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during contraction

C.A decrease in entropy during expansion, and an increase in entropy during contraction

D.The breaking of salt bridges during expansion, and reformation of the salt bridges during

contractionE. Hydroxylation of elastin during expansion, and decarboxylation of elastin during contraction

3. The underlying mechanism by which GAGs allow for the formation of a gel-like substance in the

ECM is which one of the following?

A.Charge attraction between GAG chains

B.Charge repulsion between GAG chains

C.Hydrogen bonding between GAG chains

D.Covalent cross-linking between GAG chains

E.Hydroxylation of adjacent GAG chains

4.The movement of tumor cells from their site of origin to other locations within the body requires the

activity of which one of the following proteins? A. Collagen

B. Laminin

C. Proteoglycans D. Elastin

E. MMPs

5.Fibronectin is frequently absent in malignant fibroblast cells. One of the major functions of

fibronectin is which one of the following? A. To inhibit the action of MMPs

B. To coordinate collagen deposition within the ECM C. To fix the position of cells within the ECM

D. To regulate GAG production

E. To extend GAG chains using nucleotide sugars

6.Which one of the following alterations would reduce the ability of cartilage to cushion weightbearing activities at joints?

A. Loss of negative charges on the proteoglycans B. Loss of positive charges on the proteoglycans C. Gain of negative charges on the proteoglycans

D. Increased concentration of glucuronic acid residues

E. Increased concentration of sulfated sugars on the proteoglycans

7.A newborn displays the symptoms of a moderate case of OI. Analysis of the child’s collagen by

sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS-PAGE) indicates a molecular

species with a greater-than-normal molecular weight. Treatment of the child’s collagen with β-

mercaptoethanol prior to SDS-PAGE results in a normal-sized collagen. The mutation in this child is

most likely which one of the following? A. Proline to hydroxyproline

B. Glycine to cysteine C. Proline to glycine D. Glycine to proline E. Serine to proline

8.Bisphosphonate treatment of children with OI is based on which one of the following?

A. Stimulation of osteoclast activityB. Inhibition of osteoclast activity C. Stimulation of osteoblast activity

D. Inhibition of osteoblast activity E. Stimulation of laminin synthesis F.

Inhibition of laminin synthesis

9.Collagen provides great tensile strength to connective tissue by its structure as a triple helix. Which

amino acid is critical in allowing triple-helix formation? A. Proline

B. Hydroxyproline

C.Lysine

D.Glycine

E.Elastin

10. A common feature of the mucopolysaccharidoses is the accumulation of heparin sulfate. Which of the

following disorders leads to an accumulation of that particular GAG? Choose the one best answer.

ANSWERS TO REVIEW QUESTIONS

1.The answer is E. Scurvy is caused by a deficiency of vitamin C. Vitamin C is a required cofactor

for the hydroxylation of both proline and lysine residues in collagen. The hydroxyproline residues

that are formed stabilize the collagen fiber through the formation of hydrogen bonds with other

collagen triple helices within the fiber. The loss of this stabilizing force greatly reduces the

strength of the collagen fibers. The hydroxylation of lysine allows carbohydrates to be attached to

collagen, which appear to be necessary for efficient transport of tropocollagen from the cell to the

ECM. Vitamin C is not required for disulfide bond formation, the formation of lysyl cross-links

(that enzyme is lysyl oxidase), transcription of the collagen genes, or the formation of collagen

fibrils. Thus, all the other choices are incorrect.

2.The answer is C. When elastin expands as a result of outside forces (such as the respiratory

muscles causing the lungs to expand with air), hydrophobic regions of elastin are exposed to the

aqueous environment, resulting in a decrease in the entropy of water. When the outside force is

removed (by relaxation of the respiratory muscles), the driving force for contraction of elastin is

an increase in the entropy of water, so that the hydrophobic residues of elastin are again shielded

from the environment. The expansion and contraction of elastin does not involve covalent

modifications (thus, A, B, and E are incorrect), nor does it involve extensive changes in saltbridge formation (thus, D is also incorrect).

3.The answer is B. GAG chains contain negative charges, resulting from the presence of acidic

sugars and the sulfated sugars in the molecule. Thus, in their characteristic bottleneck structure, the

chains repel each other (thus, A is incorrect), yet they also attract positively charged cations and

water into the spaces between the chains. The water forms hydrogen bonds with the sugars and a

gel-like space is created. This gel acts as a diffusion sieve for materials that leave, or enter, this

space. Hydroxylation and cross-linking of chains does not occur (thus, D and E are incorrect), nor

does hydrogen bonding between chains (they are too far apart because of the charge repulsion, but

they do form hydrogen bonds with water).

4.The answer is E. In order for cells to migrate, they must free themselves from the ECM material,

which requires remodeling of the matrix components. Because of the unique structural aspects of

these components, only a small subset of proteases, the metalloproteinases, is capable of doing

this. The other answers listed are all components of the matrix, which must be remodeled in order

for cell migration to occur.

5.The answer is C. Fibronectin binds to integrins on the cell surface as well as to various ECM

components (collagen and GAGs). This binding fixes the position of the cell within the matrix.

Loss of these binding components can lead to undesirable cell movement. Fibronectin plays no

role in any of the other functions listed as possible answers.

6.The answer is A. The proteoglycans, containing the GAGs, are highly negatively charged. The

sugars often contain a carboxylic acid group (glucuronic and iduronic acids) and are often

sulfated. This high level of negative charges attracts cations to the proteoglycans, bringing with the

cations water through an osmotic effect. When weight is placed on the joint the water in the space

cushions the force generated, and when the weight is removed, water can return to the space.

Losing negative charges would reduce the amount of water in the joint and the ability of the joint

to prevent bone–bone interactions. The proteoglycans are not positively charged and do not attract

anions. Increasing the negative charges exhibited by the proteoglycans would enhance the

cushioning effect, as would increasing the concentration of glucuronic acid residues and sulfated

sugars (because both of those changes increase the concentration of negative charges in the joint).

7.The answer is B. Glycine is present at every third residue within a collagen monomer because it

is the only amino acid side chain that can fit in the triple helix when the three chains wind about

each other. Substitution of glycine with any other amino acid can lead to a weakened collagen

structure. However, when cysteine is present instead of a glycine, the cysteine has the capability

of forming disulfide bonds, which can stabilize the unstable collagen triple helix. A glycine-tocysteine substitution requires the change of only one nucleotide in the DNA sequence. When the

child’s collagen is run on an SDS-PAGE gel, the molecular weight is greater than native collagen

because of the cross-links in the collagen. Mercaptoethanol will break those links, so after treating

with mercaptoethanol the molecular weight of collagen would appear normal in the gel.

Conversion of proline to hydroxyproline is a normal event in collagen biosynthesis and allows for

hydrogen bonding to occur, which will stabilize the collagen triple helix. Proline to glycine will

not lead to cross-links in collagen, nor will glycine or serine to proline. The latter mutations may

disrupt triple-helix formation and lead to a form of osteogenesis imperfecta, but they would notlead to the biochemical findings of cross-linking.

8.The answer is B. Osteoclasts resorb bone, whereas osteoblasts produce bone. Normally, there is

a balance between osteoclast and osteoblast activity within bones, allowing the appropriate

amount of bone tissue to be generated and then turned over and resynthesized. However, certain

conditions can lead to enhanced osteoclast activity, such as reduced levels of collagen being

produced or altered collagen molecules being produced. Under these conditions, the osteoclasts

resorb more bone than the osteoblasts can synthesize, leading to weak and fragile bones.

Bisphosphonates inhibit osteoclast activity, thereby allowing more bone to be produced, even if

the collagen being produced is not normal. Laminin is not involved in bone

formation. Inhibition

of osteoblast activity would lead to reduced bone formation, which is the opposite of what one

wants to occur under these conditions.

9.The answer is D. The three polypeptide chains of the triple helix are linked by interchain

hydrogen bonds. Each turn of the helix contains three amino acid residues with every third amino

acid in close contact with the other two strands in the center of the structure. Only glycine, which

lacks a side chain, can fit in this position. The other amino acids listed are important amino acids

in collagen but cannot fit into the central position critical for the triple helix. Elastin is a protein,

not an amino acid. The proline is required for each chain to form a polyprolyl helix, but the

glycine is essential for allowing triple-helix formation.

10.The answer is F. Maroteaux-Lamy is deficient in N-acetylgalactosamine sulfatase

and

accumulates dermatan sulfate. All the others listed accumulate heparin sulfate (+/− dermatan

sulfate).Patient Index

NOTE: Page numbers followed by f denote figures; page numbers followed by t denote tables.

AA l M.

alcohol-induced acidosis in, 703, 710, 781 alcohol-induced pancreatitis in, 595, 597, 598, 599, 602 beriberi heart disease in, 143, 458, 465, 474, 781 blood alcohol level in, 151, 154, 161, 164

ethanol effects in, 170, 173, 184–185

ethanol metabolism in, 154, 156, 161, 164, 182, 184–185, 703

glucose 6-phosphate dehydrogenase deficiency in, 544–545, 549, 559–560 hypoglycemia in, 568, 575, 584–585

steatorrhea in, 598, 599

thiamin deficiency in, 129, 136, 143, 465, 546, 781 Amy B.

abdominal CT in, 911, 913 amoebiasis in, 911, 913, 914 antiparasitic therapy for, 914 immunoassay in, 914

liver enzyme levels in, 912 liver function of, 914

Amy L.

amyloidosis in, 101, 105, 114, 122 Bence–Jones proteins in, 122 plasma cell dyscrasia in, 101, 114 renal biopsy in, 105

serum protein electrophoresis in, 114 Anne J.

aspirin therapy for, 643, 659 HDL levels in, 688

hypercholesterolemia in, 667–668, 687, 695 lipid-lowering therapy for, 667–668, 682, 688, 695, 696 myocardial infarction in, 81, 95, 101, 122

angina in, 81, 101

cardiac enzymes in, 81, 91, 95, 116, 122 myoglobin levels in, 111 radioimmunoassay in, 116

Ann R.

amenorrhea in, 35, 40anorexia nervosa in, 19, 35, 40–41, 151, 191, 207 basal metabolic rate of, 9, 10, 11

blood glucose levels in, 568, 579

chemical messengers in, 191, 192, 194, 197, 207 daily energy expenditure of, 10, 11

dietary analysis for, 6, 7 glucagon and insulin levels in, 387 glucose levels of, 38, 41

iron-deficiency anemia in, 295, 309, 314, 458, 474, 484 ketone body levels of, 38

malnutrition in, 35, 40–41

metabolism in, 151, 152, 153, 159, 163, 164, 191 vitamin deficiencies in, 458, 461, 463, 474 weight and weight loss of, 4, 10, 11, 13, 19

BB eatrice T.

vitamin B12 deficiency in, 791, 802 vitamin B12 malabsorption in, 802 CC

alvin A.

biopsy of moles, 231, 246, 345, 363 melanoma in, 231, 240, 246, 345, 346, 353 survival and surveillance for, 240 warning signs in, 363

Candice S.

aldolase deficiency in, 451 dietary restrictions in, 436

fructose 1-phosphate levels in, 442, 451

hereditary fructose intolerance in, 436, 442, 451–452 Carrie S.

genetic testing for fiancé, 335, 339 sickle cell trait/testing in, 320, 330, 339 Catherine T.

mushroom poisoning in, 252, 254, 268 supportive therapy for, 268

Charles F.

doxorubicin toxicity in, 482 interferon therapy for, 308 miRNA expression in, 313

non-Hodgkin lymphoma in, 295, 308, 313, 482 R-CHOP chemotherapy for, 295, 313, 819 Chet S.

ACTH and cortisol levels in, 855, 856, 857, 864 body fat distribution in, 847, 858

Cushing disease in, 847, 855, 856, 857, 858, 864 differential diagnosis for, 855

explanation of symptoms, 856 hyperglycemia in, 856 muscle wasting in, 847, 856 striae of, 847, 856

Christy L. arterial pH of, 634 lu

ng surfactant deficiency in, 655 lu

ng surfactant therapy for, 659

premature birth of, 634respiratory distress syndrome of newborn in, 634, 655, 659 Clark T.

colon cancer in, 214, 225–226, 345, 363, 796, 802 5-fluorouracil for, 214, 224, 226, 345, 791, 796, 819 follow-up and surveillance after, 363, 791, 802 metastasis of, 214, 224, 226, 345

oncogene in, 346

colonoscopies in, 214, 224, 225–226, 345, 363, 791, 802 colon polyps (adenomas) in, 214, 224, 225–226

Connie C.

hypoglycemia in, 377, 381, 382, 383, 386

insulinoma in, 377, 382, 383, 385, 386, 389, 720, 724, 728 Cora N.

angina pectoris in, 395

arrhythmia in, 505

aspirin therapy for, 643, 659

familial combined hyperlipidemia in, 634, 658–659 heart failure in, 395, 409

hypoxia in, 395

ischemia in, 450, 481, 487

ischemia–reperfusion injury in, 499, 505, 507, 509, 514, 519–520 nitroprusside for, 489

thrombolytic therapy for, 481, 498–499 DD

avid K.

amino acid transport/metabolism in, 739, 743, 746 cystinuria in, 87, 95, 739, 743, 746, 776

kidney stones in, 81, 87, 95, 739 preventive measures for, 739 Deborah S.

diabetes mellitus type 2 in, 377, 388–389, 581

blood glucose levels in, controlling, 417, 426, 430, 441 dietary management for, 417, 426

glipizide therapy for, 384 glucose intolerance in, 581 glycogen metabolism in, 535 hemoglobin A1c levels in, 379

hyperglycemia in, 377, 379, 388–389, 417, 430, 535, 585 insulin resistance in, 385, 388–389, 724, 725, 726 microvascular complications in, 585, 991–992

diabetic nephropathy in, 979, 991–992 azotemia in, 979

creatinine level in, 979

glomerular basement membrane in, 991–992 uremia in, 979, 991–992

glycogen metabolism in, 535

lipid levels of, 720, 724, 725, 726, 728 obesity of, 377, 720

sorbitol levels in, 441 Denise V.

dietary management for, 429 la

ctase deficiency in, 424, 429 la

ctose intolerance in, 417, 424, 429 over-the-counter products for, 424, 429 Dennis V.

cholera in, 170, 185, 191, 207, 430ADP-ribosylation in, 182, 185 antibiotics for, 170, 207

cholera toxin in, 175, 185, 191, 205

cystic fibrosis transmembrane conductance regulator (CFTR) in, 177, 182, 185, 191, 205

diarrhea and dehydration in, 170, 175, 185, 191, 205 hypovolemic shock in, 191

rehydration therapy for, 170, 185, 207

Vibrio cholerae as causative agent of, 170, 171, 185 malathion poisoning in, 129, 140, 143

salicylate overdose by, 48, 52, 57, 496 Dianne A.

amino acid metabolism in, 626

blood glucose levels of, 45, 46, 48, 56, 246, 581

diabetes mellitus type 1 in, 56, 201, 383, 385, 388–389, 581 diabetic ketoacidosis in, 48, 56, 609, 626, 720, 726

blood and cellular pH in, 48, 52, 53, 55, 56, 609 coma in, 48, 50

follow-up in, 63

“fruity” odor of acetone in, 48, 63, 609 hyperventilation in, 55, 56

ketone body measurement in, 63, 64, 75, 609, 624

Kussmaul breathing in, 54, 56, 609, 624 rehydration therapy for, 50, 51, 56 urine/nitroprusside test for, 63

fatty acid metabolism in, 48, 56, 626, 723, 724, 726, 728 glucose monitoring in, 63, 75

glucose transport in, 176 hemoglobin A1C in, 101, 120, 122

human leukocyte antigen (HLA) defect in, 383 hyperglycemia in, 48, 56, 388–389, 535, 585, 724 hypoglycemic coma in, 568, 579

insulin therapy for, 56, 81, 95, 335 lipid levels of, 720, 723, 724, 726, 728 microvascular complications in, 585 muscle wasting in, 201

osmotic diuresis in, 50, 56 polyuria in, 50

signal transduction in, 201 sorbitol levels in, 441

urinary tract infection in, 231, 233, 246 EE

dna R.

diphtheria vaccine for daughter, 275, 284, 287 hepatitis B vaccine for, 320, 335, 338

work in blood bank, 545, 556, 560–561 Edward R.

enlarged spleen in, 870, 886–887 reticulocytes in, 870

spectrin deficiency in, 886–887 spherocytosis in, 870, 886–887 splenectomy for, 887

Emma W.

asthma treatment for, systemic vs. inhaled, 633–634, 658 glucocorticoid-induced hyperglycemia in, 568, 571, 577, 585 Erin G.

galactosemia in, 436, 442, 452jaundice in, 436, 551 Evan A.

referral for bariatric surgery, 973 serotonin levels in, 965, 973 weight-loss drugs for, 954, 965, 973 GGr

etchen C.

Apgar score of, 526 bradycardia in, 526

glycogen stores of, 532, 536, 538 maternal malnutrition and, 526, 532, 538

neonatal hypoglycemia in, 526, 532, 536, 538–539 HH

orace S.

biochemical studies in, 776

cystathione β-synthase deficiency in, 779, 784–785 homocystinuria in, 776, 779, 780, 784–785

inborn error of metabolism in, 772 skeletal mineralization in, 772

vascular events/cerebral infarct in, 772, 785 vitamin B6 for, 785

II sabel S.

HIV in, 214, 225

HIV testing for friend of, 320, 324

HIV treatment for, 216, 231, 234, 246, 494, 499 myopathy in, 482, 494, 499

tuberculosis in, 252, 253, 260, 268, 320 zidovudine (AZT) therapy for, 494, 499 Ivan A.

aspirin therapy for, 643, 659

basal metabolic rate of, 9, 10, 11 daily energy expenditure of, 10, 11 dental caries in, 436, 444, 451 diabetes mellitus type 2 in, 27, 30, 389 dietary analysis for, 7, 8

dietary plans for, 19, 27, 30 ethanol metabolism in, 703, 708, 711 HDL levels in, 689

hyperglycemia in, 27, 30 hypertension in, 4, 25

lipid levels in, 25, 29, 30, 687 lipid-lowering therapy for, 695–696 metabolic syndrome in, 30, 667, 695–696

weight and obesity of, 4, 10, 11, 13, 18–19, 25, 29–30 JJa

y S.

genetic testing in, 275, 287

hexosaminidase A deficiency in, 275, 287, 561 psychomotor development of, 275, 545 Tay–Sachs disease in, 275, 287, 545, 561 Jean T.

alcohol-induced cirrhosis in, 712–713, 911, 926blood glucose levels of, 927 ethanol consumption by, 703, 911

fatty acid metabolism in, 927

folate deficiency and anemia in, 791, 792, 796, 797, 802 ketone body production in, 927

vomiting of blood, 911 Jim B.

anabolic steroid use by, 526, 539 insulin overdose in, 526–527, 538, 539 KKa

therine B.

negative nitrogen balance in, 827, 836

sepsis and hypercatabolic state in, 824, 827, 836–837 Katie C.

adrenal surgery for, 963, 973 catecholamine levels in, 963, 964, 973 hypertension in, 954

phenoxybenzamine for, 963, 973 pheochromocytoma in, 954, 963, 964, 973 propranolol for, 973

LL es G.

catecholamine measurements in, 506 lipofuscin in, 509

monoamine oxidase inhibitor for, 508, 519 Parkinson disease in, 505, 508, 509, 519 Linda F.

COPD in, 435, 445 hypotension in, 435, 450–451

hypoxemia in, 435, 444, 445, 450–451 Lisa N.

β-thalassemia in, 252, 268, 275, 287, 290t

genetic mutations in, 256, 261, 268, 278–279, 290t, 887 intermediate type of, 252, 256, 268, 275, 287

stem (precursor) cells in, 314

fetal hemoglobin persistence in, 870, 887 osteoporosis and fracture in, 870

Lola B.

fasting effects on, 608–609, 625–626

fatty acid metabolism in, 609, 615, 620, 625–626 MCAD deficiency in, 615, 625–626

Lotta T.

chemical messaging in, 195

gout in, 63, 75, 129, 143, 170, 185, 807, 818

allopurinol for, 75, 129, 142, 143, 170, 185, 807, 818 colchicine for, 75, 143, 170, 183, 185, 807 inflammatory response in, 74, 180, 185, 195

le

ukotrienes in, 195

uric acid/urate crystals in, 74, 180, 818 MMa

nnie W.

chronic myelogenous leukemia in, 295, 303, 308, 313–314, 345, 362 hemorrhagic signs in, 345

interferon therapy for, 308, 362lymp hocyte percentage in, 295

Philadelphia chromosome in, 295, 303, 314, 345, 349, 362 white blood cell count of, 295, 362

Mia S.

acetylcholine/ACh receptors in, 191, 193, 206 anticholinesterase inhibitors for, 206–207 edrophonium chloride testing in, 193 myasthenia gravis in, 191, 193, 206–207 neurophysiologic testing in, 206

prognosis for, 206 Michael T.

brain metastases in, 345, 363 lu

ng cancer in, 231, 246, 345, 346, 363 smoking history of, 231, 240, 246, 361 TNM staging in, 363

NN ina M.

fructose malabsorption in, 418, 423, 430 hydrogen breath test for, 423

OO tto S.

basal metabolic rate of, 395, 400 body mass index (BMI) of, 4, 18 daily energy requirement of, 402 dietary plan for, 18, 406, 409 dietary supplements for, 608, 613 ethanol intake of, 406 exercise/physical conditioning by blood glucose levels in, 584

electron-transport chain in, 451, 459, 467, 473, 617, 624 fatty acid metabolism in, 609, 617, 624–625

improved capacity in, 458, 467, 473, 568, 624–625 insulin and counterregulatory hormones in, 609 ketosis in, 625

la

ctate production in, 449, 451, 473, 624–625 muscle metabolism of glucose in, 944, 945 oxidative phosphorylation in, 449 recommendation for, 409

succinate as fuel for, 462, 463 training for race, 436

tricarboxylic acid cycle in, 449, 459, 462, 463, 467, 473 MyPlate Personalized Plan for, 18

weight gain in, 4, 395, 400, 409, 436, 568 weight goals of, 4, 18, 568

weight loss in, 458 PP

aul T.

pneumonia in, 214, 275

antibiotic sensitivity of, 275, 281, 282, 283 azithromycin for, 214, 225, 226, 275, 283, 287 sputum culture in, 214, 275

Percy V.

anthropometric measurements of, 35

counseling for, 40creatinine-height index of, 35, 40 depression-related malnutrition in, 4, 14, 19, 35, 37, 40 glucose levels of, 37, 40

hypercaloric diet in, 634, 649, 658 hyperventilation in, 48, 55, 57 ketone body levels of, 37

liver enzyme levels in, 755, 757 nutrient deficiencies in, 14, 16, 19, 40 protein levels of, 38, 40

viral hepatitis (hepatitis A) in, 753, 755, 757, 760, 764 Peter K.

factor VIII deficiency in, 894, 898 factor VIII therapy for, 904–905 hematoma in, 894, 904

hemophilia A in, 894, 904–905 Petria Y.

dietary intervention for, 784

Guthrie bacterial inhibition assay in, 772 phenylketonuria in, 772, 783, 784

RRe nee F.

creatinine level in, 933, 941, 948 glomerular filtration rate in, 941, 948

poststreptococcal glomerulonephritis in, 933, 941, 948 SS

am A.

diabetes mellitus in, 851, 864 growth hormone levels in, 850, 864

pituitary tumor and acromegaly in, 847, 849, 850, 851, 864 Sarah L.

antibody assay in, 262 anti-inflammatory therapy for, 269 butterfly rash of, 252 immunosuppressive therapy for, 269 joint inflammation in, 979, 990–991

proteolytic action of chondrocytes in, 990–991

systemic lupus erythematosus in, 252, 262, 269, 979, 990–991 Stanley T.

fuel oxidation in, 403, 409 goiter in, 409, 481

Graves disease in, 481, 499 heart rate and beat in, 395, 409

heat intolerance in, 395, 403, 481, 499 hyperthyroidism in, 395, 401, 403, 409, 481, 499 thyroid hormone levels in, 395, 401, 409

Susan F.

CFTR deficiency in, 320

chloride channel defect in, 320, 741

cystic fibrosis in, 320, 332–333, 339, 419, 739, 741, 745–746 genetic testing in, 332, 333, 339

protein malnutrition/metabolism in, 739, 745–746 Pseudomonas aeruginosa infection in, 320, 739 VVe

ra L.androgen excess in, 694, 695, 696–697 hirsutism in, 668, 694, 695

virilization in, 668, 690, 696–697 Victoria T.

DNA fingerprinting in case, 334, 339 rape and murder of, 320

semen/DNA samples from, 320, 329, 334, 339 WWill

S.

bilirubin levels in, 81, 82, 595, 598, 602, 883 cholecystitis/gallstones in, 81, 595, 598, 602, 883