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1

A cell adhesion molecule, dystroglycan, is implicated in homeostatic plasticity

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Figiel I., Krzystyniak A., Bartkowiak-Kaczmarek A., Roszkowska M., Bijata M., Wlodarczyk J.
Acta Neurobiologiae Experimentalis
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2017
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tom 77
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nr Suppl.1
INTRODUCTION: A number of studies have demonstrated that regulated proteolysis of synaptically expressed cell adhesion molecules plays a fundamental role in the morphological reorganization of synapses underlying homeostatic plasticity. One of the major modulators of these processes is matrix metalloproteinase-9 (MMP-9), an extracellularly operating protease. AIM(S): The main aim of our study is to investigate the subcellular localization of β‑dystroglycan (β‑DG), a well-known substrate of MMP-9, and its involvement in structural plasticity. METHOD(S): We analyzed isolated mouse synaptosomes from P2 fraction with flow cytometry after immunostaining with antibodies against synaptosomal markers and β‑DG. We also performed triple immunofluorescence labelling on primary hippocampal neurons. To study whether proteolytic cleavage of β‑DG influences the dendritic spine shape we performed life imaging of MMP-9-treated primary hippocampal cultures, previously infected with lentiviral vector (LV) coding shRNA specifically silencing DG or LV carrying GFP. Furthermore, we investigated the correlation between β‑DG localization and MMP-9 activity by using (FRET)-based MMP-9 activity biosensor. RESULTS: We found out that β‑DG is present on a small subset of synaptosomes that exhibit expression of both post-synaptic markers (psd-95 and gephyrin). Using immunofluorescence staining of primary neurons with pre-synaptic marker antibodies (v-GAT and v-GLUT) we confirmed β‑DG localization at both inhibitory and excitatory synapses. We also found changes in the number of β‑DG‑containing synapses in response to chemically induced LTP (cLTP). Morphometric analysis of live-cell imaging experiments revealed that β‑DG exerts an influence on dendritic spine structure. Moreover, the results concerning spatial location of MMP‑9 activity and β‑DG will be presented CONCLUSIONS: Our findings indicate β‑DG involvement in synaptic structural plasticity. FINANCIAL SUPPORT: This study has been supported by research grant 2015/19/B/NZ3/01376 from National Science Centre Poland.
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The role of s-palmitoylation and s-nitrosylation interplay in the chronic stress disorders

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Zareba-Koziol M., Bartkowiak-Kaczmarek A., Krzystyniak A., Bijata M., Figiel I., Wlodarczyk J.
Acta Neurobiologiae Experimentalis
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2017
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tom 77
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nr Suppl.1
Chronic stress exposure is a key environmental factor for development of neuropsychiatric disorders such as major depression and anxiety disorders. Chronic stress-related emotional and cognitive impairment is associated with alternations in synaptic organization. One of the best described mechanism of synaptic proteins regulation are posttranslational modifications. S-palmitoylation is the covalent lipid reversible modification of cysteine with palmitate which regulates diverse aspects of neuronal protein trafficking and function. The reversible nature of palmitoylation allows proteins to associate with membranes, what regulate their sorting, localization and functions. Intracellular protein S-palmitoylation is controlled by family of protein acyl-transferases and palmitoyl-thioesterases. Recent study shows alternative mechanism of S-palmitoylation regulation by S-nitrosylation. S-nitrosylation is the covalent modification of cysteine by a nitric oxide (NO). The main aim is to understand the functional consequences of alerted protein S-palmitoylation and S-nitrosylation interplay induced by chronic restraint stress. Using mass spectrometry based approaches we profiled endogenous S-palmitoylation and S-nitrosylation. We identified massive changes at the level of proteins and exact sites of modifications in the mouse model of chronic stress. In the physiological conditions we observed excellent competitive effect, over 50% of cysteines were identified only in the one form S-nitrosylated or S-palmitoylated. After chronic stress, we demonstrated that almost all identified proteins were simultaneously modified by palmitate and NO. Summarizing, our results suggest that altered mechanism of interplay between S-palmitoylation and S-nitrosylation of synaptic proteins might be one of the main events associated with chronic stress disorder, leading to destabilization in synaptic networks. FINANCIAL SUPPORT: Financial Support: NCN OPUS 2015/17/B/NZ3/00557.
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Glycogen phosphorylase inhibition - a new fountain of youth?

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Drulis-Fajdasz D., Krzystyniak A., Miazek A., Zalas M., Wlodarczyk J., Rakus D.
Acta Biochimica Polonica
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2018
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tom 65
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nr S2
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