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The developing rat cerebellum is vulnerable to thyroid hormone (TH) deficiency. The present study addresses the molecular mechanisms involved in this response. Specifically, the study focuses on the expression of selected cerebellar proteins that are known to be directly [protein expressing 3-fucosyl-N-acetyl-lactosamine antigen (CD15), neuronal cell adhesion molecule (L1)] or indirectly [glial fibrillary acidic protein (GFAP)], involved in glial-neuronal interactions and thus regulation of cell proliferation and granule cell migration. Cerebellar mass, structure, and protein expression in rat neonates exposed to antithyroid drug propylthiouracil (PTU) from the embryonic day (E) 16 to postnatal day (P) 21 were compared against rat neonates that received replacement of thyroxin (T4) starting on day P1 or untreated controls. Cerebellar proteins were analyzed by quantitative Western blots. PTU-treated rats lagged in growth and showed reduction in cerebellar mass and alterations in cerebellar structure on P15. Daily treatment of neonates with T4 restored normal cerebellum-to-body-mass ratio, cerebellar structure, and cerebellar protein expression. Densitometric analysis of Western blots revealed altered expression of selected proteins in the cerebella of hypothyroid neonates. A decrease of CD15 (46%, p = 0.031) was observed on P10 and was accompanied by a decrease in GFAP expression (64%, p = 0.039). Furthermore, a shift in the developmental GFAP profile was observed in the PTU-treated cerebellum. L1 expression was not significantly affected in the hypothyroid cerebellum. Altered expression of cerebellar proteins is likely to affect cell-cell interactions and consequently cell proliferation and migration and contribute to structural and functional alterations seen in the hypothyroid rat neonates. [ABSTRACT FROM AUTHOR]

In the crystal structure of the title compound, C20H21N3O, intra­molecular C—H⋯N hydrogen bonds stabilize the conformation of the mol­ecule. [ABSTRACT FROM AUTHOR]

In the title compound, C23H16N2O4, the mol­ecules form a supramolecular structure via inter­molecular C—H⋯O hydrogen bonds and inter­molecular π–π inter­actions. [ABSTRACT FROM AUTHOR]

In the title compound, C17H25N3OS, the mean plane of the imidazolinone system makes a dihedral angle of 83.07 (1)° with the phenyl ring. The crystal packing is stabilized by intermolecular N—H...N and C—H...O hydrogen-bonding interactions. The hexyl group is disordered over two sites with approximate occupancy factors 0.7:0.3. [ABSTRACT FROM AUTHOR]

In the crystal structure of the title compound, C22H21N3O2, the packing of the mol­ecules is mainly governed by inter­molecular C—H⋯O hydrogen bonds and π–π inter­actions. [ABSTRACT FROM AUTHOR]

In the crystal structure of the title compound, C17H23N3O3, intermolecular N—H⋯O and C—H⋯O hydrogen bonds are present. The planar heterocyclic ring makes a dihedral angle of 64.4 (1)° with the phenyl ring. [ABSTRACT FROM AUTHOR]

In the title compound, C19H16N6O4, all ring atoms in the triazolopyrimidinone unit are almost coplanar. The packing of the mol­ecules in the crystal structure is mainly due to inter­molecular C—H⋯O hydrogen-bonding inter­actions. [ABSTRACT FROM AUTHOR]

In the title compound, C22H23Cl2N5O3, the triazole ring is essentially planar. The crystal packing is determined by van der Waals forces and hydrogen bonds, no π–π stacking inter­actions being observed. [ABSTRACT FROM AUTHOR]