Cutaneous Bacillus anthracis infection.
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Adult↗
Biomedical subjects
B E Strober
Publications and source records attributed to B E Strober.
Eyelash hypertrichosis in a patient treated with topical latanoprost.
We describe a female patient with a history of primary open-angle glaucoma who, following treatment with topical latanoprost, a synthetic prostaglandin F2 alpha analog, developed hypertrichosis of the eyelashes. Hypertrichosis, a recently described side effect of latanoprost--together with iridal pigmentation--represents a potentially permanent cosmetic side effect associated with the use of this highly effective intraocular pressure-lowering agent. The molecular mechanism underlying latanoprost-induced hypertrichosis is unknown.
Aged↗
Lupus panniculitis (lupus profundus).
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Anti-Inflammatory Agents, Non-Steroidal↗
Functional interactions between the hBRM/hBRG1 transcriptional activators and the pRB family of proteins.
hBRG1 and hBRM are mammalian homologs of the SNF2/SW12 yeast transcriptional activator. These proteins exist in a large multisubunit complex that likely serves to remodel chromatin and, in so doing, facilitates the function of specific transcription factors. The retinoblastoma protein (pRB) inhibits cell cycle progression by repressing transcription of specific growth-related genes. Using the yeast two-hybrid system, we demonstrate that the members of the hBRG1/hBRM family of proteins interact with the pRB family of proteins, which includes pRB, p107, and p130. Interaction between the hBRG1/hBRM family with the pRB family likely influences cellular proliferation, as both hBRG1 and hBRM, but not mutants of these proteins unable to bind to pRB family members, inhibit the formation of drug-resistant colonies when transfected into the SW13 human adenocarcinoma cell line, which lacks endogenous hBRG1 or hBRM. Further, hBRM and two isoforms of hBRG1 induce the formation of flat, growth-arrested cells in a pRB family-dependent manner when introduced into SW13 cells. This flat-cell inducing activity is severely reduced by cotransfection of the wild-type E1A protein and variably reduced by the cotransfection of mutants of E1A that lack the ability to bind to some or all members of the pRB family.
Base Sequence↗
The retinoblastoma protein and BRG1 form a complex and cooperate to induce cell cycle arrest.
The retinoblastoma tumor suppressor protein (RB) binds several cellular proteins involved in cell cycle progression. Using the yeast two-hybrid system, we found that RB bound specifically to the protein BRG1. BRG1 shares extensive sequence similarity to Drosophila brahma, an activator of homeotic gene expression, and the yeast transcriptional activator SNF2/SW12. BRG1 contains an RB-binding motif found in viral oncoproteins and bound to the A/B pocket and the hypophosphorylated form of RB. BRG1 did not bind RB in viral oncoprotein-transformed cells. Coimmunoprecipitation experiments suggested BRG1 associates with the RB family in vivo. In the human carcinoma cell line SW13, BRG1 exhibited tumor suppressor activity by inducing formation of flat, growth-arrested cells. This activity depended on the ability of BRG1 to cooperate and complex with RB, as both an RB-nonbinding mutant of BRG1 and the sequestration of RB by adenovirus E1A protein abolished flat cell formation.
Amino Acid Sequence↗