			Home About us Contact

Specific Lectin (specific + lectin)

Distribution by Scientific Domains

Medical Sciences	50%
Life Sciences	50%

Selected Abstracts

Specific Interaction of the Legume Lectins, Concanavalin A and Peanut Agglutinin, with Phycocyanin

PHOTOCHEMISTRY & PHOTOBIOLOGY, Issue 5 2009
Gunjan Pandey
In a recent study, we found that jacalin, a T-antigen specific lectin could interact with phycocyanin (PC) in a carbohydrate-independent manner. We show here that concanavalin A and peanut agglutinin too can interact with PC, although the nature of the interaction is distinctly different from that for jacalin. The legume lectins bind PC weaker in the presence of their specific carbohydrate ligands. Like jacalin, the legume lectins too interact with PC via two distinct sites. Higher ionic strengths resulted in a weakening of the interaction at site 1 and did not affect the interaction at site 2, clearly indicating that the interactions involve charged residues at the former and hydrophobic interactions at the latter site. The implications for the use of these lectin,PC complexes in photodynamic therapy and other clinical applications are discussed. [source]

The Development of the Metanephric Kidney in the Pig

ANATOMIA, HISTOLOGIA, EMBRYOLOGIA, Issue 2005
H. Bragulla
Aims:, The metanephric kidneys of the pig are used as xenotransplants in human medicine. In order for transplants to fit within the host organisms, the subcapsular blastema and blood vessels are crucial for the development of new nephrons to sustain the organ functions. The aim of this study is to obtain data concerning the post-natal development of metanephric nephrons in the porcine kidney. Materials and Methods:, The metanephric kidneys of six porcine fetuses with a crown-rump length ranging from 40 mm to 220 mm of eight piglets aged between 6 to 10 weeks and of three adult pigs were studied. Eight lectins as well as anti-actin and anti-myosin antibodies were used for lectin- and immunohistochemistry to study the subcapsular metanephric blastema, to visualize the blood-urine barrier in the nephrons and collecting tubules, and to study the blood vessels in both the renal cortex and marrow. Results and Conclusions:, A subcapsular metanephric blastema was still present in the kidney of 10-week-old piglets. Dense condensation of mesenchymal cells surrounded the terminal branches of the collecting ducts and showed first signs of mesenchymal-epithelial transformation. Characteristic comma-shaped and s-shaped bodies were found in and underneath the subcapsular blastema. In the fibrous renal capsule of six-week-old piglets, a first faint binding reaction of anti-actin was visible and intensified in the fibrous renal capsule in ten-week-old piglets and in adult pigs. In addition, the smooth-muscle layers of the blood vessels were stained by the anti-actin and anti-myosin antibodies. The lectins showed various affinities to the endothelium of blood vessels and to the epithelial cells lining of the capsules of the metanephric renal corpuscles, the various parts of the renal tubules, as well as the collecting tubules and the renal pelvis. The affinity of the epithelial cells to a specific lectin varies in neighbouring cells, indicating different cell activities or cell cycles. [source]

Use of microbeads for the detection of binding sites on the human zona pellucida: a scanning electron microscopy (SEM) assay

ANDROLOGIA, Issue 5 2001
Prof. Dr H. W. Michelmann
Summary One prerequisite for fertilization is the specific binding of spermatozoa to the zona pellucida. However, the factors and mechanisms involved in this gamete contact are not well understood. Gamete recognition and binding are species-specific and are controlled by oligosaccharides of the zona and their corresponding carbohydrates on the spermatozoon. By using a specific lectin we developed a technique to detect those oligosaccharides on the human zona pellucida that might be involved in the binding process. Microbeads (Ø = 2.8 ,m), used as artificial spermatozoa, were coated with lectin Con A and cultured together with 75 unfertilized oocytes (group A) remaining after intracytoplasmic sperm injection. Con A binds specifically to ,-D-mannose and ,-D-glucose. As a control, 75 unfertilized oocytes after intracytoplasmic sperm injection (group B) were also cultured together with Con A-covered microbeads, but in a medium containing a binding inhibiting sugar (,-methyl-mannopyrasosid). The number and distribution of the microbeads on human oocytes of both groups were analysed on scanning electron microscopy images. Beads on oocytes of group A had binding patterns similar to those of spermatozoa. They were distributed in an extremely heterogeneous way with various numbers of bound beads both on individual and different oocytes. Most of the group A oocytes (85%) had more than 50 beads bound to the zona, in contrast to the control oocytes of group B, where 68% had less than 10 bound beads. The use of an inhibiting sugar abolished the binding capacity of the microbeads nearly completely. This technique is a powerful tool for the detection of binding sites on the zona pellucida, i.e. those sugars that are responsible for contact between spermatozoa and the zona pellucida. [source]

Cell-surface matrix proteins and sialic acids in cell-crystal adhesion; the effect of crystal binding on the viability of human CAKI-1 renal epithelial cells

BJU INTERNATIONAL, Issue 6 2003
G. Kramer
Objective To investigate the role of sialic acids and cellular matrix proteins as crystal-binding molecules in human calcium-oxalate nephrolithiasis. Materials and methods The well-defined human renal cancer cell line CAKI-1 was used a standard cell culture system. After enzymatic digestion of various cell surface molecules, the binding of ,2,6 (Sambucus nigra, SN-) and ,2,3 (Maackia amurensis, MA)-specific lectins to CAKI-1 cells was analysed. Simultaneously, the effect on adhesion and release of calcium oxalate monohydrate crystals was investigated (eight replicates). The effect of crystal adhesion on cell viability was assessed using Trypan blue exclusion (five replicates). Results Neuraminidase decreased MA-lectin binding of CAKI-1 cells by 39% (P < 0.05) but elevated SN-lectin binding by 812% (P < 0.05). Simultaneously, crystal binding to CAKI-1 cells was increased by 28% (P > 0.05). Pretreatment with collagenase type I, trypsin and dispase II reduced crystal-binding by 61,74% (P < 0.05) with no effect on sialic acid-specific lectin-binding. However, only collagenase type I and dispase (ratio 4 : 1) were also able to release crystals from their receptor-binding sites (P < 0.05). An increase in the number of cell surface-bound crystals correlated significantly with a decrease in cell viability (P < 0.05). Conclusions ,2,3-linked sialic acids protect cells from crystal-binding. Much greater SN-lectin binding associated with only moderately increased crystal binding argues against ,2,6-linked sialic acids as a main target structure of crystals. In contrast, collagen type I, type IV and/or fibronectin seem to be potent crystal-binding molecules on human renal epithelial cells, with collagen type I involved in a potential second step of crystal,cell interaction. [source]