COPPER TO TOUGHEN HERNIATED DISCS
ABSTRACT Copper is part of lysyl oxidase, which is the enzyme that cross links elastin tissue. The strength of elastin depends on its cross links (Sandberg). Upper spinal discs are made of elastin. Therefore it is imperative that copper status be brought up to normal before an operation. Sometimes an operation will not even be necessary if this is done. Copper status must be kept normal thereafter in order to prevent a recurrence by total intake of at least 3 mg per day.
INTRODUCTION
Herniated discs are the most painful, and numerous diseases in modern society. Slipped or herniated discs are estimated to cost more than 200 billion dollars directly and indirectly each year in the USAalone [http://www.futuremedicine.com/doi/pdf/10.2217/14750708.4.1.51 ]. I suspect that copper deficiency status is the most important parameter affecting them. Two hundred and eighty patients having back pains were treated with copper salicylate. A majority was believed to have a slipped disc. Improvements were considerable and rapid [Sorenson & Hangarter]. Restoring copper during that disease is imperative.
Therefore increasing copper intake should have a dramatic effect on our collective health. Copper should always be made adequate even when a disc operation is in order. If the copper status is unknown, there should be at least a week of 6 mg total intake per day prior to the operation, or at least high in copper foods such as shellfish or liver, especially sheep liver. There should not be great danger if there is a concurrent bacterial infection because a depleted liver removes free copper from the blood with extreme rapidity, [Peisach, et al], so the danger of bacterial stimulation is probably not acute. Even so, using ceruloplasmin injections might be a safer way during such an infection because copper is tightly bound in ceruloplasmin.
CAUSES of COPPER DEFICIENCY
That copper is below optimum in a large number of people is virtually certain from current evidence. This is caused by the low copper content of dairy products, loss of copper by removal of the germ from grain, and refining of sugar. Fructose (corn syrup) and sucrose sugar in fruit apparently produces a much greater need for copper once in the body [Reiser] [Fields & Lewis]. Treating vegetables with the chelating agent, ethylene diamine tetraacetate, reduces both their copper and their zinc to 20% of original values [Pfeiffer, 1972, p161]. Eating large amounts of vitamin C (ascorbic acid or ascorbate) is thought to interfere with utilization of copper within the body [Harris 1991][Underwood p71] although Evans thinks the problem is that absorption is decreased [Evans 1973b]. Vitamin C does cause greater excretion of copper via the bile and decreased absorption [Van Den Berg], so these may be the main mechanisms for vitamin C's interfering with copper. Vitamin C causes ruptures of the aorta in copper deficient animals [Owen]. Vitamin C inhibits copper sulfate injection to stimulate lysyl oxidase under a deficiency of copper if given before or at the same time as copper sulfate injection. But, strangely, if given 75 minutes later, accentuates copper's affect in stimulating lysil oxidase [Di Silvestro, 1981].
COLLAGEN TISSUE
The strength of collagen is not as badly affected because of the long length of collagen molecules close order enabling hydrogen bonds to be affective. However inadequately cross linked collagen is subject to creep. The discs below the sacroiliac of the spine are composed of collagen. The strength of pig or chick tendon is little affected by copper deficiency, even though the animals are dying of ruptured aortas and even though the tendons have 70% the cross links of normal [O'Dell] [Chou]. The normal lesser number of cross links are desirable nevertheless, for they permit the tendons to return to their original position after stress is relieved and not to cold flow as polymers held together only by hydrogen bonds do. The number of cross-links is probably optimum, because too many would make the tendon brittle. Too few cross-links would cause the tendon to become slack with time. Thus the body has a tough material which approaches steel in strength weight for weight and bones which are almost as strong as cast iron (I do not know how cross linked bone collagen is although both bone and tendon are type I collagen [O'Dell]). The lesser reliance by tendon collagen on cross-linking for strength may be the reason why the body uses collagen to repair lesions in arteries during a copper deficiency instead of elastin [Waisman, et al]. Such a strategy may be a good immediate expedient for survival, but I suspect it results in an intractable hypertension eventually because collagen is much less rubbery or elastic than elastin. It is conceivable that something like that goes on to a lesser extent in spinal discs. It might be a good idea to find out
Ankylosing spondilitis probably heals slowly because the sacral and ileal joints are made of type I cartilage [Paquin, et al].
COPPER AFFECT on the SPINAL NERVE SHEATH and FLUID
A copper deficiency produces a degeneration of the spinal cord involving the sheath around the nerve fibers, It is similar to the degeneration caused by a vitamin B-12 deficiency. Winston and Jaiser have proposed that the similarity is because of a dysfunction of the methylation cycle, which is dependant on vitamin B-12 catalyzed enzymes and may be dependant on copper catalyzed enzymes also [Winston]. Methionine synthase requires copper and they suggest that s-adenosylhomocysteine may be regulated by copper.
There is raised copper in the cerebrospinal fluid during Parkinson's disease [Beshgetoor]. Perhaps copper should be investigated for Parkinson's disease.