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At least 379 records · Page 21Linked to original sources
PubMed1998

Tissue factor and tissue factor pathway inhibitor in hemodialysis patients.

Tissue factor and tissue factor pathway inhibitor are important in extrinsic coagulation. We investigated their clinical significance in hemodialysis patients. We took blood samples, prior to initiation of routine hemodialysis, from 73 patients on hemodialysis (35 men and 38 women aged 56.1+/-11.7 years on dialysis for 82.1+/-61.0 months), and determined tissue factor and tissue factor pathway inhibitor levels by ELISA. In the patients the tissue factor level was 704.5+/-141.6 pg/ml and the tissue factor pathway inhibitor level was 44.5+/-23.3 ng/ml; both values were significantly higher than in normal controls (192.7+/-36.6 pg/ml and 18.6+/-5.7 ng/ml, respectively). In patients with shunt obstruction, tissue factor pathway inhibitor levels were significantly higher than in those without it. Therefore, the tissue factor pathway inhibitor level may be a marker of shunt obstruction.

Adult↗
PubMed1987

Tissue distribution of phenoxybenzamine in the rat. Lack of adipose tissue storage.

Rats were given the basic lipophilic drug, phenoxybenzamine, in single i.v. doses of 0.4 and 30 mg/kg. The drug was determined in plasma and 7 tissues by a new HPLC method. Adipose tissue reached peak levels after 30 minutes. At that time levels in heart, kidney, and brain were higher than in subcutaneous, epididymal, and mesenteric adipose tissues. The percentage metabolites in adipose tissue, kidney, and liver was 0, 88, and 96, respectively. Pretreatment with SKF 525-A inhibited metabolism and increased the tissue levels of unchanged drug, however, even under these conditions storage in adipose tissues did not occur, the adipose storage index being still less than unity. These results contradict findings of the 1950s which have been repeatedly reported in textbooks and reviews, but they confirm observations that basic drugs, even when highly lipophilic, are not being stored in adipose tissues.

Adipose Tissue↗
PubMed2004

Acquired disorders of elastic tissue: Part II. decreased elastic tissue.

Elastic fibers in the extracellular matrix are integral components of dermal connective tissue. The resilience and elasticity required for normal structure and function of the skin are attributable to the network of elastic tissue. Advances in our understanding of elastic tissue physiology provide a foundation for studying the pathogenesis of elastic tissue disorders. Many acquired disorders are nevertheless poorly understood owing to the paucity of reported cases. Several acquired disorders in which loss of dermal elastic tissue produces prominent clinical and histopathologic features have recently been described, including middermal elastolysis, papular elastorrhexis, and pseudoxanthoma-like papillary dermal elastolysis, which must be differentiated from more well-known disorders such as anetoderma, acquired cutis laxa, and acrokeratoelastoidosis. Learning objective At the conclusion of this learning activity, participants should have an understanding of the similarities and differences between acquired disorders of elastic tissue that are characterized by a loss of elastic tissue.

Adolescent↗
PubMed2005

Reconstruction of major forehead soft tissue defects with adjacent tissue and minimal scar formation.

Repair and reconstruction of soft tissue defects involving over 50% of the forehead using remaining forehead tissue has not been reported in the literature. The few existing reports mainly concern cases in which less than half of the forehead was involved. The forehead comprises one third of the face and with regard to its prominent position, it is one of the major contributing components to facial beauty. Considering the excellent color, thickness, and quality matching of the adjacent forehead skin, it is considered the ideal substitute for repair of forehead defects. Use of skin graft or free flaps for reconstruction of defects involving 50% or more of the forehead have not reported acceptable results because of the lack of similarity of the donor tissue with the remaining forehead tissue. In this study, we describe successful reconstruction of major forehead soft tissue defects of two thirds to three fourths of the forehead with use of a tissue expander and transverse supratrochlear pedicle flap in four patients who were diagnosed with giant hairy nevus. There were no serious complications such as hematoma, bleeding, infection, or flap necrosis. We recommend this technique for reconstruction of extensive forehead soft tissue defects.

Adolescent↗
PubMed2005

Expression of S100 proteins in normal human tissues and common cancers using tissue microarrays: S100A6, S100A8, S100A9 and S100A11 are all overexpressed in common cancers.

AIMS: To survey the expression of members of the S100 family of calcium-binding proteins in normal human tissues and common cancers using tissue microarrays. S100A6, S100A8, S100A9 and S100A11 have all been suggested to have potential roles in carcinogenesis and tumour progression but their expression has not been described in a wide range of human tissues and tumours. METHODS AND RESULTS: A custom-made tissue array, containing 291 tissue cores representing 28 tissue types and 21 tumour types, was used to produce sections that were immunostained for S100A2, S100A6, S100A8, S100A9, S100A11, calbindin 1, calbindin 2, S100B and parvalbumin. S100A6, S100A8 and S100A9 were expressed in 32%, 12% and 28% of breast cancers, respectively. There was a translocation of S100A11 expression from exclusively nuclear in normal tissues to cytoplasmic and nuclear in all common cancers. CONCLUSIONS: S100A6, S100A8, S100A9 and S100A11 are all expressed in common cancers, especially breast cancer. In addition, S100A11 undergoes a nucleocytoplasmic translocation which may have a direct influence on the proliferation of the cancer cells.

Calbindin 1↗
PubMed2002

Differential expression of matrix metalloproteinase and tissue inhibitor of MMP in serosal tissue of intraperitoneal organs and adhesions.

OBJECTIVE: To comparatively analyse the expression of matrix metalloproteinase (MMP-3) and tissue inhibitor of MMP (TIMP-2) in serosal tissue of intraperitoneal organs and adhesions, as well as peritoneal fluid and serum of subjects with and without adhesions. DESIGN: Cross sectional study. SETTING: Academic research centres. SAMPLE: Patients undergoing abdominal/pelvic surgery. METHODS: Messenger ribonucleic acid (mRNA) and protein expression using quantitative reverse transcription polymerase chain reaction (Q-RT-PCR), ELISA and immunohistochemistry. RESULTS: All the tissues examined express MMP-3 and TIMP-2 mRNA and protein at consistently varying levels ranging from 100- to 1000-fold and 2- to 10-fold mRNA and protein, respectively. Serosa of uterine, fallopian tube, ovary and partial peritoneum express a higher MMP-3 mRNA compared with small and large bowels and omentum, while TIMP-2 expression was less variable with the highest level found in uterine serosa (P < 0.05). The expression of MMP-3 and TIMP-2 mRNA in adhesions was not significantly different compared with parietal peritoneum. MMP-3 and TIMP-2 protein content in tissue extracts, peritoneal fluids and serum also varied with higher TIMP-2 than MMP-3 (P < 0.05). TIMP-2 levels were lower in serum of subjects with moderate/extensive adhesions compared with subjects without adhesions. Immunoreactive MMP-3 and TIMP-2 proteins were detected in various cell types in these tissues. There was no correlation between MMP-3 and TIMP-2 expression, and age, gender or menstrual status of subjects with or without adhesions. CONCLUSION: MMP-3 and TIMP-2 are expressed at varying levels in serosal tissues of peritoneal organs and adhesions, with higher TIMP-2 than MMP-3. Based on the knowledge that tissue injury alters the expression of MMPs and TIMPs, such variations may predispose an organ to develop more adhesions than others. In addition, the results suggest that serum level of TIMP-2 may represent a marker for subjects who will form adhesions with greater severity.

Adult↗
PubMed1996

Collagenases and tissue inhibitors of metalloproteinases: a functional balance in tissue degradation.

BACKGROUND: Members of the family of matrix metalloproteinases (MMPs; also called collagenases or matrixins) are key enzymes in matrix degradation. They function at neutral pH and can digest synergistically all the matrix macromolecules. Biochemical and clonal studies indicate that there are three major groups: the specific collagenases cleave interstitial collagens; the gelatinases degrade types IV, V, VII and XI collagens and act synergistically with collagenases by degrading denatured collagens (gelatins); and the stromelysins have broader specificity and can degrade basement membrane collagens as well as proteoglycans and matrix glycoproteins. Others not in these groups are matrilysin, metalloelastase and a recently cloned membrane-bound metalloproteinase. MMPs are Zn(2+)- and Ca(2+)-requiring endopeptidases and are secreted in a latent proform: activation involves the loss of a propeptide. Naturally occurring inhibitors, TIMPs (Tissue Inhibitors of MetalloProteinases), are important controlling factors in the actions of MMPs, and tissue destruction in disease processes often correlates with an imbalance of MMPs over TIMPs. The major inhibitor is TIMP-1 (or TIMP), a 30-kDa glycoprotein that is synthesised by most cells. A second unglycosylated inhibitor, TIMP-2, which is less abundant, has the interesting property of binding to the proform of gelatinase A and is involved in controlling its activation. BIOLOGICAL AND PSYCHOLOGICAL IMPLICATIONS: The expression of MMPs and TIMPs by cells is regulated by many cytokines (particularly interleukin-1, IL-1), growth factors and hormones, some of which are specific to cell type and others that are ubiquitous (eg transforming growth factor beta, TGF-beta). Many of these factors are products of monocytes/macrophages and their production in inflammatory situations is therefore part of the chain of events leading to tissue degradation. From many recent studies it seems that tissue destruction, both physiological and pathological, is correlated with an imbalance of inhibitors over proteinases. We proposed that one way in which pathogenic organisms might mediate tissue degradation in periodontal diseases is through the ability of cell wall antigens to stimulate cytokine production by circulating mononuclear cells. These would then induce MMP synthesis by resident gingival cells (or by the mononuclear cells themselves), thereby initiating degradative events. We have identified MMPs in human gingival biopsy specimens by using specific polyclonal antibodies and indirect immunofluorescence. Their distributions are extremely variable, both in the connective tissue and the epithelium, but the results indicate that host cell production of MMPs may contribute to tissue degradation in periodontal disease. TIMP could also be found in some situations and could be a limiting factor.

Collagenases↗
PubMed2002

Treatment of gingival recessions by combined periodontal regenerative technique, guided tissue regeneration, and subpedicle connective tissue graft. A comparative clinical study.

BACKGROUND: Many surgical techniques have been shown to be effective in correcting gingival recessions by covering the exposed root with soft tissue; however, the thickness of the gingival tissue over the root surface probably plays an important role in preventing the recurrence of tissue recession. The aim of the present study was to compare the results of a mucogingival bilaminar technique (BT), guided tissue regeneration (GTR), and a combined periodontal regenerative technique (CPRT) in achieving root coverage and increasing the gingival thickness 1 year after surgical treatment. METHODS: In 45 systemically healthy, non-smoking patients aged 33.6 +/- 4.3 years with no periodontal pockets >4 mm, a Miller's Class I or II gingival recession was treated for root coverage: 15 patients underwent BT (connective tissue with partial-thickness double pedicle graft), 15 GTR by a bioabsorbable membrane, and 15 CPRT by a collagen membrane and collagen-incorporated hydroxyapatite. Before and 1 year after surgical treatments, the following clinical parameters were recorded: gingival recession (GR), probing depth (PD), clinical attachment level (CAL), keratinized tissue width (KT), and gingival thickness (GT); the percentage of root coverage was also calculated and the data were statistically analyzed. RESULTS: All 3 techniques yielded significant improvements in terms of GR decrease, CAL and KT gain, and GT increase compared to baseline values. Mean root coverage was 90.0%, 81.01%, and 87.12% in BT, GTR, and CPRT groups, respectively. Complete root coverage was observed in 60%, 40%, and 53.3% of subjects from the BT, GTR, and CPRT groups, respectively. No significant differences were observed among the 3 techniques in GR or CAL improvements; however, BT produced a significantly (P<0.01) greater increase of KT, and BT and CPRT groups showed a significantly (P<0.01) greater increase of GT compared to the GTR group. CONCLUSIONS: BT, GTR, and CPRT successfully treated gingival recession defects, obtaining comparable percentages of root coverage, but BT and CPRT created a thick gingival tissue significantly greater than that achieved with GTR.

Absorbable Implants↗
PubMed1983

Adipose tissue content as a modifier of the tissue distribution, biological effects, and excretion of a hexachlorobiphenyl in C57BL/6J and DBA/JBOMf mice.

C57BL/6J (C57) and DBA/JBOMf (DBA) mice were used to study the role of adipose tissue as a modifier of tissue distribution, biological effects, and elimination of a lipophilic foreign chemical, 2,4,5,2',4',5'-hexachlorobiphenyl (HCB). As an indication of biological potency of the model compound, the activities of hepatic drug-metabolizing enzymes were determined. DBA mice contained twice as much body fat as C57 mice. Since the highly lipophilic HCB was primarily sequestered by the adipose tissue, DBA mice required greater doses of HCB than did C57 mice to reach similar tissue levels of the chemical. Accordingly, greater HCB doses were required by DBA mice for elevation of drug-metabolizing enzyme activities. Phenobarbital elevated enzyme activities in a similar way in both mouse strains. When the dietary intake of DBA mice was restricted, the body fat content decreased from 15% to 5% of body weight during 1 week. In these animals the tissue accumulation of HCB and enzyme induction resembled the situation in C57 mice fed ad libitum. Highest elevations were seen in the activities of 7-ethoxycoumarin-O-deethylase and arylhydrocarbon hydroxylase (EC 1.14.14.2). In addition, the activity of epoxide hydrolase (EC 3.3.2.3) was increased, whereas glutathione S-transferase as well as UDP-glucuronosyltransferase (EC 2.4.1.17) activities remained unchanged. The abundant adipose tissue content played no role in the nonresponsiveness of DBA mice to 3-methylcholanthrene since, in contrast to C57 mice, no changes in enzyme activities were detected in DBA mice deprived of food, even after large doses of 3-methylcholanthrene. The adipose tissue content also affected the rate of elimination of HCB. DBA mice excreted smaller quantities of HCB than did C57 mice after equal doses. When, however, fasted DBA mice received HCB, they excreted it at rates similar to those of C57 mice fed ad libitum. In C57 mice, concomitant to the elevation of monooxygenase activities, there was an increase in the rate of excretion of HCB. No such elevation could be seen after a dose that was too small to elevate enzyme activities.

Adipose Tissue↗
PubMed1980

[Biotension of the corneal tissue preserved in a nutrient medium for tissue cultures at 4 degrees C].

The biotension generated by cells and tissues is connected quite well with the intensity of the metabolic processes in them and in seems that it is affected considerably by a series of external factors-temperature, salt content ect. For the purposes of transplantation in the present investigation the authors examined the effect of the nutritive medium for tissue cultures T-199 on the investigated biotension of the corneal tissue during the period of its preservation. They carried out studies on 335 corneas and the results were estimated statistically. The mean rate of a change on the biotension for the single series of investigation was determined. He found that the measured biotension was affected bu the time and conditions of preservation of the corneal tissue, when he compared the dispersion in the values of the tension after the preservation of the tissue in two media moist chamber and nutritive medium for tissue cultures). The nutritive medium used probably influenced positively the rate of the adaptation processes in the tissues after its separation from the ocular buebus, delayed the processes of deterioration and to a large extent stabilized the measured biotension.

Animals↗
PubMed1984

Pharmacokinetic study on the mechanism of tissue distribution of doxorubicin: interorgan and interspecies variation of tissue-to-plasma partition coefficients in rats, rabbits, and guinea pigs.

The mechanism of interorgan and interspecies variations in the tissue distribution of doxorubicin was studied in rats, rabbits, and guinea pigs. The permeation properties of doxorubicin were investigated by using isolated rat erythrocytes as a model membrane. A significant dependency of the uptake rate constant on medium pH was observed, suggesting that only un-ionized doxorubicin is diffusible through the plasma membrane. The values of plasma unbound fraction (fp) of doxorubicin were 0.344 for rats, 0.415 for rabbits, and 0.529 for guinea pigs. The tissue DNA concentrations of rats were larger than those of rabbits and smaller than those of guinea pigs in corresponding organs or tissues. An in vitro organ model that described the distribution behavior of doxorubicin in the whole body was constructed, and an equation was derived to estimate the tissue-to-plasma partition coefficients, (Kp) from in vitro experiments. The in vitro Kp values showed comparatively good agreement with the in vivo Kp values for the various organs or tissues in all three species. Doxorubicin is exclusively bound to the nuclei in the cells. The variation of the Kp values in different organs depended on the amount of nuclei per gram of tissue. The primary determinant of the interspecies variation in the Kp values was the difference in tissue DNA concentrations among rats, rabbits, and guinea pigs, and a secondary determinant was the difference in fp values.

Animals↗
PubMed1991

Enantioselective pharmacokinetics of etodolac in the rat: tissue distribution, tissue binding, and in vitro metabolism.

The nonsteroidal anti-inflammatory agent etodolac (ET) exhibits stereoselectivity in its pharmacokinetics following administration to humans and rats. To underline the factors responsible for this stereoselectivity, the tissue distribution, in vitro tissue binding, and microsomal metabolism of ET enantiomers were studied in the rat. Following iv administration of racemic ET, the S:R AUC ratios in tissues were stereoselective, and different from that in plasma. Binding of enantiomers to tissues was stereoselective, although it did not relate well with in vivo tissue distribution. Rather, the tissue distribution of enantiomers appeared to be better explained by the unbound fractions of enantiomers in plasma. With respect to in vitro glucuronidation by liver microsomes, the Vmax of S-ET was 3.4-fold greater than that of R-ET; the enantiomers possessed similar Km. There appeared to be stereoselectivity in the oxidative metabolism of ET enantiomers by liver and kidney microsomes, in favor of the R-enantiomer. The lower AUC in rat plasma of pharmacologically active S-ET as compared with its antipode is due to its relatively greater distribution to tissues, owing to a lesser degree of binding to plasma proteins, and to its higher rate of glucuronidation.

Animals↗
PubMed1994

Comparison of quantitative whole-body autoradiographic and tissue dissection techniques in the evaluation of the tissue distribution of [14C]daptomycin in rats.

Quantitative whole-body autoradiography (QWBA) was evaluated and compared to tissue dissection/liquid scintillation counting (TD/LSC) techniques by determining the tissue distribution of radiocarbon in rats following iv administration of the antibiotic [14C]daptomycin (LY146032). QWBA, using computer-assisted video-image analysis, was initially evaluated by characterizing and calibrating commercial standards to blood and brain, kidney, liver, and lung homogenates. Frozen (carboxymethyl)cellulose blocks containing tissue homogenates spiked with [14C]glucose (370-37,000 Bq/g or 10-1000 nCi/g) were sectioned and optical densities (OD) measured. Characterization of QWBA included repeated measures data analysis to determine the significance of tissue type and intra- and inter-section and block variability. Regression models relating OD to radiocarbon concentration were also used to calibrate commercial standards for use in QWBA analyses. Results indicated that there were no substantial differences between OD readings from different tissues; however, the greatest source of variation in OD reading was section thickness. Because quantitative variations were largely attributed to section thickness, an internal standard (IS), consisting of liver homogenates spiked with [14C]glucose, was evaluated as a correction factor. Tissue concentrations of radiocarbon in male Fischer 344 rats were evaluated by QWBA and TD/LSC techniques 0.25 h following a single iv 10 mg/kg dose of [14C]daptomycin. Results indicated that tissue concentrations of radiocarbon obtained by QWBA, normalized using an IS, were comparable to those obtained by TD/LSC.

Amino Acid Sequence↗
PubMed2003

Detection of ALK gene rearrangements in formalin-fixed, paraffin-embedded tissue using a fluorescence in situ hybridization (FISH) probe: a search for optimum conditions of tissue archiving and preparation for FISH.

BACKGROUND: It is widely known that the efficiency of fluorescence in situ hybridization (FISH) probes applied to formalin-fixed, paraffin-embedded tissues is affected by the conditions under which the tissues are fixed and embedded. However, relatively few studies address exactly how tissue archiving conditions affect the performance of FISH probes. We report our experience based on use of an ALK FISH probe, during the validation of its diagnostic utility. METHODS: We applied the probe to 77 formalin-fixed, paraffin-embedded tissue blocks archived from 1991 through to 2000, and studied the interrelationship between the archival age (which ranged up to 10 years), type and condition of tissue, duration required for optimum hydrolysis, and obtainability of hybridization signals. RESULTS: We found that as archival age and tissue collagen content increased, not only did hydrolysis times have to be prolonged in order to yield interpretable hybridization signals, but also the likelihood of blocks becoming non-signaling increased. The most striking positive correlations were seen between the archival age of signaling lymphoid blocks and their requisite hydrolysis times. CONCLUSIONS: The difficulty in applying FISH on archival tissue increases with its archival age and collagen content, and may necessitate changes in laboratory protocol accordingly.

Anaplastic Lymphoma Kinase↗
PubMed2005

Fourth meeting of the European Network of Research Tissue Banks - future strategy to increase collaborations in the supply of human tissue for biomedical research.

This report records the Fourth meeting of the European Network of Research Tissue Bank (Brussels, 18th March 2004) which was attended by Mel Read MEP. The existing membership of this informal group represents European Human Research Tissue Bankers, biomedical researchers seeking access to human tissue and allied groups including animal welfare representatives. This Fourth meeting provided a forum to update members on individual activity in this area. A particular focus of this meeting was to consider the status of this group and future affiliations to increase the profile and activity of this Network. This meeting addressed differences in legislative and ethical requirements governing the use of human tissue in biomedical research in the different countries represented. Future activity of the ENRTB, planned at this meeting, will target harmonisation of current differences which are currently barriers to increased access to human tissue for biomedical research. Through the harmonisation of procurement, processing and distribution of human tissue specimens the ENRTB will provide a mechanism to benefit human health through increased use of human tissue in pharmacotoxicological studies and the associated replacement of animal tests.

Biomedical Research↗
PubMed2006

Expression of genes for gelatinases and tissue inhibitors of metalloproteinases in periodontal tissues during orthodontic tooth movement.

Orthodontic tooth movement progresses by a combination of periodontal ligament (PDL) tissue and alveolar bone remodeling processes. Besides the remodeling of alveolar bone around the moving teeth, the major extracellular matrix (ECM) components of PDLs, collagens, are degenerated, degraded, and restructured. Matrix metalloproteinases (MMPs) and their specific inhibitors, tissue inhibitors of metalloproteinases (TIMPs), act in a co-ordinated fashion to regulate the remodeling of periodontal tissues. We hypothesized that the expression levels of the genes for MMP-2, MMP-9, and TIMPs 1-3 are increased transiently in the periodontal tissue during orthodontic tooth movement. To test this hypothesis, we employed an animal model of tooth movement using rats, as well as in situ hybridization to analyze the expression levels of Mmp-2, Mmp-9, and Timps 1-3. The expression levels of these genes increased transiently in cells of periodontal tissues, which include cementoblasts, fibroblasts, osteoblasts, and osteoclasts, at the compression side of the moving teeth. The transient increases in gene expression at the tension side were mainly limited to osteoblasts and cementoblasts. In conclusion, the expression levels of Mmp-2, Mmp-9, and Timps 1-3 increase transiently during orthodontic tooth movement at both the tension and compression sides. The expression of these genes is regulated differentially in the periodontal tissue of the tension side and compression side. This altered pattern of gene expression may determine the rate and extent of remodeling of the collagenous ECM in periodontal tissues during orthodontic tooth movement.

Animals↗
PubMed1995

Trace element concentrations in cetacean liver tissues archived in the National Marine Mammal Tissue Bank.

The National Biomonitoring Specimen Bank (NBSB), a collaborative project of several U.S. government agencies, includes marine mammal tissues collected for the Alaska Marine Mammal Tissue Archival Project (AMMTAP) and the National Marine Mammal Tissue Bank (NMMTB). Tissues were collected from 139 animals representing 13 species of marine mammals from around the U.S. Recently, concentrations for up to 30 elements in liver tissues of nine long-finned pilot whales (Globicephala melas), six harbor porpoises (Phocoena phocoena), and four white-sided dolphins (Lagenorhynchus acutus) from the NMMTB were measured using instrumental neutron activation analysis. Results from analyses of these tissues are presented, compared with results for liver tissues from other marine mammals from the AMMTAP, and compared with published values.

Animals↗
PubMed1984

Proton nuclear magnetic resonance spectroscopy of normal and edematous brain tissue in vitro: changes in relaxation during tissue storage.

Proton nuclear magnetic resonance relaxation times, T1 and T2, of water in unfixed gray and white matter from normal and edematous rabbit brain tissues were measured in vitro at 23 degrees C and 100 MHz to evaluate the effects of the temperature (-25 degrees C to 37 degrees C) and duration (0 to 96 h) of tissue storage on relaxation times. T1 and T2 tended to decrease during storage, probably from slow dehydration of the tissue. This effect was greatest in tissues stored at 37 degrees C and least in those stored at 4 and -25 degrees C; decreases in T1 and T2 were greater in white matter than in gray matter. Freezing brain tissue to -25 degrees C caused a sudden decrease in the T2 of normal white matter. Relaxation times were constant for 5 h in tissues stored at 23 degrees C and for 40 h at 4 degrees C. These results correlated well with corresponding tissue water loss.

Animals↗