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Connect Tissue Res. 1998;39(1-3):207-14; discussion 221-5.
Mechanisms of mineralization in the enameloid of elasmobranchs and teleosts.

Sasagawa I.

Department of Anatomy, School of Dentistry at Niigata, The Nippon Dental University, Japan.

Ultrastructural and cytochemical studies on the mineralization of enameloid were performed using Heterodontus japonicus, an elasmobranch, and Tilapia buttikoferi, a teleost as materials. The mineralization of the enameloid in the Heterodontus was divided into the following two steps: (1) initial crystallization in the tubular vesicles that originated from the odontoblasts, and (2) crystal growth that was accompanied by the degeneration and removal of the organic matrix around the crystals. In the Tilapia, the mineralization of the cap enameloid followed three steps: (1) initial crystallization at the matrix vesicles, (2) aggregation of fine slender crystals along collagen fibrils, and (3) crystal growth with the degeneration and removal of the organic matrix. The pattern of early mineralization and the composition of organic matrix in enameloid were considerably different between the two species examined, while in both species the odontoblasts were mainly involved in the formation of the organic matrix of enameloid and in the initial mineralization. In the next step, remarkable crystal growth associated with the degeneration and removal of the organic matrix occurred in both the elasmobranch and the teleost species. The absorptive functions of the dental epithelial cells in the later stages of enameloid formation is probably similar in the two types of enameloid, and is essential for the production of well-mineralized enameloid.


online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=11063001&dopt=Abstract



Photodermatol Photoimmunol Photomed. 2000 Oct;16(5):224-8.
Collagen loss in photoaged human skin is overestimated by histochemistry.

Kligman LH, Schwartz E, Sapadin AN, Kligman AM.

Department of Dermatology, University of Pennsylvania School of Medicine, Philadelphia, PA 19104, USA.

It is well known that photoaged skin is characterized by increases in dermal matrix components that include glycosaminoglycans, proteoglycans and masses of abnormal elastic fibers accompanied by substantial collagen loss. Histochemical staining of such tissue gives the impression of "massive" loss of collagen and its replacement by these other matrix components. Early biochemical studies have lent support to this notion with a reported decrease in total collagen of approximately 45% compared to protected skin. More recent studies report considerably less, but varying, amounts of collagen loss. Rarely have the two approaches, histochemistry and biochemical analysis, been used in the same study to examine the same tissue. In this study, collagen loss was quantified biochemically in paired biopsies from sun-protected and sun-exposed arm skin of moderately photoaged female subjects (age 51-77 years). The values obtained were compared with histochemical and immunochemical findings. Quantitatively, collagen loss on a per mg protein basis was small compared to the histochemical appearance.


online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=11068862&dopt=Abstract



Osteoarthritis Cartilage. 2000 Nov;8(6):426-33.
A technique for 3D in vivo quantification of proton density and magnetization transfer coefficients of knee joint cartilage.

Hohe J, Faber S, Stammberger T, Reiser M, Englmeier KH, Eckstein F.

Musculoskeletal Research Group, Institute of Anatomy, Ludwig-Maximilians Universitat Munchen, Pettenkoferstr. 11, D-80336 Munchen, Germany. jan_hohriteme.com

OBJECTIVE: To develop an MR-based method for the in vivo evaluation of the structural composition of articular cartilage. DESIGN: Five sagittal magnetic resonance imaging (MRI) protocols were acquired throughout the knee joint of 15 healthy volunteers and the boundaries of the cartilage segmented from a previously validated sequence with high contrast between cartilage and surrounding tissue. The other sequences were matched to these data, using a 3D least-squares fit algorithm to exclude motion artefacts. In this way secondary images were computed that included information about the proton density (interstitial water content) and the magnetization transfer coefficient (macromolecules, collagen). The average signal intensities of the 3D cartilage plates were extracted from these data sets and related to a phantom. RESULTS: The signal intensity data showed a high interindividual variability for the proton density (patella 31%, lateral tibia 36%, medial tibia 29%); the patella displaying higher values than the tibia (P< 0.001). There were high correlations between the three plates. The magnetization transfer coefficient also showed high variability (patella 25%, lateral tibia 32%, medial tibia 30%) with the lowest values in the medial tibia (P< 0.01) and lower correlations between the plates. The slice-to-slice variation (medial to lateral) ranged from 9% to 24%. CONCLUSION: An MR-based method has been developed for evaluating the proton density and magnetization transfer of articular cartilage in vivo and observing systematic differences between knee joint cartilage plates. The technique has the potential to supply information about the water content and collagen of articular cartilage, in particular at the early state of osteoarthritic degeneration. 2000 OsteoArthritis Research Society International.


online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=11069727&dopt=Abstract



Connect Tissue Res. 1998;39(4):281-94.
Type V collagen in experimental granulation tissue.

Inkinen K, Wolff H, Von Boguslawski K, Ahonen J.

Fourth Department of Surgery, Helsinki University Central Hospital, Finland.

To evaluate the spatial and temporal expression of type V collagen in a wound healing model, subcutaneously implanted viscose cellulose sponges in rats were used to induce granulation tissue formation. Analyses on granulation tissue were carried out on days 3, 5, 8, 14, 21, 30, 59 and 84. Acid soluble collagens were extracted and the relative amount of type V collagen was quantified by SDS-PAGE. Specific antibodies to type I, III and V collagens were used in immunohistochemistry and specific RNA probes to proalpha1(I), proalpha1(III) and proalpha1(V) collagen in in situ hybridization. Type V collagen content increased relative to type I and III collagens up to day 8 and remained at the same level for up to the three months. Type V collagen was expressed strongly in blood vessel walls as seen in immunohistochemistry. In situ hybridization showed that all of the three types of collagen were expressed mostly in fibroblast-like cells and also in rounded cells, especially type V collagen. In conclusion, type V collagen was seen in the wound healing model in increasing amounts from day 3 onwards, its localization being highly associated with blood vessels in granulation tissue and it was synthesized by fibroblast-like and rounded cells.


online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=11063008&dopt=Abstract



Dev Biol. 2002 Nov 15;251(2):409-23.
A role for retinoic acid in regulating the regeneration of deer antlers.

Allen SP, Maden M, Price JS.

Department of Veterinary Basic Sciences, The Royal Veterinary College, London, United Kingdom, NW1 OTU.

Deer antlers are the only mammalian organs that can be repeatedly regenerated; each year, these complex structures are shed and then regrow to be used for display and fighting. To date, the molecular mechanisms controlling antler regeneration are not well understood. Vitamin A and its derivatives, retinoic acids, play important roles in embryonic skeletal development. Here, we provide several lines of evidence consistent with retinoids playing a functional role in controlling cellular differentiation during bone formation in the regenerating antler. Three receptors (alpha, beta, gamma) for both the retinoic acid receptor (RAR) and retinoid X receptor (RXR) families show distinct patterns of expression in the growing antler tip, the site of endochondral ossification. RAR alpha and RXR beta are expressed in skin ("velvet") and the underlying perichondrium. In cartilage, which is vascularised, RXR beta is specifically expressed in chondrocytes, which express type II collagen, and RAR alpha in perivascular cells, which also express type I collagen, a marker of the osteoblast phenotype. High-performance liquid chromatography analysis shows significant amounts of Vitamin A (retinol) in antler tissues at all stages of differentiation. The metabolites all-trans-RA and 4-oxo-RA are found in skin, perichondrium, cartilage, bone, and periosteum. The RXR ligand, 9-cis-RA, is found in perichondrium, mineralised cartilage, and bone. To further define sites of RA synthesis in antler, we immunolocalised retinaldehyde dehydrogenase type 2 (RALDH-2), a major retinoic acid-generating enzyme. RALDH-2 is expressed in the skin and perichondrium and in perivascular cells in cartilage, although chondroprogenitors and chondrocytes express very low levels. At sites of bone formation, differentiated osteoblasts which express the bone-specific protein osteocalcin express high levels of RALDH2. The effect of RA on antler cell differentiation was studied in vitro; all-trans-RA inhibits expression of the chondrocyte phenotype, an effect that is blocked by addition of the RAR antagonist Ro41-5253. In monolayer cultures of mesenchymal progenitor cells, all-trans-RA increases the expression of alkaline phosphatase, a marker of the osteoblastic phenotype. In summary, this study has shown that antler tissues contain endogenous retinoids, including 9-cis RA, and the enzyme RALDH2 that generates RA. Sites of RA synthesis in antler correspond closely with the localisation of cells which express receptors for these ligands and which respond to the effects of RA.


online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=12435367&dopt=Abstract







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