GERD - Acid Reflux

Dr. Brice E. Vickery

Gastroesophageal Reflux Disorder (GERD) is classified as a Functional GI Disorder, in which stomach acid (HCL) backs up (refluxes) into the esophagus. This is due to an imbalance in the neuroendocrine system, which causes both a loss of contractile ability in the esophagus and its openings in the stomach and diaphragm, as well as an overproduction of HCL (hyperchlorhydria) and unbalanced secretions of the hormone serotonin. This imbalance leads to irritation of the esophageal tissue and a decrease in motility and tone of the entire esophagus and its opening in the diaphragm.

The cause for this unbalanced neuroendecrine system could well be lesions in the spinal disks. Studies have shown intervertebral disk lesions to negatively affect the nervous system.1 In the early 1980’s, using specially designed BEV and CCT tests, Dr. Brice Vickery found that 100% of his GERD patients also had dorsal disk lesions, very often with no back pain symptoms. Instead, their symptoms included stomach and esophageal inflammation along with weakness in both the esophageal/stomach valve and the diaphragm and its opening for the esophagus. This weakness can lead to the stomach pushing up through the diaphragm in the condition known as hiatal hernia. The nervous system is closely linked to the endocrine system, and so this system that secretes chemicals such as HCL or serotonin could also be affected by any changes that occur due to disk lesions.

It is common knowledge that amino acid deficiency does affect the body’s ability to make protein. It could well follow that one cause of GERD is a general deficiency in amino acids (the building blocks of protein), resulting in a deficiency in the spinal disks, the neuroendocrine system and even the make up of the proteins involved in the production of stomach acid and serotonin. It is interesting to note that Dr. Vickery also found once he cured his GERD patients of protein deficiency, their symptoms disappeared.

Systemic protein is made up of essential (EAA) and unessential amino acids. EAA’s can only be obtained if dietary protein is fully digested . Dr. Vickery also found that 9 out of 10 of his patients did not fully digest their food. A lack of essential amino acids leads to an insufficiency in about 3000 enzymes, which cannot be synthesized without these amino acids . Enzymes play a big part in the secretion of HCL and serotonin. Hypochlorhydria (too little stomach acid) and hyperclorhydria could both be caused by the inability to digest and transform dietary protein into systemic proteins.

The essential amino acids must be present in the body or malfunctions will occur in the system.2 If we cannot digest our food into these essential amino acids, then we cannot make systemic proteins. GERD could be just another symptom in a large list of diseases and infections caused by protein deficiency.

If people, because of diet, aging, and stress are unable to produce sufficient enzymes to digest their food properly, then regular maintenance processes such as upkeep and repair of the spinal disk material will be compromised due to a lack of the systemic protein needed to keep the disks strong and flexible. As lesions begin to appear, the nervous system becomes affected and then the neuroendocrine system. Stomach motility and secretions could very well be affected

Two focal points of GERD research in medical science are HCL production by the stomach cells and the effects of serotonin on GERD symptoms. Let’s take a look at these chemicals and the proteins that are involved in their production.

HCL secretion in the stomach is dependent on an active transport system that is made up of proteins. A large portion of those proteins are essential amino acids:


The stomach lining contains certain cells called parietal cells, which are specifically oriented with one surface facing blood in capillaries and the other facing the stomach cavity, where the active transport of HCL into the stomach occurs. These cells are sealed together with tight junction proteins that create an impermeable gasket between the blood and the stomach. Carbon dioxide diffuses freely into the cell where it joins with water. The enzyme carbonic anhydrase,(a systemic protein), catalyzes the reaction between these two elements, yielding hydrogen. Chloride ions enter the cell in a process of ion exchange and on the stomach side of the cell another large protein, H+/K+ Atpase, starts the active transport “pump” for HCL production. Free energy (ATP) hydrolyzed by H+/K+ Atpase pumps out hydrogen (H+) and takes up potassium (K+). K+ flows into the stomach by diffusion through a K+ channel protein while chloride (CL-) flows into the stomach through a Cl- channel protein. This mixture creates a Ph of about .08 in the stomach, which is optimal for food digestion. How much of each protein are EAA’s?:

  • Tight junction protein - 299 total AA 151 EAA ( 18% of the EAA being valine)
  • Carbonic Anhydrase - 260 total AA 106 EAA (17 % of the EAA being leucine)
  • K+ channel protein - 392 total AA 192 EAA ( 16% of the EAA being leucine)
  • H+/K+ Atpase - 1034 total AA 500 EAA ( 10% of the EAA being leucine)3

Why is there an overproduction of acid in the GERD patient? If the proper essential amino acids must be present for the proper function of proteins, what happens if EAAs are missing? Perhaps then the protein mechanism that makes the HCL for our stomach malfunctions. How do we get these EAA’s? By digesting our food fully.


Science is also looking into the role that the hormone serotonin (5HT) plays in GERD because serotonin mediates the chemical transfer of information between the brain and gut. It does this via the central nervous system. If the nervous system has been compromised due to breakdown of the spinal disks, then messages given to the secretory system will also be compromised. If the system does not have adequate amounts of amino acids available to build secretory proteins, it will be doubly compromised . Some studies show that regulating serotonin through the use of drugs such as SSRI’s helps calm some of the symptoms of GERD. Let’s take a look at the biosynthesis of serotonin.

The essential amino acid tryptophan is the necessary precursor to serotonin and is found in foods like turkey, milk, eggs and bananas. Meat also contains tryptophan but it not the best source because it also contains significant amounts of the five other amino acids that compete with tryptophan for receptor access. Research has found the biggest rise in serotonin levels to occur after high carbohydrate meals when the release of insulin encourages certain essential amino acids to leave the blood stream and enter the organ tissues, leaving tryptophan free use albumin transportation to the brain without competition. Once tryptophan is absorbed into the blood stream, the blood protein albumin carries it to the cell where the enzyme tryptophan hydroxylase catalyzes the reaction, which creates 5HTP. Then the enzyme dopa decarboxolase catalyzes the change, which produces the hormone 5HT, or serotonin. Let’s take a look at the proteins involved in this transformation:4

First the amino acid tryptophan must be broken out of the food and absorbed. Production of the blood protein albumin requires seven of the eleven EAA’s.

  • Trytophan Hydroxylase - 74 AA 41 EAA (16% of the EAA being lysine)
  • Dopa Decarboxolase - 480 AA 237 EAA ( 9% of the EAA being leucine)
  • Serotonin - 428 AA 236 EAA (85% of the EAA being leucine)

10%–20% of GERD patients have the precancerous condition known as Barrett’s Esophagus. In this condition the tissue of the esophagus undergoes a change and though there may be no symptoms, it can result in a deadly form of cancer. These patients show a decrease in the enzyme glutathione transferase.6 This enzyme detoxifies carcinogens, drugs, environmental toxins, and oxidative stress through conjugation with the protein glutathione. Glutathione Transferase - 218 AA 129 EAA (23% of EAA being leucine)

The essential amino acid cysteine is the limiting amino acid in the synthesis of glutathione. This means that all the other amino acids in glutathione are limited in their efficiency without adequate levels of cysteine.7

Each systemic protein broken down in this article ranges from 40%-55% EAA’s. The only place we can get these AAs from is the complete digestion of our food. Without them we will become protein deficient. For instance, studies show that depriving mice of cysteine in their diets leads to lower levels of glutathione in their systems and a decreased ability to handle oxidative stress. 8 The body has a number of proteins and enzymes that are designed to help clear the toxic burden of oxidative stress from the body. If the body cannot make a sufficient number of these proteins to handle the stress load, the system will begin to experience the effects of this malfunction.

If we cannot make the proteins we need for our stomach to work properly we will begin to experience the effects of a malfunctioning system.

Studies show that a protein deficient system leads to malfunctions of the system and illness. The beginning of this breakdown may begin in the dorsal spinal disks, affecting the nervous system and, in the GERDs patient, the neuroendocrine system of the stomach. If we are not digesting our dietary protein properly we are becoming increasingly protein deficient and protein deficiency leads to systemic malfunction.


Micheal Furman MD, “Spinal Stenosis and Neurogenic Claudication.” E-Medicine, July 21, 2004.
Tracy G. Anthony, Ali K. Reiter, Joshua C. Anthony, Scot R. Kimball, and Leonard S. Jefferson, “Deficiency of dietary EAA preferentially inhibits mRNA translation of ribosomal proteins in liver of meal-fed rats.” Am J Physiol Endocrinol Metab 281: E430-E439, 2001; 0193-1849/01, Vol. 281, Issue 3, E430-E439, September 2001
Junction Adhesion Molecule 1: Q9Y624, NiceProt View of Swiss-Prot, Uni-Prot Carbonic Anhydrase 1:P00915, Bioinformatic Harvester, Stanford University. Potassium Voltage Gated Channel: KCNQ1, Bioinformatic harvester, Stanford University Gastric H+/K+ ATPase: P20648, Bioinformatic Harvester, Stanford University
Tryptophan Hydroxylase:Q86WC5 (fragment), Bioinformatic Harvester, Stanford University Dopa Decarboxolase
Andrew S. Chu, MD, “Esophagitis” E-Medicine, Nov. 19, 2004
Brabender J, Lord RV, Wickramasinghe K, Metzger R, Schneider PM, Park JM, Holscher AH, DeMeester TR, Danenberg KD, Danenberg PV., “Glutathione S-transferase-pi expression is downregulated in patients with Barrett’s esophagus and esophageal adenocarcinoma.” Journal of Gastrointestal Surgery. 2002 May-Jun;6(3):359-67.
Bounous,J, “Whey protein concentrate (WPC) and glutathione modulation in cancer treatment.”, Anticancer Res. 2000 Nov-Dec;20(6C):4785-92.
Wang ST, Chen HW, Sheen LY, Lii CK., “Methionine and cysteine affect glutathione level, glutathione-related enzyme activities and the expression of glutathione S-transferase isozymes in rat hepatocytes.” Journal of Nutrition, 1997 Nov;127(11):2135-41.