In collagen synthesis, Vitamin C is crucial for the hydroxylation of which amino acids?

Prepare for USMLE Step 1 Pathology Exam with comprehensive quizzes, flashcards, and detailed explanations. Enhance your understanding and be exam-ready!

Vitamin C plays a vital role in collagen synthesis by facilitating the hydroxylation of proline and lysine residues. This hydroxylation process is essential for the stability and strength of the collagen triple helix structure. In the absence of adequate Vitamin C, hydroxylation is impaired, leading to weakened collagen fibers and conditions such as scurvy, which is characterized by symptoms like poor wound healing, bleeding gums, and joint pain.

Proline and lysine are specific amino acids that undergo post-translational modifications critical for forming cross-links between collagen fibrils, thereby enhancing the tensile strength of the tissue. While other amino acids like arginine, threonine, cysteine, serine, glycine, and alanine serve important functions in protein structure and metabolism, they are not the primary targets of Vitamin C during collagen synthesis.

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