Anatomy
1 questionsType of collagen found in space of Disse in liver is -
NEET-PG 2013 - Anatomy NEET-PG Practice Questions and MCQs
Question 341: Type of collagen found in space of Disse in liver is -
- A. Collagen I & II
- B. Collagen III & IV (Correct Answer)
- C. Collagen II
- D. Collagen II & V
Explanation: ***Collagen III & IV*** - The **space of Disse** in the liver contains a delicate extracellular matrix predominantly composed of **collagen type III (reticular fibers)**, which provides structural support, and **collagen type IV**, a major component of basement membranes. - This specific collagen composition is crucial for regulating the exchange of solutes between **sinusoidal blood** and **hepatocytes**, as well as for the functional integrity of the liver [1]. *Collagen I & II* - **Collagen type I** is the most abundant collagen in the human body, found in connective tissues like **bone, skin, tendons, and ligaments**, but is not primary in the space of Disse. - **Collagen type II** is characteristic of **hyaline cartilage** and vitreous humor, and is not a significant component of the liver's extracellular matrix in the space of Disse. *Collagen II* - As mentioned, **collagen type II** is primarily found in **cartilage** and vitreous humor, which are distinct from the architectural requirements of the liver sinusoidal space. - Its presence in the space of Disse would not provide the necessary structural flexibility and support for the metabolic functions of the liver. *Collagen II & V* - While **collagen type V** is a minor fibrillar collagen that associates with collagen type I in many tissues, it is not a primary component of the space of Disse. - **Collagen type II** is, again, largely confined to cartilaginous structures, making this an unlikely combination for the liver microenvironment.
Biochemistry
8 questionsWhich porphyrin forms the organic component of heme?
Hay's sulfur test is used to detect which of the following?
Which of the following statements about hemoglobin is true?
Which of the following statements about chaperones is false?
Which of the following is the major glycosaminoglycan of synovial fluid?
What is the mechanism by which mercury causes damage?
Which of the following statements regarding collagen synthesis is incorrect?
Albumin is the primary transport protein in blood for which of the following substances?
NEET-PG 2013 - Biochemistry NEET-PG Practice Questions and MCQs
Question 341: Which porphyrin forms the organic component of heme?
- A. Uroporphyrin
- B. Coproporphyrin
- C. Deuteroporphyrin
- D. Protoporphyrin IX (Correct Answer)
Explanation: ***Protoporphyrin IX*** - **Heme** is formed by the insertion of an **iron atom (Fe2+)** into the center of **protoporphyrin IX**. - **Protoporphyrin IX** is the immediate precursor to heme in the **heme synthesis pathway**. *Uroporphyrin* - **Uroporphyrin** is an earlier precursor in the **heme synthesis pathway** and is much more hydrophilic than protoporphyrin. - It accumulates in diseases like **congenital erythropoietic porphyria (CEP)**, leading to photosensitivity. *Coproporphyrin* - **Coproporphyrin** is an intermediate in the **heme synthesis pathway**, formed after uroporphyrinogen. - It is also more water-soluble than protoporphyrin and its accumulation can be seen in various porphyrias. *Deuteroporphyrin* - **Deuteroporphyrin** is a synthetic porphyrin or a less common natural porphyrin that is not directly involved as the organic component of heme in mammals. - While it is structurally similar to protoporphyrin, it does not serve as the direct precursor for heme formation in the human body.
Question 342: Hay's sulfur test is used to detect which of the following?
- A. Bile salts in urine (Correct Answer)
- B. Reducing sugar in urine
- C. Ketone bodies in urine
- D. Urobilinogen in urine
Explanation: ***Bile salts in urine*** - Hay's sulfur test is a classic qualitative test used to detect the presence of **bile salts** in a urine sample. - Bile salts reduce the **surface tension** of urine, causing sulfur powder to sink when sprinkled on the surface. *Reducing sugar in urine* - Reducing sugars (like glucose) are typically detected using tests such as **Benedict's test** or glucose oxidase strips, not Hay's sulfur test. - These tests rely on color changes due to the **reduction of copper ions** or enzymatic reactions, respectively. *Ketone bodies in urine* - Ketone bodies (acetoacetate, beta-hydroxybutyrate, acetone) are detected using tests like the **Rothera's test** or dipsticks, which react with acetoacetate. - These reactions produce color changes in the presence of ketones, unrelated to surface tension. *Urobilinogen in urine* - Urobilinogen in urine is commonly detected using **Ehrlich's reagent** (e.g., in a dipstick test) which forms a red color. - Elevated urobilinogen indicates issues with liver function or hemolysis, and its detection does not involve surface tension.
Question 343: Which of the following statements about hemoglobin is true?
- A. Each hemoglobin molecule can bind up to six O2 molecules.
- B. Each hemoglobin subunit contains two heme groups, which bind oxygen.
- C. Hemoglobin consists of two alpha and two beta subunits, each capable of binding one O2 molecule. (Correct Answer)
- D. Each hemoglobin molecule is made of 6 polypeptide chains.
Explanation: ***Hemoglobin consists of two alpha and two beta subunits, each capable of binding one O2 molecule.*** - A **hemoglobin molecule is a tetramer**, meaning it is composed of four protein subunits: two alpha (α) chains and two beta (β) chains. - Each of these four subunits contains one **heme group**, which is an iron-containing porphyrin complex that can reversibly bind one molecule of **oxygen (O2)**. *Each hemoglobin molecule can bind up to six O2 molecules.* - A single hemoglobin molecule, with its **four heme groups**, can bind a maximum of **four O2 molecules**, not six. - The capacity for oxygen binding is directly proportional to the number of heme groups present in the hemoglobin molecule. *Each hemoglobin subunit contains two heme groups, which bind oxygen.* - Each individual **hemoglobin subunit (alpha or beta)** contains **only one heme group**, not two. - Therefore, a complete hemoglobin molecule (with four subunits) contains a total of four heme groups. *Each hemoglobin molecule is made of 6 polypeptides, one for each subunit.* - A hemoglobin molecule is composed of **four polypeptide chains** (two alpha and two beta), not six. - This tetrameric structure is crucial for its function and **cooperative oxygen binding**.
Question 344: Which of the following statements about chaperones is false?
- A. Are lipid in nature (Correct Answer)
- B. Cause folding of proteins
- C. Include heat shock proteins
- D. May have ATPase activity
Explanation: ***Are lipid in nature*** - Chaperones are **proteins** (typically **heat shock proteins** or **chaperonins**), not lipids. - Their function involves assisting in the proper **folding and assembly of other proteins**, and they are composed of amino acids. *Cause folding of proteins* - Chaperones **do not cause** proteins to fold; rather, they **assist in proper folding** and refolding by preventing aggregation or misfolding. - They bind to nascent or partially unfolded proteins to guide them towards their correct three-dimensional structure. *May have ATPase activity* - Many chaperones, especially **Hsp70** and **chaperonins** like GroEL/GroES, utilize **ATP hydrolysis** for their function. - This **ATPase activity** drives conformational changes essential for binding, release, and refolding of their client proteins. *Include heat shock proteins* - The **heat shock protein (Hsp)** families (e.g., Hsp70, Hsp90, Hsp60) are a major class of chaperones. - Hsps are upregulated in response to stress (like heat) to help refold damaged proteins and prevent aggregation.
Question 345: Which of the following is the major glycosaminoglycan of synovial fluid?
- A. Chondroitin sulfate
- B. Dermatan sulfate
- C. Heparan sulfate
- D. Hyaluronic acid (Correct Answer)
Explanation: ***Hyaluronic acid*** - **Hyaluronic acid** is the primary glycosaminoglycan in **synovial fluid**, providing its characteristic **viscosity** and **lubricating properties**. - It plays a crucial role in maintaining **joint health** by reducing friction and acting as a shock absorber. *Chondroitin sulfate* - **Chondroitin sulfate** is abundant in **cartilage**, contributing to its **compressive strength**. - While present in connective tissues, it is not the major glycosaminoglycan of synovial fluid. *Dermatan sulfate* - **Dermatan sulfate** is primarily found in **skin**, **blood vessels**, and **heart valves**. - Its main roles involve tissue structure and repair, not lubrication of synovial fluid. *Heparan sulfate* - **Heparan sulfate** is found on **cell surfaces** and in the **extracellular matrix**, especially in the **basement membranes**. - It regulates cell growth, adhesion, and signaling, and is not a major component of synovial fluid viscosity.
Question 346: What is the mechanism by which mercury causes damage?
- A. Causes toxicity through various mechanisms
- B. Binds to -SH groups of enzymes (Correct Answer)
- C. Inhibits electron transport chain
- D. Inhibits protein synthesis
Explanation: ***Binds to -SH groups of enzymes*** - Mercury, particularly its inorganic and organic forms, has a high affinity for **sulfhydryl (-SH) groups** found in **cysteine residues** of proteins and enzymes. - This binding disrupts the **tertiary structure** and **catalytic activity** of vital enzymes, leading to widespread cellular dysfunction and toxicity. *Causes toxicity through various mechanisms (not specific to -SH binding)* - While mercury can indeed cause toxicity through various mechanisms, the **most prominent and fundamental mechanism** underpins many of these downstream effects. - This option is too general and does not pinpoint the primary molecular interaction responsible for mercury's widespread cellular damage. *Indirectly inhibits the electron transport chain (ETC) by enzyme disruption* - This statement is partially true in that mercury's enzyme disruption can affect the ETC, but it's an **indirect consequence** rather than the primary mechanism itself. - The direct mechanism involves the initial binding to -SH groups, which then leads to the dysfunction of enzymes, including those involved in the ETC. *Indirectly inhibits protein synthesis by disrupting enzyme function* - Similar to ETC inhibition, mercury's disruption of enzyme function can ultimately impair protein synthesis, but this is an **effect down the causal chain**. - The initial and direct molecular interaction is the binding to sulfhydryl groups of key enzymes involved in various cellular processes, including protein synthesis.
Question 347: Which of the following statements regarding collagen synthesis is incorrect?
- A. Hydroxylation of lysine occurs in ER
- B. Synthesized in ribosomes as preprocollagen
- C. Triple helix assembly occurs in ER
- D. Hydroxylation of proline occurs in Golgi apparatus (Correct Answer)
Explanation: ***Hydroxylation of proline occurs in Golgi apparatus*** - This statement is incorrect because the **hydroxylation of proline** residues occurs in the **endoplasmic reticulum** (ER), not the Golgi apparatus. - This step is critical for forming stable **triple helix** structures of collagen and requires **vitamin C**. *Synthesized in ribosomes as preprocollagen* - This statement is correct. Collagen synthesis begins in the cytoplasm, where mRNA is translated by **ribosomes** into **preprocollagen**, which contains a signal peptide. - The signal peptide directs the nascent polypeptide chain into the lumen of the **endoplasmic reticulum**. *Hydroxylation of lysine occurs in ER* - This statement is correct. Following entry into the ER, specific **lysine** residues are hydroxylated by **lysyl hydroxylase** to form hydroxylysine. - This hydroxylation, along with that of proline, is crucial for **cross-linking** and stability of the collagen molecule. *Triple helix assembly occurs in ER* - This statement is correct. After hydroxylation and glycosylation of some residues, three procollagen alpha chains self-assemble to form a **triple helix** within the **endoplasmic reticulum**. - This assembly is stabilized by **disulfide bonds** at the C-terminal ends and molecular chaperones.
Question 348: Albumin is the primary transport protein in blood for which of the following substances?
- A. Free fatty acids (FFA) (Correct Answer)
- B. Thyroxine
- C. Steroid
- D. Calcium
Explanation: ***Free fatty acids (FFA)*** - **Albumin is the PRIMARY and MAJOR transport protein for free fatty acids** in the bloodstream, with each albumin molecule having **6-7 high-affinity binding sites** for FFAs. - This binding is essential for transporting water-insoluble fatty acids from **adipose tissue** (during lipolysis) to peripheral tissues for **β-oxidation and energy production**. - In the context of lipid metabolism, albumin-FFA transport is the **most quantitatively significant** and physiologically important binding function. - **Clinical relevance:** Impaired albumin levels directly affect FFA transport capacity. *Thyroxine* - While albumin does bind thyroid hormones, **thyroxine-binding globulin (TBG)** is the **primary carrier** (~70% of T4), followed by transthyretin (~15%). - Albumin binds only ~10-15% of circulating T4 with **low affinity**, serving as a secondary reserve. - TBG has **much higher affinity** for thyroid hormones than albumin. *Steroid* - Steroids are primarily transported by **specific binding globulins**: **corticosteroid-binding globulin (CBG)** for cortisol and **sex hormone-binding globulin (SHBG)** for testosterone/estrogen. - While albumin binds ~10-20% of steroids, it is a **secondary carrier** with lower affinity than the specific globulins. *Calcium* - Although ~40-45% of plasma calcium is albumin-bound (important for calcium homeostasis), this is a **passive binding function** rather than active transport. - Albumin's role with calcium is primarily **buffering** rather than the dedicated transport function it provides for FFAs. - In the context of **lipid metabolism** and **transport proteins**, FFA binding is the hallmark function of albumin.
Internal Medicine
1 questionsWhich of the following statements about hypercalcemia in sarcoidosis is false?
NEET-PG 2013 - Internal Medicine NEET-PG Practice Questions and MCQs
Question 341: Which of the following statements about hypercalcemia in sarcoidosis is false?
- A. PTHrP level is increased
- B. Parathormone level is increased (Correct Answer)
- C. Oral steroids are useful
- D. Calcitriol level is increased
Explanation: ***Parathormone level is increased*** - In **sarcoidosis-associated hypercalcemia**, the parathormone (PTH) level is typically **low or suppressed**. [1] - This is because the hypercalcemia is due to **extra-renal 1-$\alpha$ hydroxylation** of 25-hydroxyvitamin D to 1,25-dihydroxyvitamin D (calcitriol) by macrophages in granulomas, not primary hyperparathyroidism. [1] *PTHrP level is increased* - This statement is **false** for sarcoidosis. Elevated **parathyroid hormone-related peptide (PTHrP)** is a common cause of hypercalcemia in **malignancy**, particularly squamous cell carcinomas, but not in sarcoidosis. - Hypercalcemia in sarcoidosis is **PTH-independent** and not mediated by PTHrP. [1] *Oral steroids are useful* - This statement is **true**. **Corticosteroids** (like oral prednisone) are effective in treating hypercalcemia in sarcoidosis. - They work by **inhibiting the activity of 1-$\alpha$ hydroxylase** in alveolar macrophages and reducing intestinal calcium absorption. *Calcitriol level is increased* - This statement is **true**. In sarcoidosis, activated **macrophages within granulomas** aberrantly express **1-$\alpha$ hydroxylase**. [1] - This leads to the **extra-renal synthesis of calcitriol** (1,25-dihydroxyvitamin D), which increases intestinal calcium absorption and bone resorption, causing hypercalcemia. [1]