ROBBINS BASIC PATHOLOGY
10TH EDITION
AUTHOR(S)VINAY KUMAR; ABUL K.
ABBAS; JON C. ASTER
TEST BANK
1)
Reference
Ch. 1 — The Cell as a Unit of Health and Disease — The
Genome
Question Stem
A 28-year-old woman is found to have a heterozygous missense
mutation in a DNA repair gene that impairs base excision repair.
Clinically, she has increased sensitivity to oxidative stress.
Which cellular consequence best explains her increased
susceptibility to oxidative DNA damage?
Options
A. Increased rate of translesion synthesis producing more
accurate DNA replication
,B. Accumulation of small base modifications leading to point
mutations during replication
C. Enhanced removal of bulky adducts by nucleotide excision
repair
D. Increased telomere shortening due to impaired telomerase
activity
Correct Answer
B
Rationales
Correct: Base excision repair removes small base lesions (e.g.,
oxidative modifications); impairment causes accumulation of
base alterations that become fixed as point mutations during
replication. This explains heightened sensitivity to oxidative
damage.
A: Translesion synthesis is error-prone and does not increase
accuracy; it’s a bypass mechanism, not a compensatory increase
in fidelity.
C: Nucleotide excision repair removes bulky helix-distorting
lesions, not small oxidative bases; it doesn't compensate for
base excision defects.
D: Telomerase/telomere biology is unrelated to base excision
repair and oxidative base lesions.
Teaching Point
Base excision repair fixes small oxidative base lesions; its failure
→ point mutations.
,Citation
Kumar et al. (2021). Robbins Basic Pathology (10th Ed.). Ch. 1.
2)
Reference
Ch. 1 — The Cell as a Unit of Health and Disease — Cellular
Housekeeping
Question Stem
A patient’s muscle biopsy shows accumulation of
polyubiquitinated proteins within myocytes and impaired
proteasome activity. Which downstream cellular effect most
directly results from this defect?
Options
A. Increased autophagic clearance of protein aggregates with
no toxicity
B. Activation of the unfolded protein response leading to ER
stress and possible apoptosis
C. Enhanced mitochondrial biogenesis and increased ATP
production
D. Immediate membrane rupture and necrotic cell death
Correct Answer
B
Rationales
Correct: Impaired ubiquitin–proteasome degradation leads to
accumulation of misfolded proteins, provoking ER stress and
, the unfolded protein response, which can trigger apoptosis if
unresolved.
A: Autophagy may be upregulated but is often insufficient to
fully compensate; accumulation persists and toxicity can occur.
C: Proteasome impairment does not directly enhance
mitochondrial biogenesis or ATP production.
D: Immediate membrane rupture (necrosis) is not the direct
consequence of proteasome failure; ER stress–mediated
apoptosis is more characteristic.
Teaching Point
Proteasome failure → misfolded protein accumulation → ER
stress and apoptosis risk.
Citation
Kumar et al. (2021). Robbins Basic Pathology (10th Ed.). Ch. 1.
3)
Reference
Ch. 1 — The Cell as a Unit of Health and Disease — Cellular
Metabolism and Mitochondrial Function
Question Stem
A hospitalized patient develops lactic acidosis after receiving a
drug that inhibits mitochondrial complex I. Which cellular
change best explains the lactate accumulation?
Options
A. Increased oxidative phosphorylation → more pyruvate
10TH EDITION
AUTHOR(S)VINAY KUMAR; ABUL K.
ABBAS; JON C. ASTER
TEST BANK
1)
Reference
Ch. 1 — The Cell as a Unit of Health and Disease — The
Genome
Question Stem
A 28-year-old woman is found to have a heterozygous missense
mutation in a DNA repair gene that impairs base excision repair.
Clinically, she has increased sensitivity to oxidative stress.
Which cellular consequence best explains her increased
susceptibility to oxidative DNA damage?
Options
A. Increased rate of translesion synthesis producing more
accurate DNA replication
,B. Accumulation of small base modifications leading to point
mutations during replication
C. Enhanced removal of bulky adducts by nucleotide excision
repair
D. Increased telomere shortening due to impaired telomerase
activity
Correct Answer
B
Rationales
Correct: Base excision repair removes small base lesions (e.g.,
oxidative modifications); impairment causes accumulation of
base alterations that become fixed as point mutations during
replication. This explains heightened sensitivity to oxidative
damage.
A: Translesion synthesis is error-prone and does not increase
accuracy; it’s a bypass mechanism, not a compensatory increase
in fidelity.
C: Nucleotide excision repair removes bulky helix-distorting
lesions, not small oxidative bases; it doesn't compensate for
base excision defects.
D: Telomerase/telomere biology is unrelated to base excision
repair and oxidative base lesions.
Teaching Point
Base excision repair fixes small oxidative base lesions; its failure
→ point mutations.
,Citation
Kumar et al. (2021). Robbins Basic Pathology (10th Ed.). Ch. 1.
2)
Reference
Ch. 1 — The Cell as a Unit of Health and Disease — Cellular
Housekeeping
Question Stem
A patient’s muscle biopsy shows accumulation of
polyubiquitinated proteins within myocytes and impaired
proteasome activity. Which downstream cellular effect most
directly results from this defect?
Options
A. Increased autophagic clearance of protein aggregates with
no toxicity
B. Activation of the unfolded protein response leading to ER
stress and possible apoptosis
C. Enhanced mitochondrial biogenesis and increased ATP
production
D. Immediate membrane rupture and necrotic cell death
Correct Answer
B
Rationales
Correct: Impaired ubiquitin–proteasome degradation leads to
accumulation of misfolded proteins, provoking ER stress and
, the unfolded protein response, which can trigger apoptosis if
unresolved.
A: Autophagy may be upregulated but is often insufficient to
fully compensate; accumulation persists and toxicity can occur.
C: Proteasome impairment does not directly enhance
mitochondrial biogenesis or ATP production.
D: Immediate membrane rupture (necrosis) is not the direct
consequence of proteasome failure; ER stress–mediated
apoptosis is more characteristic.
Teaching Point
Proteasome failure → misfolded protein accumulation → ER
stress and apoptosis risk.
Citation
Kumar et al. (2021). Robbins Basic Pathology (10th Ed.). Ch. 1.
3)
Reference
Ch. 1 — The Cell as a Unit of Health and Disease — Cellular
Metabolism and Mitochondrial Function
Question Stem
A hospitalized patient develops lactic acidosis after receiving a
drug that inhibits mitochondrial complex I. Which cellular
change best explains the lactate accumulation?
Options
A. Increased oxidative phosphorylation → more pyruvate
