SPARC-like protein 1 (SPARCL1)

SPARC-like protein 1 (SPARCL1), also known as hevin, is a secreted extracellular matrix glycoprotein and a member of the SPARC family of matricellular proteins. It is characterized by a highly acidic domain, a follistatin-like domain, and an extracellular calcium-binding (EC) domain. SPARCL1 modulates cell adhesion, migration, proliferation, and differentiation, and is critically involved in neural development and synapse regulation. In oncology, SPARCL1 acts predominantly as a tumor suppressor: its expression is frequently downregulated in multiple cancers, where low SPARCL1 correlates with aggressive phenotypes, poor differentiation, and higher metastatic risk. It is considered a negative regulator of cell growth and plays a role in inhibiting metastasis by restriction of RHOC GTPase signaling and MAPK pathway inactivation. SPARCL1 serves as a valuable prognostic biomarker for tumor progression but is not currently directly targetable with approved pharmacological agents. Its precise role in normal and pathological processes remains under investigation, especially concerning nervous system development and cancer biology.

Other names

hevinSC1high endothelial venule proteinMAST9

Not directly targeted by drugs; its reported mechanisms—when overexpressed or restored—include inhibition of migration via suppression of RHOC GTPase and inactivation of the p38/JNK/ERK MAPK pathway, leading to reduced tumor cell proliferation and migration