Domestication of the Emblematic White Cheese-Making Fungus Penicillium camemberti and Its Diversification into Two Varieties

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Effect of new founders on retention of gene diversity in captive populations: A formalization of the nucleus population concept

A nucleus population is a small captive population genetically supported by periodic importation of wild caught animals. Periodic importation will allow nucleus populations to maintain the same amount of gene diversity as larger captive populations that do not import wild caught animals. The function of nucleus populations as envisioned by the IUCN/SSC Captive Breeding Specialist Group (CBSG) is to make additional captive space available for endangered taxa not currently maintained in captivity. In this article, mathematical models are developed to assess the effectiveness of the nucleus population concept in reducing the population sizes necessary to maintain appreciable amounts of gene diversity in captive populations. It is shown that the Nucleus I population concept, as defined and promoted by the CBSG, requires an importation rate 10–20 times greater than they have indicated. Whereas nucleus populations are not appropriate for maintenance of significant amounts of gene diversity in long-term breeding programs, small populations can be valuable for research, education, and reintroduction projects with short-term goals. Decisions have to be made on which of the many endangered taxa will be maintained and for what purposes, if captive breeding is to be an effective component of species conservation. © 1993 Wiley-Liss, Inc.     

DNA Methylation and Histone H1 Jointly Repress Transposable Elements and Aberrant Intragenic Transcripts

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Evaluation of cetuximab as a candidate for targeted α-particle radiation therapy of HER1-positive disseminated intraperitoneal disease

Although the epidermal growth factor receptor (EGFR), also known as HER1, has been studied for over a decade, it continues to be a molecule of great interest and focus of investigators for development of targeted therapies. The marketed monoclonal antibody cetuximab binds to HER1, and thus might serve as the basis for creation of imaging or therapies that target this receptor. The potential of cetuximab as a vehicle for the delivery of α-particle radiation was investigated in an intraperitoneal tumor mouse model. The effective working dose of 10 μCi of ²¹²Pb-cetuximab was determined from a dose (10–50 μCi) escalation study. Toxicity, as indicated by the lack of animal weight loss, was not evident at the 10 μCi dose of ²¹²Pb-cetuximab. A subsequent study demonstrated ²¹²Pb-cetuximab had a therapeutic efficacy similar to that of ²¹²Pb-trastuzumab (p = 0.588). Gemcitabine given 24 h prior to ²¹²Pb-cetuximab increased the median survival from 174 d to 283 d, but carboplatin suppressed the effectiveness of ²¹²Pb-cetuximab. Notably, concurrent treatment of tumor-bearing mice with ²¹²Pb-labeled cetuximab and trastuzumab provided therapeutic benefit that was greater than either antibody alone. In conclusion, cetuximab proved to be an effective vehicle for targeting HER1-expressing tumors with α-radiation for the treatment of disseminated intraperitoneal disease. These studies provide further evidence that the multimodality therapy regimens may have greater efficacy and benefit in the treatment of cancer patients.     

A protein in rat prostatic interacting with androgen regulated gene

2M NaCl-insoluble fraction of rat ventral prostatechromatin(residual proteins)contain proteins able tointeract specifically with androgen-receptor complex andis,therefore,a part of the acceptor complex.Amongresidual proteins,a 97 KDa protein has been found whichbinds signifieantly to a genomic fragment containingan androgen-regulated gene coding for a 22 KDa protein.The biological significance of this binding in androgenaction need to be further studied. A mini-plasmid clone containing 22 KDa proteincoding sequence was cloned into Charon 4A genomiclibrary from which a 5.7 Kb genomic fragment wasisolated,identified by hybridization with a 5' and a 3'cDNA probes,and shown to contain the 5' flankingsequence.Restriction enzyme treatment of this fragmentyielded a 4.7 Kb restriction fragment representingthe 5' upstream region and a 1.0 Kb containing part ofthe coding sequence.Deletion studies indicated that the97 KDa protein bound only to a subclone of about 300 bpsegment.Furthermore,gel shifting experiment supportedits DNA-prptein binding.     

An Optimized Proteomics Approach Reveals Novel Alternative Proteins in Mouse Liver Development

Alternative ORFs (AltORFs) are unannotated sequences in genome that encode novel peptides or proteins named alternative proteins (AltProts). Although ribosome profiling and bioinformatics predict a large number of AltProts, mass spectrometry as the only direct way of identification is hampered by the short lengths and relative low abundance of AltProts. There is an urgent need for improvement of mass spectrometry methodologies for AltProt identification. Here, we report an approach based on size-exclusion chromatography for simultaneous enrichment and fractionation of AltProts from complex proteome. This method greatly simplifies the variance of AltProts discovery by enriching small proteins smaller than 40 kDa. In a systematic comparison between 10 methods, the approach we reported enabled the discovery of more AltProts with overall higher intensities, with less cost of time and effort compared to other workflows. We applied this approach to identify 89 novel AltProts from mouse liver, 39 of which were differentially expressed between embryonic and adult mice. During embryonic development, the upregulated AltProts were mainly involved in biological pathways on RNA splicing and processing, whereas the AltProts involved in metabolisms were more active in adult livers. Our study not only provides an effective approach for identifying AltProts but also novel AltProts that are potentially important in developmental biology.