PDF herunterladen
CC BY-NC-ND 4.0 · Indian Journal of Neurosurgery 2020; 9(02): 106-114
DOI: 10.1055/s-0040-1713059
Original Article

The Possible Inhibition Effect of Lycium barbarum Polysaccharides on Rat Intracerebral Hemorrhage Secondary Neuronal Apoptosis through Intervening Endogenous/Exogenous Pathways of Apoptosis

Yourui Zou
1   Department of Neurosurgery, General Hospital of Ningxia Medical University, Yinchuan, China
,
ShengYu Sun
1   Department of Neurosurgery, General Hospital of Ningxia Medical University, Yinchuan, China
,
Usama Ilyas Sharif
2   Department of Neurosurgery. General Hospital of Ningxia Medical University, Yinchuan, China
,
Abdul Wasie
2   Department of Neurosurgery. General Hospital of Ningxia Medical University, Yinchuan, China
,
Hui Ma
1   Department of Neurosurgery, General Hospital of Ningxia Medical University, Yinchuan, China
3   Ningxia Key Laboratory for Cranio-cerebral Diseases, Ningxia Medical University, Yinchuan, China
› Institutsangaben Funding This study was supported by Natural Science Foundation of China (Grant no. 81760449) and Natural Science Foundation of Ningxia (Grant no. NZ16127).
› Weitere Informationen
   Lizenzen und Reprints

Abstract

Objective The aim of this study was to explore the inhibition effect and possible mechanism of Lycium barbarum polysaccharides (LBP) on rat intracerebral hemorrhage (ICH) secondary neuronal apoptosis.

Materials and Methods High-, medium-, and low-dose LBP (50, 100, and 200 mg•kg) and nimodipine (10 mg•kg) groups were given once daily by 15-day gavage before operation, while the sham operation and ICH groups were given the equal volume of saline. An ICH model was established by autologous blood injection and the neurological function in each group was scored at 4, 8, 12, 24, and 48 hours after modeling. Furthermore, terminal deoxynucleotidyl transferase dUTP nick end labeling analysis was performed to detect neuronal apoptosis, while western blot, immunohistochemistry, and real-time-polymerase chain reaction were used to study the influence of LBP on ICH secondary neuronal apoptosis.

Results The neurological function score was significantly decreased after ICH, and the intervention effect of a single drug was not evident. The apoptotic nerve cells increased significantly in the ICH group but decreased considerably in the LBP groups. Furthermore, tumor necrosis factor alpha (TNF-α) expression decreased significantly, while B-cell lymphoma 2 expression increased substantially in the high- and medium-dose LBP groups compared with ICH group, suggesting that LBP could reduce the effect of ICH. However, the impact of LBP did not correlate positively with the dose.

Conclusion The application of LBP may not significantly improve neurological function after ICH, but it can inhibit rat ICH secondary neuronal apoptosis.

Keywords

Lycium barbarum polysaccharides - rat intracerebral hemorrhage - neuronal apoptosis - TNF-α - Bcl-2


Publikationsverlauf

Artikel online veröffentlicht:
26. August 2020

© .

Thieme Medical and Scientific Publishers Private Ltd.
A-12, Second Floor, Sector -2, NOIDA -201301, India

 

  • References

  • 1 Naval NS, Nyquist PA, Carhuapoma JR. Management of spontaneous intracerebral hemorrhage. Neurol Clin 2008; 26 (02) 373-384, vii vii
    CrossrefPubMedGoogle Scholar
  • 2 Hwang BY, Appelboom G, Ayer A. et al. Advances in neuroprotective strategies: potential therapies for intracerebral hemorrhage. Cerebrovasc Dis 2011; 31 (03) 211-222
    CrossrefPubMedGoogle Scholar
  • 3 Qureshi AI, Suri MF, Ostrow PT. et al. Apoptosis as a form of cell death in intracerebral hemorrhage. Neurosurgery 2003; 52 (05) 1041-1047, discussion 1047–1048
    CrossrefPubMedGoogle Scholar
  • 4 Krysko DV, Vanden Berghe T, D’Herde K, Vandenabeele P. Apoptosis and necrosis: detection, discrimination and phagocytosis. Methods 2008; 44 (03) 205-221
    CrossrefPubMedGoogle Scholar
  • 5 Trabert J, Steiner T. Medical versus surgical management of intracerebral hematomas. Curr Atheroscler Rep 2012; 14 (04) 366-372
    CrossrefPubMedGoogle Scholar
  • 6 Tariq N, Adil MM, Saeed F, Chaudhry SA, Qureshi AI. Outcomes of thrombolytic treatment for acute ischemic stroke in dialysis-dependent patients in the United States. J Stroke Cerebrovasc Dis 2013; 22 (08) e354-e359
    CrossrefPubMedGoogle Scholar
  • 7 Siddiq F, Adil MM, Norby KE, Rahman HA, Qureshi AI. Rates and outcomes of neurosurgical treatment for postthrombolytic intracerebral hemorrhage in patients with acute ischemic stroke. World Neurosurg 2014; 82 (05) 678-683
    CrossrefPubMedGoogle Scholar
  • 8 Li Q, Yang CH, Xu JG, Li H, You C. Surgical treatment for large spontaneous basal ganglia hemorrhage: retrospective analysis of 253 cases. Br J Neurosurg 2013; 27 (05) 617-621
    CrossrefPubMedGoogle Scholar
  • 9 Chen Z, Kwong Huat Tan B, Chan SH. Activation of T lymphocytes by polysaccharide-protein complex from Lycium barbarum L. Int Immunopharmacol 2008; 8 (12) 1663-1671
    CrossrefPubMedGoogle Scholar
  • 10 Miao Y, Xiao B, Jiang Z. et al. Growth inhibition and cell-cycle arrest of human gastric cancer cells by Lycium barbarum polysaccharide. Med Oncol 2010; 27 (03) 785-790
    CrossrefPubMedGoogle Scholar
  • 11 Yu MS, Lai CS, Ho YS. et al. Characterization of the effects of anti-aging medicine Fructus lycii on beta-amyloid peptide neurotoxicity. Int J Mol Med 2007; 20 (02) 261-268
    PubMedGoogle Scholar
  • 12 Li SY, Yang D, Yeung CM. et al. Lycium barbarum polysaccharides reduce neuronal damage, blood-retinal barrier disruption and oxidative stress in retinal ischemia/reperfusion injury. PLoS One 2011; 6 (01) e16380
    CrossrefPubMedGoogle Scholar
  • 13 Ho YS, Yu MS, Yang XF, So KF, Yuen WH, Chang RC. Neuroprotective effects of polysaccharides from wolfberry, the fruits of Lycium barbarum, against homocysteine-induced toxicity in rat cortical neurons. J Alzheimers Dis 2010; 19 (03) 813-827
    CrossrefPubMedGoogle Scholar
  • 14 Wang T, Li Y, Wang Y. et al. Lycium barbarum polysaccharide prevents focal cerebral ischemic injury by inhibiting neuronal apoptosis in mice. PLoS One 2014; 9 (03) e90780
    CrossrefPubMedGoogle Scholar
  • 15 Raicević R, Jovicić A, Aleksić P. et al. [Role of nimodipine in the therapy of subarachnoid and intracerebral hemorrhage]. Vojnosanit Pregl 1999; 56 (06) 593-598
    PubMedGoogle Scholar
  • 16 Ma B, Zhang J. Nimodipine treatment to assess a modified mouse model of intracerebral hemorrhage. Brain Res 2006; 1078 (01) 182-188
    CrossrefPubMedGoogle Scholar
  • 17 Korenkov AI, Pahnke J, Frei K. et al. Treatment with nimodipine or mannitol reduces programmed cell death and infarct size following focal cerebral ischemia. Neurosurg Rev 2000; 23 (03) 145-150
    CrossrefPubMedGoogle Scholar
  • 18 Deinsberger W, Vogel J, Kuschinsky W, Auer LM, Böker DK. Experimental intracerebral hemorrhage: description of a double injection model in rats. Neurol Res 1996; 18 (05) 475-477
    CrossrefPubMedGoogle Scholar
  • 19 Zhou ZH, Qu F, He X. et al. An improved autologous blood ICH model of rat: double injection and double withdrawal. Chin J Clin Neurosci 2004; 4: 408
    PubMedGoogle Scholar
  • 20 Garcia JH, Wagner S, Liu KF, Hu XJ. Neurological deficit and extent of neuronal necrosis attributable to middle cerebral artery occlusion in rats. Statistical validation. Stroke 1995; 26 (04) 627-634, discussion 635
    CrossrefPubMedGoogle Scholar
  • 21 Li SY, Fu ZJ, Ma H. et al. Effect of lutein on retinal neurons and oxidative stress in a model of acute retinal ischemia/reperfusion. Invest Ophthalmol Vis Sci 2009; 50 (02) 836-843
    CrossrefPubMedGoogle Scholar
  • 22 Li P, Nijhawan D, Budihardjo I. et al. Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade. Cell 1997; 91 (04) 479-489
    CrossrefPubMedGoogle Scholar
  • 23 Hall NC, Packard BA, Hall CL, de Courten-Myers G, Wagner KR. Protein oxidation and enzyme susceptibility in white and gray matter with in vitro oxidative stress: relevance to brain injury from intracerebral hemorrhage. Cell Mol Biol 2000; 46 (03) 673-683
    PubMedGoogle Scholar
  • 24 Ardizzone TD, Zhan X, Ander BP, Sharp FR. SRC kinase inhibition improves acute outcomes after experimental intracerebral hemorrhage. Stroke 2007; 38 (05) 1621-1625
    CrossrefPubMedGoogle Scholar
  • 25 Gong C, Boulis N, Qian J, Turner DE, Hoff JT, Keep RF. Intracerebral hemorrhage-induced neuronal death. Neurosurgery 2001; 48 (04) 875-882, discussion 882–883
    PubMedGoogle Scholar
  • 26 Qureshi AI, Ling GS, Khan J. et al. Quantitative analysis of injured, necrotic, and apoptotic cells in a new experimental model of intracerebral hemorrhage. Crit Care Med 2001; 29 (01) 152-157
    CrossrefPubMedGoogle Scholar
  • 27 Solá S, Morgado AL, Rodrigues CM. Death receptors and mitochondria: two prime triggers of neural apoptosis and differentiation. Biochim Biophys Acta 2013; 1830 (01) 2160-2166
    CrossrefPubMedGoogle Scholar
  • 28 Riedl SJ, Salvesen GS. The apoptosome: signalling platform of cell death. Nat Rev Mol Cell Biol 2007; 8 (05) 405-413
    CrossrefPubMedGoogle Scholar
  • 29 Depraetere V, Golstein P. Fas and other cell death signaling pathways. Semin Immunol 1997; 9 (02) 93-107
    CrossrefPubMedGoogle Scholar
  • 30 Kuang AA, Diehl GE, Zhang J, Winoto A. FADD is required for DR4- and DR5-mediated apoptosis: lack of trail-induced apoptosis in FADD-deficient mouse embryonic fibroblasts. J Biol Chem 2000; 275 (33) 25065-25068
    CrossrefPubMedGoogle Scholar
  • 31 Locksley RM, Killeen N, Lenardo MJ. The TNF and TNF receptor superfamilies: integrating mammalian biology. Cell 2001; 104 (04) 487-501
    CrossrefPubMedGoogle Scholar
  • 32 Hakem R, Hakem A, Duncan GS. et al. Differential requirement for caspase 9 in apoptotic pathways in vivo. Cell 1998; 94 (03) 339-352
    CrossrefPubMedGoogle Scholar
  • 33 Youle RJ, Strasser A. The BCL-2 protein family: opposing activities that mediate cell death. Nat Rev Mol Cell Biol 2008; 9 (01) 47-59
    CrossrefPubMedGoogle Scholar
  • 34 Ola MS, Nawaz M, Ahsan H. Role of Bcl-2 family proteins and caspases in the regulation of apoptosis. Mol Cell Biochem 2011; 351 (1-2) 41-58
    CrossrefPubMedGoogle Scholar
  • 35 Merry DE, Veis DJ, Hickey WF, Korsmeyer SJ. bcl-2 protein expression is widespread in the developing nervous system and retained in the adult PNS. Development 1994; 120 (02) 301-311
    CrossrefPubMedGoogle Scholar
  • 36 Merry DE, Korsmeyer SJ. Bcl-2 gene family in the nervous system. Annu Rev Neurosci 1997; 20: 245-267
    CrossrefPubMedGoogle Scholar