Trends and determinants of IUD use in the USA, 2002-2012.

Study Question: What factors and subgroups have propelled the recent increase in intrauterine device (IUD) use in the USA?

Summary Answer: The increase in IUD use, from 1.8 to 9.5% in the USA between 2002 and 2012, was driven primarily by a marked uptake among parous women who intended to have more children.

Structure of the calcium-rich signature domain of human thrombospondin-2.

Thrombospondins (THBSs) are secreted glycoproteins that have key roles in interactions between cells and the extracellular matrix. Here, we describe the 2.6-A-resolution crystal structure of the glycosylated signature domain of human THBS2, which includes three epidermal growth factor-like modules, 13 aspartate-rich repeats and a lectin-like module.

A polymorphism in thrombospondin-1 associated with familial premature coronary artery disease alters Ca2+ binding.

A single nucleotide polymorphism that results in substitution at residue 700 of a serine (Ser-700) for an asparagine (Asn-700) in thrombospondin-1 is associated with familial premature coronary artery disease. The polymorphism is located in the first of 13 Ca2+ -binding motifs, within a consensus sequence in which Asn-700 likely coordinates Ca2+. Equilibrium dialysis of constructs comprised of the adjoining epidermal growth factor-like module and the Ca2+ -binding region (E3Ca) demonstrated that E3Ca Ser-700 binds significantly less Ca2+ than E3Ca Asn-700 at low [Ca2+].

Extracellular matrix molecules regulate endothelial cell migration stimulated by lysophosphatidic acid.

Background: Lysophosphatidic acid (LPA) and sphingosine 1-phosphate (S1P) are lipids that bind G-protein coupled receptors and differentially promote transmigration of endothelial cells.

Objective: To determine if endothelial cell transmigration stimulated by LPA, not S1P, is dependent on the extracellular matrix.

Methods: Bovine pulmonary artery (BPAE) endothelial cell transmigration and locomotion were measured using a modified-Boyden chamber and video microscopy, respectively.

Interactions among the three structural motifs of the C-terminal region of human thrombospondin-2.

The C-terminal regions of thrombospondins (TSPs) contain three elements, EGF-like modules (E), a series of Ca(2+)-binding repeats (Ca), and a C-terminal sequence (G). We have looked for interactions among these elements in four recombinant proteins based on human TSP-2: E3CaG-2, CaG-2, E3Ca-2, and Ca-2. When bound Ca(2+) was assayed by atomic absorption spectroscopy or an equilibrium dialysis protocol in which Ca(2+) was removed from the proteins prior to equilibrium dialysis, E3CaG-2 bound 22-27 Ca(2+), CaG-2 bound 17-20 Ca(2+), and E3Ca-2 and Ca-2 bound 14-20 Ca(2+).

A polymorphism in thrombospondin-1 associated with familial premature coronary heart disease causes a local change in conformation of the Ca2+-binding repeats.

A single nucleotide polymorphism that substitutes a serine for an asparagine at residue 700 in the Ca2+-binding repeats of thrombospondin-1 is associated with familial premature coronary heart disease. We expressed the Ca2+-binding repeats alone (Ca) or with the third epidermal growth factor-like module (E3Ca), without (Asn-700) or with (Ser-700) the disease-associated polymorphism. The intrinsic fluorescence of a single tryptophan (Trp-698) adjacent to the polymorphic residue was quenched cooperatively by adding Ca2+.

Effects on mood of a life-styles program for the rehabilitation of injured workers.

This study reports an examination into the effects on daily mood of participation in a life-styles program by injured workers. In the current prospective study, 14 participants completed the Memorial University Mood Scale (MUMS) prior to starting the program, at 1 month, 2 months, and at 3 months. They also completed the Memorial University Scale of Happiness (MUNSH) prior to entry and after three months.