Distribution of desmosomal components in the tissues of vertebrates, studied by fluorescent antibody staining

1984 ◽  
Vol 66 (1) ◽  
pp. 119-132
Author(s):  
P. Cowin ◽  
D. Mattey ◽  
D. Garrod
Keyword(s):  
Molecular Weight ◽  
Salmo Trutta ◽  
Fluorescent Antibody ◽  
Mammalian Species ◽  
Ambystoma Mexicanum ◽  
Immunofluorescent Staining ◽  
Antibody Staining ◽  
Lower Vertebrates ◽  
Lacerta Viridis ◽  
Trout Gill

In previous work we used immunofluorescent staining with specific antibodies to study the distribution of five desmosomal antigens in the epithelia of different vertebrate animals. We showed that all five antigens were present in all epithelia studied in human, bovine, rat, guinea pig, chick and frog (Rana pipiens) tissues. It was concluded that desmosomes are highly conserved structures. This paper extends those studies: by including three other species, a lizard (Lacerta viridis), the axolotl (Ambystoma mexicanum) and the trout (Salmo trutta), and by looking at several tissues in more detail. The principal results are as follows. The epidermis of all species down to the frog stain with equal intensity for all desmosomal antigens. In the epidermis of axolotl and trout, staining for desmosomal plaque constituents is present, but staining for the desmosomal glycoproteins is greatly reduced or absent. Within mammalian species as well as chick, lizard and frog, staining for the 115 X 10(3) and 100 X 10(3) molecular weight desmosomal glycoproteins is less intense in non-epidermal tissues than in the epidermis, while staining for desmosomal plaque constituents and for the 150 X 10(3) molecular weight glycoprotein is undiminished. It is possible, therefore, that slight differences exist between certain glycoproteins of epidermis and non-epidermal epithelia. The hearts of lower vertebrates (lizard, frog, axolotl and trout) stain only for individual desmosomal plaque antigens. The pillar cells of trout gill stain, adjacent to their collagenous columns, for one desmosomal plaque antigen. There is a fibrous cytoplasmic mat in this position but no desmosomes. Thus one of the desmosomal antigens may have a function outside the desmosome.

scholarly journals Localization of creatine kinase isoenzymes in myofibrils. II. Chicken heart muscle.

1977 ◽  
Vol 75 (2) ◽  
pp. 318-325 ◽  
Author(s):  
T Wallimann ◽  
H J Kuhn ◽  
G Pelloni ◽  
D C Turner ◽  
H M Eppenberger
Keyword(s):  
Skeletal Muscle ◽  
Creatine Kinase ◽  
Heart Muscle ◽  
Fluorescent Antibody ◽  
Immunofluorescent Staining ◽  
Absolute Amount ◽  
Chicken Heart ◽  
Antibody Staining ◽  
Line Region ◽  
Almost All

Chicken heart muscle contains almost exclusively the BB isoenzyme of creatine kinase (CK), its myofibrils, moreover, lack an M-line. This tissue thus provides an interesting contrast to skeletal muscle, in which some of the MM-CK present as predominant CK isoenzyme is bound at the myofibrillar M-line. Approx. 2% of the total CK activity in a chicken heart homogenate remains bound to the myofibrillar fraction after repeated washing cycles; both the fraction and the absolute amount of CK bound are about threefold lower than in skeletal muscle. Almost all of the bound enzyme is located within the Z-line region of each sarcomere, as revealed by indirect fluorescent-antibody staining with antiserum against purified chicken BB-CK. After incubation with exogenous purified MM-CK, positive immunofluorescent staining for M-type CK at the H-region of heart myofibrils was observed, along with weaker fluorescence in the Z-line region. Chicken heart myofibrils may thus possess binding sites for both M and B forms of CK.

FLUORESCENT ANTIBODY STAINING IN THE SERODIAGNOSIS OF TRICHINOSIS

1963 ◽  
Vol 9 (4) ◽  
pp. 625-628 ◽  
Author(s):  
R. K. Baratawidjaja ◽  
Ann Hewson ◽  
N. A. Labzoffsky
Keyword(s):  
Complement Fixation ◽  
Trichinella Spiralis ◽  
Fluorescent Antibody ◽  
Immunofluorescent Staining ◽  
Staining Procedure ◽  
Fluorescent Staining ◽  
Antibody Staining ◽  
Human Sera ◽  
Fluorescent Antibody Staining

A fluorescent staining procedure for Trichinella spiralis and the appearance of the stained larvae are described. The applicability of the method to the sero-diagnosis of trichinosis was investigated. The results obtained both with the experimental and human sera agreed well with the complement-fixation results. In titrating 9 experimental sera and 36 sera from parasitologically proved or clinically diagnosed cases of trichinosis in humans, higher titers were obtained by the immunofluorescent staining, indicating that this test is somewhat more sensitive.

scholarly journals New Functions of Low-Molecular-Weight Hyaluronic Acid on Epidermis Filaggrin Production and Degradation

Cosmetics ◽  
2021 ◽  
Vol 8 (4) ◽  
pp. 118
Author(s):  
Moe Hashimoto ◽  
Kazuhisa Maeda
Keyword(s):  
Molecular Weight ◽  
Hyaluronic Acid ◽  
Fluorescent Antibody ◽  
Three Dimensional ◽  
3D Models ◽  
Low Molecular Weight ◽  
Mrna Levels ◽  
Protein Levels ◽  
Degrading Enzymes ◽  
Antibody Staining

Hyaluronic acid (HA) is a high-molecular-weight polysaccharide with high moisturizing power. It is composed of repeating disaccharides of N-acetyl-D-glucosamine and D-glucuronic acid. Low-molecular-weight hyaluronan (LMHA) is obtained by changing the molecular weight or modifying the functional groups of HA and is commonly used together with HA in cosmetics. The objective of this study was to determine whether LMHA promotes the synthesis of filaggrin (FLG). We also investigated whether LMHA activates FLG-degrading enzymes. Three-dimensional (3D) models of the human epidermis were cultured with LMHA. Real-time PCR was used to quantify the mRNA levels of profilaggrin (proFLG), involucrin (IVL), and FLG-degrading enzymes. FLG protein levels were measured by fluorescent antibody staining and Western blotting. The mRNA was quantified using a 3D epidermis model, and it was observed that the mRNA levels of proFLG, IVL, caspase-14 (CASP14), and bleomycin hydrolase were increased by the application of LMHA. Immunofluorescence results showed an increase in FLG proteins, and results from experiments using 3D epidermis models showed that LMHA increased the activity of CASP14. This suggests that the topical application of LMHA would result in an increase in natural moisturizing factor and promote moisturization of the stratum corneum.

An investigation of the molecular components of desmosomes in epithelial cells of five vertebrates

1986 ◽  
Vol 81 (1) ◽  
pp. 223-242 ◽  
Author(s):  
A. Suhrbier ◽  
D. Garrod
Keyword(s):  
Molecular Weight ◽  
Mdck Cells ◽  
Fluorescent Antibody ◽  
Cross Reactivity ◽  
Protein Domain ◽  
Nasal Epithelium ◽  
Molecular Weights ◽  
Antibody Staining ◽  
A Cell ◽  
Molecular Components

We have shown previously, by fluorescent antibody staining, that desmosomal antigens are widely distributed in the tissues of vertebrate animals. Furthermore, we have demonstrated mutual desmosome formation between cells derived from man, cow, dog, chicken and frog. In this paper we have studied the components of desmosomes in a tissue or a cell line from each of these animals by immunoblotting with antibodies raised against the desmosomal components isolated from bovine nasal epithelium. Blotting was carried out on bovine nasal epithelial desmosomal cores, desmosome-enriched fractions derived from chicken and frog epidermis, nuclear matrix-intermediate filament scaffolds derived from Madin-Darby bovine and canine cells (MDBK and MDCK), and unextracted cultured human foreskin keratinocytes. The results show that desmosomes from all these sources contain high molecular weight proteins (desmoplakins) of similar or identical molecular weights (250 000 and 215 000). Antibodies against the two lower molecular weight desmosomal proteins (83 000 and 75 000) always recognized one or two bands in very similar molecular weight regions of the gels. The desmosomal glycoproteins were found to be much more variable than the proteins: they vary between sources in molecular weight, heterogeneity and antibody cross-reactivity. For instance, antibody specific for a group of glycoprotein bands of 175 000, 169 000 and 164 000 (Mr) in bovine nasal epithelium recognizes three bands of 245 000, 230 000 and 210 000 in MDCK cells but only a single band of 190 000 in keratinocytes. In mammals, the 175 000–164 000 glycoproteins and the desmosomal adhesion molecules, the desmocollins (Mr 130 000 and 115 000 in cow's nose), are immunologically distinct. In chicken and frog, however, there are glycoproteins that react with both anti-175 000–164 000 and anti-desmocollin antibodies, but there are also distinct desmocollin bands. The significance of these results is discussed in relation to conservation of desmosomal components and adhesion mechanisms. It is suggested that adhesion may be performed by a well-conserved protein domain and that the variation between desmosomal glycoproteins from different sources may be due to differences in their carbohydrate composition.

A Most Probable Number Method for the Enumeration of Legionella Bacteria in Water

1991 ◽  
Vol 24 (2) ◽  
pp. 143-147 ◽  
Author(s):  
N. A. Grabow ◽  
R. Kfir ◽  
W. O. K. Grabow
Keyword(s):  
Water Samples ◽  
Membrane Filtration ◽  
Quantitative Method ◽  
Fluorescent Antibody ◽  
Most Probable Number ◽  
Probable Number ◽  
Comparative Tests ◽  
Antibody Staining ◽  
Direct Fluorescent Antibody ◽  
Yeast Extract Agar

A new quantitative method for the enumeration of Legionella bacteria in water is described. Appropriate tenfold serial dilutions of water samples concentrated by membrane filtration are plated in triplicate on buffered charcoal yeast extract agar. After incubation for 3 days representative smears from individual plates are tested for the presence of Legionella by direct fluorescent antibody staining. The number of positive plates in each dilution is used to calculate the Legionella count by means of conventional most probable number statistics. In comparative tests on a variety of water samples this method yielded significantly higher counts than previously used procedures.

scholarly journals Novel Role for Albumin in Innate Immunity: Serum Albumin Inhibits the Growth of Blastomyces dermatitidis Yeast Form In Vitro

2003 ◽  
Vol 71 (11) ◽  
pp. 6648-6652 ◽  
Author(s):  
Steven Giles ◽  
Charles Czuprynski
Keyword(s):  
Molecular Weight ◽  
Inhibitory Activity ◽  
Mammalian Species ◽  
Blastomyces Dermatitidis ◽  
Low Molecular Weight ◽  
Rat Serum ◽  
Yeast Form ◽  
Domain Iii

ABSTRACT In this study we found that serum inhibitory activity against Blastomyces dermatitidis was principally mediated by albumin. This was confirmed in experiments using albumin from several mammalian species. Analbuminemic rat serum did not inhibit B. dermatitidis growth in vivo; however, the addition of albumin restored inhibitory activity. Inhibitory activity does not require albumin domain III and appears to involve binding of a low-molecular-weight yeast-derived growth factor.

scholarly journals Low‐molecular‐weight phosphotyrosyl protein phosphatase expression in brain of chicken and some lower vertebrates

2002 ◽  
Vol 69 (2) ◽  
pp. 97-102
Author(s):  
Livia Lucentini ◽  
Antonella Angiolillo ◽  
Emanuela Varasano ◽  
Fausto Panara
Keyword(s):  
Molecular Weight ◽  
Protein Phosphatase ◽  
Low Molecular Weight ◽  
Lower Vertebrates

How Can Female Germline Stem Cells Contribute to the Physiological Neo-Oogenesis in Mammals and Why Menopause Occurs?

2010 ◽  
Vol 17 (4) ◽  
pp. 498-505 ◽  
Author(s):  
Antonin Bukovsky
Keyword(s):  
Stem Cells ◽  
Adult Mouse ◽  
Mammalian Species ◽  
Reproductive Period ◽  
Germline Stem Cells ◽  
Environmental Threats ◽  
Ovarian Stem Cells ◽  
Lower Vertebrates ◽  
Female Germline ◽  
Prevailing View

AbstractAt the beginning of the last century, reproductive biologists have discussed whether in mammalian species the fetal oocytes persist or are replaced by neo-oogenesis during adulthood. Currently the prevailing view is that neo-oogenesis is functional in lower vertebrates but not in mammalian species. However, contrary to the evolutionary rules, this suggests that females of lower vertebrates have a better opportunity to provide healthy offspring compared to mammals with oocytes subjected to environmental threats for up to several decades. During the last 15 years, a new effort has been made to determine whether the oocyte pool in adult mammals is renewed as well. Most recently, Ji Wu and colleagues reported a production of offspring from female germline stem cells derived from neonatal and adult mouse ovaries. This indicates that both neonatal and adult mouse ovaries carry stem cells capable of producing functional oocytes. However, it is unclear whether neo-oogenesis from ovarian somatic stem cells is physiologically involved in follicular renewal and why menopause occurs. Here we review observations that indicate an involvement of immunoregulation in physiological neo-oogenesis and follicular renewal from ovarian stem cells during the prime reproductive period and propose why menopause occurs in spite of persisting ovarian stem cells.

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