Hemin accumulation and identification of a heme‐binding protein clan in K562 cells by proteomic and computational analysis

血红素 血红素 生物化学 原卟啉IX 胞浆 血红素蛋白 化学 细胞内 细胞质 细胞生物学 生物 有机化学 光动力疗法
作者
Vasiliki‐Dimitra C. Tsolaki,Sofia K. Georgiou‐Siafis,Athina I. Tsamadou,Stefanos A. Tsiftsoglou,Martina Samiotaki,George Panayotou,Asterios S. Tsiftsoglou
出处
期刊:Journal of Cellular Physiology [Wiley]
卷期号:237 (2): 1315-1340 被引量:12
标识
DOI:10.1002/jcp.30595
摘要

Abstract Heme (iron protoporphyrin IX) is an essential regulator conserved in all known organisms. We investigated the kinetics of intracellular accumulation of hemin (oxidized form) in human transformed proerythroid K562 cells using [ 14 C]‐hemin and observed that it is time and temperature‐dependent, affected by the presence of serum proteins, as well as the amphipathic/hydrophobic properties of hemin. Hemin‐uptake exhibited saturation kinetics as a function of the concentration added, suggesting the involvement of a carrier‐cell surface receptor‐mediated process. The majority of intracellular hemin accumulated in the cytoplasm, while a substantial portion entered the nucleus. Cytosolic proteins isolated by hemin‐agarose affinity column chromatography (HACC) were found to form stable complexes with [ 59 Fe]‐hemin. The HACC fractionation and Liquid chromatography‐mass spectrometry analysis of cytosolic, mitochondrial, and nuclear protein isolates from K562 cell extracts revealed the presence of a large number of hemin‐binding proteins (HeBPs) of diverse ontologies, including heat shock proteins, cytoskeletal proteins, enzymes, and signaling proteins such as actinin a4, mitogen‐activated protein kinase 1 as well as several others. The subsequent computational analysis of the identified HeBPs using HemoQuest confirmed the presence of various hemin/heme‐binding motifs [C(X)nC, H, Y] in their primary structures and conformations. The possibility that these HeBPs contribute to a heme intracellular trafficking protein network involved in the homeostatic regulation of the pool and overall functions of heme is discussed.
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