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J Hand Surg [Br]. 2000 Apr;25(2):183-7.
Hyaluronic acid modulates cell proliferation unequally in intrasynovial and extrasynovial rabbit tendons in vitro.
Wiig M, Abrahamsson SO.
Department of Hand Surgery, Uppsala University Hospital, Malmo, Sweden. monica.wiiand.uas.lul.se
As tendons differ in biochemical composition and cellular capacities, we have compared dose response effects of hyaluronic acid on cell proliferation and synthesis of matrix components in intermediate and proximal segments of intrasynovial deep flexor tendons and extrasynovial peroneus rabbit tendons in vitro. Compared with matched control tendons, hyaluronic acid inhibited cell proliferation in intermediate and proximal intrasynovial flexor tendon segments at the concentrations of 0.1-2.0 mg/ml and 0.5-2.0 mg/ml respectively, but in extrasynovial tendon segments only at the concentration of 0.5 mg/ml. Hyaluronic acid did not affect synthesis of proteoglycan, collagen and non-collagen protein in either type of tendon. These results show that hyaluronic acid modulates cell proliferation unequally in intra- and extrasynovial tendons without affecting the synthesis of matrix components in the two types of tendons, indicating differential hyaluronic acid sensitivity and a possible mechanism of action. 2000 The British Society for Surgery of the Hand.
online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=11062579&dopt=Abstract
J Hand Surg [Br]. 2000 Apr;25(2):175-9.
Histogenesis and morphology of the flexor tendon pulley system in the human embryonic hand.
Sbernardori MC, Fenu G, Pirino A, Fabbriciani C, Montella A.
Department of Orthopaedics, University School of Medicine, Sassari, Italy. tereiscalinet.it
The number, position, structural and ultrastructural features of the flexor tendon pulley system in six human embryonic hands, aged from 6 to 12 weeks, were studied by light and electron microscope. The pulley system can be recognized from the ninth week; later, at 12 weeks, the structures are easily identified around the flexor tendon in positions closely correlated to those found during post-natal growth and in the adult hand. Structurally and ultrastructurally the pulleys are not simply thickened portions of the sheath. They are formed by three layers: an inner layer, one or two cells thick, probably representing a parietal synovial tendon sheath; a middle layer formed by collagen bundles and fibroblasts whose direction is mainly perpendicular to the underlying phalanx; and an outermost layer consisting of mesenchymal tissue with numerous vessels which extends dorsally in an identical layer, forming a ring that includes flexor and extensor tendons and the cartilaginous model of the phalanx. The pulley does not have a semicircular shape but a much more complicated one, owing to the middle layer which in part runs dorsally and in part ventrally, under the flexor tendons. 2000 The British Society for Surgery of the Hand.
online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=11062577&dopt=Abstract
Matrix Biol. 2000 Nov;19(6):511-20.
Stability and networks of hydrogen bonds of the collagen triple helical structure: influence of pH and chaotropic nature of three anions.
Zanaboni G, Rossi A, Onana AM, Tenni R.
Dipartimento di Biochimica 'A. Castellani', Universita di Pavia, via Taramelli 3b, 27100, Pavia, Italy.
The thermal stability of the trimeric species formed by seven type I collagen CNBr peptides was determined at neutral and acidic pH. Melting temperature of peptide trimers and free energy change for monomer to trimer transition were used as indices of trimer stability. A greater stability at neutral pH than at acidic pH was found for all peptides analysed because in most conditions an entropic gain overwhelms an enthalpic cost. Enthalpic reasons are prevailing only in some conditions of the more acidic peptides. The overlap zone of type I collagen fibrils is more basic than the gap zone and is therefore more sensitive to variations of pH from neutral to acidic, e.g. in bone degradation when osteoclasts acidify the lacuna lying between cell and bone. Peptide trimer stability in neutral conditions is influenced also by the chaotropic nature and the concentration of three anions: chloride, sulfate and phosphate. This was more evident for sulfate at the highest concentration used (0.5 M) when a greater stability is caused by entropic reasons. The contribution of hydroxyproline to the stability of peptide trimers is greater at neutral than at acidic pH, particularly at the highest concentration of sulfate. All our data indicate that pH, chaotropic nature and concentration of three anions influence the networks of hydrogen bonds present in the collagen triple helical structure.
online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=11068205&dopt=Abstract
Osteoarthritis Cartilage. 2002 Nov;10(11):879-89.
Human articular chondrocytes immortalized by HPV-16 E6 and E7 genes: Maintenance of differentiated phenotype under defined culture conditions.
Grigolo B, Roseti L, Neri S, Gobbi P, Jensen P, Major EO, Facchini A.
Laboratory of Molecular Medicine and Neuroscience, National Institute of Neurological Disorders and Stroke, NIH, Bethesda, MD, USA.
OBJECTIVE: To establish an immortalized normal human articular chondrocyte line which could be useful for a better understanding of cell molecular mechanisms relevant for the development of new therapeutic approaches in rheumatic diseases. DESIGN: Chondrocytes from human adult articular healthy cartilage were transfected in primary culture with a plasmid containing two human papilloma virus type 16 (HPV-16) early function genes: E6 and E7, using the highly efficient cationic liposome-mediated (lipofection) procedure. The transfection was verified by reverse transcriptase-polymerase chain reaction analysis of E7 mRNA and by immunofluorence localization of the E7 protein in the cell cytoplasm. The established chondrocyte cell line was examined in monolayer and in two culture conditions that were described to re-induce differentiated characteristics: culturing in a serum-free defined medium supplemented with an insulin-containing serum substitute and seeding on a hyaluronan-based non-woven structured biomaterial. The expression of markers characteristic of cartilage was shown in the mRNA by reverse transcriptase-polymerase chain reaction. Immunohistological staining and Western blotting analysis were performed to evaluate type II collagen synthesis. Proteoglycans deposition was detected by Alcian Blue staining. A Field Emission In Lens Scanning Microscopy was used to look at the morphology of the immortalized cells at very high magnification. RESULTS: Normal human articular chondrocytes were efficiently transfected leading to the establishment of an immortalized cell line as confirmed by HPV-16 E7 mRNA and protein detection. These cells were able to re-express type II collagen both at mRNA and protein levels under the two defined cultured conditions we used, still maintaining type I collagen expression. Collagen IX mRNA was present only in early primary culture while collagen type X and aggrecan transcripts were always detected. Alcian Blue staining showed a proteoglycan-rich matrix production. The ultrastructural analysis of the immortalized cells revealed that their morphology strictly resembled that of normal chondrocytes. CONCLUSIONS: The cell line that we obtained may be a useful tool for increasing our knowledge of the genetic and biochemical events involved in the processes of cartilage growth and differentiation. Moreover, it appears to be a suitable model for pharmacological and toxicological studies related to rheumatic diseases relevant to humans.
online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=12435333&dopt=Abstract
Br J Dermatol. 2000 Oct;143(4):821-3.
An extract of cultured A431 cells contains major tissue antigens of autoimmune bullous diseases.
Lee CW.
Department of Dermatology, Hanyang University Hospital, Sungdong-ku, Seoul 133-792, Korea. cwlemail.hanyang.ac.kr
BACKGROUND: Autoantibodies that are characteristic of autoimmune bullous diseases (AIBDs) can be detected by immunoblot assay using epidermal or dermal extracts. However, none of the substrates obtained by ordinary methods seems to contain a sufficient amount of all of the autoantigens involved in AIBDs, and diagnosis may require the use of several different substrates. OBJECTIVES: To examine the potential of A431 cell extracts as a substrate for immunoblotting. METHODS: Fourteen sera obtained from patients with major AIBDs (pemphigus vulgaris, pemphigus foliaceus, paraneoplastic pemphigus, bullous pemphigoid and epidermolysis bullosa acquisita) were tested using this substrate. RESULTS: Bands corresponding to desmoglein 1 and 3, desmoplakin 1 and 2, periplakin, BPAG1, BPAG2 and type VII collagen were identified distinctly with these sera. CONCLUSIONS: This finding suggests that culture extracts of A431 cells provide an effective substrate for the diagnosis and differential diagnosis of major AIBDs.
online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=11069463&dopt=Abstract
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