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Type VII collagen, the major component of anchoring fibrils, consists of a central collagenous triple-helical domain flanked by two noncollagenous, globular domains, NC1 and NC2. Approximately 50% of the molecular mass of the molecule is consumed by the NC1 domain. We previously demonstrated that NC1 binds to various extracellular matrix components including a complex of laminin 5 and laminin 6 (Chen et al, 1997a). In squalane cleanser , we examined the interaction of NC1 with laminin 5 (a component of anchoring filaments). Both authentic and purified recombinant NC1 bound to human and rat laminin 5 as measured by enzyme-linked immunosorbant assay and by binding of 125I-radiolabeled NC1 to laminin 5-coated wells, but not to laminin 1 or albumin. NC1 bound predominantly to the beta3 chain of laminin 5, but also to the gamma2 chain when examined by a protein overlay assay.

The binding of 125I-NC1 to laminin 5 was inhibited by a 50-fold excess of unlabeled NC1 or de-glycosylated NC1, as well as a polyclonal antibody to laminin 5 or a monoclonal antibody to the beta3 chain. In contrast, the NC1-laminin 5 interaction was not affected by a monoclonal antibody to the alpha3 chain. Using NC1 deletion mutant recombinant proteins, a 285 AA (residues 760-1045) subdomain of NC1 was identified as the binding site for laminin 5. IgG from an epidermolysis bullosa acquisita serum containing autoantibodies to epitopes within NC1 that colocalized with the laminin 5 binding site inhibited the binding of NC1 to laminin 5. Thus, perturbation of the NC1-laminin 5 interaction may contribute to the pathogenesis of epidermolysis bullosa [Age-related changes in the intercellular substance of human hyalin and Dedukh NV, Malyshkina SV, Kern M, Pankov EIa.The articular cartilage of the hip joint and the intervertebral disks (LIV and LV), obtained from 42 corpses without any signs of pathology in these tissues, have been investigated. Six age groups have been distinguished: 21-30, 31-40, 41-50, 51-60, 61-70, 71 years of age and older.

After the topo-optic reactions have been get, double refraction of glycosamineglycans (GAG) and collagen is studied in the structure and orientational regularity is estimated in these macromolecules in the matrix. The peculiarities on distribution of the collagenous fiber fasciculi in the intercellular substance in the hyalin and collagen-fibrillar cartilaginous tissue are demonstrated at the areas and depending on the age. Correlations in qualitative and quantitative changes of the GAG and collagen with age are analysed; this gives certain possibilities to reveal signs of similarity and difference in morphogenesis of hyalin and collagen-fibrillar cartilage tissue. Basing on the comparative analysis performed concerning the GAG and collagen state in the age aspect, as well as taking into account the data of previously performed investigations, the collagenous carcass can be characterized as the most stable component of the intercellular substance of cartilages, possessing a great reserve of strength. Homokinesis of the cartilaginous tissue is performed at the expense of the GAG; this ensures a high ability of the cartilaginous tissue to adaptation. A hypothesis on the GAG role in realization of adaptive rearrangements of the cartilaginous matrix at the macromolecular level is put forward.Collagen metabolism in obesity: the effect of weight loss.

OBJECTIVE: To investigate the impact of obesity, fat distribution and weight loss on collagen turnover using serum concentrations of the carboxyterminal propeptide of type I procollagen (S-PICP) and the aminoterminal propeptide of type III pro-collagen (S-PIIINP) as markers for collagen turnover.DESIGN: Blood samples were obtained once at baseline, and after 8 and 16 weeks of dietary treatment (5 MJ/day diet).SETTING: Outpatient clinic of Hvidovre University Hospital.MAIN OUTCOME MEASURES: S-PICP, S-PIIINP, fat distribution and weight loss.RESULTS: S-PIIINP was associated with body weight (r = 07; P = 004), height (r = 07; P = 04), waist circumference (r = 05; P = 007), as well as with WHR (r = 03; P = 01) and was inversely correlated to age (r = -00; P = 002). Compared with randomly selected controls from a large pool of healthy volunteers, the obese patients had elevated S-PIIINP values before as well as during weight loss, whereas S-PICP levels were within the normal range and did not correlate with any anthropometric measures. The average weight loss after 16 weeks dietary treatment was 8 kg (s.

d. = 0). S-PIIINP decreased during the 16 weeks of energy restriction (P < 05) and changes in S-PIIINP was correlated to body weight loss (r = 02; P < 05) and to changes in waist circumference (r = 04; P < 05) as well as changes in WHR (r = 00; P < 05).CONCLUSION: S-PIIINP is elevated in obesity and associated with body fat distribution, suggesting an increased turnover of type III collagen related to obesity in general and to abdominal obesity in particular. squalane -PIIINP levels decreases during weight loss in obese subjects, whereas S-PICP levels seems un-related to obesity and weight loss.The time course of the change in antibody titres in herpes gestationis.The time course of the change in antibody titres was examined postpartum after treatment in two patients with herpes gestationis.