Anatomy
1 questionsTrigone of bladder is derived from?
NEET-PG 2015 - Anatomy NEET-PG Practice Questions and MCQs
Question 521: Trigone of bladder is derived from?
- A. Mesonephric duct (Correct Answer)
- B. Paramesonephric duct
- C. Absorbed anal membrane
- D. Mullerian duct
Explanation: The trigone of the bladder is formed from the caudal ends of the **mesonephric ducts**, which are absorbed into the primitive bladder wall [1]. This mesenchymal origin explains why the trigone has a smooth lining [1] and is less prone to infection compared to the rest of the bladder. *Paramesonephric duct* - The **paramesonephric ducts** (Müllerian ducts) are involved in forming the female reproductive organs, specifically the fallopian tubes, uterus [2], and upper vagina. - They do not contribute to the formation of the urinary bladder or its trigone. *Absorbed anal membrane* - The **anal membrane** separates the endoderm-derived hindgut from the ectoderm-derived anal pit. - Its absorption is relevant to the development of the anus, not the urinary bladder. *Mullerian duct* - The **Müllerian ducts** are synonymous with the paramesonephric ducts and are primarily involved in the development of the female reproductive tract [2]. - They play no role in the development of the urinary bladder or its trigone.
Biochemistry
4 questionsEnzyme deficient in Hers disease -
Fumarate is formed from which amino acid?
Citrate synthase is inhibited by -
Which of the following processes primarily utilizes lactate produced anaerobically?
NEET-PG 2015 - Biochemistry NEET-PG Practice Questions and MCQs
Question 521: Enzyme deficient in Hers disease -
- A. Muscle phosphorylase
- B. Liver phosphorylase (Correct Answer)
- C. Acid maltase
- D. Debranching enzyme
Explanation: ***Liver phosphorylase*** - Hers disease, also known as Glycogen Storage Disease Type VI, is specifically caused by a deficiency of **liver phosphorylase**. - This enzyme is crucial for the breakdown of **glycogen in the liver**, leading to an inability to release glucose into the bloodstream during fasting. *Muscle phosphorylase* - Deficiency of **muscle phosphorylase** (myophosphorylase) causes **McArdle disease** (Glycogen Storage Disease Type V), which primarily affects muscle energy. - Patients typically present with exercise intolerance, muscle pain, and cramps, not the hepatic symptoms seen in Hers disease. *Acid maltase* - Deficiency of **acid maltase** (also known as alpha-glucosidase) is responsible for **Pompe disease** (Glycogen Storage Disease Type II), a lysosomal storage disorder. - This enzyme deficiency leads to glycogen accumulation in lysosomes in various tissues, including muscle, liver, and heart, causing muscle weakness and cardiomyopathy. *Debranching enzyme* - A deficiency in the **debranching enzyme** (amylo-1,6-glucosidase) causes **Cori disease** or **Forbes disease** (Glycogen Storage Disease Type III). - This results in the accumulation of abnormally structured glycogen with short outer branches in the liver, muscle, and heart.
Question 522: Fumarate is formed from which amino acid?
- A. Methionine
- B. Valine
- C. Histidine
- D. Tyrosine (Correct Answer)
Explanation: ***Tyrosine*** - **Tyrosine** is a **glucogenic and ketogenic amino acid** that is catabolized to acetoacetate and fumarate. - **Fumarate** then enters the **citric acid cycle (Krebs cycle)**, whereas acetoacetate is a ketone body. *Methionine* - **Methionine** is an **essential amino acid** and a precursor for **S-adenosylmethionine (SAM)**, a methyl donor in many reactions. - Its catabolism produces **succinyl CoA**, not fumarate, through a series of steps via propionyl CoA. *Valine* - **Valine** is a **branched-chain amino acid (BCAA)** that is exclusively **glucogenic**. - Its catabolism ultimately leads to the formation of **succinyl CoA**, which can enter the citric acid cycle. *Histidine* - **Histidine** is an **essential amino acid** that is catabolized to **formiminoglutamate (FIGLU)**. - FIGLU is then converted to **glutamate**, which can eventually be deaminated to α-ketoglutarate, a citric acid cycle intermediate, but not directly fumarate.
Question 523: Citrate synthase is inhibited by -
- A. Insulin
- B. Glucagon
- C. ADP
- D. ATP (Correct Answer)
Explanation: ***ATP*** - **Citrate synthase**, a key enzyme in the Krebs cycle, is inhibited by **high levels of ATP**, indicating a high energy state in the cell. - This allosteric inhibition helps regulate the metabolic flux through the cycle, slowing it down when energy is abundant. *ADP* - **ADP** typically signifies a low energy state and would generally act as an **activator** rather than an inhibitor for metabolic pathways that produce ATP. - In this context, ADP would promote the activity of enzymes involved in energy generation, including those in the Krebs cycle. *Insulin* - **Insulin** is a hormone that promotes fuel storage and utilization, generally **activating** metabolic pathways rather than directly inhibiting enzymes like citrate synthase. - Its primary role is to regulate blood glucose levels and promote glucose uptake and utilization. *Glucagon* - **Glucagon** is a hormone that mobilizes fuel from storage and is typically associated with **catabolic processes**, often increasing metabolic activity in response to low blood glucose. - It does not directly inhibit citrate synthase; its main actions are on glucoregulation.
Question 524: Which of the following processes primarily utilizes lactate produced anaerobically?
- A. Cori cycle (Correct Answer)
- B. Gluconeogenesis
- C. TCA cycle
- D. Glycolysis
Explanation: ***Cori cycle*** - The **Cori cycle** (lactic acid cycle) involves the transport of **lactate** produced during anaerobic metabolism in muscles to the liver. - In the **liver**, this lactate is then converted back to **glucose** via gluconeogenesis, which can be returned to the muscles. *Gluconeogenesis* - **Gluconeogenesis** is the synthesis of glucose from non-carbohydrate precursors, one of which is lactate. - While it uses lactate, it is only one component of the broader **Cori cycle**, which describes the inter-organ cooperation. *Glycolysis* - **Glycolysis** is the metabolic pathway that breaks down glucose into pyruvate, which can then be converted to lactate under anaerobic conditions. - This process *produces* lactate but does not *utilize* it, acting upstream of lactate production. *TCA cycle* - The **TCA cycle** (Krebs cycle) is a central part of aerobic respiration that oxidizes acetyl-CoA to produce ATP, NADH, and FADH2. - It does not directly utilize lactate; instead, lactate is typically converted to pyruvate before potentially entering the TCA cycle under aerobic conditions.
Pharmacology
3 questionsWhat is the mechanism of action of ticagrelor?
Which of the following conditions is not associated with an increased risk of neuropathy caused by Isoniazid (INH)?
Which of the following is the longest acting carbapenem?
NEET-PG 2015 - Pharmacology NEET-PG Practice Questions and MCQs
Question 521: What is the mechanism of action of ticagrelor?
- A. Reversible inhibition of ADP action (Correct Answer)
- B. Irreversible inhibition of ADP action
- C. Reversible inhibition of GPIIb/IIIa
- D. Irreversible inhibition of GPIIb/IIIa
Explanation: ***Reversible inhibition of ADP action*** - **Ticagrelor** is a **P2Y12 receptor antagonist** that works by preventing ADP from binding to its receptor on platelets [2]. - This binding is **reversible**, meaning ticagrelor can dissociate from the receptor, allowing for some recovery of platelet function over time [2]. *Irreversible inhibition of ADP action* - **Clopidogrel** and **prasugrel** are examples of **irreversible P2Y12 inhibitors**, forming a permanent bond with the receptor [2]. - Irreversible inhibition leads to a longer duration of platelet inhibition, as new platelets must be generated for function to return [2]. *Reversible inhibition of GPIIb/IIIa* - **GPIIb/IIIa inhibitors** like **eptifibatide** and **tirofiban** block the final common pathway of platelet aggregation by preventing fibrinogen binding [1]. - While their action is reversible, they target a *different* mechanism than ticagrelor. *Irreversible inhibition of GPIIb/IIIa* - **Abciximab** is a GPIIb/IIIa inhibitor that binds **irreversibly** (or with very slow dissociation) to the receptor [1]. - Unlike reversible GPIIb/IIIa inhibitors, abciximab is a monoclonal antibody with a prolonged antiplatelet effect [1]. - This is still an incorrect answer as ticagrelor targets the P2Y12 receptor, not GPIIb/IIIa.
Question 522: Which of the following conditions is not associated with an increased risk of neuropathy caused by Isoniazid (INH)?
- A. Uremia
- B. Diabetes mellitus
- C. Poor nutrition
- D. Hyperthyroidism (Correct Answer)
Explanation: ***Hyperthyroidism*** - **Hyperthyroidism** is not typically associated with an increased risk of isoniazid-induced neuropathy. The neuropathy due to INH is primarily linked to **pyridoxine (vitamin B6) deficiency**. - While hyperthyroidism can cause its own set of neurological symptoms, it does not directly impair pyridoxine metabolism or exacerbate INH's neurotoxic effects. *Uremia* - **Uremia** (renal failure) can increase the risk of INH-induced neuropathy due to impaired drug excretion, leading to higher plasma concentrations of INH and its metabolites. - Patients with uremia often have compromised nutritional status and may experience vitamin deficiencies, further contributing to pyridoxine depletion. *Diabetes mellitus* - **Diabetes mellitus** is a significant risk factor for INH-induced neuropathy because it is an independent cause of **peripheral neuropathy** itself, making patients more susceptible to additional nerve damage. - Diabetic patients may also have altered pyridoxine metabolism or suboptimal nutritional intake, predisposing them to INH toxicity. *Poor nutrition* - **Poor nutrition**, particularly malabsorption or inadequate dietary intake, directly contributes to **pyridoxine (vitamin B6) deficiency**. - Isoniazid's mechanism of neurotoxicity involves interfering with pyridoxine metabolism, so pre-existing deficiency significantly increases the risk of neuropathy.
Question 523: Which of the following is the longest acting carbapenem?
- A. Imipenem
- B. Meropenem
- C. Doripenem
- D. Ertapenem (Correct Answer)
Explanation: ***Ertapenem*** - **Ertapenem** has the **longest half-life** among the carbapenems, allowing for once-daily dosing. - Its prolonged action is due to its **chemical structure**, which provides high protein binding and reduced renal clearance compared to other carbapenems. *Imipenem* - **Imipenem** has a **relatively short half-life** and requires co-administration with cilastatin to prevent its renal metabolism by dehydropeptidase-1. - Its short duration of action necessitates **frequent dosing**, typically every 6 to 8 hours. *Meropenem* - **Meropenem** has a **shorter half-life** than ertapenem, generally requiring dosing every 8 hours. - Although it does not require cilastatin, its pharmacokinetic profile is not as extended as ertapenem's. *Doripenem* - **Doripenem** also has a **shorter half-life** than ertapenem, necessitating administration every 8 hours. - Its spectrum of activity is similar to meropenem, but it does not offer the same extended duration of action.
Physiology
2 questionsRebound increase in gastric acid secretion after stopping proton pump inhibitor therapy is due to?
The major role of 2,3-bisphosphoglycerate in RBCs is -
NEET-PG 2015 - Physiology NEET-PG Practice Questions and MCQs
Question 521: Rebound increase in gastric acid secretion after stopping proton pump inhibitor therapy is due to?
- A. Parietal cell hyperplasia
- B. Increased histamine release
- C. Hypergastrinemia (Correct Answer)
- D. Hypersensitivity of Ach receptors
Explanation: ***Hypergastrinemia*** - Proton pump inhibitors (PPIs) create a state of **hypochlorhydria** (reduced stomach acid), which in turn stimulates the **G cells** in the stomach to produce more **gastrin**. - This elevated gastrin level leads to a compensatory increase in the number and activity of **parietal cells**, causing a rebound hypersecretion of acid when PPI therapy is discontinued. *Parietal cell hyperplasia* - While parietal cell hyperplasia can occur, it is a consequence of chronic **hypergastrinemia**, not the primary driver of rebound acid secretion. - The direct effect of increased gastrin stimulating existing parietal cells is more immediate and significant for the rebound phenomenon. *Increased histamine release* - Elevated histamine release from **enterochromaffin-like (ECL) cells** is a downstream effect of hypergastrinemia, as gastrin stimulates ECL cells. - While increased histamine contributes to acid secretion, the root cause for its increase in this context is the **hypergastrinemia** induced by PPIs. *Hypersensitivity of Ach receptors* - **Acetylcholine (Ach) receptors** on parietal cells are involved in direct neural stimulation of acid secretion. - There is no evidence that stopping PPIs causes an increased sensitivity of these receptors, or that this is the primary mechanism of rebound acid secretion.
Question 522: The major role of 2,3-bisphosphoglycerate in RBCs is -
- A. Acid-base balance
- B. Reversal of glycolysis
- C. Release of oxygen (Correct Answer)
- D. Binding of oxygen
Explanation: ***Release of oxygen*** - **2,3-bisphosphoglycerate (2,3-BPG)** binds allosterically to **deoxyhemoglobin**, stabilizing its T (tense) state. - This binding reduces hemoglobin's affinity for oxygen, promoting the **release of oxygen** to tissues. *Acid-base balance* - While red blood cells play a role in **acid-base balance** through the bicarbonate buffer system, 2,3-BPG's primary role is not buffering. - The **chloride shift** and **carbonic anhydrase** are more directly involved in RBC acid-base regulation. *Reversal of glycolysis* - 2,3-BPG is an intermediate of the **Rapoport-Luebering shunt**, a side pathway of glycolysis. - It does not reverse glycolysis but rather is produced during glycolysis to serve a specific function in oxygen transport. *Binding of oxygen* - 2,3-BPG **decreases** hemoglobin's affinity for oxygen, thus promoting its *release* from hemoglobin, not its binding. - Oxygen binding to hemoglobin occurs primarily at the **heme iron** without 2,3-BPG.