Int J Biochem Mol Biol 2011;2(1):47-57
Review Article
Heat shock protein 10 (Hsp10) in immune-related diseases: one coin, two sides
Haibo Jia, Amadou I. Halilou, Liang Hu, Wenqian Cai, Jing Liu, Bo Huang
Department of Biology Science, College of Life Science and Technology; Department of Biochemistry & Molecular Biology, Tongji Medical
College; Huazhong University of Science & Technology, Wuhan 430030, The People’s Republic of China
Received December 14, 2010; accepted December 22, 2010; Epub December 25, 2010; published February 15, 2011
Abstract: Heat shock protein 10 (Hsp10) in eukaryotes, originally identified as a mitochondrial chaperone, now is also known to be present in
cytosol, cell surface, extracellular space and peripheral blood. Functionally besides participating in mitochondrial protein folding in association
with Hsp60, Hsp10 appears to be related to pregnancy, cancer and autoimmune inhibition. Hsp10 can be released to peripheral blood at very
early time point of pregnancy and given another name called early pregnancy factor (EPF), which seems to play a critical role in developing a
pregnant niche. In malignant disorders, Hsp10 is usually abnormally expressed in the cytosol of malignant cells and further released to
extracellular space, resulting in tumor-promoting effect from various aspects. Furthermore, distinct from other heat shock protein members,
whose soluble form is recognized as danger signal by immune cells and triggers immune responses, Hsp10 after release, however, is
designed to be an inhibitory signal by limiting immune response. This review discusses how Hsp10 participates in various physiological and
pathological processes from basic protein molecule folding to pregnancy, cancer and autoimmune diseases, and emphasizes how important
the location is for the function exertion of a molecule. (IJBMB1012002).
Keywords: Hsp10, location, pregnancy, autoimmune disese, cancer
Full Text PDF
Address all correspondence to:
Dr. Bo Huang
Department of Biochemistry & Molecular Biology, Tongji Medical College
Huazhong University of Science & Technology
Wuhan 430030, The People’s Republic of China.
E-mail: tjhuangbo@hotmail.com
Review Article
Heat shock protein 10 (Hsp10) in immune-related diseases: one coin, two sides
Haibo Jia, Amadou I. Halilou, Liang Hu, Wenqian Cai, Jing Liu, Bo Huang
Department of Biology Science, College of Life Science and Technology; Department of Biochemistry & Molecular Biology, Tongji Medical
College; Huazhong University of Science & Technology, Wuhan 430030, The People’s Republic of China
Received December 14, 2010; accepted December 22, 2010; Epub December 25, 2010; published February 15, 2011
Abstract: Heat shock protein 10 (Hsp10) in eukaryotes, originally identified as a mitochondrial chaperone, now is also known to be present in
cytosol, cell surface, extracellular space and peripheral blood. Functionally besides participating in mitochondrial protein folding in association
with Hsp60, Hsp10 appears to be related to pregnancy, cancer and autoimmune inhibition. Hsp10 can be released to peripheral blood at very
early time point of pregnancy and given another name called early pregnancy factor (EPF), which seems to play a critical role in developing a
pregnant niche. In malignant disorders, Hsp10 is usually abnormally expressed in the cytosol of malignant cells and further released to
extracellular space, resulting in tumor-promoting effect from various aspects. Furthermore, distinct from other heat shock protein members,
whose soluble form is recognized as danger signal by immune cells and triggers immune responses, Hsp10 after release, however, is
designed to be an inhibitory signal by limiting immune response. This review discusses how Hsp10 participates in various physiological and
pathological processes from basic protein molecule folding to pregnancy, cancer and autoimmune diseases, and emphasizes how important
the location is for the function exertion of a molecule. (IJBMB1012002).
Keywords: Hsp10, location, pregnancy, autoimmune disese, cancer
Full Text PDF
Address all correspondence to:
Dr. Bo Huang
Department of Biochemistry & Molecular Biology, Tongji Medical College
Huazhong University of Science & Technology
Wuhan 430030, The People’s Republic of China.
E-mail: tjhuangbo@hotmail.com
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