Vlodavsky Israel, Kayal Yasmin, Hilwi Maram, Soboh Soaad, Sanderson Ralph D, Ilan Neta
Technion Integrated Cancer Center, Technion Rappaport Faculty of Medicine Haifa Israel.
Department of Pathology University of Alabama at Birmingham Birmingham Alabama USA.
Proteoglycan Res. 2023 Jul 1;1(3):e6. doi: 10.1002/pgr2.6. Epub 2023 Jul 9.
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.
乙酰肝素酶(Hpa1)由肿瘤细胞和肿瘤微环境中的细胞表达,并在细胞外发挥作用,重塑细胞外基质(ECM),调节与ECM结合的因子的生物利用度,除其他作用外,还可增强基因转录、自噬、外泌体形成和硫酸乙酰肝素(HS)周转。乙酰肝素酶对肿瘤进展的许多影响与其在介导肿瘤-宿主相互作用中的功能有关,使肿瘤微环境更有利于支持肿瘤生长、转移和化疗耐药性。该酶似乎履行一些正常功能,例如与囊泡运输、基于溶酶体的分泌、自噬、HS周转和基因转录相关的功能。它激活先天免疫系统的细胞,促进外泌体和自噬体的形成,并通过酶促和非酶促活性刺激信号转导途径。这些作用动态影响多个调节途径,共同驱动肿瘤生长、扩散、耐药性以及炎症反应。新出现的观点是,肿瘤细胞、免疫细胞、内皮细胞和肿瘤微环境中的其他细胞表达的乙酰肝素酶是癌症侵袭性表型的关键调节因子,是癌症患者预后不良的重要因素,也是一个有效的治疗靶点。然而,到目前为止,基于抗乙酰肝素酶的治疗尚未在临床上实施。与乙酰肝素酶不同,乙酰肝素酶-2(Hpa2)是乙酰肝素酶(Hpa1)的紧密同源物,不经过蛋白水解加工,因此缺乏乙酰肝素酶的标志性内在HS降解活性。Hpa2保留结合肝素/HS的能力,并且对HS的亲和力甚至高于乙酰肝素酶,从而竞争HS结合并抑制乙酰肝素酶的酶活性。似乎Hpa2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,共同强调了维持Hpa?和Hpa2之间适当平衡的重要性。