. α2-macroglobulin

36. Ceruloplasmin

37. Thyroxine-binding globulin

38. Alpha 2-antiplasmin

39. Protein C

40. Alpha 2-lipoprotein

42. Plasminogen

43. Angiostatins

44. Properdin

45. sex hormone binding globulin

47. Gamma globulin injections are usually given in an attempt to temporarily boost a patient's immunity against disease. Injections are most commonly used on patients who have been exposed to hepatitis A or measles, or to make a kidney donor and recipient compatible regardless of blood type of tissue match.Gamma globulin infusions are also used to treat immunological diseases, such as idiopathic thrombocytopenia purpura (ITP), a disease in which the platelets are being attacked by antibodies, leading to seriously low platelet counts. Gamma globulin apparently causes the spleen to ignore the antibody-tagged platelets, thus allowing them to survive and function.

49. An excess is known as hypergammaglobulinemia. A deficiency is known as hypogammaglobulinemia.

50. A disease of gamma globulins is called a "gammopathy" (for example, in monoclonal gammopathy of undetermined significance.)

51. Pseudoglobulins and Euglobulins

54. Collagen works hand-in-hand with elastin in supporting the body’s tissues. Basically, it gives body tissues form and provides firmness and strength and works with keratin to provide the skin with strength, smoothness, elasticity and resilience.

56. Collagen is important to your health because it is the principal protein of skin, connective tissues, tendons, bones, teeth and cartilage

57. Collagen supports the internal organs. In these areas, collagen molecules create extensive sheets of strong connective tissue.

59. TYPE I -This is the most abundant collagen of the human body. It is found in tendons, skin, artery walls, many connective tissues and the organic part of bones and teeth.

60. TYPE II - Makes up 50% of all cartilage protein. Vitreous humour of the eye.

62. TYPE IV - Also serves as part of the filtration system in capillaries and it is found in basal lamina and eye lens.

64. Bone

65. Skin

66. Joints

68. composed of simple amino acids such as glycine, valine, alanine, and proline

69. made by linking many soluble tropoelastin protein molecules

70. it has a unique conformation and pattern of crosslinking ex. Tropoelastin

71. also composed of unique amino acids such as desmosine and isodesmosine

72. high capacity to stretch and recoil(elasticity)

73. highly hydrophobic*Collagen and elastin are similar, but elastin can be more easily stretched and is less abundant in the body. Both collagen and elastin production decreases with age, making skin sag.

74. ELASTIN: STRUCTURE DESMOSINE ISODESMOSINE IUPAC NAMEMOLECULARFORMULA 4-(4-amino-4-carboxybutyl)-1-(5-amino-5-carboxypentyl) C24H40N5O8 3,5-bis(3-amino-3-carboxypropyl)pyridinium

76. enables the artery wall to alternately stretch and rebound a blood pulses

77. allows the air sacs of the lungs to expand

79. Contain a high percentage of sulfur-containing amino acids, largely cysteine, which form disulfide bridges between the individual molecules.

80. Formed by keratinocytes.

83. Insoluble, due to extensive disulfide bonding.

84. Has a fairly rigid structure due to disulfide bridges between Individual molecules.

85. Unpleasant odor when burned due to high levels of sulfur in keratin.