Human salivary histatin 1 regulating IP3R1/GRP75/VDAC1 mediated mitochondrial-associated endoplasmic reticulum membranes (MAMs) inhibits cell senescence for diabetic wound repair

Difficulty in skin wound healing is a concern for diabetic patients across the world. Impaired mitochondrial dysfunction and aging-related vascular dysfunction in human umbilical vein endothelial cells (HUVECs) caused by oxidative stress are major impediments to diabetic wound healing. However, research on skin repair at the mechanistic level by improving mitochondrial function and inhibiting oxidative stress-induced HUVEC senescence remains lacking. Human saliva effectively inhibits the natural aging of HUVECs through immunodepletion experiments. Histatin 1 (Hst1), a short peptide comprising 38 amino acids, is the primary component of human saliva that prevents HUVEC aging. Based on in vitro findings, Hst1 decreased staining for senescence-associated β-galactosidase activity and expression of mediators of senescence signaling, including p53, p21, and p16. Mechanistically, HUVEC senescence is associated with Hst1-modulated nuclear factor Nrf2 signaling as Hst1 induces ERK-mediated Nrf2 nuclear translocation through NADPH oxidase-dependent ROS regulation, reinforced Nrf2 antioxidant response, and suppressed oxidative stress. RNA sequencing identified that the mitochondrial-related gene set was enriched in the Hst1 group. Coimmunoprecipitation indicated that Hst1 delayed hydrogen peroxide-induced HUVEC senescence by inhibiting mitochondria-associated endoplasmic reticulum (ER) membrane formation mediated by inositol 1,4,5-trisphosphate receptor 1-glucose-regulated protein 75-voltage-dependent anion channel 1 (VDAC1) complex interactions. Furthermore, in aging HUVECs, Hst1 treatment or VDAC1 silencing with small interfering RNA hindered calcium (Ca 2+ ) transfer from the ER to the mitochondria, thereby ameliorating mitochondrial Ca 2+ overload and restoring mitochondrial function. In an in vivo mouse model of diabetes mellitus skin defects, Hst1 facilitated wound healing by stimulating the new blood vessel formation and impeding the expression of senescent biomarkers. This study proposes a theoretical solution that Hst1 can restore mitochondrial function by inhibiting oxidative stress or cellular senescence, thereby promoting angiogenesis and diabetic wound repair. A schematic model illustrating the effects of Hst1 on H 2 O 2 -induced mitochondrial dysfunction, HUVEC senescence, and STZ-induced diabetic wounds. Hst1 mitigates cellular senescence and restores mitochondrial function in oxidative-stressed tissues by activating the ERK pathway, enhancing Nrf2 nuclear translocation, and inhibiting the IP3R1/GRP75/VDAC1-dependent overformation of MAMs. Hst1 treatment or VDAC1 gene silencing (a key gene in MAMs) inhibits ER-mitochondrial Ca 2+ transport, antagonizes mitochondrial oxidative stress and Ca 2+ overload, and maintains mitochondrial homeostasis. Hst1 also promotes wound regeneration by stimulating neovascularization and suppressing the expression of senescence biomarkers in a diabetic wound mouse model. • By NOX-dependent ROS regulation, Hst1 initiates ERK-mediated Nrf2 nuclear translocation, enhancing the expression of senescence-induced biomarkers. • Hst1 reduces MAM overformation under oxidative stress by decreasing the interaction of the IP3R1/GRP75/VDAC1 complex. • Hst1 hinders ER-mitochondrial Ca2+ transport by modulating VDAC1 expression, diminishing mitochondrial oxidative stress and preventing Ca2+ overload, thus retarding HUVECs aging process. • Hst1 accelerates skin restoration and angiogenesis of DM models by promoting re-epithelization and suppressing the expression of senescent biomarkers.

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Journal
Free Radical Biology and Medicine
Published
2024-09-27
DOI
https://doi.org/10.1016/j.freeradbiomed.2024.09.046
Citations
14
Primary Topic
Wound Healing and Treatments
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article
Field-Weighted Citation Impact
3.50
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article

Human salivary histatin 1 regulating IP3R1/GRP75/VDAC1 mediated mitochondrial-associated endoplasmic reticulum membranes (MAMs) inhibits cell senescence for diabetic wound repair

Hao Bin Wu, Jiaqing Zhang, Tinghui Xian, Benben Peng et al.
14 citations
Free Radical Biology and Medicine
Wound Healing and Treatments
3.50
article

Human salivary histatin 1 regulating IP3R1/GRP75/VDAC1 mediated mitochondrial-associated endoplasmic reticulum membranes (MAMs) inhibits cell senescence for diabetic wound repair

Hao Bin Wu, Jiaqing Zhang, Tinghui Xian, Benben Peng, Lin Liang, Yi Liu, Jie Huang, Zhen Lin, Yongsheng Ye
article en
14 citations

Abstract

Difficulty in skin wound healing is a concern for diabetic patients across the world. Impaired mitochondrial dysfunction and aging-related vascular dysfunction in human umbilical vein endothelial cells (HUVECs) caused by oxidative stress are major impediments to diabetic wound healing. However, research on skin repair at the mechanistic level by improving mitochondrial function and inhibiting oxidative stress-induced HUVEC senescence remains lacking. Human saliva effectively inhibits the natural aging of HUVECs through immunodepletion experiments. Histatin 1 (Hst1), a short peptide comprising 38 amino acids, is the primary component of human saliva that prevents HUVEC aging. Based on in vitro findings, Hst1 decreased staining for senescence-associated β-galactosidase activity and expression of mediators of senescence signaling, including p53, p21, and p16. Mechanistically, HUVEC senescence is associated with Hst1-modulated nuclear factor Nrf2 signaling as Hst1 induces ERK-mediated Nrf2 nuclear translocation through NADPH oxidase-dependent ROS regulation, reinforced Nrf2 antioxidant response, and suppressed oxidative stress. RNA sequencing identified that the mitochondrial-related gene set was enriched in the Hst1 group. Coimmunoprecipitation indicated that Hst1 delayed hydrogen peroxide-induced HUVEC senescence by inhibiting mitochondria-associated endoplasmic reticulum (ER) membrane formation mediated by inositol 1,4,5-trisphosphate receptor 1-glucose-regulated protein 75-voltage-dependent anion channel 1 (VDAC1) complex interactions. Furthermore, in aging HUVECs, Hst1 treatment or VDAC1 silencing with small interfering RNA hindered calcium (Ca 2+ ) transfer from the ER to the mitochondria, thereby ameliorating mitochondrial Ca 2+ overload and restoring mitochondrial function. In an in vivo mouse model of diabetes mellitus skin defects, Hst1 facilitated wound healing by stimulating the new blood vessel formation and impeding the expression of senescent biomarkers. This study proposes a theoretical solution that Hst1 can restore mitochondrial function by inhibiting oxidative stress or cellular senescence, thereby promoting angiogenesis and diabetic wound repair. A schematic model illustrating the effects of Hst1 on H 2 O 2 -induced mitochondrial dysfunction, HUVEC senescence, and STZ-induced diabetic wounds. Hst1 mitigates cellular senescence and restores mitochondrial function in oxidative-stressed tissues by activating the ERK pathway, enhancing Nrf2 nuclear translocation, and inhibiting the IP3R1/GRP75/VDAC1-dependent overformation of MAMs. Hst1 treatment or VDAC1 gene silencing (a key gene in MAMs) inhibits ER-mitochondrial Ca 2+ transport, antagonizes mitochondrial oxidative stress and Ca 2+ overload, and maintains mitochondrial homeostasis. Hst1 also promotes wound regeneration by stimulating neovascularization and suppressing the expression of senescence biomarkers in a diabetic wound mouse model. • By NOX-dependent ROS regulation, Hst1 initiates ERK-mediated Nrf2 nuclear translocation, enhancing the expression of senescence-induced biomarkers. • Hst1 reduces MAM overformation under oxidative stress by decreasing the interaction of the IP3R1/GRP75/VDAC1 complex. • Hst1 hinders ER-mitochondrial Ca2+ transport by modulating VDAC1 expression, diminishing mitochondrial oxidative stress and preventing Ca2+ overload, thus retarding HUVECs aging process. • Hst1 accelerates skin restoration and angiogenesis of DM models by promoting re-epithelization and suppressing the expression of senescent biomarkers.

Free Radical Biology and MedicineVol. 225
Jinan University (CN), Dongguan People’s Hospital (CN), Stomatology Hospital (CN), First Affiliated Hospital of Jinan University (CN), Guangzhou Medical University (CN)
Zero hunger
Openalex Percentile: Top 7%
Wound Healing and Treatments
3.50
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