A reader asks:
When you talk about taking 20 grams of vitamin C a day, I am wondering what would be the best way to accomplish this. It seems that choking down 20 1 gram horse pills would be a real deterrent. N.S., Rainbow Valley, Oregon
First, a few useful facts: the reason we need to dose ourselves with vitamin C at all is because, unlike most mammals who make it in the liver, our apparatus for making it metabolically is damaged beyond repair at birth. Then, the foods that contain useful amounts of vitamin C also contain sugar which we don’t need. On top of that, the sugar can crowd vitamin C out of places it’s needed, especially the collagen where it is vital! And, as if that weren’t enough, the vitamin C found in foods doesn’t absorb very well and much of it is wasted. Holy nolie! What are we to do?
Luckily, vitamin C can be made in a factory and it’s almost as cheap as sugar and salt. Dr. Clark keeps ascorbic acid powder on the table in a confectioner’s sugar shaker and uses it all day long where the sour flavor adds zest to the food. Dr. Pauling and Dr. Cathcart talked about divided doses because a lot of vitamin C taken all at once can cause the trots. It’s true. Look what happened to Richard when he was trying to cure his flu! The U.S. Navy has verified this but your M.D. is probably in the dark. Next time you go in, ask him what he is doing and tell him what you are doing; fair trade, I’d say. Don’t forget to send your bill.
Now we have liposomal vitamin C invented by a baker. It comes in a minuscule buckyball made out of a phospholipid and it goes right to the cell and merges with the fatty film. Bingo! By weathering the gastrointestinal storms intact, it can deliver a full complement directly to the cell wall. That means you can take less and get the same benefit and there is little or no effect on elimination. Moreover, if there’s an emergency, like your valuable airplane crashes, you can double or triple the amount without having to sprint for the porta-pottie.
Still, there is a place for the kind you buy at the grocery store. It’s handy, cheap and easy to measure. Put a handful in a baggie in your pocket and take one every hour. When you get home, take a spoonful of liposomal C liquid before dinner. Mission accomplished. With the powdered kind, if you carry a water bottle, make some stevia tea, cool, and then add enough dull ascorbic acid crystals to make it into lemonade. Pour that into your water bottle and you’re good to go. And, it keeps. If you find a forgotten bottle in the car after a week or two, it’s still good.
Right now, I am taking between 5 and 15 grams per day because I eat very little sugar of any kind. That lowers my requirement because the oxidative stress of metabolizing a lot of sugar isn’t ever there. Can you call this calorie restriction? I’m sure Dr. Feinman and Dr. Walford would call it that. I’ll just call it ‘ordinary prudence’.
Take a look at the AskDrPangloss website some more and if you don’t get all the answers you want, give me a shout and I’ll be by your side, electronically, that is…
Yours in good health and freedom to pursue happiness wherever it might be found,
Saccharopleonexia™, n. a condition where the appetite for sugars is compelling and not easily satiated.
Otherwise, sugar greed, craving for sweets, sweet tooth, chocaholic, sugar freak, carbolust™
[Please forgive the technical language used here. One of these days, I will translate it for you and we can be friends again. –DrP.]
Mammals produce enzymes which modify proteins and enable chemical reactions
L-gulonolactone oxidase (GULO) [GLO] is step four in the mammalian process to convert glucose into L-Ascorbate
Primates, affected by a particular birth [genetic] defect, lack a functional gene
Scripting for GULO enzyme fails ab initio, therefore, primates produce none in vivo
Thus, little or no 3-Keto-L-gulofuranolactone (L-Ascorbate)) is produced in primates
L-Ascorbate in sweet tasting fruits & vegetables is fortuitous, but poorly absorbed
Such dietary sources provide inadequate L-Ascorbate resulting in chronic sub-clinical scurvy
Where scant L-Ascorbate is available in the diet, various work-arounds have appeared
(E.g., apolipoprotein(a) acting as a surrogate for L-Ascorbate to maintain arterial integrity)
Soma senses low L-Ascorbate as craving for glucose precursor (sweet tasting foods)
Scorbutic pancreas produces & retains insulin for two hours m/l thereby raising blood glucose
Biochemical processes anticipate presence of GULO [or GLO] and reactions begin
Steps one, two, & three accomplished, step four defeated, metabolites remain in sera
Superfluous sugars etc. circulate, competing for insulin & occupying sites coded for 3KLGF
Impeded collagen formation promotes scorbutic symptoms even when some L-Ascorbate present
L-Ascorbate-supported free radical scavenging impeded [but]
Visceral fat, subcutaneous adipose formation, endothermic reactions, & activity levels promoted
Spurious sugars & metabolites may affect brain function via protein tangles, plaques etc
Spurious adipose retains fat-soluble toxins indefinitely
Glycolysated proteins etc. accumulate and impede normal somatic processes
Abnormal somatic processes promote abnormal psychological processes [mental symptoms]
Adverse effects occur from ill-considered self-doctoring aimed at reducing symptoms
Iatragenic conditions arise when therapeutic measures treat symptoms not causes
(E.g., scorbutic and cardiovascular dementia doctored with psychopharmaceutical agents)
1. modify genetic code to permit on demand GULO synthesis in vivo
2. identify effective dietary method to assist four-step enzymatic process
3. other (e.g., Cinamomum zeylanicum vera) [see Anderson, R.]
Possible problems: Homo sapiens sapiens may have come to depend on higher blood sugar contents to maintain fat, ketone and glucose supplies to an enlarged brain, to provide warmth in more Northerly climates, and to allow additional muscular energy and stamina for chase and escape. The revamping of H.s. sapiens to the normal in vivo mammalian production method of L-Ascorbate on demand may put him at a distinct disadvantage when compared to the present genetically modified version.
Nonetheless, if the professional medical community better understood the mechanism of disease as related to sub-clinical scorbutic conditions and Saccharopleonexia™, they could better serve mankind by actually doing no harm and using L-Ascorbate properly as a prophylactic and in the therapeutic setting.
All rights reserved
Reference 1: [keep scrolling]
Journal Article: Intragenic deletion in the gene encoding L-gulonolactone oxidase causes vitamin C deficiency in pigs [note: a wild variety has been identified also.]
Journal: Mammalian Genome
Publisher: Springer, New York
ISSN: 0938-8990 (Print) 1432-1777 (Online)
Issue: Volume 15, Number 4 / April, 2004
Subject Collection: Biomedical and Life Sciences
SpringerLink Date Tuesday, April 27, 2004
Intragenic deletion in the gene encoding L-gulonolactone oxidase causes vitamin C deficiency [scurvy] in pigs
Lara Hasan1, Peter Vögeli1 Contact Information, Peter Stoll2, Scaronpela Scaronpilar Gerald Kramer Stranzinger1 and Stefan Neuenschwander1
(1) Institute of Animal Sciences, Tannenstrasse 1, ETH-Zentrum, CH-8092 Zurich, Switzerland
(2) Swiss Federal Research Station for Animal Production, CH-1725 Posieux, Switzerland
Received: 19 August 2003 Accepted: 12 November 2003
ABSTRACT The absence of L-ascorbic acid (L-AA, or AA) synthesis in scurvy-prone organisms, including humans, other primates, guinea pigs, and flying mammals, was traced to the lack of L-gulonolactone oxidase (GULO) activity. GULO is a microsomal enzyme that catalyzes the terminal step in the biosynthesis of L-AA. Clinical cases of scurvy were described in a family of Danish pigs. This trait is controlled by a single autosomal recessive allele designated od (osteogenic disorder). Here we demonstrate that the absence of GULO activity and the associated vitamin C deficiency in od/od pigs is due to the occurrence of a 4.2-kbp deletion in the GULO gene. This deletion includes 77 bp of exon VIII, 398 bp of intron 7 and 3.7 kbp of intron 8, which leads to a frame shift. The mutant protein is truncated to 356 amino acids, but only the first 236 amino acids are identical to the wild-type GULO protein. In addition, the od allele seems to be less expressed in deficient and heterozygous pigs compared with the normal allele in heterozygous and wild-type animals as determined by ribonuclease protection assay. We also developed a DNA-based test for the diagnosis of the deficient allele. However, we failed to identify the mutated allele in other pig populations.
(Stefan Neuenschwander) Present address: University Hospital Zurich, Department of Surgery, CH-8091 Zurich, Switzerland. The nucleotide sequence data reported in this paper have been submitted to GeneBank and have been assigned the accession number AF440259.
Contact Information: Peter Vögeli
Referenced by 2 newer articles [as of publication date]
Linster, Carole L. (2006) Vitamin C.. FEBS Journal 0(0)
Mohan, Subburaman (2005) Spontaneous Fractures in the Mouse Mutant sfx Are Caused by Deletion of the Gulonolactone Oxidase Gene, Causing Vitamin C Deficiency [see Kalokerinos, A]. Journal of Bone and Mineral Research 20(9)
See also Maeda, N. http://www.jlr.org/content/50/Supplement/S178.full.pdf
and http://adipofat.com/pubs [—Ed.]
Chunzhi Dou, Dian Peng Xu and William W. Wells1
[ www.pnas.org/content/92/25/11869.full.pdf ]
Department of Biochemistry, Michigan State University, East Lansing, Michigan, 48824
Received 6 January 1997.
Available online 19 April 2002.
Pancreatic islets from young normal and scorbutic male guinea pigs were examined for their ability to release insulin when stimulated with depolarizing levels of KCl (45 mM) and by 20 mM -glyceraldehyde. Islets from normal guinea pigs released insulin in a K+and -glyceraldehyde dependent manner showing a rapid initial secretion phase followed by secondary waves of insulin release during a 120 min period. Islets from scorbutic guinea pigs were able to respond to elevated K+in a manner identical to that of the control islets. In contrast, insulin release from ascorbic acid deficient islets in response to the secretagogue,Image -glyceraldehyde, was significantly delayed and decreased responses were observed during the 120 min period after -glyceraldehyde stimulation. The results are consistent with the site of action of ascorbic acid on energy-dependent insulin release lying between the triose-phosphate level of glycolysis and the generation of ATP by oxidative phosphorylation. www.pnas.org/content/92/25/11869.full.pdf
1 To whom correspondence should be addressed. Fax: (517) 353-9334. E-mail: firstname.lastname@example.org.
Elsevier.com (Opens new window)
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Biochemical and Biophysical Research Communications
Volume 231, Issue 3, 24 February 1997, Pages 820-822
Perifusion of saurian pancreatic islets and biphasic insulin release following glucose stimulation
Comparative Biochemistry and Physiology Part A: Physiology, Volume 45, Issue 4, 1 August 1973, Pages 1001-1002, IN5, 1003-1007
William B. Rhoten
1. 1. The effect of low and high concentrations of glucose on insulin release from pancreatic islets of Anolis carolinensis in an in vitro perifusion system has been determined.
2. 2. A biphasic pattern of insulin secretion is obtained in the presence of a high concentration of glucose.
3. 3. The temporal relationships of the biphasic response following glucose stimulation are similar to those observed in vivo and in vitro with mammals.
Dynamics of somatostatin and insulin release from isola…
Dynamics of somatostatin and insulin release from isolated rat pancreatic islets: Evidence for intraislet interactions between B cells and D cells
Metabolism, Volume 27, Issue 9, Supplement 1, September 1978, Pages 1211-1214
Peter Schauder, Christopher McIntosh, Uwe Panten, Jan Arends, Rudolph Arnold, Heiko Frerichs, Werner Creutzfeldt
Glucose stimulates the release of somatostatin and insulin from isolated rat pancreatic islets. 1 This stimulation appears to be mediated via the islet’s adenylate cyclase-phosphodiesterase system. 2 However, the dynamics of both secretory processes are different. In particular, islets previously exposed to a medium containing a high glucose concentration respond with an immediate decrease in insulin release and a transient increase in somatostatin release when the glucose concentration is suddenly lowered. 3 This suggests that somatostatin release is stimulated by glucose but might be inhibited by phenomena associated with a high secretory activity of B cells. The aim of the present study is to further characterize the apparent intraislet interactions between B cells and D cells.
Cationic Events Stimulated by D-Glucose in Depolarized Islet Cells
Cellular Signalling, Volume 9, Issues 3-4, May 1997, Pages 283-290
Hassan Jijakli, Willy J. Malaisse
Pancreatic islets prelabelled with either 86Rb or 45Ca were exposed to a rise in D-glucose concentration from 2.8 to 16.7 mM whilst perifused in the presence of 2 μM glibenclamide, 30 mM extracellular K+ and both 30 mM K+ and 250 μM diazoxide. In all three situations, the rise in glucose concentration provoked a dramatic increase in insulin output, despite unchanged or even increased efflux of 86Rb from the prelabelled islets. Also in all three situations, glucose sharply decreased effluent radioactivity from islets prelabelled with 45Ca but perifused in the absence of extracellular Ca2+, whilst augmenting 45Ca efflux, to a variable extent, from islets perifused at normal extracellular Ca2+ concentration (1.0 mM). It is proposed, therefore, that the insulinotropic action of D-glucose in depolarized islets, and presumably also under normal conditions, may involve the gating of voltage-insensitive Ca2+ channels.
Glucose-induced, calcium-mediated protein phosphorylation in intact pancreatic islets
Archives of Biochemistry and Biophysics, Volume 231, Issue 2, June 1984, Pages 320-327
Anjaneyulu Kowluru, Michael J. MacDonald
Conditions for studying protein phosphorylation in intact pancreatic islets were developed in order to study the effects of glucose and other effectors. Islets were incubated in Krebs-Ringer bicarbonate buffer containing 5 mimage malate and 5 mimage pyruvate (metabolic fuels that are not insulin secretagogues) for 150 min to permit incorporation of 32Pi into islet phosphate pools. Glucose or other effectors were then added, and the incubation was terminated after 10 to 30 min. Glucose increased phosphorylation of four islet peptides with molecular weights of 20,000, 33,000, 43,000 and 57,000. The calcium channel blockers, verapamil and D-600, inhibited phosphorylation of each of the four proteins, and trifluoperazine inhibited phosphorylation of the proteins with molecular weights of 20,000 and 57,000. The results indicate that glucose-induced insulin release may be mediated in part by protein phosphorylation, and that calcium may act as an intracellular messenger in coupling the glucose stimulus to the secretory process.
Molecular and Cellular Endocrinology, Volume 36, Issue 3, July 1984, Pages 175-180
Abdullah Sener, Ramon Gomis, Philippe Lebrun, André Herchuelz, Francine Malaisse-Lagae, Willy J. Malaisse
Pancreatic islet homogenates display Ca2+-dependent transglutaminase activity. Methylamine inhibits the enzyme activity, accumulates in intact islet cells, is incorporated in endogenous islet proteins, and inhibits glucose-stimulated insulin release. The inhibition by methylamine of both enzyme activity and insulin release is inversely related to the ambient Ca2+ concentration. Dimethylamine also inhibits transglutaminase activity and glucose-stimulated insulin release. However, trimethylamine, which does not affect transglutaminase activity, again inhibits glucose-stimulated insulin release, the latter inhibition being also inversely related to the Ca2+ concentration. It is concluded that the impairment of insulin release by methylamines is not necessarily linked to inhibition of transglutaminase activity.
William W. Wells Lectureship in Biochemistry
Professor William W. Wells was born in Traverse City, Michigan and was educated in East Lansing schools. He graduated from East Lansing High School where he was both a scholar and athlete. After service in the Navy in World War II, he obtained B.S. and M.S. degrees from the University of Michigan and his Ph.D. in Biochemistry from the University of Wisconsin. His first faculty appointment was in Biochemistry at the University of Pittsburgh where he served for about ten years before being recruited to East Lansing in 1966 as Professor of Biochemistry at Michigan State University.
Bill Wells has had an illustrious scholarly career having made fundamental contributions to our understanding of the metabolism of steroids, phosphoinositides and vitamin C. He has authored more than 125 refereed publications and 18 invited book chapters. Dr. Wells has served on the editorial boards of Hypertension and the Journal of Biological Chemistry and numerous advisory panels and study sections for NIH, NSF, the American Heart Association, and the American Chemical Society. Dr. Wells is an Established Investigator of the American Heart Association and recipient of a Distinguished Faculty Award from the College of Human Medicine. He has trained over 40 Ph.D. students and postdoctoral fellows. FIN