Disease relevance of Dbil5

• The genomic sequence of the functional ELP gene as well as that of a pseudogene were analysed from independent bacteriophage clones of a 129sv mouse genomic library [1].
• To test this hypothesis, we synthesized a thermally responsive ELP with a T1 of 41 degrees C and a thermally unresponsive control ELP in Escherichia coli using recombinant DNA techniques [2].

High impact information on Dbil5

• The endocytotic uptake of a thermally responsive ELP was also observed to be significantly enhanced by the thermally triggered phase transition of the polypeptide in cell culture for three different tumor cell lines [3].
• In addition, the in vivo stability of the (14)C-labeled ELP in plasma was determined along with its plasma pharmacokinetics [4].
• We chose a thermally responsive elastin-like polypeptide (ELP) as a model polypeptide for this study because of its utility in various biotechnology applications such as drug delivery and tissue engineering [4].
• Furthermore, an optimal concentration of isopropyl-beta-d-thiogalactopyranoside was determined for induction of ELP expression to achieve high yield (mg/L culture) of the ELP [4].
• We synthesized two thermally responsive polymers that were designed to exhibit a lower critical solution temperature (LCST) transition slightly above physiological temperature: (1) a genetically engineered elastin-like polypeptide (ELP) and (2) a copolymer of N-isopropylacrylamide (NIPAAm) and acrylamide (AAm) [5].

Biological context of Dbil5

• Structure and expression of the mouse gene encoding the endozepine-like peptide from haploid male germ cells [1].
• The ELP gene and its product thus offer an ideal system with which to investigate the differentiation of late haploid stages of spermatogenesis [1].
• We conclude that ELP is an intracytoplasmic peptide exclusively expressed in post-meiotic spermatozoa and which may be involved in the energy metabolism of the mature sperm [6].
• Unlike the ACBP gene, which comprises four exons, the ELP gene has only a single intron within the region of the 5' untranslated region, suggesting that, like some other haploid expressed genes, the ELP gene might have evolved by retroposon-mediated gene duplication [1].

Anatomical context of Dbil5

• ELP mRNA was found exclusively in the late spermatid stages of spermatogenesis in the testes of sexually mature mice and in no other tissue or cell type examined [6].
• These antibodies identified the predicted endogenous ELP in extracts of mouse testis and epididymis and in no other tissue [6].
• Immunohistochemical analysis using an ELP-specific antibody showed that expression was very restricted within the testis to the postmeiotic germ cells, and in the ovary to interstitial/luteal cells, cell-types known to express GCNF and SF-1, respectively [1].

Associations of Dbil5 with chemical compounds

• The amidolytic and fibrinolytic activities of extracts were measured using Suc-Ala-Tyr-Leu-Val-pNA for elastase-like protease (ELP) and Suc-Tyr-Leu-Phe-pNA (or Suc-Ile-Pro-Phe-pNA) for chymotrypsin-like protease (CLP) [7].

Analytical, diagnostic and therapeutic context of Dbil5

• Immunohistochemistry confirmed that the ELP antigen was present only in late spermatids and spermatozoa, particularly within the cytoplasmic droplet which is retained by the mature spermatozoa during their transit into the epididymis [6].
• A cDNA clone encoding a novel endozepine-like peptide (ELP) was isolated from mouse testes, sequenced, and its mRNA expression characterized by northern and in situ hybridization [6].
• We observed aggregates of the thermally responsive ELP by fluorescence videomicroscopy within the heated tumor microvasculature but not in control experiments, which demonstrates that the phase transition of the thermally responsive ELP carrier can be engineered to occur in vivo at a specified temperature [2].
• As an example of the utility of this method, the in vitro stability of (14)C-labeled ELP in PBS and mouse serum was conveniently quantified by SDS-PAGE and autoradiography [4].

References