scholarly journals Distribution of the beta 1 subgroup of the integrins in human cells and tissues.

1989 ◽  
Vol 37 (3) ◽  
pp. 299-307 ◽  
Author(s):  
B De Strooper ◽  
B Van der Schueren ◽  
M Jaspers ◽  
M Saison ◽  
M Spaepen ◽  
...  
Keyword(s):  
Wide Distribution ◽  
Beta Subunits ◽  
Fibronectin Receptor ◽  
Activated T Lymphocytes ◽  
Primary Amino ◽  
Beta 1 Integrin ◽  
Human Fibronectin ◽  
Beta 2 ◽  
Integrin Family

We studied the distribution of the beta 1 integrin subfamily in human tissues and cells by light microscopy, electron microscopy, and immunoblotting, using monoclonal antibody DH12, previously shown to react with the beta 1 subunit of the human fibronectin receptor. Crossreaction with the other beta subunits of the integrin family, which have 45% and 47% primary amino acid sequence identity with the beta 1 subunit, was excluded, as MAb DH12 did not react with the beta 2 subunit in granulocytes and the beta 3 subunit in thrombocytes. Reactivity with the anti-beta 1 antibody was found in skin, lung, heart, striated and smooth muscle, blood cells, liver, kidney, intestine, spleen and placenta. Thus, cells of mesodermal, ectodermal, and entodermal origin express the beta 1 subunit. In skin fibroblasts cultured in vitro, beta 1 subunit was also detected intracellularly. The wide distribution of the beta 1 family, originally detected in activated T-lymphocytes after prolonged culture in vitro, contrast with the restricted distribution of the beta 2 integrins on leucocytes.

A spectrin-like protein from mouse brain membranes: phosphorylation of the 235,000-dalton subunit

1984 ◽  
Vol 247 (1) ◽  
pp. C61-C73 ◽  
Author(s):  
S. R. Goodman ◽  
I. S. Zagon ◽  
C. F. Whitfield ◽  
L. A. Casoria ◽  
S. B. Shohet ◽  
...  
Keyword(s):  
Mouse Brain ◽  
Beta Subunit ◽  
Beta Subunits ◽  
Mouse Erythrocyte ◽  
Alpha Beta ◽  
Beta 2 ◽  
Independent Protein ◽  
Brain Spectrin

A mouse brain spectrin-like protein, which was an immunoreactive analogue of erythrocyte spectrin, has been isolated from demyelinated membranes. This spectrin analogue was a 10.5 S, 972,000 molecular weight (Mr) (alpha beta)2 tetramer containing subunits of 240,000 (alpha) and 235,000 (beta) Mr. We demonstrated that in vivo only the 235,000 Mr beta subunit of the mouse brain spectrin-like protein was phosphorylated, which was an analogous situation to mouse erythrocyte spectrin in which only the 220,000 Mr beta subunit was phosphorylated. Incubation of isolated membrane fractions with [gamma-32P]ATP +/- adenosine 3',5'-cyclic monophosphate (cAMP) indicated that mouse brain spectrin-like protein, mouse erythrocyte spectrin, and human erythrocyte spectrin's beta subunits were all phosphorylated in vitro by membrane-associated cAMP-independent protein kinases.

scholarly journals Vinculin, talin, and integrins are localized at specific adhesion sites of malignant B lymphocytes

Blood ◽  
1988 ◽  
Vol 72 (2) ◽  
pp. 830-833
Author(s):  
PC Marchisio ◽  
L Bergui ◽  
GC Corbascio ◽  
O Cremona ◽  
N D'Urso ◽  
...  
Keyword(s):  
B Lymphocytes ◽  
Synthetic Peptide ◽  
Close Contact ◽  
Lymphocytic Leukemia ◽  
Contact Sites ◽  
Rgd Sequence ◽  
Adhesion Sites ◽  
Beta 1 Integrin ◽  
Beta 2

The microanatomy of the dot-shaped, close-contact sites called podosomes and the mechanism of their formation have been investigated in vitro in the malignant lymphocytes of B chronic lymphocytic leukemia (B-CLL). In this paper the authors demonstrate that in B-CLL podosomes: (1) vinculin, talin, and beta 2 integrin (CD18) rings surround an F- actin core; (2) the beta 1 integrin is localized within the F-actin core; (3) the beta 3 integrin is not present. This distribution and organization of adhesion-related molecules appears to be unique to B- CLL lymphocytes, since it has not been observed in normal B cells. B- CLL adhesion and podosome formation are inhibited by the synthetic peptide GRGDSP that contains the Arg-Gly-Asp (RGD) sequence.

scholarly journals Vinculin, talin, and integrins are localized at specific adhesion sites of malignant B lymphocytes

Blood ◽  
1988 ◽  
Vol 72 (2) ◽  
pp. 830-833 ◽  
Author(s):  
PC Marchisio ◽  
L Bergui ◽  
GC Corbascio ◽  
O Cremona ◽  
N D'Urso ◽  
...  
Keyword(s):  
B Lymphocytes ◽  
Synthetic Peptide ◽  
Close Contact ◽  
Lymphocytic Leukemia ◽  
Contact Sites ◽  
Rgd Sequence ◽  
Adhesion Sites ◽  
Beta 1 Integrin ◽  
Beta 2

Abstract The microanatomy of the dot-shaped, close-contact sites called podosomes and the mechanism of their formation have been investigated in vitro in the malignant lymphocytes of B chronic lymphocytic leukemia (B-CLL). In this paper the authors demonstrate that in B-CLL podosomes: (1) vinculin, talin, and beta 2 integrin (CD18) rings surround an F- actin core; (2) the beta 1 integrin is localized within the F-actin core; (3) the beta 3 integrin is not present. This distribution and organization of adhesion-related molecules appears to be unique to B- CLL lymphocytes, since it has not been observed in normal B cells. B- CLL adhesion and podosome formation are inhibited by the synthetic peptide GRGDSP that contains the Arg-Gly-Asp (RGD) sequence.

Down-regulation of the chicken alpha 5 beta 1 integrin fibronectin receptor during development

Development ◽  
1991 ◽  
Vol 113 (1) ◽  
pp. 327-337 ◽  
Author(s):  
J.L. Muschler ◽  
A.F. Horwitz
Keyword(s):  
Cell Types ◽  
Embryonic Cell ◽  
Alpha Subunit ◽  
Down Regulation ◽  
Fibronectin Receptor ◽  
Alpha Subunits ◽  
Adult Tissues ◽  
Beta 1 Integrin ◽  
Integrin Fibronectin Receptor ◽  
Integrin Family

We have characterized the diversity of the chicken beta 1 integrin family and studied the expression of individual receptors during development. The diversity of the beta 1 integrin family was investigated by affinity purifying the beta 1 integrins from a variety of adult and embryonic tissues. These purifications reveal the relative levels of expression and also the differential expression of the alpha subunits in those tissues. Monoclonal antibodies were generated against the prominent ‘band 1’ of the embryonic chicken integrins and used to characterize the expression of this alpha subunit in embryonic and adult tissues. This alpha subunit is shown to be the chicken homologue of human alpha 5 fibronectin receptor. The chicken alpha 5 beta 1 integrin is the most prominent beta 1 integrin in the embryo and is expressed on the majority of cell types through the day 17 stage. The distribution of this receptor in the embryo closely parallels the distribution of its ligand, fibronectin. In adult tissues, expression of this receptor is greatly diminished relative to the expression of other alpha subunits. The cell type distribution is highly restricted: limited primarily to the vasculature and to connective tissue regions. These studies reveal a prominent role for the alpha 5 beta 1 integrin in embryonic cell types and a down-regulation of this receptor on many cell types during development.

Embryonic mesodermal defects in alpha 5 integrin-deficient mice

Development ◽  
1993 ◽  
Vol 119 (4) ◽  
pp. 1093-1105 ◽  
Author(s):  
J.T. Yang ◽  
H. Rayburn ◽  
R.O. Hynes
Keyword(s):  
Embryonic Stem ◽  
Loss Of Function ◽  
Cellular Functions ◽  
Fibronectin Receptor ◽  
Beta 1 Integrin ◽  
Integrin Gene ◽  
Posterior Trunk ◽  
Mutant Cells ◽  
Deficient Mice

A loss of function mutation of the murine alpha 5 integrin gene generated by gene targeting in embryonic stem cells is a recessive embryonic lethal. The mutant embryos start to show observable defects by day 9 of gestation and die around day 10–11. The alpha 5-null embryos have pronounced defects in posterior trunk and yolk sac mesodermal structures, suggesting a role for alpha 5 beta 1 integrin in mesoderm formation, movement or function. However, the embryos progress significantly further than embryos null for fibronectin, for which alpha 5 beta 1 integrin is a receptor, suggesting the involvement of other fibronectin receptors. In vitro studies on cells derived from the alpha 5-null embryos confirm that the alpha 5 beta 1 integrin is not expressed on mutant cells and show that the mutant cells are able to assemble fibronectin matrix, form focal contacts, and migrate on fibronectin despite the complete absence of the alpha 5 beta 1 fibronectin receptor integrin. All these functions have previously been thought to involve or require alpha 5 beta 1. The results presented show that these cellular functions involving fibronectin can proceed using other receptors.

scholarly journals Fibronectin receptor functions in embryonic cells deficient in alpha 5 beta 1 integrin can be replaced by alpha V integrins.

1996 ◽  
Vol 7 (11) ◽  
pp. 1737-1748 ◽  
Author(s):  
J T Yang ◽  
R O Hynes
Keyword(s):  
Integrin Subunit ◽  
Embryonic Cells ◽  
Wild Type ◽  
Matrix Assembly ◽  
Fibronectin Receptor ◽  
Focal Contacts ◽  
Genes Encoding ◽  
Beta 1 Integrin

alpha 5 beta 1 integrin mediates cell adhesion to extracellular matrix by interacting with fibronectin (FN). Mouse lines carrying null mutations in genes encoding either the alpha 5 integrin subunit or FN have been generated previously. Both mutations are embryonic lethal with overlapping defects, but the defects of alpha 5-null embryos are less severe. Primary embryonic cells lacking alpha 5 beta 1 are able to adhere to FN, form focal contacts, migrate on FN, and assemble FN matrix. These results suggest the involvement of (an)other FN receptors(s). In this study, we examined functions of alpha 4 beta 1 and alpha V integrins in embryonic cells lacking alpha 5 beta 1. Our analysis of cells lacking both alpha 4 beta 1 and alpha 5 beta 1 showed that alpha 4 beta 1 is also not required for these FN-dependent functions. Using alpha V-specific blocking reagents, we showed that alpha V integrins are required for alpha 5-null cells, but not wild-type cells, to adhere and spread on FN. Our data also showed that, although the expression levels of alpha V integrins on the wild-type and alpha 5-null cells are similar, there is an increase in recruitment of alpha V integrins into focal contacts in alpha 5-null cells plated on FN, indicating that alpha V integrins can compensate functionally for the loss of alpha 5 beta 1 in focal contacts of alpha 5-null cells. Finally, our data suggested possible roles for alpha V integrins in replacing the role of alpha 5 beta 1 in FN matrix assembly in vitro and in FN-dependent embryonic functions in vivo.

RAPID IN VITRO PROPAGATION OF WESTERN GHATS CULTIVAR - COLOCASIA ESCULENTA FOR THE HIGH FREQUENCY OF PLANTLETS

2019 ◽  
Vol 7 (2) ◽  
Author(s):  
Jyothi R ◽  
Srinivasa Murthy K M ◽  
Hossein . ◽  
Veena .
Keyword(s):  
Tissue Culture ◽  
Wide Distribution ◽  
Colocasia Esculenta ◽  
Limiting Factor ◽  
Promising Alternative ◽  
Rapid Multiplication ◽  
Medical Plant ◽  
Total Fat ◽  
Planting Materials

Colocasia esculenta is commonly known as Taro, it is referred to as cocoyam in Nigeria. They are cherished for their rich taste, nutritional and medicinal properties. Every 100 g of taro corms possess 112 Kcal, 26.46 g carbohydrate, 1.50 g protein, 0.20 g total fat and 4.1g fiber (USDA National Nutrient Data Base). Besides its nutritional value, taro is used as a medical plant and provides bioactive compounds used as an anti-cancer drugs. Traditionally, cocoyams are vegetative propagated from tuber fragments, a practice that encourages pathogen distribution. Colocasia esculenta is a widely distributed food crop in the humid tropics and subtropics. Despite of its wide distribution, Taro plants are commonly infected with DsMV and other pathogens. This virus induces conspicuous mosaic, malformation, dwarfing or feathering on leaves in taro. As the results of infection, it reduces the quality and yield of taro production greatly. This virus is thus considered as a major limiting factor in the production of taro. Here plays the importance of  tissue culture plays a major role in producing the disease resistant plants round the year with high quality. For rapid multiplication and production of quality planting materials, tissue culture technology offers promising alternative compared to the traditional production methods. KEYWORDS: Colocasia esculenta, Virus, Pathogens, Conventional propagation, Micropropagation, Yield, Rapid multiplication, Quality

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