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

详细信息    查看全文

• 作者：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
• 关键词：Small heat shock protein ; α ; A ; Pancreas ; AP-1 ; Smad2/3/5 ; TGFβ ; Pancreatic cancer ; Cell migration ; Lens
• 刊名：Biochimica et Biophysica Acta (BBA)/Molecular Basis of Disease
• 出版年：2010
• 出版时间：July-August 2010
• 年：2010
• 卷：1802
• 期：7-8
• 页码：621-631
• 全文大小：1886 K

文摘

The small heat shock protein αA-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 TGFβ pathway. Finally, expression of αA-crystallin in a pancreatic cancer cell line, MiaPaCa, results in retarded cell migration. Together, these results suggest that αA-crystallin seems to negatively regulate pancreatic carcinogenesis.