HISTOLOGY AND HISTOPATHOLOGY

Cellular and Molecular Biology

Review

The possible role of colligin/HSP47, a collagen-binding protein, in the pathogenesis of human and experimental fibrotic diseases

M.S. Razzaque1 and T. Taguchi

The Second Department of Pathology, Nagasaki University School of Medicine, Nagasaki, Japan
1Present address: Division of Nephrology, Department of Medicine, Pennsylvania State University-College of Medicine, Hershey, Pennsylvania 17033, USA

Offprint requests to: M.S. Razzaque, M.B.B.S., Ph.D., The Second Department of Pathology, Nagasaki University School of Medicine, 1-12-4, Sakamoto, Nagasaki 852-8523, Japan. e-mail: razzaque@net.nagasaki-u.ac.jp

 

Summary. Colligin or heat shock protein 47 (HSP47) is a stress protein that resides in the endoplasmic reticulum and is thought to participate in intracellular processing, folding, assembly and secretion of procollagens. Irrespective of the tissue site and organ, induction of colligin/HSP47 expression is always noted during the process of fibrosis, particularly in and around the fibrotic lesions in both humans and experimental models. Its expression is highly tissue- and cell-specific, and restricted to mostly phenotypically altered collagen-producing cells. These observations suggest that up-regulation of this collagen-specific chaperone-colligin/
HSP47 may play an important role in the subsequent fibrotic process, possibly by regulating increased synthesis/assembly of collagens. Histol. Histopathol. 14, 1199-1212 (1999)

Key words: Colligin/Heat shock protein 47, Collagen, Glomerulosclerosis, Fibrosis, Human, Rat


DOI: 10.14670/HH-14.1199