Frontiers in Bioscience-Landmark (FBL) is published by IMR Press from Volume 26 Issue 5 (2021). Previous articles were published by another publisher on a subscription basis, and they are hosted by IMR Press on imrpress.com as a courtesy and upon agreement with Frontiers in Bioscience.
Academic Editor: Philip Patston
Hsp47 was originally discovered as a cell surface collagen binding protein, colligin, and was later shown to be an endoplasmic reticulum (ER) resident protein with collagen binding properties in chick fibroblasts. Hsp47 has been termed J6, gp46, CB48 and CBP2 in various other organisms and has been mapped to human chromosome 11q13.5 a known "hot spot" in a number of human cancers. Hsp47 has been shown to be constitutively expressed with collagens; it is heat inducible and binds to both helical and non-helical forms of collagens. Hsp47 binds closely to procollagen in the ER, but dissociates from it in the cis-Golgi to allow fibril formation. Hsp47 is over-expressed in many fibrotic diseases including: glomerulosclerosis, pulmonary fibrosis, liver cirrhosis, cicatricial pemphigoid, epidermolysis bullosa acquista and keloids. Hsp47 is associated with fibrosis following myocardial infarction and has been localized in artherosclerotic arteries. Among a number of rheumatoid conditions, Hsp47 manifests properties of an autoantigen and in some cancers appears to be a biomarker. The unique properties of Hsp47 in modulating collagen production and its location to the cell membrane in many forms of cancer have designated Hsp47 as a potential biomarker and/or therapeutic target for a number of conditions and diseases.