Overexpression of the natural tetrapeptide acetyl-N-ser-asp-lys-pro derived from thymosin beta 4 in neoplastic diseases

Jian-Miao Liu; Maria-Concepcion Garcia-Alvarez; Jerome Bignon; Michal Kusinski; Krzysztof Kuzdak; Andrew Riches; Joanna Wdzieczak-Bakala

doi:10.1111/j.1749-6632.2010.05488.x

Overexpression of the natural tetrapeptide acetyl-N-ser-asp-lys-pro derived from thymosin beta 4 in neoplastic diseases

Jian-Miao Liu, Maria-Concepcion Garcia-Alvarez, Jerome Bignon, Michal Kusinski, Krzysztof Kuzdak, Andrew Riches, Joanna Wdzieczak-Bakala

School of Medicine

Research output: Chapter in Book/Report/Conference proceeding › Conference contribution

21 Citations (Scopus)

Abstract

The natural tetrapeptide acetyl-ser-asp-lys-pro (AcSDKP) is formed in vivo by enzymatic cleavage of the N terminus of thymosin beta 4 by prolyl oligopeptidase (POP). Recently, AcSDKP was shown to promote angiogenesis. Because of the critical role of neovascularization in cancer development, the levels of AcSDKP and POP activity in a number of different malignant tissues were investigated. Our studies revealed that AcSDKP levels were markedly elevated in neoplastic diseases including hematologic malignancies and solid neoplasms. Consistent with this finding, the enhanced activity of POP was also detected in all analyzed specimens of cancer tissues. Both these novel findings are in concert with the previously reported overexpression of thymosin beta 4 in a large variety of malignant tumors and with its potential role in cancerogenesis. The physiological relevance of these findings awaits further studies; however, our first results strongly suggest a key role for AcSDKP in the pathogenesis of cancer.

Original language	English
Title of host publication	THYMOSINS IN HEALTH AND DISEASE
Editors	E Garaci, AL Goldstein
Place of Publication	OXFORD
Publisher	Blackwell
Pages	53-59
Number of pages	7
ISBN (Print)	978-1-57331-801-3
DOIs	https://doi.org/10.1111/j.1749-6632.2010.05488.x
Publication status	Published - 2010
Event	2nd International Symposium on Thymosins in Health and Disease - Catania Duration: 30 Sept 2009 → 2 Oct 2009

Conference

Conference	2nd International Symposium on Thymosins in Health and Disease
City	Catania
Period	30/09/09 → 2/10/09

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1111/j.1749-6632.2010.05488.x

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Liu, J.-M., Garcia-Alvarez, M.-C., Bignon, J., Kusinski, M., Kuzdak, K., Riches, A., & Wdzieczak-Bakala, J. (2010). Overexpression of the natural tetrapeptide acetyl-N-ser-asp-lys-pro derived from thymosin beta 4 in neoplastic diseases. In E. Garaci, & AL. Goldstein (Eds.), THYMOSINS IN HEALTH AND DISEASE (pp. 53-59). Blackwell. https://doi.org/10.1111/j.1749-6632.2010.05488.x

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title = "Overexpression of the natural tetrapeptide acetyl-N-ser-asp-lys-pro derived from thymosin beta 4 in neoplastic diseases",

abstract = "The natural tetrapeptide acetyl-ser-asp-lys-pro (AcSDKP) is formed in vivo by enzymatic cleavage of the N terminus of thymosin beta 4 by prolyl oligopeptidase (POP). Recently, AcSDKP was shown to promote angiogenesis. Because of the critical role of neovascularization in cancer development, the levels of AcSDKP and POP activity in a number of different malignant tissues were investigated. Our studies revealed that AcSDKP levels were markedly elevated in neoplastic diseases including hematologic malignancies and solid neoplasms. Consistent with this finding, the enhanced activity of POP was also detected in all analyzed specimens of cancer tissues. Both these novel findings are in concert with the previously reported overexpression of thymosin beta 4 in a large variety of malignant tumors and with its potential role in cancerogenesis. The physiological relevance of these findings awaits further studies; however, our first results strongly suggest a key role for AcSDKP in the pathogenesis of cancer.",

author = "Jian-Miao Liu and Maria-Concepcion Garcia-Alvarez and Jerome Bignon and Michal Kusinski and Krzysztof Kuzdak and Andrew Riches and Joanna Wdzieczak-Bakala",

year = "2010",

doi = "10.1111/j.1749-6632.2010.05488.x",

language = "English",

isbn = "978-1-57331-801-3",

pages = "53--59",

editor = "E Garaci and AL Goldstein",

booktitle = "THYMOSINS IN HEALTH AND DISEASE",

publisher = "Blackwell",

note = "2nd International Symposium on Thymosins in Health and Disease ; Conference date: 30-09-2009 Through 02-10-2009",

}

Liu, J-M, Garcia-Alvarez, M-C, Bignon, J, Kusinski, M, Kuzdak, K, Riches, A & Wdzieczak-Bakala, J 2010, Overexpression of the natural tetrapeptide acetyl-N-ser-asp-lys-pro derived from thymosin beta 4 in neoplastic diseases. in E Garaci & AL Goldstein (eds), THYMOSINS IN HEALTH AND DISEASE. Blackwell, OXFORD, pp. 53-59, 2nd International Symposium on Thymosins in Health and Disease, Catania, 30/09/09. https://doi.org/10.1111/j.1749-6632.2010.05488.x

Overexpression of the natural tetrapeptide acetyl-N-ser-asp-lys-pro derived from thymosin beta 4 in neoplastic diseases. / Liu, Jian-Miao; Garcia-Alvarez, Maria-Concepcion; Bignon, Jerome et al.
THYMOSINS IN HEALTH AND DISEASE. ed. / E Garaci; AL Goldstein. OXFORD: Blackwell, 2010. p. 53-59.

Research output: Chapter in Book/Report/Conference proceeding › Conference contribution

TY - GEN

T1 - Overexpression of the natural tetrapeptide acetyl-N-ser-asp-lys-pro derived from thymosin beta 4 in neoplastic diseases

AU - Liu, Jian-Miao

AU - Garcia-Alvarez, Maria-Concepcion

AU - Bignon, Jerome

AU - Kusinski, Michal

AU - Kuzdak, Krzysztof

AU - Riches, Andrew

AU - Wdzieczak-Bakala, Joanna

PY - 2010

Y1 - 2010

N2 - The natural tetrapeptide acetyl-ser-asp-lys-pro (AcSDKP) is formed in vivo by enzymatic cleavage of the N terminus of thymosin beta 4 by prolyl oligopeptidase (POP). Recently, AcSDKP was shown to promote angiogenesis. Because of the critical role of neovascularization in cancer development, the levels of AcSDKP and POP activity in a number of different malignant tissues were investigated. Our studies revealed that AcSDKP levels were markedly elevated in neoplastic diseases including hematologic malignancies and solid neoplasms. Consistent with this finding, the enhanced activity of POP was also detected in all analyzed specimens of cancer tissues. Both these novel findings are in concert with the previously reported overexpression of thymosin beta 4 in a large variety of malignant tumors and with its potential role in cancerogenesis. The physiological relevance of these findings awaits further studies; however, our first results strongly suggest a key role for AcSDKP in the pathogenesis of cancer.

AB - The natural tetrapeptide acetyl-ser-asp-lys-pro (AcSDKP) is formed in vivo by enzymatic cleavage of the N terminus of thymosin beta 4 by prolyl oligopeptidase (POP). Recently, AcSDKP was shown to promote angiogenesis. Because of the critical role of neovascularization in cancer development, the levels of AcSDKP and POP activity in a number of different malignant tissues were investigated. Our studies revealed that AcSDKP levels were markedly elevated in neoplastic diseases including hematologic malignancies and solid neoplasms. Consistent with this finding, the enhanced activity of POP was also detected in all analyzed specimens of cancer tissues. Both these novel findings are in concert with the previously reported overexpression of thymosin beta 4 in a large variety of malignant tumors and with its potential role in cancerogenesis. The physiological relevance of these findings awaits further studies; however, our first results strongly suggest a key role for AcSDKP in the pathogenesis of cancer.

U2 - 10.1111/j.1749-6632.2010.05488.x

DO - 10.1111/j.1749-6632.2010.05488.x

M3 - Conference contribution

SN - 978-1-57331-801-3

SP - 53

EP - 59

BT - THYMOSINS IN HEALTH AND DISEASE

A2 - Garaci, E

A2 - Goldstein, AL

PB - Blackwell

CY - OXFORD

T2 - 2nd International Symposium on Thymosins in Health and Disease

Y2 - 30 September 2009 through 2 October 2009

ER -

Overexpression of the natural tetrapeptide acetyl-N-ser-asp-lys-pro derived from thymosin beta 4 in neoplastic diseases

Abstract

Conference

UN SDGs

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