庚二酸--具有多种酶和非酶功能的单一蛋白质。

Proteoglycan research Pub Date : 2023-07-01 Epub Date: 2023-07-09 DOI:10.1002/pgr2.6
Israel Vlodavsky, Yasmin Kayal, Maram Hilwi, Soaad Soboh, Ralph D Sanderson, Neta Ilan
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引用次数: 0

摘要

肝素酶(Hpa1)由肿瘤细胞和肿瘤微环境细胞表达,在细胞外发挥重塑细胞外基质(ECM)和调节 ECM 结合因子生物利用度的功能,除其他作用外,还能增强基因转录、自噬、外泌体形成和硫酸肝素(HS)周转。硫酸肝素酶对肿瘤进展的影响主要与其介导肿瘤-宿主串联的功能有关,它可使肿瘤微环境更好地支持肿瘤生长、转移和化疗抗性。这种酶似乎能发挥一些正常功能,例如与囊泡运输、溶酶体分泌、自噬、HS 更替和基因转录有关的功能。它能激活先天性免疫系统细胞,促进外泌体和自噬体的形成,并通过酶和非酶活性刺激信号转导途径。这些作用对多种调节途径产生动态影响,共同推动肿瘤的生长、扩散、耐药性和炎症反应。新的前提是,由肿瘤细胞、免疫细胞、内皮细胞和肿瘤微环境中其他细胞表达的肝素酶是癌症侵袭表型的关键调节因子,是导致癌症患者预后不良的重要因素,也是有效的治疗靶点。然而,迄今为止,基于抗肝素酶的疗法尚未应用于临床。与肝素酶不同,肝素酶-2(Hpa2)是肝素酶(Hpa1)的近缘同源物,不经过蛋白水解加工,因此缺乏肝素酶的标志--内在的HS降解活性。Hpa2 保留了与肝素/HS 结合的能力,对 HS 的亲和力甚至比肝素酶更高,从而竞争性地与 HS 结合并抑制肝素酶的酶活性。由此看来,Hpa2 的功能是作为 Hpa1 的天然抑制剂,调节维持组织止血和正常功能的特定基因的表达,并对癌症和炎症起到保护作用。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

Heparanase-A single protein with multiple enzymatic and nonenzymatic functions.

Heparanase-A single protein with multiple enzymatic and nonenzymatic functions.

Heparanase-A single protein with multiple enzymatic and nonenzymatic functions.

Heparanase (Hpa1) is expressed by tumor cells and cells of the tumor microenvironment and functions extracellularly to remodel the extracellular matrix (ECM) and regulate the bioavailability of ECM-bound factors, augmenting, among other effects, gene transcription, autophagy, exosome formation, and heparan sulfate (HS) turnover. Much of the impact of heparanase on tumor progression is related to its function in mediating tumor-host crosstalk, priming the tumor microenvironment to better support tumor growth, metastasis, and chemoresistance. The enzyme appears to fulfill some normal functions associated, for example, with vesicular traffic, lysosomal-based secretion, autophagy, HS turnover, and gene transcription. It activates cells of the innate immune system, promotes the formation of exosomes and autophagosomes, and stimulates signal transduction pathways via enzymatic and nonenzymatic activities. These effects dynamically impact multiple regulatory pathways that together drive tumor growth, dissemination, and drug resistance as well as inflammatory responses. The emerging premise is that heparanase expressed by tumor cells, immune cells, endothelial cells, and other cells of the tumor microenvironment is a key regulator of the aggressive phenotype of cancer, an important contributor to the poor outcome of cancer patients and a valid target for therapy. So far, however, antiheparanase-based therapy has not been implemented in the clinic. Unlike heparanase, heparanase-2 (Hpa2), a close homolog of heparanase (Hpa1), does not undergo proteolytic processing and hence lacks intrinsic HS-degrading activity, the hallmark of heparanase. Hpa2 retains the capacity to bind heparin/HS and exhibits an even higher affinity towards HS than heparanase, thus competing for HS binding and inhibiting heparanase enzymatic activity. It appears that Hpa2 functions as a natural inhibitor of Hpa1 regulates the expression of selected genes that maintain tissue hemostasis and normal function, and plays a protective role against cancer and inflammation, together emphasizing the significance of maintaining a proper balance between Hpa1 and Hpa2.

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