Loss of polyadenylation protein tauCstF-64 causes spermatogenic defects and male infertility.

Polyadenylation, the process of eukaryotic mRNA 3' end formation, is essential for gene expression and cell viability. Polyadenylation of male germ cell mRNAs is unusual, exhibiting increased alternative polyadenylation, decreased AAUAAA polyadenylation signal use, and reduced downstream sequence element dependence. CstF-64, the RNA-binding component of the cleavage stimulation factor (CstF), interacts with pre-mRNAs at sequences downstream of the cleavage site.

Horizontal and vertical integration of academic disciplines in the medical school curriculum.

A rapid expansion of new scientific information and the introduction of new technology in operative and diagnostic medicine has marked the last several decades. Medical educators, because of and parallel to these developments, initiated a search for a more effective system of presenting core material to medical students. The new educational trends, although varying somewhat from one institution to another, concentrated on the following pedagogical shifts: 1) expansion of conceptual presentation of material at the expense of detail-oriented education; 2) amplification of an integrated approach, as opposed to subject-oriented instruction; 3) scheduling of elective courses to compliment required courses in the curriculum; and 4) institution of small group instruction (i.

Cubilin, a binding partner for galectin-3 in the murine utero-placental complex.

Galectin-3 is a lectin important in animal development and regulatory processes and is found selectively localized at the implantation site of the mouse embryo. To better understand the role of galectin-3 at the maternal-fetal interface, a binding partner was isolated and characterized. Homogenates of uteroplacental tissue were incubated with immobilized recombinant galectin-3, and specifically bound proteins were eluted using lactose.

Spatio-temporal pattern for expression of galectin-3 in the murine utero-placental complex: evidence for differential regulation.

In mice, immunoreactive galectin-3 protein has previously been localized in uterine epithelial cells adjacent to implanting blastocysts as well as in the decidualized endometrium of implantation sites, uterine natural killer cells, and several types of placental trophoblast cells. Because galectin-3 is a soluble extracellular molecule, protein localization by immunohistochemical methods does not demonstrate its cellular origin. Therefore, the present study was undertaken to determine precisely which cell types in the utero-placental complex express galectin-3 mRNA.

Differential expression of two beta-galactoside-binding lectins in the reproductive tracts of pregnant mice.

Two beta-galactoside-binding proteins were isolated from uteroplacental complexes of pregnant mice and identified as the S-Lac lectins galectin-1 and galectin-3. The spatiotemporal pattern of appearance of those proteins was determined by immunocytochemistry. Galectin-1 was present in all tissue compartments of the uterus except the luminal and glandular epithelium.