Endogenous mammalian lectin localized extracellularly in lung elastic fibers

Cerra, R. F.

doi:10.1083/jcb.98.4.1580

Cited by 79 publications

(36 citation statements)

References 38 publications

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“…Isolation of RL-14.5 lectin cDNA Our previous immunocytochemical studies showed that subsets of central and peripheral neurons express a lectin of approximately 14 kDa that is recognized by antisera raised against a rat lung lectin of similar size (RL-14.5; Cerra et al, 1984;Regan et al, 1986). cDNA clones encoding a 14 kDa lectin isolated from rat lung have been isolated and sequenced (Clerch et al, 1988).…”

Section: Resultsmentioning

confidence: 99%

“…The Hep-2 cDNA is similar or identical to the sequence of the cDNA encoding a mouse 14 kDa lectin (Wilson et al, 1989). In addition, a XGTl 1 cDNA library constructed from embryonic day 15 rat spinal cord RNA was screened with antisera generated against the RL-14.5 lectin isolated from rat lung (Cerra et al, 1984). A series of cDNA clones identified with antibody or cDNA probes were sequenced.…”

Section: Resultsmentioning

confidence: 99%

“…In addition, a XGTll cDNA expression library prepared from RNA of El5 spinal cord (S. Temple and T. M. Jessell, unpublished observations) was screened with antibodies against RL-14.5 (Cerra et al, 1984) using published procedures (Young and Davis, 1983;Snyder and Davis, 1985). cDNAs were subcloned into M 13 vectors (Vierira and Messing, 1982) and sequenced using the dideoxy chain-termination technique (Sanger et al, 1977).…”

Section: Methodsmentioning

confidence: 99%

“…Two of these are soluble (non-membrane-bound) lectins that bind lactosamine-based carbohydrate structures (Barondes, 1984). Soluble lectins have been detected in a variety of cell types where they can be seen in the cytoplasm and appear to be secreted (Beyer and Barondes, 1982;Cerra et al, 1984). Upon isolation, these molecules can mediate the agglutination of a variety of different cell types (Barondes, 1984).…”

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confidence: 99%

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Selective expression of an endogenous lactose-binding lectin gene in subsets of central and peripheral neurons

et al. 1990

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Cellular interactions in a variety of vertebrate non-neural tissues are thought to be mediated by cell surface carbohydrate structures. The detection of cell-specific surface carbohydrates and carbohydrate- binding proteins within the embryonic nervous system has raised the possibility that carbohydrate recognition may also contribute to the interactions of developing neurons. Soluble lactose-binding lectins constitute one class of carbohydrate-binding proteins expressed in the vertebrate nervous system. We describe here the isolation of cDNAs from rat brain libraries encoding one of these lectins, RL-14.5, and demonstrate that this protein is not only homologous to other soluble lectins, but also identical in primary sequence to a lectin present in at least one non-neural tissue. RNA blot analysis and in situ hybridization reveal a restricted pattern of expression of RL-14.5 mRNA within the rat nervous system. High levels of RL-14.5 mRNA are present in primary sensory neurons and motoneurons in the spinal cord and brain stem. Moreover, expression of RL-14.5 mRNA in sensory and motoneurons is detectable soon after neuronal differentiation. These findings, together with previous studies demonstrating the selective expression of oligosaccharide ligands for RL-14.5 on the same neurons, are consistent with the idea that carbohydrate-mediated interactions contribute to the development of this subset of mammalian neurons.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

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confidence: 99%

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Selective expression of an endogenous lactose-binding lectin gene in subsets of central and peripheral neurons

et al. 1990

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“…In some species multiple forms of soluble lectins have been detected (3,9,10). Three acidic forms have been isolated from rat and human lung (3,10).…”

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Subunit structure of Ca dependent soluble goat hepatic lectin: Evidence that it has antigenic structural relationship with soluble 14K lectin family

Ali¹,

Ola

Bhat

1996

IUBMB Life

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Summary:The subunit structure of soluble goat hepatic lectin was studied by determining molecular weight under nondenaturing conditions by gel filtration and denaturing conditions by SDS PAGE. Affinity purified lectin was subjected to HPLC on asahipack column equilibrated with 10 mM Tris-HC1 pH 7.5, containing lmM CaC121mM 2-mercaptoethanol and 0.1M NaC1. The lectin was eluted under single peak at retention time of 12 rain. corresponding to molecular weight of 38Kd. On SDS-PAGE in the presence and absence of 2-mercaptoethanol protein moved as single band with Rm 0.45, which corresponds to molecular weight of 20 Kd. The results suggest that soluble goat hepatic lectin is a dimmer of identical subunits which are linked together by noncovalent interactions. The interaction of monoclonal antibodies raised against soluble goat hepatic lectin (MGHL/20) with hemagglutinin from different species as sheep, human, rat, bovine and chicken was studied in PBS by solid phase binding assay. MGHL/20 showed 29-89% binding with these lectin. However no binding was found with Ca ++ dependent membrane bound lectin. These results indicate that soluble goat hepatic lectin possesses antigenic structural relationship with soluble 14 K lectin family.

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Endogenous sugar-binding proteins in human breast tissue and benign and malignant breast lesions

Gabius

Bodanowitz²,

Schauer³

1988

Cancer

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Binding of carbohydrate moieties was detected in tissue sections of human breast by employing two types of labeled ligands: neoglycoproteins (chemically glycosylated, histochemically inert carrier protein) and desialylated naturally occurring glycoproteins. Paraffin-embedded, formalin-fixed sections from 40 benign and malignant breast lesions were examined for the presence and distribution of endogenous sugar receptors, employing a panel of 13 biotinylated neoglycoproteins, representing carbohydrates commonly found in naturally occurring glycoconjugates, and four biotinylated glycoproteins. Benign and malignant breast lesions revealed staining with mannosylated carrier neoglycoprotein in comparison to normal breast. A mixed pattern of staining localization and intensity was seen for different types of malignancy with this neoglycoprotein. Similarly, receptors for lactose and N-acetylglucosamine could only be detected within the cytoplasm for certain types of malignancy. Their nuclear localization, however, could also be seen in normal breast specimens. The extent of staining with different glycoproteins, containing different types of galactoside-terminal sugar chains, also appeared to differ between various types of breast cancer. The detection of endogenous sugar receptors by neoglycoproteins is proposed to contribute to an understanding of malignancy-associated alterations in the structure of their potential physiological ligands, the glycoconjugates. Changes in the structure and abundance of such glycoconjugates have commonly been detected with the use of plant lectins in histopathologic studies.

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Endogenous mammalian lectin localized extracellularly in lung elastic fibers

Cited by 79 publications

References 38 publications

Selective expression of an endogenous lactose-binding lectin gene in subsets of central and peripheral neurons

Selective expression of an endogenous lactose-binding lectin gene in subsets of central and peripheral neurons

Subunit structure of Ca dependent soluble goat hepatic lectin: Evidence that it has antigenic structural relationship with soluble 14K lectin family

Endogenous sugar-binding proteins in human breast tissue and benign and malignant breast lesions

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