Age-related changes of anti-elastin antibodies in senescence-accelerated mice.

Background: Antibodies recognizing the elastin precursor tropoelastin (ATEAb) or degradation products alpha-elastin (AEAb) are found in the serum of healthy human subjects, as a part of a homeostatic mechanism which assembles new or clears altered elastin structures. Serum ATEAb (reflecting elastin synthesis) and AEAb (reflecting elastin destruction) appear to correlate with the production and breakdown of the elastic tissue, respectively.

Objective: The aim of this study was to investigate plasma levels of AEAb and ATEAb in senescence-accelerated prone (SAMP8) and senescence-accelerated resistant (SAMR1) mice, compared with imprinting control region (ICR) mice in order to evaluate their age-related changes.

Non-enzymatic glycation of human fibrillin-1.

Non-enzymatic glycation of proteins is one of the key mechanisms in the pathogenesis of diabetic complications and may be significant in the age-related changes of tissues. We isolated and investigated the in vitro glycation of human aortic fibrillin-1. Fibrillin-1 was prepared from thoracic aortas of 9 accident victims distributed in three age groups.

Detection of elastin derived peptides in cerebrospinal fluid of patients with first ever ischaemic stroke.

Objective: We have previously reported the optimized methods for the detection of elastin derived peptides (EDP) in the serum, synovial fluid, and bronchoalveolar lavage. The aim of the present study was to investigate whether EDP are detectable in cerebrospinal fluid (CSF) of patients with acute brain ischaemia.

Patients And Methods: Twenty-seven first ever ischaemic stroke patients (mean age 61.

Age-related changes in the glycation of human aortic elastin.

Non-enzymatic glycation of proteins is a consequence of hyperglycemia in diabetes and correlates with aging. The aim of the study was to investigate age-related changes in the glycation of human aortic elastin in healthy subjects by two approaches: (1) assessment by fluorescence method of formed in vivo advanced glycation end products (AGEs) of elastins, purified from human aortas, obtained from different age groups; (2) in vitro glycation of elastins from different age groups and investigation of their capacity to form early (by colorimetric nitroblue tetrazolium method) and AGEs (fluorescence method). Human insoluble elastins were prepared from macro- and microscopic unaltered regions of thoracic aortas, obtained from 68 accident victims, distributed in 15 age-groups, using the method of Starcher and Galione.

Detection of serum collagen type IV in children with type 1 (insulin-dependent) diabetes mellitus--a longitudinal study.

The basement membrane is a major focus of scientific interest because of its role in a variety of diseases. In diabetes mellitus, a thickening of the capillary basement membrane results in microangiopathic lesions. To monitor the metabolism of the basement membrane protein collagen type IV (CIV) in diabetes mellitus, serum levels of CIV were measured using an enzyme-linked immunosorbent assay (ELISA) method in 28 children with type 1 diabetes mellitus over a period of 6 years.