Department of Microbiology and Immunology, Indiana University School of Medicine, Indianapolis, IN 46202, USA.
Blood. 2013 Jul 11;122(2):161-9. doi: 10.1182/blood-2013-02-487470. Epub 2013 May 1.
Dipeptidylpeptidase (DPP) 4 has the potential to truncate proteins with a penultimate alanine, proline, or other selective amino acids at the N-terminus. DPP4 truncation of certain chemokines, colony-stimulating factors, and interleukins have recently been linked to regulation of hematopoietic stem/progenitor cells, more mature blood cells, and other cell types. We believe that the potential role of DPP4 in modification of many regulatory proteins, and their subsequent effects on numerous stem/progenitor and other cell-type functions has not been adequately appreciated. This review addresses the potential implications of the modifying effects of DPP4 on a large number of cytokines and other growth-regulating factors with either proven or putative DPP4 truncation sites on hematopoietic cells, and subsequent effects of DPP4-truncated proteins on multiple aspects of steady-state and stressed hematopoiesis, including stem/progenitor cell, and more mature cell, function.
二肽基肽酶 (DPP) 4 具有将带有倒数第二个丙氨酸、脯氨酸或其他选择性氨基酸的蛋白质在 N 末端截断的潜力。最近发现,DPP4 对某些趋化因子、集落刺激因子和白细胞介素的截断与造血干细胞/祖细胞、更成熟的血细胞和其他细胞类型的调节有关。我们认为,DPP4 在许多调节蛋白的修饰作用中的潜在作用,以及它们随后对许多干细胞/祖细胞和其他细胞类型功能的影响尚未得到充分认识。这篇综述讨论了 DPP4 对大量细胞因子和其他生长调节因子的修饰作用的潜在影响,这些因子在造血细胞上具有已证实或推测的 DPP4 截断位点,以及 DPP4 截断蛋白对稳态和应激造血的多个方面的影响,包括干细胞/祖细胞和更成熟细胞的功能。