1/99
Looks like no tags are added yet.
Name | Mastery | Learn | Test | Matching | Spaced |
---|
No study sessions yet.
megaloblastic anemia
folate deficiency
pernicious anemia
vitamin B12 deficiency due to lack of intrinsic factor
homocysteine is increased with
folate and B12 deficiency
schilling test
distinguished pernicious anemia from other causes of B12 deficiency
folate deficiency anemia symptoms
weakness and pallor, degeneration of surface mucosal tissue allowing mucosal ulceration and possible infection. sore tongue, GI disturbances, diarrhea, and malabsorption
in folate deficiency anemia, there are decreased
WBCs and platelets
etiology of folate deficiency anemia
poor diet of low animal products, low green vegetables, alcoholic, tea and toast of "elderly", poor intestinal absorption, increased metabolic demands of late pregnancy, growth (early infancy), concurrent vit. C deficiency
good sources of folate include
dark green vegetables, liver, kidney, yeast
folate is easily destroyed by
inadequate handling, storage, and exposure to heat
sources of B12
meat, milk, and eggs
etiology of B12 deficiency anemia
deficient in strictest vegetarian diet, lack of intrinsic factor, heredity, gastrectomy, small bowel disease
food sources of thiamin
pork, whole grains, enriched cereals, liver, poultry, fish, eggs, potatoes, legumes, nuts, dark green vegetables, brewer's yeast, and wheat germ
thiamin is easily
destroyed by heat and alkalinity
thiamin exists in
free form in plant foods
thiamin in animal foods is primarily as
thiamine diphosphate or thiamine pyrophosphate
thiamin must be phosphorylated in
intestine
the absorption of thiamin is
usually high
thiamin phosphates are digested to yield
free thiamin
absorption of thiamin
occurs primarily in the jejunum, secondarily in the duodenum and ileum
what reduces thiamin absorption?
alcohol
thiamin is transported by an
active, sodium- dependent mechanism
thiamin is transported _______ , bound to ______________ , or as ________________ __________________
free, albumin, thiamine monophosphate
thiamin functions
energy production and nutrient metabolism (coenzyme role), synthesis of pentoses and nicotinamide adenine dinucleotide phosphate (NADPH), nervous system functions
functions of thiamin
metabolism and release of energy from carbs, oxidative decarboxylation of a- ketoacids and 2-keto sugars, conversion of pyruvate to acetyl CoA, reactions in the krebs cycle, anti- inflammatory, pentose phosphate pathway, membrane conduction of nerve tissue, branched- chain amino acid metabolism
thiamin is excreted _____________ or _______________.
intact, catabolized
beriberi
thiamin deficiency (mental confusion, muscular problems, cardiac disorders, CNS problems, anorexia, and fluid imbalance)
there is no tolerable upper intake level of
thiamin
wernicke- korsakoff syndrome
thiamin deficiency (clinical triad of confusion, ataxia, and nystagmus)
riboflavin is important in
energy metabolism
what are the 2 coenzyme forms of riboflavin?
Flavin mononucleotide (FMN)
Flavin adenine dinucleotide (FAD), which are both involved in the transfer of electrons.
riboflavin is
light sensitive; sunlight
dietary sources of riboflavin
milk, dairy, leafy green vegetables, liver, beef, meat, enriched cereals, and grains
riboflavin as FAD, FMN, and riboflavin phosphate are
freed prior to absorption
riboflavin is absorbed by
energy- dependent transporter in proximal small intestine
FAD and FMN are released in the
upper part of the small intestine
riboflavin is absorbed by a
saturable, sodium- dependent transport system
bile salts facilitate the uptake of
riboflavin
riboflavin is transported in the plasma bound to
albumin or other blood proteins
riboflavin is phosphorylated to _____ and then dephosphorylated back to ___________.
FMN, riboflavin
riboflavin is transported to liver for conversion to _____ and _____.
FMN and FAD
the greatest concentrations of riboflavin are found in
liver, kidney, and heart
riboflavin is excreted
primarily in urine
riboflavin turns urine a
bright orange- yellow color
functions of riboflavin
facilitation and the release of energy from carbs, protein, and fat. krebs cycle activity, electron transfer mechanisms, accepting electrons in biochemical reactions, flavoproteins in the ET chain, vitamin B6 metabolism and choline catabolism, used by l- amino oxidase, oxidative decarboxylation of pyruvate, succinate dehydrogenase, fatty acid B- oxidation, coenzyme for an oxidase such as xanthine oxidase, synthesis of folate as 5- methyl THF, synthesis of niacin from tryptophan, gluathione, thioredoxin, ribonucleotide reductases, some neurotransmitters
ariboflavinosis
riboflavin deficiency (angular stomatitis, cheilosis, glossitis, hyperemia, edema
riboflavin has no
tolerable upper intake level established
deficiency conditions of riboflavin
suppressed energy release, nervous system failing to properly glean energy, photophobia, poor coordination, cheilosis, inflammation of the mouth, waxy skin, anorexia
pellagra
niacin deficiency disease
coenzyme forms of niacin
nicotinamide adenine dinucleotide (NAD) and nicotinamide adenine dinucleotide phosphate (NADP)
food sources of niacin
brewer's yeast, fish, pork, beef, poultry, mushrooms, potatoes, some plants, dairy foods, enriched cereals, and grains
nicotinic acid can be formed from
tryptophan in humans
digestion and absorption of niacin
digested to nicotinamide, most absorption in the small intestine, absorbed by sodium- dependent and saturable, facilitated diffusion mechanism and by some simple passive diffusion (larger concentrations)
niacin is found in
fish, meats, and enriched grain products
niacin is supplemented as
nicotinamide
1 mg niacin= how much tryptophan?
60 mg tryptophan
niacin digestion, absorption, transport, and storage
NAD and NADP hydrolyzed to free nicotinamide, absorbed in small intestine, absorbed mostly by sodium- dependent, carrier- mediated diffusion, transported primarily as nicotinamide and as nicotinic acid, found trapped as NAD/ NADP in cell
4 D's of pellagra
dermatitis, diarrhea, dementia, death
large doses of niacin are used to treat
hyperlipidemia
UL for niacin
35 mg per day
niacin functions
involved with numerous enzyme reactions, reduction/ oxidation reductions, glycolysis, krebs cycle, b- oxidation, alcohol metabolism, electron transport chain, pyridoxal metabolism, donor of ADP ribose in chromosomes, component of glucose tolerance factor, fatty acid synthesis, cholesterol synthesis, steroid hormone synthesis, synthesis of deoxynucleotides for DNA, reduction of dehydroascorbic acid to ascorbic acid
NAD+ and NADH+ has a significant role in
mitochondrial health and age- related disorders
niacin influences
insulin secretion, gluconeogenesis, mitochondrial biogenesis, endothelial function, lipid metabolism, cell cycling, and apoptosis
niacin controls
fatty acid metabolism and protection from oxidative stress
pharmacologic use of niacin
lowers total blood cholesterol, LDL cholesterol, and triglyceride levels
large doses of niacin may produce
toxic effects
there are six chemical forms of ________ existing in humans.
vitamin B6
dietary sources of B6
pyridoxine is found in plant foods, such as bananas, navy beans, and walnuts.
pyridoxal and pyridoxamine and their phosphorylated derivates are found in
animal products, meat, fish, and poultry
in vitamin B6 digestion, absorption, and metabolism, phosphate groups are
removed during digestion
absorption of the nonphosphorylated form of vitamin B6 takes place by
diffusion
absorption of B6 is
efficient
liver is the primary organ for
B6 metabolism
what is the main circulating form of vitamin B6?
PLP
PLP is transported either within cells
RBCs or bound to albumin
pyridoxal 5' phosphate (PLP) is the active coenzyme form of
vitamin B6 and the most common measure of B6 blood levels in the body
functions of vitamin B6
transamination reactions, deamination and decarboxylation reactions, creation of nonessential amino acids, transulfhydration and desulfhydration reactions, formation of neurotransmitters, breakdown of glycogen, heme production and iron incorporation into heme, sphigolipid and phospholipid synthesis, immunity
deficiencies of vitamin B6 are
rare
various drugs can cause deficiencies of
vitamin B6
alcohol can destroy some
vitamin B6 structures
vitamin B6 supplements can decrease the
duration and intensity of anticonvulsant drugs (dilantin)
raw egg white can bind
biotin
biotin is a stable vitamin in
heat and light
biotin is widespread in foods, but excellent sources include
organ meats, eggs, yolks, brewer's yeast, legumes, nuts, soy flour, soybeans, whole grains, and some fish
avidin in egg whites will bind biotin and
decrease its availability for absorption
biotin is either free or
bound to proteins
biotin is absorbed by
facilitative diffusion (Na- dependent)
biotin deficiency is
rare, but marginal status is possible with the chronic consumption of raw eggs.
cooking eggs denatures
avidin
biotin is excreted by
urinary filtration
biotin is stored in
muscles, brain, and liver tissue
biotin is needed to metabolize
carbohydrates, fatty acids, and leucine
biotin may play a role in other reactions involving
amino acids and purine synthesis
inborn errors of metabolism may produce biotin deficiency. the main symptom is
dry, scaly skin with a gray hue
symptoms of biotin deficiency
loss of epithelial cells, atrophy of tongue and GI tract cells, anorexia, nausea, alopecia, growth retardation, hearing and visual loss, metabolic acidosis, and elevated blood ammonia
pantothenic acid was first identified as a
growth factor for yeast and an antidermatitis factor in chicks
pantothenic acid is the
active form and is a structural component of coenzyme A
pantothenic acid is
stable in air and light
pantothenic acid is readily destroyed by
heat, alkali, and acid pH
pantothenic acid is widespread in
foods
excellent sources of pantothenic acid include
organ meats, egg yolks, meats, fish, whole grain cereals, legumes, mushrooms, broccoli, avocados, and royal jelly (from bees)