Simeonovic Charmaine J, Popp Sarah K, Starrs Lora M, Brown Debra J, Ziolkowski Andrew F, Ludwig Barbara, Bornstein Stefan R, Wilson J Dennis, Pugliese Alberto, Kay Thomas W H, Thomas Helen E, Loudovaris Thomas, Choong Fui Jiun, Freeman Craig, Parish Christopher R
Department of Immunology and Infectious Disease, The John Curtin School of Medical Research, The Australian National University, Canberra, Australian Capital Territory, Australia.
Department of Internal Medicine III, Carl Gustav Carus Medical School, Technical University of Dresden, Dresden, Germany.
PLoS One. 2018 Feb 7;13(2):e0191360. doi: 10.1371/journal.pone.0191360. eCollection 2018.
Type 1 diabetes (T1D) is an autoimmune disease in which insulin-producing beta cells in pancreatic islets are progressively destroyed. Clinical trials of immunotherapies in recently diagnosed T1D patients have only transiently and partially impacted the disease course, suggesting that other approaches are required. Our previous studies have demonstrated that heparan sulfate (HS), a glycosaminoglycan conventionally expressed in extracellular matrix, is present at high levels inside normal mouse beta cells. Intracellular HS was shown to be critical for beta cell survival and protection from oxidative damage. T1D development in Non-Obese Diabetic (NOD) mice correlated with loss of islet HS and was prevented by inhibiting HS degradation by the endoglycosidase, heparanase. In this study we investigated the distribution of HS and heparan sulfate proteoglycan (HSPG) core proteins in normal human islets, a role for HS in human beta cell viability and the clinical relevance of intra-islet HS and HSPG levels, compared to insulin, in human T1D. In normal human islets, HS (identified by 10E4 mAb) co-localized with insulin but not glucagon and correlated with the HSPG core proteins for collagen type XVIII (Col18) and syndecan-1 (Sdc1). Insulin-positive islets of T1D pancreases showed significant loss of HS, Col18 and Sdc1 and heparanase was strongly expressed by islet-infiltrating leukocytes. Human beta cells cultured with HS mimetics showed significantly improved survival and protection against hydrogen peroxide-induced death, suggesting that loss of HS could contribute to beta cell death in T1D. We conclude that HS depletion in beta cells, possibly due to heparanase produced by insulitis leukocytes, may function as an important mechanism in the pathogenesis of human T1D. Our findings raise the possibility that intervention therapy with dual activity HS replacers/heparanase inhibitors could help to protect the residual beta cell mass in patients recently diagnosed with T1D.
1型糖尿病(T1D)是一种自身免疫性疾病,其中胰岛中产生胰岛素的β细胞会逐渐被破坏。对新诊断的T1D患者进行免疫疗法的临床试验仅对病程产生了短暂且部分的影响,这表明需要其他方法。我们之前的研究表明,硫酸乙酰肝素(HS)是一种通常在细胞外基质中表达的糖胺聚糖,在正常小鼠β细胞内含量很高。细胞内HS对β细胞存活及免受氧化损伤至关重要。非肥胖糖尿病(NOD)小鼠的T1D发展与胰岛HS的丧失相关,并且通过抑制内切糖苷酶乙酰肝素酶对HS的降解得以预防。在本研究中,我们调查了HS和硫酸乙酰肝素蛋白聚糖(HSPG)核心蛋白在正常人胰岛中的分布、HS在人β细胞活力中的作用以及与胰岛素相比,胰岛内HS和HSPG水平在人类T1D中的临床相关性。在正常人胰岛中,HS(由10E4单克隆抗体识别)与胰岛素共定位,但不与胰高血糖素共定位,并且与XVIII型胶原(Col18)和syndecan-1(Sdc1)的HSPG核心蛋白相关。T1D胰腺的胰岛素阳性胰岛显示HS、Col18和Sdc1显著丧失,并且胰岛浸润白细胞强烈表达乙酰肝素酶。用HS模拟物培养的人β细胞显示存活显著改善且对过氧化氢诱导的死亡具有保护作用,这表明HS的丧失可能导致T1D中的β细胞死亡。我们得出结论,β细胞中HS的消耗可能是由于胰岛炎白细胞产生的乙酰肝素酶,这可能是人类T1D发病机制中的一个重要机制。我们的发现增加了一种可能性,即使用具有双重活性的HS替代物/乙酰肝素酶抑制剂进行干预治疗可能有助于保护新诊断为T1D的患者中残余的β细胞群。