PubMed · 10499712
The source did not provide an abstract. Follow the original record for more information.
Explore connections, maps & timelines
P Rosen, R D Berlin, G P Poore. Appendagitis masquerading as appendicitis.. https://pubmed.ncbi.nlm.nih.gov/10499712/
Cite the original work for its findings. Save a collection to share your selection of sources.
KEEP EXPLORING
Decellularized tissues provide biological cues owing to the wealth of structural and regulatory factors that promote angiogenesis, adipogenesis, and myogenesis and facilitate neurite outgrowth. Here, we demonstrated the advantages of decellularized adipose tissue (adipoECM) over defined collagen-based biomaterials for host tissue integration. Three batches of human adipose tissue were decellularized using a rapid decellularization protocol and analyzed using mass spectrometry. To assess the biological activity of the decellularized materials, adipoECM and a reference standard of care biomaterial (Integra®DRT, also containing collagen I and glycosaminoglycans) were implanted subcutaneously, but far from the wound bed (in anatomical potential spaces) of immunocompetent BALB/c mice. The mice were euthanized in the acute (1 day) and chronic (day 60) inflammatory reaction phases, followed by biomaterial excision and Masson’s trichrome immunohistofluorescence imaging of the paraffin-embedded specimens. Each batch of processed tissue passed a quality control check, showing a low level of donor genomic DNA, lack of nuclei, lipids, endotoxins, and bacterial contamination. Mass spectrometry revealed that all batches of decellularized tissue mainly contained collagen I and, to a lesser degree, collagen III, collagen IV, collagen V, laminin, fibrillin, fibronectin, tenascin, and elastin. No acute inflammatory reaction was observed in either material one day post-transplantation. At 60 days post-implantation, different cell types were detected in adipoECM specimens, whereas Integra®DRT remained acellular. Additional immunohistochemical staining of adipoECM revealed CD31-positive cells in the blood vessels. Mesenchymal (CD90 positive) and myeloid (CD14 positive) cells were also detected. Primary cell types involved in soft tissue healing and remodeling were found in the adipoECM-treated group. The ingrowth of blood vessels and mesenchymal cells confirmed the effective integration of adipoECM with host tissues. Our results demonstrate that decellularized adipose tissue implanted away from the wound bed possesses contextual biological activities that promote efficient integration with host tissues.
Cellular retinol-binding protein, type I (CRBP-I) and type II (CRBP-II) are the only members of the fatty acid-binding protein (FABP) family that process intracellular retinol. Heart and skeletal muscle take up postprandial retinol but express little or no CRBP-I or CRBP-II. We have identified an intracellular retinol-binding protein in these tissues. The 134-amino acid protein is encoded by a cDNA that is expressed primarily in heart, muscle and adipose tissue. It shares 57 and 56% sequence identity with CRBP-I and CRBP-II, respectively, but less than 40% with other members of the FABP family. In situ hybridization demonstrates that the protein is expressed at least as early as day 10 in developing heart and muscle tissue of the embryonic mouse. Fluorescence titrations of purified recombinant protein with retinol isomers indicates binding to all-trans-, 13-cis-, and 9-cis-retinol, with respective K(d) values of 109, 83, and 130 nm. Retinoic acids (all-trans-, 13-cis-, and 9-cis-), retinals (all-trans-, 13-cis-, and 9-cis-), fatty acids (laurate, myristate, palmitate, oleate, linoleate, arachidonate, and docosahexanoate), or fatty alcohols (palmityl, petrosenlinyl, and ricinolenyl) fail to bind. The distinct tissue expression pattern and binding specificity suggest that we have identified a novel FABP family member, cellular retinol-binding protein, type III.
To bridge the gap between studies demonstrating leptin's role in protecting fat stores when food is scarce and other studies demonstrating the effects of treatment with leptin at doses that increase plasma levels to values found in overfed animals, we investigated whether leptin serves an adipostatic function within the normal range of free-feeding lean animals, i.e. within the very small range of endogenous plasma levels at which no leptin resistance occurs. For this purpose we applied recombinant leptin via mini-osmotic pumps to rats between 15 and 24 days of age and between 25 and 34 days of age and studied its dose-dependent effects on body mass and fat mass at plasma leptin concentrations extending down to the normal levels in lean animals. Using percentage change of fat mass (relative to that of saline-treated littermates) as the measure, a linear dose-response curve was found up to doses of 2 microg g(-1) day(-1), corresponding to plasma leptin concentrations between the normal physiological range and 50 ng ml(-1). In 15- to 24-day-old animals, analysis of the correlation (r = -0.89) between individual plasma concentrations and the corresponding leptin-induced changes of body fat content for a range extending down towards zero (i.e. towards the average fat content of the controls) yielded a zero value of 3.1 ng ml(-1), which was within the 2-4 ng ml(-1) range of plasma leptin concentrations found in the control pups. Likewise, regression analysis for the data from the 25- to 34-day-old pups (r = -0.88), for which the control range was 1-3 ng ml(-1), yielded a zero value of 1.9 ng ml(-1). We conclude that normal plasma leptin levels represent an adipostatic signal. Steady-state levels of plasma leptin in free-feeding lean animals thus provide a signal not only for protecting sufficiency but also for limiting increases of body fat stores.