All animals, including humans, are made up of cells. The
cell, the basic unit of life, can be identified under a microscope by its outer
membrane and a nucleus within the membrane.
Some cells are able to produce a protein called collagen. In this book, the term "collagen" refers to collagen as well as collagen-like proteins. This process occurs inside the cell. Little globules called vesicles carry the collagen from the inside of the cell to the cell membrane where it is released to the outside of the cell. There, the collagen thickens into fibers.
The five different types of cells capable of producing and releasing collagen in this way are:
Some cells are able to produce a protein called collagen. In this book, the term "collagen" refers to collagen as well as collagen-like proteins. This process occurs inside the cell. Little globules called vesicles carry the collagen from the inside of the cell to the cell membrane where it is released to the outside of the cell. There, the collagen thickens into fibers.
The five different types of cells capable of producing and releasing collagen in this way are:
- fibroblasts, which produce collagen for the structural support of skin, tendons, ligaments and muscle;
- chondroblasts, which produce collagen for the structual support of cartilage;
- osteoblasts, which produce collagen for the structual foundation and framework upon which calcium and phosphate are deposited, giving rise to bone;
- ameloblasts, which produce collagen for the structural foundation and framework upon which calcium and phosphate are deposited, giving rise to tooth enamel.
- odontoblasts, which produce collagen for the structual foundation and framework upon which calcium and phosphate are deposited, giving rise to the inner part of the tooth. This material is called dentin.
Like other proteins, collagen is composed of amino acids
linked together in a chain. However, collagen contains two additional amino
acids, hydroxyproline and hydroxylysine, not found in other proteins. Thus when
collagen breaks down, the hydroxyproline and hydroxylysine levels in the blood
and urine increase.
Researchers from Harvard University and the National Institutes of Health knew in the 1960s that fluoride disrupted collagen synthesis. It was not until 1979-1981, however, that a new flurry of research activity in this area began.
Researchers from Harvard University and the National Institutes of Health knew in the 1960s that fluoride disrupted collagen synthesis. It was not until 1979-1981, however, that a new flurry of research activity in this area began.
In 1981, Dr. Kakuya Ishida of the Kanagawa Dental University in Japan reported the results of studies in which he fed laboratory animals 1 part per million fluoride in their drinking water and analyzed the urine for hydroxyproline. He found that urinary hydroxyproline levels increased in those animals. This indicates that as little as 1 part per million fluoride interferes with collagen metabolism and leads to its breakdown.
Dr. Marian Drozdz and co-workers from the Institute of Bioanalytical and Environmental Studies in Katowice, Poland found increased hydroxyproline and hydroxylysine levels in the blood and urine as well as a decrease in skin and lung collagen levels in rats fed 1 part per million fluoride in their drinking water.
Dr. Anna Put and co-workers from the Department of Pharmacology of the Pomorska Akademy of Medicine in Szczecin, Poland also found that fluoride increased hydroxyproline levels in urine.
Drs. A.K. Susheela, Y.D. Sharma and co-workers from the All-India Institute of Medical Sciences found that fluoride exposure disrupts the synthesis of collagen and leads to the breakdown of collagen in bone, tendon, muscle, skin, cartilage, lung, kidney, and trachea.
As already noted, small vesicles transport collagen from the inside of the cell to the outside of the cell. Drs. Harold Fleming and Val Greenfield of Yale University School of Medicine found a larger number of these vesicles in collagen forming cells (ameloblasts) in animals exposed to fluoride. This work was recently confirmed by S. Chen and D. Eisenmann of the University of Illinois, who also found a fluoride-induced increase of these granules in ameloblasts.
It appears that fluoride disruption of collagen synthesis in cells responsible for laying down collagen leads these cells to try to compensate for their inability to put out intact collagen by producing larger quantities of imperfect collagen and/or noncollagenous protein.
In 1983, Dr. John R. Farley and co-workers from Loma Linda University showed that treatment of bone cells with less than 1 part per million fluoride increased collagen formation by 50 percent. One year later, Dr. J.R. Smid and co-workers from the Department of Oral Biology at the University of Queensland in Australia found that fluoride ingestion led to an increase of noncollagen proteins as well as collagen proteins.
This is supported by the works of Drs. J.H. Bowes and M.M. Murray, Dr. Kh.A. Abishev and co-workers, and Dr. B.R. Bhussry who report a vastly higher protein content in teeth and bone damaged by fluoride. Clinical findings also show that new irregular bone growth is stimulated by fluoride.
The drawings below illustrate the effect of fluoride on collagen metabolism.
While collagen is made by many different types of cells and, under normal circumstances, is only mineralized in teeth and bones, the body obviously has some mechanism to mineralize the collagen of some tissues while leaving the collagen of other tissues, such as skin, ligaments, tendons, etc., unmineralized.
During the aging process, the body loses its ability to discriminate between which tissues should be mineralized and which tissues should not. As will be shown, consumption of fluoride results in the same loss of the body's ability to discriminate. In other words, mineralization of tissue, such as bone, which should be mineralized, is disrupted, and tendons, ligaments, muscles, and other soft tissue which should not be mineralized start to become mineralized as a result of fluoride exposure.
By interfering with collagen production, fluoride leads to the production of larger quantites of imperfect collagen and/or other types of protein and thus interferes with the body's normal regulation of collagen mineralization.
The type and array of collagen and collagen-related proteins made by the various collagen-producing cells determine whether or not the collagen framework will be mineralized. During the aging process, cumulative damage to these cells leads to the diseases attributed to "old age" - arthritis, arteriosclerosis, brittle bones, wrinkled skin, etc. Consumption of fluoride produces the same effects and results in the same diseases.
Fluoride probably acts by interfering with enzymes essential for setting up the proper conditions for producing intact collagen. Thus, as has already been indicated, larger amounts of imperfect or deformed collagen fibers are formed and the body's ability to regulate collagen formation and mineralization is hindered...
Chapter 6 - Aging the Bone: The Degenerative Effects of Skeletal Fluorosis
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