Henoch-Schönlein purpura under the age of 2 years is characterized clinically by oedema and a purpuric skin rash which frequently affects the face. Involvement of the joints, kidneys and gastro-intestinal tract is uncommon and the prognosis is excellent. The clinical spectrum in this age group is a continuation with that of Henoch-Schönlein purpura in older children suggesting a nosological entity.

Myofibroblasts are resident cells of wound healing, contractures and fibroses; these tissues are often referred to as fibroproliferative. Whether myofibroblasts themselves proliferate is of interest. Since many in vitro cultures are heterogeneous, staining in situ is required to identify the myofibroblast. We have tested a newly available fluorescent staining kit using ethynyl deoxyuridine (EdU) and click chemistry to identify EdU incorporation into the replicated DNA of proliferative cells. The proliferation stain was combined with the definitive myofibroblast immunostain for alpha smooth muscle actin (α-sma). Fibroblasts were grown on coverslips and within attached collagen lattices. Cultures were pulsed with EdU 4 h prior to fixation. Different standard methods of fixation and permeabilization were used to test the effects of these variables on EdU and α-sma labeling. Images of the stained samples were quantified as the total percentage of proliferative cells, as well as the proportion of fibroblasts and myofibroblasts that were proliferating. Proliferative myofibroblasts were identified in both culture conditions and with all preparation methods tested. Proliferation within the fibroblast population was greater than within the myofibroblast population in both culture conditions. Fixation and permeabilization had little effect on EdU or α-sma labeling. This method of identifying proliferative myofibroblasts will be useful in future studies of myofibroblast proliferation within heterogeneous populations.

Proteolytic enzymes play a significant role in malignancy including, loss of growth regulation, invasiveness and metastases formation. Alpha-1 antitrypsin (A1AT) is a secretory glycoprotein produced mainly in liver and monocytes. It is the most abundant serine protease inhibitor in human plasma. Deficiency of A1AT is an inherited disorder characterized by reduced serum level of A1AT. Protease inhibitor Z (PiZ) and protease inhibitor S (PiS) are the most common deficient genotypes of A1AT. The association of deficient A1AT subtypes with several tumors such as primary liver carcinoma, lung cancer, bladder cancer and malignant hepatoma was reported. This study was aimed to test the relationship between A1AT genotypes Z and S and breast cancer in Jordanian female patients. Blood samples were collected from 111 patients. DNA was isolated and polymerase chain reaction (PCR) was performed to amplify the regions contain the Z and S mutations in exon V, and III, respectively. Genotyping of Z and S alleles was performed by restriction fragment length polymorphism technique using Taq1 restriction enzyme. Our results demonstrated that 100% of the breast cancer patients were homozygous for the normal allele Protease inhibitor MM (PiMM) and no PiZ and PiS genotypes were found. In conclusion, there is no relationship between A1AT deficient genotypes Z and S and breast cancer in Jordanian female patients.