Abstract
BackgroundHeat shock protein 47 (HSP47), a collagen-binding protein, has a specific role in the intracellular processing of procollagen production. HSP47 expression is associated with cancer growth and metastasis in several types of cancers. However, none of the studies have assessed whether HSP47 expression is associated with the risk of postoperative recurrence of lung cancer until now. Therefore, we aimed to assess this association.MethodsThe study population consisted of a cohort of consecutive patients who underwent surgery for lung cancer at Nagasaki University Hospital, Nagasaki, Japan, from January 2009 to December 2010. Patient characteristics, survival and disease-free survival (DFS), and laboratory findings were compared between patients who tested positive and negative for HSP47 expression in lung cancer cells and between those who showed high and low numbers of HSP47-positive fibroblasts in cancer stroma.ResultsA total of 133 patients underwent surgery for lung cancer. Sixty-seven patients (50.4%) had HSP47-positive cancer cells, and 91 patients (68.4%) had a higher number of HSP47-positive fibroblasts. The patients with a high number of HSP47-positive fibroblasts had a shorter DFS than those with a low number of HSP47-positive fibroblasts. Multivariate analysis identified only the presence of a high number of HSP47-positive fibroblasts as an independent risk factor for recurrence of lung cancer after surgery (odds ratio, 4.371; 95% confidence interval, 1.054–29.83; P = 0.042).ConclusionThe present study demonstrated that the presence of a high number of HSP47-positive fibroblasts in the cancer stroma was a risk factor for recurrence of lung cancer after surgery.
Highlights
Heat shock protein 47 (HSP47), a collagen-binding protein, has a specific role in the intracellular processing of procollagen production
Heat shock protein 47 (HSP47) is a collagen-binding, stress-inducible protein localized in the endoplasmic reticulum, and it plays a specific role in the intracellular processing of procollagen production as a collagenspecific molecular chaperone [1]
The present study showed that patients with a higher number of HSP47-positive fibroblasts in the lung cancer stroma had a shorter disease-free survival (DFS) than those with few HSP47positive fibroblasts
Summary
Heat shock protein 47 (HSP47), a collagen-binding protein, has a specific role in the intracellular processing of procollagen production. HSP47 has been reported to be associated with several types of cancers, including cervical, breast, pancreatic, gastric, and colon cancer [8,9,10,11]. It is encoded by the SERPINH1 gene located on chromosome 11q13.5; this region is one of the most frequently amplified in human cancer [12]. HSP47 expression promotes cancer progression in part by enhancing the deposition of extracellular matrix (ECM) proteins, including collagens
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