Cysteine-rich secretory protein 3 (CRISP3)

Cysteine-rich secretory protein 3 (CRISP3) is a member of the CRISP family, secreted mainly by exocrine tissues. Its molecular structure features two domains: a larger N-terminal CAP domain (Pathogenesis-related 1 domain) and a smaller C-terminal cysteine-rich domain, joined by a hinge region[1][3][5]. It contains multiple conserved cysteine residues forming intramolecular disulfide bonds critical for its structure[1][3][5]. CRISP3 is glycosylated, and its glycosylation sites show species-specific patterns that may relate to distinct tissue and functional specificity[1]. Biologically, CRISP3 is most highly expressed in salivary glands, prostate, and pancreas, with additional low-level expression in other tissues[2][6]. It is implicated in immune functions, possibly in innate immunity, and shows preferential male reproductive tract expression across vertebrates[3][5]. CRISP3 has been studied as a biomarker for prostate cancer, where its upregulation associates with ERG gene rearrangement and PTEN loss, and for cervical cancer, where expression decreases with increasing tumor severity[2][4]. No known drugs currently target CRISP3, and its application in therapy is limited to its use as a diagnostic or prognostic biomarker[2][4]. Protein-protein interaction analyses identify links to immune-relevant molecules such as estrogen and androgen receptors, interleukins, and partner proteins like alpha-1B-glycoprotein (A1BG), suggesting broader roles in immunity and tissue homeostasis[1][4].

Other names

CRISP3CRISP-3SGP28CRS3dJ442L6.3Aeg2Specific granule protein of 28 kDa