The small heat shock protein α A-crystallin is expressed in pancreas and acts as a negative regulator of carcinogenesis

Mi Deng, Pei Chao Chen, Sisi Xie, Junqiong Zhao, Lili Gong, Jinping Liu, Lan Zhang, Shuming Sun, Jiao Liu, Haili Ma, Surinder K. Batra, David Wan Cheng Li

Research output: Contribution to journalArticlepeer-review

21 Scopus citations

Abstract

The small heat shock protein α A-crystallin is a structural protein in the ocular lens. In addition, recent studies have also revealed that it is a molecular chaperone, an autokinase and a strong anti-apoptotic regulator. Besides its lenticular distribution, a previous study demonstrates that a detectable level of αA-crystallin is found in other tissues including thymus and spleen. In the present study, we have re-examined the distribution of αA-crystallin in various normal human and mouse tissues and found that the normal pancreas expresses a moderate level of αA-crystallin. Moreover, αA-crystallin is found significantly downregulated in 60 cases of pancreatic carcinoma of different types than it is in 11 normal human pancreas samples. In addition, we demonstrate that αA-crystallin can enhance the activity of the activating protein-1 (AP-1) through modulating the function of the MAP kinase, and also upregulates components of TGFα pathway. Finally, expression of αA-crystallin in a pancreatic cancer cell line, MiaPaCa, results in retarded cell migration. Together, these results suggest that α A-crystallin seems to negatively regulate pancreatic carcinogenesis.

Original languageEnglish (US)
Pages (from-to)621-631
Number of pages11
JournalBiochimica et Biophysica Acta - Molecular Basis of Disease
Volume1802
Issue number7-8
DOIs
StatePublished - Jul 2010

Keywords

  • AP-1
  • Cell migration
  • Lens
  • Pancreas
  • Pancreatic cancer
  • Smad2/3/5
  • Small heat shock protein
  • TGFα
  • αA

ASJC Scopus subject areas

  • Molecular Medicine
  • Molecular Biology

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