Characterization of barnacle ( Balanus eburneus and B. cenatus  ) adhesive proteins

1997 ◽  
Vol 127 (4) ◽  
pp. 629-635 ◽  
Author(s):  
M. J. Naldrett ◽  
D. L. Kaplan
Keyword(s):  
Adhesive Proteins ◽  
Balanus Eburneus

Characterization of Bone Marrow Laminins and Identification of 5-Containing Laminins as Adhesive Proteins for Multipotent Hematopoietic FDCP-Mix Cells

Blood ◽  
1999 ◽  
Vol 93 (8) ◽  
pp. 2533-2542 ◽  
Author(s):  
Yuchen Gu ◽  
Lydia Sorokin ◽  
Madeleine Durbeej ◽  
Tord Hjalt ◽  
Jan-Ingvar Jönsson ◽  
...  
Keyword(s):  
Bone Marrow ◽  
Mouse Bone Marrow ◽  
Bone Marrow Cultures ◽  
Adhesive Interactions ◽  
Adhesive Proteins ◽  
Polypeptide Chains ◽  
Laminin 1

Abstract Laminins are extracellular matrix glycoproteins that influence the phenotype and functions of many types of cells. Laminins are heterotrimers composed of , β, and γ polypeptides. So far five , three β, and two γ polypeptide chains, and 11 variants of laminins have been proposed. Laminins interact in vitro with mature blood cells and malignant hematopoietic cells. Most studies have been performed with laminin-1 (1β1γ1), and its expression in bone marrow is unclear. Employing an antiserum reacting with most laminin isoforms, we found laminins widely expressed in mouse bone marrow. However, no laminin 1 chain but rather laminin 2, 4, and 5 polypeptides were found in bone marrow. Our data suggest presence of laminin-2 (2β1γ1), laminin-8 (4β1γ1), and laminin-10 (5β1γ1) in bone marrow. Northern blot analysis showed expression of laminin 1, 2, 4, and 5 chains in long-term bone marrow cultures, indicating upregulation of laminin 1 chain expression in vitro. Laminins containing 5 chain, in contrast to laminin-1, were strongly adhesive for multipotent hematopoietic FDCP-mix cells. Integrin 6 and β1 chains mediated this adhesion, as shown by antibody perturbation experiments. Our findings indicate that laminins other than laminin-1 are functional in adhesive interactions in bone marrow.

Characterization of Bone Marrow Laminins and Identification of 5-Containing Laminins as Adhesive Proteins for Multipotent Hematopoietic FDCP-Mix Cells

Blood ◽  
1999 ◽  
Vol 93 (8) ◽  
pp. 2533-2542 ◽  
Author(s):  
Yuchen Gu ◽  
Lydia Sorokin ◽  
Madeleine Durbeej ◽  
Tord Hjalt ◽  
Jan-Ingvar Jönsson ◽  
...  
Keyword(s):  
Bone Marrow ◽  
Mouse Bone Marrow ◽  
Bone Marrow Cultures ◽  
Adhesive Interactions ◽  
Adhesive Proteins ◽  
Polypeptide Chains ◽  
Laminin 1

Laminins are extracellular matrix glycoproteins that influence the phenotype and functions of many types of cells. Laminins are heterotrimers composed of , β, and γ polypeptides. So far five , three β, and two γ polypeptide chains, and 11 variants of laminins have been proposed. Laminins interact in vitro with mature blood cells and malignant hematopoietic cells. Most studies have been performed with laminin-1 (1β1γ1), and its expression in bone marrow is unclear. Employing an antiserum reacting with most laminin isoforms, we found laminins widely expressed in mouse bone marrow. However, no laminin 1 chain but rather laminin 2, 4, and 5 polypeptides were found in bone marrow. Our data suggest presence of laminin-2 (2β1γ1), laminin-8 (4β1γ1), and laminin-10 (5β1γ1) in bone marrow. Northern blot analysis showed expression of laminin 1, 2, 4, and 5 chains in long-term bone marrow cultures, indicating upregulation of laminin 1 chain expression in vitro. Laminins containing 5 chain, in contrast to laminin-1, were strongly adhesive for multipotent hematopoietic FDCP-mix cells. Integrin 6 and β1 chains mediated this adhesion, as shown by antibody perturbation experiments. Our findings indicate that laminins other than laminin-1 are functional in adhesive interactions in bone marrow.

scholarly journals Proteogenomic Characterization of the Cement and Adhesive Gland of the Pelagic Gooseneck Barnacle Lepas anatifera

2021 ◽  
Vol 22 (7) ◽  
pp. 3370
Author(s):  
Dany Domínguez-Perez ◽  
Daniela Almeida ◽  
Josef Wissing ◽  
André M. Machado ◽  
Lothar Jänsch ◽  
...  
Keyword(s):  
Amino Acid ◽  
Chemical Cues ◽  
Protein Composition ◽  
Adhesive System ◽  
Goose Barnacle ◽  
Gooseneck Barnacle ◽  
Components Analysis ◽  
Adhesive Proteins ◽  
Floating Objects

We focus on the stalked goose barnacle L. anatifera adhesive system, an opportunistic less selective species for the substrate, found attached to a variety of floating objects at seas. Adhesion is an adaptative character in barnacles, ensuring adequate positioning in the habitat for feeding and reproduction. The protein composition of the cement multicomplex and adhesive gland was quantitatively studied using shotgun proteomic analysis. Overall, 11,795 peptide sequences were identified in the gland and 2206 in the cement, clustered in 1689 and 217 proteinGroups, respectively. Cement specific adhesive proteins (CPs), proteases, protease inhibitors, cuticular and structural proteins, chemical cues, and many unannotated proteins were found, among others. In the cement, CPs were the most abundant (80.5%), being the bulk proteins CP100k and -52k the most expressed of all, and CP43k-like the most expressed interfacial protein. Unannotated proteins comprised 4.7% of the cement proteome, ranking several of them among the most highly expressed. Eight of these proteins showed similar physicochemical properties and amino acid composition to known CPs and classified through Principal Components Analysis (PCA) as new CPs. The importance of PCA on the identification of unannotated non-conserved adhesive proteins, whose selective pressure is on their relative amino acid abundance, was demonstrated.

scholarly journals Characterization of serum adhesive proteins that block tumor necrosis factor-mediated cell death

1997 ◽  
Vol 4 (8) ◽  
pp. 779-786 ◽  
Author(s):  
Nan-Shan Chang ◽  
Nicole Joki ◽  
Jeff Mattison ◽  
Tuan Dinh ◽  
Seenian John
Keyword(s):  
Cell Death ◽  
Tumor Necrosis Factor ◽  
Tumor Necrosis ◽  
Adhesive Proteins ◽  
Necrosis Factor

scholarly journals Identification and Characterization of a Novel 38.5-Kilodalton Cell Surface Protein of Staphylococcus aureus with Extended-Spectrum Binding Activity for Extracellular Matrix and Plasma Proteins

2001 ◽  
Vol 183 (23) ◽  
pp. 6778-6786 ◽  
Author(s):  
Muzaffar Hussain ◽  
Karsten Becker ◽  
Christof von Eiff ◽  
Jacques Schrenzel ◽  
Georg Peters ◽  
...  
Keyword(s):  
Staphylococcus Aureus ◽  
Extracellular Matrix ◽  
Cell Surface ◽  
Binding Protein ◽  
Clinical Strain ◽  
Calculated Molecular Mass ◽  
Extended Spectrum ◽  
Strain Collection ◽  
Adhesive Proteins

ABSTRACT The ability to attach to host ligands is a well-established pathogenic factor in invasive Staphylococcus aureusdisease. In addition to the family of adhesive proteins bound to the cell wall via the sortase A (srtA) mechanism, secreted proteins such as the fibrinogen-binding protein Efb, the extracellular adhesion protein Eap, or coagulase have been found to interact with various extracellular host molecules. Here we describe a novel protein, the extracellular matrix protein-binding protein (Emp) initially identified in Western ligand blots as a 40-kDa protein due to its broad-spectrum recognition of fibronectin, fibrinogen, collagen, and vitronectin. Emp is expressed in the stationary growth phase and is closely associated with the cell surface and yet is extractable by sodium dodecyl sulfate. The conferring gene emp (1,023 nucleotides) encodes a signal peptide of 26 amino acids and a mature protein of a calculated molecular mass of 35.5 kDa. Using PCR,emp was demonstrated in all 240 S. aureusisolates of a defined clinical strain collection as well as in 6S. aureus laboratory strains, whereas it is lacking in all 10 S. epidermidis strains tested. Construction of an allelic replacement mutant (mEmp50) revealed the absence of Emp in mEmp50, a significantly decreased adhesion of mEmp50 to immobilized fibronectin and fibrinogen, and restoration of these characteristics upon complementation of mEmp50. Emp expression was also demonstrable upon heterologous complementation of S. carnosus. rEmp expressed in Escherichia coli interacted with fibronectin, fibrinogen, and vitronectin in surface plasmon resonance experiments at a K d of 21 nM, 91 nM, and 122 pM, respectively. In conclusion, the biologic characterization of Emp suggests that it is a member of the group of secreted S. aureus molecules that interact with an extended spectrum of host ligands and thereby contribute to S. aureuspathogenicity.

Morphological Characterization of Mycobacteriophage R1

1974 ◽  
Vol 32 ◽  
pp. 254-255
Author(s):  
B. L. Soloff ◽  
T. A. Rado
Keyword(s):  
Carbon Source ◽  
Stationary Phase ◽  
Growth Phase ◽  
Minimal Medium ◽  
Morphological Characterization ◽  
Logarithmic Growth Phase ◽  
Complete Lysis ◽  
Lysogenic Culture ◽  
Logarithmic Growth

Mycobacteriophage R1 was originally isolated from a lysogenic culture of M. butyricum. The virus was propagated on a leucine-requiring derivative of M. smegmatis, 607 leu−, isolated by nitrosoguanidine mutagenesis of typestrain ATCC 607. Growth was accomplished in a minimal medium containing glycerol and glucose as carbon source and enriched by the addition of 80 μg/ ml L-leucine. Bacteria in early logarithmic growth phase were infected with virus at a multiplicity of 5, and incubated with aeration for 8 hours. The partially lysed suspension was diluted 1:10 in growth medium and incubated for a further 8 hours. This permitted stationary phase cells to re-enter logarithmic growth and resulted in complete lysis of the culture.

AEM analysis of crystallization in Ti-based amorphous alloys

1983 ◽  
Vol 41 ◽  
pp. 270-271
Author(s):  
A.R. Pelton ◽  
A.F. Marshall ◽  
Y.S. Lee
Keyword(s):  
Magnetic Properties ◽  
Amorphous Alloys ◽  
Amorphous Materials ◽  
Isothermal Annealing ◽  
Amorphous Matrix ◽  
Nucleation And Growth ◽  
Current Interest ◽  
Amorphous Films ◽  
Electrical And Magnetic Properties

Amorphous materials are of current interest due to their desirable mechanical, electrical and magnetic properties. Furthermore, crystallizing amorphous alloys provides an avenue for discerning sequential and competitive phases thus allowing access to otherwise inaccessible crystalline structures. Previous studies have shown the benefits of using AEM to determine crystal structures and compositions of partially crystallized alloys. The present paper will discuss the AEM characterization of crystallized Cu-Ti and Ni-Ti amorphous films.Cu60Ti40: The amorphous alloy Cu60Ti40, when continuously heated, forms a simple intermediate, macrocrystalline phase which then transforms to the ordered, equilibrium Cu3Ti2 phase. However, contrary to what one would expect from kinetic considerations, isothermal annealing below the isochronal crystallization temperature results in direct nucleation and growth of Cu3Ti2 from the amorphous matrix.

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