Disparities in Access to Neurologic Telemedicine During the COVID-19 Pandemic: A Bronx Tale.

Objective: To determine whether there is a disparity in access to telemedical care that may be a function of socioeconomic status, language, or other demographic factors during the peak of the coronavirus disease 2019 (COVID-19) pandemic at a highly affected urban center (Montefiore Medical Center) in Bronx, NY.

Methods: We retrospectively investigated potential patient characteristics that might be associated with an increased likelihood of receiving a telephone visit as opposed to a televideo visit for patients followed in the pediatric neurology, adult epilepsy, and general neurology practices at Montefiore Medical Center during the 30-day period starting April 2, 2020, at the peak of the COVID-19 pandemic in New York.

Results: We found that patients who had telephone encounters, as opposed to televideo encounters, were overall older, less likely to have commercial insurance, and more likely to have Medicaid.

High-molecular-weight kininogen preadsorbed to glass surface markedly reduces neutrophil adhesion.

Adsorbed proteins on biomaterial surfaces determine whether cells adhere, but rheological variables are also critical. Neutrophil adhesion under well-defined radial flow conditions was studied on glass preadsorbed with plasma proteins or plasma protein domain fragments. Fibrinogen, low-molecular-weight kininogen (LK), high-molecular-weight kininogen (HK), cleaved HK (HKa), and recombinant HK domains 3 and 5 (D3 and D5H) were used.

Thrombin-induced platelet aggregation is inhibited by the heptapeptide Leu271-Ala277 of domain 3 in the heavy chain of high molecular weight kininogen.

The ability of kininogens to modulate thrombin-induced aggregation of human platelets has been assigned to domain 3 (D3) in the common heavy chain coded for by exons 7, 8, and 9 of kininogen gene. We expressed each of the exons 7, 8, and 9, and various combinations as glutathione S-transferase fusion proteins in Escherichia coli. Each of the exon products 7 (Lys236-Gln292), 9 (Val293-Gly328), and 8 (Gln329-Met357), and their combinations were evaluated for the ability to inhibit thrombin induced platelet aggregation.

Neutrophil adhesion on surfaces preadsorbed with high molecular weight kininogen under well-defined flow conditions.

The adhesion of neutrophils and other leukocytes to biomaterial surfaces is an important phenomenon in the host response to biomaterials because the number of adherent leukocytes is often related to the inflammatory response after implantation. After adhering to biomaterial surfaces, other leukocyte reactions, such as phagocytosis, respiratory burst, and protease release, may occur and result in the deterioration of the implanted biomaterial and injury to peripheral tissue. This study of neutrophil adhesion quantitatively characterizes neutrophil adhesion under well-defined laminar flow conditions using a radial flow chamber.

Determination of gene structure by intron trapping using polymerase chain reaction: application to the human plasma prekallikrein gene.

We have devised a method to determine gene structure that utilizes the known gene structure of homologous proteins and the polymerase chain reaction (PCR). Because homologous proteins have evolved from a common ancestral gene, it is possible to design primers corresponding to the adjacent exon sequences in the protein of interest. These primers could then be used in a PCR using normal genomic DNA as template.

High molecular weight kininogen binds to Mac-1 on neutrophils by its heavy chain (domain 3) and its light chain (domain 5).

High molecular weight kininogen (HK) binds specifically, saturably, and reversibly to neutrophils and also reciprocally inhibits the binding of fibrinogen to neutrophils. Since fibrinogen binds to the leukocyte integrin CD11b/18 (Mac-1, alpha M beta 2), we investigated whether HK bound to Mac-1 and whether the binding site was similar to that for factor X. We also examined whether one or both chains of cleaved HK (HKa) were involved.