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FHB > Nutrition > Flashcards

Nutrition Flashcards

0
Q

What are the implications of bypassing the stomach?

A

No IF binding to Vit. B12 –> decreased B12 absorption

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1
Q

Following gastric bypass, what nutrients are most often deficient?

A

Thiamine and Vit. A

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2
Q

What is dumping syndrome?

A

No regulation of chyme entry into duodenum. Less transit time, digestion, and absorption.

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3
Q

What is Thiamin a coenzyme for?

What is the active form?

A

Pyruvate Dehydrogenase Complex

Active form = TPP

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4
Q

What causes Dry Beriberi?

What are the symptoms?

A

Thiamin deficiency

Symptoms: peripheral neuropathy; bilateral wrist/ankle drop; symmetric impairment of motor, sensory, & reflex function

Affects limb segments primarily

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5
Q

Wet Beriberi symptoms?

A

Also called Cardiac Beriberi

Edema, tachycardia, cardiomegaly, CHF, and neuropathies seen in dry beriberi.

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6
Q

Cerebral beriberi symptoms?

A

Wernicke’s encephalopathy (Wernicke-Korsakoff Syndrome)
Mental confusion
bilateral 6th cranial nerve paralysis
Seen in severe alcoholism (poor diet & decreased thiamin absorption)

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7
Q

What is the treatment for alcoholic thiamin deficiency?

A

IV thiamin. This must be done prior to giving glucose or rapid spike in blood glucose could cause coma & death.

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8
Q

Why is a low phosphorus diet suggested for dialysis patients?

A

It can’t be removed from the blood.

High phosphorus –> ^ PTH –> Bone resorption –> renal osteodystrophy and soft-tissue calcification

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9
Q

Symptoms of Iron Deficiency Anemia in children?

A

Inattentive, distracted, unhappy, low hematocrit, slow growth

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10
Q

What type of anemia does Iron deficiency yield?

A

Microcytic, hypochromic

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11
Q

What type of anemia does Folate/B12 deficiency yield?

A

Megaloblastic anemia

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12
Q

What is the recommended distribution of kcals in a patient’s diet?

A

Less than 30% from fat (<1% trans fats)
15% from protein
55% from carbohydrates

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13
Q

What is the difference between primary and secondary PEM?

A

PEM = Protein-Energy Malnutrition

Primary caused by insufficient energy intake
Secondary caused by hypercatabolism

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14
Q

What is stunted grown defined as?
Underweight?
Marasmus?
Kwashiorkor?

A

Stunting = linear growth slowed to preserve body systems. Due to chronic, mild PEM.

Underweight = weight-for-age 2 SD below mean

Marasmus = wasting. Defined as weight-for-height 2 SD below mean. Caused by acute PEM

Kwashiorkor = inadequate protein (acute PEM)
Symptoms: loss of body fat & muscle, edema, change in hair color, renal impairment, hepatomegaly

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15
Q

Which type of Fatty Acid lowers LDL and HDL?
Which type only lowers LDL?
Which is better then?

A

Polyunsaturated FA’s lower both LDL and HDL
Monounsaturated FA’s lower just LDL
So MUFA’s may be better for you

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16
Q

What are the omega-3 Fatty Acids?

A

Alpha-Linolenic
Eicopentaenoic
Docosahexaenoic

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17
Q

What are the active forms of retinol?

A

Retinal

Retinoic acid

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18
Q

What form of Vit. A is found in plant sources?

A

beta-Carotene

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19
Q

How does retinol function in the eye?

A

It binds with opsin when stimulated by light. This initiates a nerve impulse.

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20
Q

What are the primary functions of Vitamin A?

A

Retinol

It is a prosthetic group of visual pigments and a nuclear modulator of gene expression.

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21
Q

What are the symptoms of a Vitamin A deficiency?

A

Night blindness, epithelial keratinization (de-differentiation of epithelia), poor appetite, poor growth.

Xerophthalmia is the CARDINAL clinical sign.

22
Q

What are the symptoms of Vitamin A toxicity (acute and chronic)?

A

Retinol

Acute: vomiting, headache, skin peeling
Chronic: weight loss, fever, itchy rash, bone tenderness

Cardinal chronic sign is bright red margins of gingiva.

23
Q

How is Vitamin D synthesized?

A

Synthesized from cholesterol in the epidermis. Light is necessary for previtamin-D3 –> Vitamin D3. Travels to liver, where it is processed to 25-OH-D3 (clinically relevant form). The kidney then finishes activating it to 1,25-(OH)2-D3 (active form)

24
Q

What are the primary functions of Vitamin D?

A

Maintains serum Ca2+ & P concentrations.

Increases intestinal absorption, bone resorption, and renal reabsorption. This is done by augmenting gene expression.

25
Q

What is caused by a Vitamin D (Cholecalciferol) deficiency?

Who is most at risk?

A

Osteomalacia (Rickets in children)
Breastfed infants of color at highest risk

Bowlegged
Skull malformations
Harrison’s Sulcus = indentation of lower ribs where diaphragm attaches

26
Q

What is the function of the Vitamin E family?

A

Tocopherols

They protect cell membranes as an antioxidant. They also inhibit platelet aggregation and increase vasodilation.

27
Q

What is Vitamin K a coenzyme for?

A

Vit. K = Phylloquinone

Coenzyme for Y-glutamyl carboxylase

There are many Vit. K-dependent proteins in blood clotting cascade.

28
Q

What are the symptoms of a Vitamin K deficiency?

A

Vit. K = Phylloquinone

Bleeding is the primary manifestation.

All newborns in America are given Vit. K upon birth to prevent hemorrhagic disease of the newborn.

29
Q

What is the general function of all water-soluble vitamins?

A

Function as coenzymes

30
Q

What are the symptoms of a Niacin deficiency?

A

Pellegra = Niacin deficiency

Symptoms: photosensitive dermatitis, CASAL’S NECKLACE

4 D’s: Dermatitis, Diarrhea, Dementia, Death

31
Q

How can Niacin be synthesized in the body?

A

From tryptophan

32
Q

What enzyme is Vit. C a coenzyme for?

A

Vit. C = Ascorbic Acid

Prolyl Hydroxylase (collagen formation)

33
Q

What are the symptoms of a Vit. C deficiency?

A

Vit. C = Ascorbic Acid

Scurvy:
Inflamed & bleeding gums
Petechiae (small blood vessel ruptures under skin)
Perifollicular hemorrhages
Poor wound healing
34
Q

What enzyme is Folate a coenzyme for?

A

Methyl transfer reactions: Thymidylate Synthase

(dUMP –> dTMP in pyrimidine synthesis)

Forms a “methyl trap”

35
Q

What enzymes are Vit. B12 a coenzyme for?

A

Vit. B12 = Cobalamin

1 Carbon transfers: Methionine Synthase & Methylmalonyl-CoA Mutase

36
Q

How is Vit. B12 ingested?

A

It is produced by bacteria that are only found in animal tissue. Only VERY strict vegas are at risk of deficiency.

37
Q

What are the symptoms of both B12 and Folate deficiency?

How can you distinguish them?

A

Both: megaloblastic anemia, hyperhomocysteinemia, defective DNA/RNA synthesis, neural tube defects in fetus

Cobalamin –> high methylmalonic acid (MMA)

38
Q

What can hyperhomocysteinemia cause?

What deficiency is associated with this?

A

Can cause CVD effects.

Folate and Cobalamin deficiency can yield this

39
Q

What are homeostatic Ca2+ levels?

A

2.5 mM = 10 mg/dL

40
Q

What proteins within enterocytes are regulated by Vitamin D?

A

Calbindin and Ca2+ ATPase

41
Q

What are Ca2+ primary functions?

A

Bone
Intracellular messenger
Cofactor for clotting & proteases

42
Q

What is Refeeding Syndrome?

A

Severely malnourished, dehydrated people given glucose & saline

Volume expansion –> rapid glycogen synthesis –> depleted plasma concentration –> cardiac arrhythmias.

Caused by phosphorous, K+, Mg2+, and vitamins dropping in blood.

43
Q

What form of iron is found in animal sources?
Plant sources?

What kind can be absorbed in the gut?

A

Heme iron only found in animal sources (Fe2+)
Non-heme iron found in animal and plant sources (Fe2+ & Fe3+)

Ferrous iron can be absorbed in the gut. It is reduced at the apical membrane prior to absorption.

44
Q

What form of Iron can bind Ferritin?

Transferrin?

A 
Ferritin = Fe2+ (storage)
Transferrin = Fe3+ (plasma transport)
45
Q

What does Hepcidin do?

A

When the liver has adequate Iron, hepcidin monitors this and prevents BL absorption in the intestine by binding to ferroportin.

46
Q

What does HFE protein do?

A

Monitors plasma Iron concentrations by monitoring the interaction between transferrin and the transferrin receptor.

47
Q

What occurs to maintain cellular homeostasis during Fe deficiency?
During excess?

A

Deficiency: Upregulation of transferrin receptors & downregulation of ferritin

Excess: Upregulation of ferritin & downregulation of transferrin

48
Q

What are the functions of Iron in the body?

A

Iron-sulfur complexes (ox. phos.)

Heme-containing compounds (Hb, Mb, peroxidase, cytochromes)

49
Q

What is the active form of Vit. B6?

A

Pyridoxal Phosphate

50
Q

What can cause genetic Iron toxicity?

Acute Iron toxicity?

A

Genetic: Hereditary hemochromatosis = a mutation in the HFE protein gene. Leads to increased absorption of iron, which deposits in tissues.

Acute: Too much iron can oxidize intestinal mucosa, allowing iron to reach circulation –> death.

51
Q

What is the most prevalent nutritional deficiency in the world?

A

Iron deficiency anemia

52
Q

What is Iodine used for in the body?

A

A component of Thyroxine/Tetraiodothyronine (T4) and Triiodothyronine (T3)

53
Q

What are the symptoms of Iodine deficiency?

A

Hypothyroidism
Deficiency seen during periods of rapid growth
CNS requires thyroid hormone, especially during prenatal & neonatal times

FHB (8 decks)

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