Cysteine-rich protein 2 (CRIP2)

Cysteine-rich protein 2 (CRIP2) is a low molecular weight LIM domain-containing protein with high affinity for zinc and copper ions[1][2][3]. It is predominantly expressed in the heart and present in a variety of tissues including brain, lung, kidney, and intestine[1][2][3]. Functionally, it is implicated in regulation of cellular differentiation, apoptosis, angiogenesis, and epithelial-mesenchymal transition through its role as a transcriptional repressor, notably of NF-κB target genes such as pro-angiogenic cytokines and VEGF[1][2]. CRIP2 acts as a tumor suppressor in multiple cancers by repressing tumor formation and angiogenesis[1][2]. It holds promise as a clinical biomarker for cancers and cardiovascular disease, though is not currently the direct target of any approved drugs[1][2][3]. The protein's LIM domains mediate protein–protein interactions central to its regulatory functions.

Other names

Cysteine-rich intestinal protein 2CRIP2CRP2CRP-2ESP1Protein ESP1CRIPcysteine-rich protein 2Cysteine-rich intestinal proteinLIM domain protein ESP1/CRP2

Not applicable (no known drugs currently act directly via CRIP2)