The Arg-Gly-Asp Motif in the Cell Adhesion Molecule L1 Promotes Neurite Outgrowth via Interaction with the αv��3 Integrin

The cell adhesion molecule L1 is a potent inducer of neurite outgrowth and it has been implicated in X-linked hydrocephalus and related neurological disorders. To investigate the mechanisms of neurite outgrowth stimulated by L1, attempts were made to identify the neuritogenic sites in L1. Fusion proteins containing different segments of the extracellular region of L1 were prepared and different neuronal cells were assayed on substrate-coated fusion proteins. Interestingly, both immunoglobulin (Ig)-like domains 2 and 6 (Ig2, Ig6) promoted neurite outgrowth from dorsal root ganglion cells, whereas neural retinal cells responded only to Ig2. L1 Ig2 contains a previously identified homophilic binding site, whereas L1 Ig6 contains an Arg-Gly-Asp (RGD) sequence. The neuritogenic activity of Ig6 was abrogated by mutations in the RGD site. The addition of RGD-containing peptides also inhibited the promotion of neurite outgrowth from dorsal root ganglion cells by glutathione S-transferase-Ig6, implicating the involvement of an integrin. The monoclonal antibody LM609 against αv��3 integrin, but not an anti-β1 antibody, inhibited the neuritogenic effects of Ig6. These data thus provide the first evidence that the RGD motif in L1 Ig6 is capable of promoting neurite outgrowth via interaction with the αv��3 integrin on neuronal cells.

Direct measurement of oligonucleotide binding stoichiometry of gene V protein by mass spectrometry.

The binding stoichiometry of gene V protein from bacteriophage f1 to several oligonucleotides was studied using electrospray ionization-mass spectrometry (ESI-MS). Using mild mass spectrometer interface conditions that preserve noncovalent associations in solution, gene V protein was observed as dimer ions from a 10 mM NH4OAc solution. Addition of oligonucleotides resulted in formation of protein-oligonucleotide complexes with stoichiometry of approximately four nucleotides (nt) per protein monomer. A 16-mer oligonucleotide gave predominantly a 4:1 (protein monomer: oligonucleotide) complex while oligonucleotides shorter than 15 nt showed stoichiometries of 2:1. Stoichiometries and relative binding constants for a mixture of oligonucleotides were readily measured using mass spectrometry. The binding stoichiometry of the protein with the 16-mer oligonucleotide was measured independently using size-exclusion chromatography and the results were consistent with the mass spectrometric data. These results demonstrate, for the first time, the observation and stoichiometric measurement of protein-oligonucleotide complexes using ESI-MS. The sensitivity and high resolution of ESI-MS should make it a useful too] in the study of protein-DNA interactions.

Plea in the case of Hamilton v. Saunders, 1763

Plea in response to the plaintiff's declaration. Signed: (Charles) Pinckney, defendant's attorney, and John Rutledge (plaintiff's attorney?). Note on verso: Filed 4th May 1763.

Notice of trial in the case of Jonathan Fish [et al.] v. William Betts, 12 April 1774

Document addressed to Thomas Hicks (attorney for the defendant) informing him that Scott (attorney for the plaintiff) intends to bring the case to trial "at the next Supreme Court of Judicature to be held for the Province of New York." Signed by Scott.

Subpoena in Cocke v. Tye, 12 July 1733

Subpoena to answer a petition by James Powell Cocke. Signed by William Hamlin.

Terrae Yemen maxima Pars. seu Imperii Imami, Principatus Kaukebân, nec non ditionum Haschid U Bekîl, Nehhm, Chaulân, Abu Arîsch Et Aden Tabula: ex observationibus astronomicis et hodometricis jussu et suntibus Potentissimor: Daniae Regnum Friderici V et Christiani VII institutis

delineata Auctore C. Niebuhr ; Gustav Conrad Lotter Sculps.

Aḥv��l-ʼi chahār darv��sh : manuscript, undated

Title from caption (fol. 1v).

V��ek:vaḏo : manuscript, 1890?

Foreign wove paper, probably German; watermark: Keferstein & Sohn, 1871.

[ v��rā:mārā:dhan:pûtr:māeā:sarve:karmī:kahīe] : manuscript, ca. 1887

Local paper. Pages slightly discolored.

Prof. James V. Campbell Law Dept.

First Dean of University of Michigan Law School, 1859-1871. On verso: Sam B. Revenaugh's Photographic Establishment, 28 Huron Street, Ann Arbor, Michigan