SP-C Inhibitors

Amiodarone, a Class III antiarrhythmic drug, indirectly inhibits SP-C by modulating lysosomal function. It accumulates in lysosomes, causing phospholipidosis, altering lipid metabolism, and potentially disrupting SP-C processing and trafficking.

Chloroquine, an antimalarial drug, indirectly impacts SP-C by interfering with lysosomal function. By raising lysosomal pH, chloroquine disrupts the proteolytic processing of surfactant proteins, potentially affecting SP-C maturation and secretion.

Brefeldin A, a fungal metabolite, directly inhibits SP-C trafficking by disrupting the structure and function of the Golgi apparatus. This interference prevents the proper post-translational modification and transport of SP-C to the lamellar bodies, impacting its incorporation into surfactant and compromising lung function.

Nelfinavir, an HIV protease inhibitor, indirectly modulates SP-C by affecting endoplasmic reticulum (ER) stress. It induces ER stress, potentially leading to misfolding and degradation of SP-C.

Azithromycin, an antibiotic, can indirectly influence SP-C by targeting mitochondrial function. Through its interaction with mitochondria, azithromycin may impact cellular energy metabolism, potentially affecting SP-C synthesis and processing.

Bafilomycin A1, a vacuolar H+-ATPase inhibitor, indirectly inhibits SP-C by disrupting lysosomal acidification. This interference leads to abnormalities in lysosomal function, potentially affecting SP-C processing and degradation.

Dexamethasone, a corticosteroid, indirectly modulates SP-C by influencing transcriptional regulation. It can affect SP-C expression by interacting with glucocorticoid receptors and modulating the activity of transcription factors involved in surfactant protein gene regulation.

Rapamycin, an mTOR inhibitor, indirectly influences SP-C by impacting cellular processes related to surfactant synthesis. By inhibiting mTOR, rapamycin can affect translation and lipid metabolism, potentially influencing the production and secretion of SP-C.

Concanamycin A, a vacuolar H+-ATPase inhibitor, indirectly inhibits SP-C by disrupting lysosomal acidification. This interference leads to abnormalities in lysosomal function, potentially affecting SP-C processing and degradation.

Tunicamycin, an N-linked glycosylation inhibitor, indirectly impacts SP-C by interfering with protein folding and ER-associated degradation. By inhibiting N-linked glycosylation, tunicamycin can induce ER stress, potentially leading to misfolding and degradation of SP-C.