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排序方式: 共有93条查询结果,搜索用时 46 毫秒
21.
角质形成细胞生长因子(KGF)在喉粘膜良性、癌前及恶性病变中的mRNA水平分析 总被引:1,自引:0,他引:1
利用原位杂交的方法检测KGFmRNA在正常喉粘膜上皮(N)、慢性非特异性炎症(IF)、不典型增生(DYS)及鳞癌(SCC)中的转录水平,探讨KGF在喉粘膜良性及恶性病变中的分布和可能的作用。结果表明,KGFmRNA不仅在间质中的成纤维细胞中表达,少量的炎细胞及血管内皮细胞中亦表达,而且从N、IF、DYS到SCC、KGFmRNA转录水平逐渐增强;上皮细胞及肿瘤性上皮细胞不表达KGFmRNA,KGFmRNA在分化差的SCC周围间质中表达较分化好的SCC周围间质增多。结论:KGF在上皮与间充质细胞的交互作用中发挥着重要的作用,对维持喉粘膜正常结构、代谢及喉癌的发生发展具有重要意义。 相似文献
22.
Odunuga OO Longshaw VM Blatch GL 《BioEssays : news and reviews in molecular, cellular and developmental biology》2004,26(10):1058-1068
Molecular chaperones facilitate the correct folding of other proteins under physiological and stress conditions. Recently it has become evident that various co-chaperone proteins regulate the cellular functions of these chaperones, particularly Hsp70 and Hsp90. Hop is one of the most extensively studied co-chaperones that is able to directly associate with both Hsp70 and Hsp90. The current dogma proposes that Hop functions primarily as an adaptor that directs Hsp90 to Hsp70-client protein complexes in the cytoplasm. However, recent evidence suggests that Hop can also modulate the chaperone activities of these Hsps, and that it is not dedicated to Hsp70 and Hsp90. While the co-chaperone function of Hop within the cytoplasm has been extensively studied, its association with nuclear complexes and prion proteins remains to be elucidated. This article will review the structural features of Hop, and the evidence that its biological function is considerably broader than previously envisaged. 相似文献
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Molecular chaperones have been used for the improved expression of target proteins within heterologous systems; however, the chaperone and target protein have seldom been matched in terms of origin. We have developed a heterologous co-expression system that allows independent expression of the plasmodial chaperone, PfHsp70, and a plasmodial target protein. In this study, the target was Plasmodium falciparum GTP cyclohydrolase I (PfGCHI), the first enzyme in the plasmodial folate pathway. The sequential expression of the molecular chaperone followed by the target protein increased the expression of soluble functional PfGCHI. His-tagged PfGCHI was successfully purified using nickel affinity chromatography, and the specific activity was determined by high performance liquid chromatography with spectrofluorometeric detection to be 5.93nmol/h/mg. This is the first report of a heterologous co-expression system in which a plasmodial chaperone is harnessed for the improved production and purification of a plasmodial target protein. 相似文献
27.
Taryn Bodill Anne C. Conibear Marius K.M. Mutorwa Jessica L. Goble Gregory L. Blatch Kevin A. Lobb Rosalyn Klein Perry T. Kaye 《Bioorganic & medicinal chemistry》2013,21(14):4332-4341
DOXP-reductoisomerase (DXR) is a validated target for the development of antimalarial drugs to address the increase in resistant strains of Plasmodium falciparum. Series of aryl- and heteroarylcarbamoylphosphonic acids, their diethyl esters and disodium salts have been prepared as analogues of the potent DXR inhibitor fosmidomycin. The effects of the carboxamide N-substituents and the length of the methylene linker have been explored using in silico docking studies, saturation transfer difference NMR spectroscopy and enzyme inhibition assays using both EcDXR and PfDXR. These studies indicate an optimal linker length of two methylene units and have confirmed the importance of an additional binding pocket in the PfDXR active site. Insights into the constraints of the PfDXR binding site provide additional scope for the rational design of DXR inhibitors with increased ligand–receptor interactions. 相似文献
28.
Cancer procoagulant is present only in malignant tumours and the undifferentiated tissues of human placenta. Its possible role in angiogenesis and metastasis was investigated. Cancer procoagulant increased the steady-state mRNA level of L1 cell adhesion molecule (L1CAM) in MCF-7 breast cancer cells and E14 mouse embryonic stem cells (MESCs), while an increase in angiogenin mRNA was observed in MDA-MB-231 breast cancer cells. Furthermore, production of vascular endothelial growth factor (VEGF) protein in MCF-7 breast cancer cells and E14 MESCs, but decreased in MDA-MB-231 breast cancer cells. We conclude that cancer procoagulant could potentially play a part in angiogenesis in cancer and vascular development during embryonic development. 相似文献
29.
Malaria is caused by Plasmodium species, whose transmission to vertebrate hosts is facilitated by mosquito vectors. The transition from the cold blooded
mosquito vector to the host represents physiological stress to the parasite, and additionally malaria blood stage infection
is characterised by intense fever periods. In recent years, it has become clear that heat shock proteins play an essential
role during the parasite's life cycle. Plasmodium falciparum expresses two prominent heat shock proteins: heat shock protein 70 (PfHsp70) and heat shock protein 90 (PfHsp90). Both of
these proteins have been implicated in the development and pathogenesis of malaria. In eukaryotes, Hsp70 and Hsp90 proteins
are functionally linked by an essential adaptor protein known as the Hsp70–Hsp90 organising protein (Hop). In this study,
recombinant P. falciparum Hop (PfHop) was heterologously produced in E. coli and purified by nickel affinity chromatography. Using specific anti-PfHop antisera, the expression and localisation of PfHop
in P. falciparum was investigated. PfHop was shown to co-localise with PfHsp70 and PfHsp90 in parasites at the trophozoite stage. Gel filtration
and co-immunoprecipitation experiments suggested that PfHop was present in a complex together with PfHsp70 and PfHsp90. The
association of PfHop with both PfHsp70 and PfHsp90 suggests that this protein may mediate the functional interaction between
the two chaperones. 相似文献
30.
Tal Dagan Jan Riedel Pradipta Mandal Eva R. Pesce Gregory L. Blatch Brendan S. Crabb Paul R. Gilson Jude M. Przyborski 《Cellular microbiology》2012,14(11):1784-1795
Malaria parasites modify their host cell, the mature human erythrocyte. We are interested in the molecules mediating these processes, and have recently described a family of parasite‐encoded heat shock proteins (PfHsp40s) that are targeted to the host cell, and implicated in host cell modification. Hsp40s generally function as co‐chaperones of members of the Hsp70 family, and until now it was thought that human Hsp70 acts as the PfHsp40 interaction partner within the host cell. Here we revise this hypothesis, and identify and characterize an exported parasite‐encoded Hsp70, referred to as PfHsp70‐x. PfHsp70‐x is exported to the host erythrocyte where it forms a complex with PfHsp40s in structures known as J‐dots, and is closely associated with PfEMP1. Interestingly, Hsp70‐x is encoded only by parasite species that export the major virulence factor EMP1, implying a possible role for Hsp70‐x in EMP1 presentation at the surface of the infected erythrocyte. Our data strongly support the presence of parasite‐encoded chaperone/co‐chaperone complexes within the host erythrocyte, which are involved in protein traffic through the host cell. The host–pathogen interaction within the infected erythrocyte is more complex than previously thought, and is driven notonly by parasite co‐chaperones, but also by the parasite‐encoded chaperone Hsp70‐x itself. 相似文献