Cardiovascular Risk and Statin Eligibility of Young Adults After an MI: Partners YOUNG-MI Registry.

Background: Despite significant progress in primary prevention, the rate of MI has not declined in young adults.

Objectives: The purpose of this study was to evaluate statin eligibility based on the 2013 American College of Cardiology/American Heart Association guidelines for treatment of blood cholesterol and 2016 U.S.

[Incidence and risk factors of endoleak in endovascular aortic aneurysm repair].

Background: endovascular aneurysm repair (EVAR) reduces morbidity and hospital stay compaired with open surgical repair. Endoleak is a common complication of the procedure. The resulting increase of pressure within the sac may expand the aneurysm with the following risk of rupture.

Hydroxylation of recombinant human collagen type I alpha 1 in transgenic maize co-expressed with a recombinant human prolyl 4-hydroxylase.

Background: Collagens require the hydroxylation of proline (Pro) residues in their triple-helical domain repeating sequence Xaa-Pro-Gly to function properly as a main structural component of the extracellular matrix in animals at physiologically relevant conditions. The regioselective proline hydroxylation is catalyzed by a specific prolyl 4-hydroxylase (P4H) as a posttranslational processing step.

Results: A recombinant human collagen type I α-1 (rCIα1) with high percentage of hydroxylated prolines (Hyp) was produced in transgenic maize seeds when co-expressed with both the α- and β- subunits of a recombinant human P4H (rP4H).

Laparoscopic transperitoneal and retroperitoneal nephrectomies in children: a change of practice.

Introduction: Laparoscopic nephrectomies (LNs) may be performed in children with benign renal disease by the transperitoneal (TP) or retroperitoneal (RP) approach.

Objectives: The aim of this study was to present our early results from using both the laparoscopic transperitoneal and retroperitoneal approach, highlighting the change in the approach to a better, simpler procedure performed by experienced surgeons.

Materials And Methods: Between February 2002 and June 2006, 30 LNs were performed, with the first 10 patients by TP (group 1) and the remaining patients by RP (group 2).

Production of a recombinant full-length collagen type I alpha-1 and of a 45-kDa collagen type I alpha-1 fragment in barley seeds.

Recombinant DNA technology can be used to design and express collagen and gelatin-related proteins with predetermined composition and structure. Barley seed was chosen as a production host for a recombinant full-length collagen type I alpha1 (rCIa1) and a related 45-kDa rCIa1 fragment. The transgenic barley seeds were shown to accumulate both the rCIa1 and the 45-kDa rCIa1 fragment.

Purification and characterization of a transgenic corn grain-derived recombinant collagen type I alpha 1.

Corn offers advantages as a transgenic host for producing recombinant proteins required at large volumes (1,000's of tons per year) and low cost (less than US$50/kg) by generating them as co-products of biorefining. We describe the purification and characterization of a corn grain-derived mammalian structural protein having such market characteristics: a full length recombinant collagen type I alpha 1 (rCI alpha 1) chain. Material properties of interest are gelation behavior, which would depend on as yet unverified ability of corn to carry out post-translational prolyl hydroxylation and formation of triple helical conformation.

Purification and characterization of a 44-kDa recombinant collagen I alpha 1 fragment from corn grain.

This paper demonstrates that a fibrous, repetitive amino acid sequence collagen-related protein, a 44-kDa fragment of human collagen I alpha 1 (CIalpha1), was expressed in corn grain molecularly equivalent to that produced in recombinant yeast. The recombinant CIalpha1 was extracted and purified from early generation plants having low levels of recombinant protein accumulation. It was selectively extracted at low pH and purified by ion exchange and gel filtration chromatography, resulting in a 44-kDa CIalpha1 with >70% purity and 60% recovery.

Recombinant microbial systems for the production of human collagen and gelatin.

The use of genetically engineered microorganisms is a cost-effective, scalable technology for the production of recombinant human collagen (rhC) and recombinant gelatin (rG). This review will discuss the use of yeast (Pichia pastoris, Saccharomyces cerevisiae, Hansenula polymorpha) and of bacteria (Escherichia coli, Bacillus brevis) genetically engineered for the production of rhC and rG. P.

Cutaneous tuberculosis diagnosis in an inhospitable Amazonian region by means of telemedicine and molecular biology.

We report on a 13-year-old boy who displayed a chronic granulomatous inflammatory reaction of 5 years duration. The lesion was resistant to different antibiotic schemes; his routine laboratory tests and chest radiographs were normal. Teledermatologic consultation and histopathologic study of skin biopsy suggested scrofulodermal tuberculosis.

The application of recombinant human collagen in tissue engineering.

Collagen is the main structural protein in vertebrates. It plays an essential role in providing a scaffold for cellular support and thereby affecting cell attachment, migration, proliferation, differentiation, and survival. As such, it also plays an important role in numerous approaches to the engineering of human tissues for medical applications related to tissue, bone, and skin repair and reconstruction.

Recombinant collagen and gelatin for drug delivery.

The tools of recombinant protein expression are now being used to provide recombinant sources of both collagen and gelatin. The primary focus of this review is to discuss alternatives to bovine collagen for biomedical applications. Several recombinant systems have been developed for production of human sequence collagens.

Biotransformations of the cardiovascular drugs mexrenone and canrenone.

Microbial transformation studies of the cardiovascular drugs mexrenone (1) and canrenone (2) were conducted. Thirty-nine biotransformations of mexrenone and 84 biotransformations of canrenone were analyzed. Metabolism of the substrate was observed in the majority of these cases.