Abstract
The human pineal gland regulates day‐night dynamics of multiple physiological processes, especially through the secretion of melatonin. Using mass‐spectrometry‐based proteomics and dedicated analysis tools, we identify proteins in the human pineal gland and analyze systematically their variation throughout the day and compare these changes in the pineal proteome between control specimens and donors diagnosed with autism. Results reveal diverse regulated clusters of proteins with, among others, catabolic carbohydrate process and cytoplasmic membrane‐bounded vesicle‐related proteins differing between day and night and/or control versus autism pineal glands. These data show novel and unexpected processes happening in the human pineal gland during the day/night rhythm as well as specific differences between autism donor pineal glands and those from controls.
Highlights
The pineal gland is a small endocrine gland located at the border between the mesencephalon and diencephalon of the brain.[1,2] Unlike much of the rest of the brain, the pineal gland is not isolated from the body by the blood-brain barrier and belongs to the so-called “circumventricular” organs.[3,4] It is highly vascularized and composed of a large and dense anastomosed network of capillaries.[3,5,6] The main known function of the pineal gland is to produce the hormone melatonin.[7]
We identified five enriched Gene Ontology (GO) clusters (Figure 1): catabolic carbohydrate process (GPI, TPI1, MDH1, MDH2, PGAM1, ENO1, ENO2, ENO3, HK1, LDHB, LDHA, PKM, PGK1, ALDOC, ALDOA, GAPDH, PFKM, PGD, ATP5O, GOT1, GOT2, HADHB, ACLY, GLUD1, HADHA), unfolded protein folding (ERP29, CCT5, HSPA1A, PPIB, CRYAB, HSPA8, HSP90AA1, HSP90AB1, HSPA9, CCT3, CCT2, HSPD1, protein disulfide isomerase A6 (PDIA6), CCT6A, tailless complex polypeptide 1 (TCP1), HSP90B1, CALR, CCT7, CANX, PPIA), cytoplasmic membrane-bounded vesicle (ERP29, ATP6V1B2, P4HB, PPIB, CTSD, RAB7A, protein disulfide isomerase A3 (PDIA3), YWHAE, HSPA8, HSP90AA1, HSP90AB1, AHCY, HSPA5, ANXA2, CLTC, PDIA6, YWHAZ, HSP90B1, PRDX1, CANX), carbon-oxygen lyase (GLO1, ENO1, ENO2, ENO3, RPS3, GOT1, ALDOC, XRCC6, ALDOA, CA1, ACO2, HADHB, ACLY, HADHA) and negative regulation of programmed death (GSTP1, HSPA1A, GLO1, PRDX6, PRDX5, TF, HSPB1, CRYAB, PRDX2, CFL1, NEFL, HSPA9, HSPA5, ANXA5, HSPD1, YWHAZ, HSP90B1, ANXA1, XRCC5)
We identified several chaperones such as the protein disulfide isomerase (PDI) family largely expressed in the endoplasmic reticulum (ER),[81] and heat shock proteins (HSPs), which act as molecular chaperones in conditions of stress including carcinogenesis.[82,83]
Summary
Institute for Data Valorization (IVADO); Université Paris Diderot; Cognacq-Jay foundation; Centre National de la Recherche Scientifique; Bettencourt-Schueller foundation; Conny-Maeva foundation; Institut National de la Santé et de la Recherche Médicale; Agence Nationale de la Recherche, Grant/Award Number: Eranet-Neuron (ALTRUISM), Labex BioPsy and Labex GenMed; Fonds de Recherche du Québec - Santé; Assistance Publique - Hôpitaux de Paris; Orange foundation; Institut Pasteur; FondaMental foundation; Fondation de France
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