1Faiza Maqsood, 2Dr. Zahra Masood, 3Mansoor Musa, 4Qamar Abbas, 5Dr. Muhammad Zubair, 6Isma Abbas
Submission: 06 December 2025 | Acceptance: 11 January 2026 | Publication: 19 February 2026
1UHS Lahore
2National University of Medical Sciences (NUMS)
3UHS Lahore
4PIMS Islamabad
5Associate Professor of Pathology Saidu Medical College, Swat/ Saidu group of Teaching Hospitals,Swat.
6PIMS Islamabad
ABSTRACT:
Background: Post-translational modifications (PTMs) are crucial processes that regulate protein function and contribute to various cellular activities. These modifications, such as phosphorylation, acetylation, and glycosylation, can alter protein structure and activity, thereby playing significant roles in disease pathogenesis, including cancer, neurodegenerative disorders, and metabolic diseases. Understanding the mechanisms of PTMs is vital for developing therapeutic strategies targeting specific modifications to modulate protein function in disease conditions.
Aim: This study aimed to investigate the role of post-translational modifications in protein function and their contribution to disease pathogenesis.
Methods: This study was conducted at Services Hospital, Lahore, from May 2024 to April 2025. A total of 90 participants were included in the study, consisting of patients diagnosed with various diseases associated with PTMs. Protein samples were collected from tissue biopsies and blood samples. The study utilized mass spectrometry and western blotting techniques to identify and analyze specific PTMs in disease-related proteins. Data were analyzed to correlate the identified PTMs with disease severity, progression, and therapeutic responses.
Results: The study identified several PTMs that were significantly associated with disease pathogenesis. Notably, phosphorylation and acetylation were found to regulate key proteins involved in cell cycle progression and apoptosis, influencing cancer progression. Glycosylation patterns were altered in neurodegenerative disease samples, correlating with neuroinflammation and protein aggregation. Furthermore, PTMs in metabolic disease-related proteins were linked to insulin resistance and dysregulated lipid metabolism. These findings suggest that PTMs play a critical role in modulating protein function and contribute to the development of various diseases.
Conclusion: Post-translational modifications were found to be integral to the regulation of protein function and disease pathogenesis. These modifications offer potential targets for therapeutic intervention, providing new avenues for the development of precision medicine approaches for treating diseases associated with dysregulated PTMs.
Keywords: Post-translational modifications, protein function, disease pathogenesis, phosphorylation, acetylation, glycosylation, cancer, neurodegenerative disorders, metabolic diseases, precision medicine.