2.3 Alpha Phi Alpha Fraternity, Inc. Alpha Psi Chapter Lincoln University, 1934-35

https://bluetigercommons.lincolnu.edu/lgaines_sec1/1009/thumbnail.jpg

2.3 University of Missouri building

The university’s defense, led by William Hogsett, countered that the University was bound by law to reject Gaines’ application and stated that Lincoln University had to provide higher education for Negroes. This is the point that Houston wanted the court to address. Houston got Canada to admit the only students he would bar would be of African descent. Hogsett, on the other hand, was unable to unnerve young Mr. Gaines with speculation that the NAACP had put him up to applying at MU. Gaines replied,” No, that is my idea; about the [law] suit.”

2.3 Eddie Mae Page, Friend of Lloyd Gaines in Chicago

During this time Lloyd Gaines took meals at the home of Eddie Mae Page; a friend from St. Louis. Running low on funds, he stayed at the Alpha Phi Alpha house where members took up a collection for him. On a rainy night, March 19, 1939, Lloyd Gaines told friends that he was going to buy stamps and would be right back. To this day, Lloyd L. Gaines has never been located.

Inactivation of tyrosine hydroxylase by nitration following exposure to peroxynitrite and 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP)

The decrement in dopamine levels exceeds the loss of dopaminergic neurons in Parkinson’s disease (PD) patients and experimental models of PD. This discrepancy is poorly understood and may represent an important event in the pathogenesis of PD. Herein, we report that the rate-limiting enzyme in dopamine synthesis, tyrosine hydroxylase (TH), is a selective target for nitration following exposure of PC12 cells to either peroxynitrite or 1-methyl-4-phenylpyridiniun ion (MPP+). Nitration of TH also occurs in mouse striatum after MPTP administration. Nitration of tyrosine residues in TH results in loss of enzymatic activity. In the mouse striatum, tyrosine nitration-mediated loss in TH activity parallels the decline in dopamine levels whereas the levels of TH protein remain unchanged for the first 6 hr post MPTP injection. Striatal TH was not nitrated in mice overexpressing copper/zinc superoxide dismutase after MPTP administration, supporting a critical role for superoxide in TH tyrosine nitration. These results indicate that tyrosine nitration-induced TH inactivation and consequently dopamine synthesis failure, represents an early and thus far unidentified biochemical event in MPTP neurotoxic process. The resemblance of the MPTP model with PD suggests that a similar phenomenon may occur in PD, influencing the severity of parkisonian symptoms.

Enzymatic Macrocyclization of 1,2,3-Triazole Peptide Mimetics

Funded by European Research Council. Grant Number: 339367 UK Biotechnology and Biological Sciences Research Council. Grant Number: K015508/1 The Wellcome Trust. Grant Number: 094476 EPSRC Acknowledgements This work was supported by the European Research Council (339367), UK Biotechnology and Biological Sciences Research Council (K015508/1), The Wellcome Trust (TripleTOF 5600 mass spectrometer (094476), the MALDI TOF-TOF Analyser (079272AIA), 700 NMR) and the EPSRC UK National Mass Spectrometry Facility at Swansea University. J.H.N. is a Royal Society Wolfson Merit Award Holder and 1000 talent scholar at Sichuan University.

Desensitization of the Neurokinin-1 Receptor (NK1-R) in Neurons: Effects of Substance P on the Distribution of NK1-R, Gαq/11, G-Protein Receptor Kinase-2/3, and β-Arrestin-1/2

Observations in reconstituted systems and transfected cells indicate that G-protein receptor kinases (GRKs) and β-arrestins mediate desensitization and endocytosis of G-protein–coupled receptors. Little is known about receptor regulation in neurons. Therefore, we examined the effects of the neurotransmitter substance P (SP) on desensitization of the neurokinin-1 receptor (NK1-R) and on the subcellular distribution of NK1-R, Gαq/11, GRK-2 and -3, and β-arrestin-1 and -2 in cultured myenteric neurons. NK1-R was coexpressed with immunoreactive Gαq/11, GRK-2 and -3, and β-arrestin-1 and -2 in a subpopulation of neurons. SP caused 1) rapid NK1-R–mediated increase in [Ca2+]i, which was transient and desensitized to repeated stimulation; 2) internalization of the NK1-R into early endosomes containing SP; and 3) rapid and transient redistribution of β-arrestin-1 and -2 from the cytosol to the plasma membrane, followed by a striking redistribution of β-arrestin-1 and -2 to endosomes containing the NK1-R and SP. In SP-treated neurons Gαq/11 remained at the plasma membrane, and GRK-2 and -3 remained in centrally located and superficial vesicles. Thus, SP induces desensitization and endocytosis of the NK1-R in neurons that may be mediated by GRK-2 and -3 and β-arrestin-1 and -2. This regulation will determine whether NK1-R–expressing neurons participate in functionally important reflexes.