Developmentally regulated lectin in embryonic chick muscle and a myogenic cell line

Nowak, Thomas; Haywood, Patricia L.; Barondes, Samuel H.

doi:10.1016/0006-291x(76)91195-5

Cited by 255 publications

(88 citation statements)

References 8 publications

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“…Interestingly, enhanced expression of ␣7␤1 integrin has been shown to prevent the onset of the dystrophic process in the mouse model for Duchenne muscular dystrophy (Burkin et al, 2001). These data suggest a role for galectin-1 in muscle differentiation, and this role is substantiated by several lines of evidence that show an increased fusion of myoblasts to the multinucleate muscle fiber stage in vitro in the presence of the lectin (Gartner and Podleski, 1975;Nowak et al, 1976;Watt et al, 2004). In both chick (Nowak et al, 1976) and mouse (Poirier et al, 1992) skeletal muscle development, the level of galectin-1 is highest during the maximum stage of myoblast fusion, implicating a role for the molecule in the myoblast recognition-fusion process (Nowak et al, 1976).…”

Section: Introductionmentioning

confidence: 85%

“…Puche et al (1996) report that galectin-1 may be implicated in neuronal pathfinding in mammals, and McGraw et al (2005a) report a reduction in nociception as well as a reduced regeneration of injured axons (McGraw et al, 2005b) in the galectin-1 null mice. Despite the fact that galectin-1 has been shown to play a role in myoblast fusion in vitro (Gartner and Podleski, 1975;Nowak et al, 1976;Den and Malinzak, 1977;Goldring et al, 2002), superficial examination of adult skeletal muscle of the galectin-1 null mouse revealed no obvious abnormalities. However, a detailed examination of skeletal muscle of the null mouse had never been undertaken.…”

Section: Introductionmentioning

confidence: 99%

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Lack of galectin‐1 results in defects in myoblast fusion and muscle regeneration

Georgiadis

Stewart

Pollard

et al. 2007

Developmental Dynamics

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Galectin-1 has been implicated in the development of skeletal muscle, being maximally expressed at the time of myofiber formation. Furthermore, in the presence of exogenous galectin-1, mononuclear myoblasts show increased fusion in vitro. In the current study, we have used the galectin-1 null mouse to elucidate the role of galectin-1 in skeletal muscle development and regeneration. Myoblasts derived from the galectin-1 mutant showed a reduced ability to fuse in vitro. In galectin-1 null mutants, there was evidence of a delay in muscle fiber development at the neonatal stage and muscle fiber diameter was reduced when compared with wild-type at the adult stage. Muscle regeneration was also compromised in the galectin-1 mutant with the process being delayed and a reduced fiber size being maintained. These results, therefore, show a definitive role for galectin-1 in fusion of myoblasts both in vitro, in vivo, and in regeneration after recovery from induced injury. Developmental Dynamics 236:1014 -1024, 2007.

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Section: Introductionmentioning

confidence: 85%

Section: Introductionmentioning

confidence: 99%

Lack of galectin‐1 results in defects in myoblast fusion and muscle regeneration

Georgiadis

Stewart

Pollard

et al. 2007

Developmental Dynamics

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“…Hemagglutination Assays-Trypsin-treated, glutaraldehyde fixed rabbit erythrocytes were prepared and tested in an agglutination assay according to the method of Nowak et al (12). Agglutination assays were performed in 96-well V-shaped microtiter plates with serial 2-fold dilutions of samples in 25 l of DES (0.15 M NaCl, 2 mM EDTA, 2 mM dithiothreitol), 50 l of 0.5% (w/v) BSA in 0.15 M NaCl and 25 l of a 4% suspension of rabbit erythrocytes.…”

Section: Table I Primers and Adapters Utilized In Low Stringency And mentioning

confidence: 99%

Isolation and Characterization of a Novel Eosinophil-specific Galectin Released into the Lungs in Response to Allergen Challenge

Dunphy¹,

Barcham²,

Bischof³

et al. 2002

Journal of Biological Chemistry

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A novel galectin cDNA (galectin-14) was cloned from ovine eosinophil-rich leukocytes by low stringency reverse transcriptase-PCR and cDNA library screening. Data base searches indicate that this gene encodes a novel prototype galectin that contains one putative carbohydrate recognition domain and exhibits most identity to galectin-9/ecalectin, a potent eosinophil chemoattractant. The sugar binding properties of the recombinant molecule were confirmed by a hemagglutination assay and lactose inhibition. The mRNA and protein of galectin-14 are expressed at high levels in eosinophilrich cell populations. Flow cytometry and cytospot staining demonstrate that the protein localizes to the cytoplasmic, but not the granular, compartment of eosinophils. In contrast, galectin-14 mRNA and protein were not detected in neutrophils, macrophages, or lymphocytes. Western blot analysis of bronchoalveolar lavage fluid indicates that galectin-14 is released from eosinophils into the lumen of the lungs after challenge with house dust mite allergen. The restricted expression of this novel galectin to eosinophils and its release into the lumen of the lung in a sheep asthma model indicates that it may play an important role in eosinophil function and allergic inflammation.The immune response of mammals to multicellular parasite infections and allergens is characterized by the recruitment of eosinophils (1, 2). The role eosinophils play in both parasite infections and allergic reactions remains controversial, and little is known of the specific function of eosinophil constituents in combating multicellular parasites or exacerbating allergic responses. The presence of eosinophils and eosinophil-derived products in the respiratory tract does, however, correlate with the pathological manifestations of allergic asthma (2-4).One of the limitations in the study of eosinophils is the scarcity of this cell population in normal individuals and the difficulty in obtaining sufficient numbers of unmanipulated cells from allergic tissues. Sheep offer a unique experimental system in which large numbers of eosinophils can be obtained using the relatively non-invasive procedure of mammary infusion of allergens followed by "milking" of the mammary gland to obtain the inflammatory cells recruited into the lumen (5, 6). Using this experimental system, the present study describes the identification of a novel galectin (galectin-14) specifically expressed by eosinophils. The expression of galectin-14 was up-regulated in the lung tissue of sensitized sheep challenged with house dust mite extract (HDM), 1 and the protein was released into the bronchoalveolar lavage (BAL) fluid.Galectins are carbohydrate binding proteins that have been increasingly implicated in both adaptive and innate immune responses. The eosinophil-specific expression of galectin-14 and its secretion into the lumen of the lung in a sheep asthma model indicates that it may play an important role in regulating the activity of eosinophils during allergic responses and further highlights the i...

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“…Trypsinization of red cells was carried out by the method of Nowak et al (9). Lectin unit (LU) was defined as the reciprocal of the highest dilution giving visible agglutination of the erythrocytes after 30 min of incubation.…”

Section: Trypsinization Of Red Cellsmentioning

confidence: 99%

Screening for carbohydrate-binding proteins in extracts of Uruguayan plants

Plá

Alonso

Batista‐Viera

et al. 2003

Braz J Med Biol Res

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The presence of carbohydrate-binding proteins, namely lectins, ß-galactosidases and amylases, was determined in aqueous extracts of plants collected in Uruguay. Twenty-six extracts were prepared from 15 Uruguayan plants belonging to 12 Phanerogam families. Among them, 18 extracts caused hemagglutination (HAG) that was inhibited by mono-and disaccharides in 13 cases, indicating the presence of lectins. The other 8 extracts did not cause any HAG with the four systems used to detect HAG activity (rabbit and mouse red cells, trypsin-treated rabbit and mouse red cells). For the extracts prepared from Solanum commersonii, HAG activity and HAG inhibition were similar for those prepared from tubers, leaves and fruits, with the chitocompounds being responsible for all the inhibitions. Purification of the S. commersonii tuber lectin was carried out by affinity chromatography on asialofetuin-Sepharose, and SDS-PAGE under reducing conditions gave a single band of M r of approximately 80 kDa. The monomer N-acetylglucosamine did not inhibit HAG induced by the purified lectin, but chitobiose inhibited HAG at 24 mM and chitotriose inhibited it at 1 mM. ß-Galactosidase activity was detected in leaves and stems of Cayaponia martiana, and in seeds from Datura ferox. Only traces of amylase activity were detected in some of the extracts analyzed. The present screening increases knowledge about the occurrence of carbohydrate-binding proteins present in regional plants.

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Developmentally regulated lectin in embryonic chick muscle and a myogenic cell line

Cited by 255 publications

References 8 publications

Lack of galectin‐1 results in defects in myoblast fusion and muscle regeneration

Lack of galectin‐1 results in defects in myoblast fusion and muscle regeneration

Isolation and Characterization of a Novel Eosinophil-specific Galectin Released into the Lungs in Response to Allergen Challenge

Screening for carbohydrate-binding proteins in extracts of Uruguayan plants

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